WO1998003195A9 - Procedes et compositions de modulation du taux de croissance - Google Patents
Procedes et compositions de modulation du taux de croissanceInfo
- Publication number
- WO1998003195A9 WO1998003195A9 PCT/US1997/012498 US9712498W WO9803195A9 WO 1998003195 A9 WO1998003195 A9 WO 1998003195A9 US 9712498 W US9712498 W US 9712498W WO 9803195 A9 WO9803195 A9 WO 9803195A9
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- cell
- abl
- cells
- nucleic acid
- tumor
- Prior art date
Links
- 230000004044 response Effects 0.000 title abstract description 22
- 239000000203 mixture Substances 0.000 title description 57
- 230000012010 growth Effects 0.000 title description 37
- 230000000051 modifying Effects 0.000 title description 2
- 201000011510 cancer Diseases 0.000 claims abstract description 31
- 210000004027 cells Anatomy 0.000 claims description 278
- 101710026335 TP53 Proteins 0.000 claims description 207
- 102100019730 TP53 Human genes 0.000 claims description 206
- 230000014509 gene expression Effects 0.000 claims description 112
- 230000000694 effects Effects 0.000 claims description 88
- 150000007523 nucleic acids Chemical class 0.000 claims description 68
- 108020004707 nucleic acids Proteins 0.000 claims description 64
- 239000003795 chemical substances by application Substances 0.000 claims description 48
- 210000004881 tumor cells Anatomy 0.000 claims description 32
- 229920001184 polypeptide Polymers 0.000 claims description 31
- 230000001404 mediated Effects 0.000 claims description 30
- 241000701161 unidentified adenovirus Species 0.000 claims description 30
- 230000001965 increased Effects 0.000 claims description 29
- 230000003612 virological Effects 0.000 claims description 27
- 206010028980 Neoplasm Diseases 0.000 claims description 26
- 230000006907 apoptotic process Effects 0.000 claims description 26
- 206010059512 Apoptosis Diseases 0.000 claims description 24
- 239000000126 substance Substances 0.000 claims description 22
- 210000001519 tissues Anatomy 0.000 claims description 22
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 19
- 239000002502 liposome Substances 0.000 claims description 18
- 238000002360 preparation method Methods 0.000 claims description 17
- 238000002965 ELISA Methods 0.000 claims description 14
- 238000001890 transfection Methods 0.000 claims description 14
- 241001430294 unidentified retrovirus Species 0.000 claims description 13
- 229960004857 Mitomycin Drugs 0.000 claims description 12
- NWIBSHFKIJFRCO-WUDYKRTCSA-N Mytomycin Chemical compound C1N2C(C(C(C)=C(N)C3=O)=O)=C3[C@@H](COC(N)=O)[C@@]2(OC)[C@@H]2[C@H]1N2 NWIBSHFKIJFRCO-WUDYKRTCSA-N 0.000 claims description 12
- LXZZYRPGZAFOLE-UHFFFAOYSA-L transplatin Chemical compound [H][N]([H])([H])[Pt](Cl)(Cl)[N]([H])([H])[H] LXZZYRPGZAFOLE-UHFFFAOYSA-L 0.000 claims description 12
- 239000007924 injection Substances 0.000 claims description 11
- 239000008194 pharmaceutical composition Substances 0.000 claims description 11
- VSJKWCGYPAHWDS-FQEVSTJZSA-N Camptothecin Chemical compound C1=CC=C2C=C(CN3C4=CC5=C(C3=O)COC(=O)[C@]5(O)CC)C4=NC2=C1 VSJKWCGYPAHWDS-FQEVSTJZSA-N 0.000 claims description 10
- 229960004316 cisplatin Drugs 0.000 claims description 10
- 238000002347 injection Methods 0.000 claims description 10
- AOJJSUZBOXZQNB-TZSSRYMLSA-N ADRIAMYCIN Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 claims description 9
- 229960004679 Doxorubicin Drugs 0.000 claims description 9
- VJJPUSNTGOMMGY-MRVIYFEKSA-N Etoposide Chemical compound COC1=C(O)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3[C@@H](O[C@H]3[C@@H]([C@@H](O)[C@@H]4O[C@H](C)OC[C@H]4O3)O)[C@@H]3[C@@H]2C(OC3)=O)=C1 VJJPUSNTGOMMGY-MRVIYFEKSA-N 0.000 claims description 9
- 229960005420 Etoposide Drugs 0.000 claims description 9
- 239000002246 antineoplastic agent Substances 0.000 claims description 9
- 210000004072 Lung Anatomy 0.000 claims description 8
- 230000002950 deficient Effects 0.000 claims description 8
- GHASVSINZRGABV-UHFFFAOYSA-N 5-flurouricil Chemical compound FC1=CNC(=O)NC1=O GHASVSINZRGABV-UHFFFAOYSA-N 0.000 claims description 7
- 229960002949 Fluorouracil Drugs 0.000 claims description 7
- 239000002245 particle Substances 0.000 claims description 7
- 229940009456 Adriamycin Drugs 0.000 claims description 6
- 210000004185 Liver Anatomy 0.000 claims description 6
- 238000001262 western blot Methods 0.000 claims description 6
- 241000432074 Adeno-associated virus Species 0.000 claims description 4
- 229960000640 Dactinomycin Drugs 0.000 claims description 4
- 108010092160 Dactinomycin Proteins 0.000 claims description 4
- 210000003491 Skin Anatomy 0.000 claims description 4
- 241000700618 Vaccinia virus Species 0.000 claims description 4
- 206010047461 Viral infection Diseases 0.000 claims description 4
- 208000001756 Virus Disease Diseases 0.000 claims description 4
- RJURFGZVJUQBHK-IIXSONLDSA-N actinomycin D Chemical compound C[C@H]1OC(=O)[C@H](C(C)C)N(C)C(=O)CN(C)C(=O)[C@@H]2CCCN2C(=O)[C@@H](C(C)C)NC(=O)[C@H]1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)N[C@@H]4C(=O)N[C@@H](C(N5CCC[C@H]5C(=O)N(C)CC(=O)N(C)[C@@H](C(C)C)C(=O)O[C@@H]4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-IIXSONLDSA-N 0.000 claims description 4
- 238000004520 electroporation Methods 0.000 claims description 4
- 230000004927 fusion Effects 0.000 claims description 4
- 230000002601 intratumoral Effects 0.000 claims description 4
- 241001529453 unidentified herpesvirus Species 0.000 claims description 4
- 230000017613 viral reproduction Effects 0.000 claims description 4
- 210000001185 Bone Marrow Anatomy 0.000 claims description 3
- 210000002307 Prostate Anatomy 0.000 claims description 3
- 210000000952 Spleen Anatomy 0.000 claims description 3
- SGTNSNPWRIOYBX-UHFFFAOYSA-N Verapamil Chemical compound C1=C(OC)C(OC)=CC=C1CCN(C)CCCC(C#N)(C(C)C)C1=CC=C(OC)C(OC)=C1 SGTNSNPWRIOYBX-UHFFFAOYSA-N 0.000 claims description 3
- 238000001638 lipofection Methods 0.000 claims description 3
- 210000001938 protoplasts Anatomy 0.000 claims description 3
- 229960001722 verapamil Drugs 0.000 claims description 3
- 210000004369 Blood Anatomy 0.000 claims description 2
- 210000000601 Blood Cells Anatomy 0.000 claims description 2
- 210000004556 Brain Anatomy 0.000 claims description 2
- 210000000481 Breast Anatomy 0.000 claims description 2
- 210000001072 Colon Anatomy 0.000 claims description 2
- 210000004696 Endometrium Anatomy 0.000 claims description 2
- 210000003238 Esophagus Anatomy 0.000 claims description 2
- ZCOLJUOHXJRHDI-FZHKGVQDSA-N Genistein 7-O-glucoside Natural products O([C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](CO)O1)c1cc(O)c2C(=O)C(c3ccc(O)cc3)=COc2c1 ZCOLJUOHXJRHDI-FZHKGVQDSA-N 0.000 claims description 2
- ZCOLJUOHXJRHDI-CMWLGVBASA-N Genistin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=CC(O)=C2C(=O)C(C=3C=CC(O)=CC=3)=COC2=C1 ZCOLJUOHXJRHDI-CMWLGVBASA-N 0.000 claims description 2
- 210000003128 Head Anatomy 0.000 claims description 2
- 210000003734 Kidney Anatomy 0.000 claims description 2
- 210000001165 Lymph Nodes Anatomy 0.000 claims description 2
- 210000003739 Neck Anatomy 0.000 claims description 2
- OSTGTTZJOCZWJG-UHFFFAOYSA-N Nitrosourea Chemical compound NC(=O)N=NO OSTGTTZJOCZWJG-UHFFFAOYSA-N 0.000 claims description 2
- 210000001672 Ovary Anatomy 0.000 claims description 2
- 210000000496 Pancreas Anatomy 0.000 claims description 2
- 210000002784 Stomach Anatomy 0.000 claims description 2
- 210000001550 Testis Anatomy 0.000 claims description 2
- 239000008280 blood Substances 0.000 claims description 2
- 210000000813 small intestine Anatomy 0.000 claims description 2
- 241001655883 Adeno-associated virus - 1 Species 0.000 claims 1
- 238000002648 combination therapy Methods 0.000 abstract description 5
- 230000001640 apoptogenic Effects 0.000 abstract description 3
- 230000006882 induction of apoptosis Effects 0.000 abstract 1
- 102100002185 EP300 Human genes 0.000 description 84
- 101700011490 EP300 Proteins 0.000 description 84
- 101710036042 NOTCH1 Proteins 0.000 description 84
- 229920003013 deoxyribonucleic acid Polymers 0.000 description 70
- 108090001123 antibodies Proteins 0.000 description 43
- 102000004965 antibodies Human genes 0.000 description 43
- 230000027455 binding Effects 0.000 description 43
- 101700048555 CDK2 Proteins 0.000 description 39
- 101710022308 CDKN1A Proteins 0.000 description 39
- 102100002974 CDKN1A Human genes 0.000 description 39
- 101700045377 mvp1 Proteins 0.000 description 39
- 101700033061 GRA5 Proteins 0.000 description 38
- 101700045188 NSG1 Proteins 0.000 description 38
- 101700020165 RHOA Proteins 0.000 description 38
- 101710029715 TCEAL1 Proteins 0.000 description 38
- 101700073473 TPT1 Proteins 0.000 description 38
- 101700009395 orf8 Proteins 0.000 description 38
- 101700012276 wos2 Proteins 0.000 description 38
- 235000018102 proteins Nutrition 0.000 description 37
- 102000004169 proteins and genes Human genes 0.000 description 37
- 108090000623 proteins and genes Proteins 0.000 description 37
- 239000000523 sample Substances 0.000 description 37
- 230000003321 amplification Effects 0.000 description 35
- 238000003199 nucleic acid amplification method Methods 0.000 description 35
- 108091000081 Phosphotransferases Proteins 0.000 description 31
- 102000001253 Protein Kinases Human genes 0.000 description 31
- 238000000034 method Methods 0.000 description 30
- 229920000160 (ribonucleotides)n+m Polymers 0.000 description 29
- MBABOKRGFJTBAE-UHFFFAOYSA-N Methyl methanesulfonate Chemical compound COS(C)(=O)=O MBABOKRGFJTBAE-UHFFFAOYSA-N 0.000 description 27
- 239000000047 product Substances 0.000 description 27
- 231100000277 DNA damage Toxicity 0.000 description 22
- 150000001875 compounds Chemical class 0.000 description 20
- 230000001939 inductive effect Effects 0.000 description 20
- 230000036191 S Phase Effects 0.000 description 18
- 230000018199 S phase Effects 0.000 description 18
- 239000000427 antigen Substances 0.000 description 18
- 102000038129 antigens Human genes 0.000 description 18
- 108091007172 antigens Proteins 0.000 description 18
- 230000001419 dependent Effects 0.000 description 18
- 238000001514 detection method Methods 0.000 description 18
- 230000004913 activation Effects 0.000 description 17
- 230000015572 biosynthetic process Effects 0.000 description 17
- 230000002708 enhancing Effects 0.000 description 17
- 239000003550 marker Substances 0.000 description 17
- 230000035897 transcription Effects 0.000 description 17
- 241000700605 Viruses Species 0.000 description 16
- 239000003623 enhancer Substances 0.000 description 15
- 239000000243 solution Substances 0.000 description 15
- 238000000338 in vitro Methods 0.000 description 14
- 229920000023 polynucleotide Polymers 0.000 description 14
- 239000002157 polynucleotide Substances 0.000 description 14
- 108010047814 Antigen-Antibody Complex Proteins 0.000 description 13
- 238000004458 analytical method Methods 0.000 description 13
- 230000001105 regulatory Effects 0.000 description 13
- 230000035492 administration Effects 0.000 description 12
- 238000004166 bioassay Methods 0.000 description 12
- 230000001738 genotoxic Effects 0.000 description 12
- 231100000024 genotoxic Toxicity 0.000 description 12
- 108020003175 receptors Proteins 0.000 description 12
- 102000005962 receptors Human genes 0.000 description 12
- 230000002194 synthesizing Effects 0.000 description 12
- 230000003828 downregulation Effects 0.000 description 11
- 238000003786 synthesis reaction Methods 0.000 description 11
- 238000002560 therapeutic procedure Methods 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- 238000007792 addition Methods 0.000 description 10
- 230000022131 cell cycle Effects 0.000 description 10
- 230000010261 cell growth Effects 0.000 description 10
- 230000001809 detectable Effects 0.000 description 10
- 230000003993 interaction Effects 0.000 description 10
- 239000000463 material Substances 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 9
- 230000002068 genetic Effects 0.000 description 9
- 238000002318 immunoblotting Methods 0.000 description 9
- 230000002401 inhibitory effect Effects 0.000 description 9
- 239000003446 ligand Substances 0.000 description 9
- 239000006166 lysate Substances 0.000 description 9
- 239000002609 media Substances 0.000 description 9
- 230000035772 mutation Effects 0.000 description 9
- 238000006366 phosphorylation reaction Methods 0.000 description 9
- 230000000865 phosphorylative Effects 0.000 description 9
- 230000001225 therapeutic Effects 0.000 description 9
- 238000005406 washing Methods 0.000 description 9
- 239000005089 Luciferase Substances 0.000 description 8
- 230000033228 biological regulation Effects 0.000 description 8
- 230000001413 cellular Effects 0.000 description 8
- 239000003814 drug Substances 0.000 description 8
- 229940079593 drugs Drugs 0.000 description 8
- 238000001415 gene therapy Methods 0.000 description 8
- 241000894007 species Species 0.000 description 8
- 229920000272 Oligonucleotide Polymers 0.000 description 7
- -1 dipstick Substances 0.000 description 7
- 210000002950 fibroblast Anatomy 0.000 description 7
- 210000004962 mammalian cells Anatomy 0.000 description 7
- 230000002018 overexpression Effects 0.000 description 7
- 230000001177 retroviral Effects 0.000 description 7
- 239000011780 sodium chloride Substances 0.000 description 7
- 230000002103 transcriptional Effects 0.000 description 7
- 108010035563 Chloramphenicol O-Acetyltransferase Proteins 0.000 description 6
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 6
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 6
- 102000033147 ERVK-25 Human genes 0.000 description 6
- 108020004999 Messenger RNA Proteins 0.000 description 6
- 229920001850 Nucleic acid sequence Polymers 0.000 description 6
- 238000003782 apoptosis assay Methods 0.000 description 6
- 239000007864 aqueous solution Substances 0.000 description 6
- 239000002585 base Substances 0.000 description 6
- 230000000295 complement Effects 0.000 description 6
- 201000009910 diseases by infectious agent Diseases 0.000 description 6
- 238000005755 formation reaction Methods 0.000 description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- 230000003211 malignant Effects 0.000 description 6
- 229920002106 messenger RNA Polymers 0.000 description 6
- 230000005522 programmed cell death Effects 0.000 description 6
- 239000002904 solvent Substances 0.000 description 6
- 230000001131 transforming Effects 0.000 description 6
- 206010006187 Breast cancer Diseases 0.000 description 5
- 229920001405 Coding region Polymers 0.000 description 5
- 229920002676 Complementary DNA Polymers 0.000 description 5
- 229940110715 ENZYMES FOR TREATMENT OF WOUNDS AND ULCERS Drugs 0.000 description 5
- 101710038044 ERVK-6 Proteins 0.000 description 5
- 229940088598 Enzyme Drugs 0.000 description 5
- 108060001084 Luciferase family Proteins 0.000 description 5
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 5
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 5
- 241000700159 Rattus Species 0.000 description 5
- 239000002168 alkylating agent Substances 0.000 description 5
- 239000002775 capsule Substances 0.000 description 5
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- 239000011248 coating agent Substances 0.000 description 5
- 238000000576 coating method Methods 0.000 description 5
- 239000002299 complementary DNA Substances 0.000 description 5
- 239000006185 dispersion Substances 0.000 description 5
- 238000009472 formulation Methods 0.000 description 5
- 230000000977 initiatory Effects 0.000 description 5
- 238000000021 kinase assay Methods 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- 230000023603 positive regulation of transcription initiation, DNA-dependent Effects 0.000 description 5
- 230000035755 proliferation Effects 0.000 description 5
- 238000001959 radiotherapy Methods 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 5
- 230000035916 transactivation Effects 0.000 description 5
- 239000003981 vehicle Substances 0.000 description 5
- 210000000170 Cell Membrane Anatomy 0.000 description 4
- 230000004568 DNA-binding Effects 0.000 description 4
- 241000668709 Dipterocarpus costatus Species 0.000 description 4
- 108010092799 EC 2.7.7.49 Proteins 0.000 description 4
- 101710003775 ERVK-10 Proteins 0.000 description 4
- 101710037030 ERVK-11 Proteins 0.000 description 4
- 101710009283 ERVK-18 Proteins 0.000 description 4
- 101710009286 ERVK-19 Proteins 0.000 description 4
- 101710035700 ERVK-25 Proteins 0.000 description 4
- 101710014468 ERVK-7 Proteins 0.000 description 4
- 101710014482 ERVK-8 Proteins 0.000 description 4
- 101710043924 HERVK_113 Proteins 0.000 description 4
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 4
- 101710029649 MDV043 Proteins 0.000 description 4
- 102000007981 Ornithine carbamoyltransferases Human genes 0.000 description 4
- 108091000036 Ornithine carbamoyltransferases Proteins 0.000 description 4
- 102000014961 Protein Precursors Human genes 0.000 description 4
- 108010078762 Protein Precursors Proteins 0.000 description 4
- 101710006375 RNASEH1 Proteins 0.000 description 4
- 101700078434 RT67 Proteins 0.000 description 4
- 102000006601 Thymidine Kinase Human genes 0.000 description 4
- 108020004440 Thymidine Kinase Proteins 0.000 description 4
- 108010067390 Viral Proteins Proteins 0.000 description 4
- 102000016350 Viral Proteins Human genes 0.000 description 4
- 239000004480 active ingredient Substances 0.000 description 4
- 230000036755 cellular response Effects 0.000 description 4
- 230000000973 chemotherapeutic Effects 0.000 description 4
- 238000002512 chemotherapy Methods 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 239000012133 immunoprecipitate Substances 0.000 description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
- 238000001990 intravenous administration Methods 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 230000001613 neoplastic Effects 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 238000004806 packaging method and process Methods 0.000 description 4
- 230000037361 pathway Effects 0.000 description 4
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 4
- 230000001402 polyadenylating Effects 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- OZAIFHULBGXAKX-UHFFFAOYSA-N precursor Substances N#CC(C)(C)N=NC(C)(C)C#N OZAIFHULBGXAKX-UHFFFAOYSA-N 0.000 description 4
- DNIAPMSPPWPWGF-UHFFFAOYSA-N propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 4
- 101700086982 rnh Proteins 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 241001515965 unidentified phage Species 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 229920001817 Agar Polymers 0.000 description 3
- 229940098773 Bovine Serum Albumin Drugs 0.000 description 3
- 108091003117 Bovine Serum Albumin Proteins 0.000 description 3
- WOVKYSAHUYNSMH-RRKCRQDMSA-N Bromodeoxyuridine Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(Br)=C1 WOVKYSAHUYNSMH-RRKCRQDMSA-N 0.000 description 3
- 229950004398 Broxuridine Drugs 0.000 description 3
- 208000005623 Carcinogenesis Diseases 0.000 description 3
- 210000000349 Chromosomes Anatomy 0.000 description 3
- 102000020504 Collagenase family Human genes 0.000 description 3
- 108060005980 Collagenase family Proteins 0.000 description 3
- 102000012605 Cystic Fibrosis Transmembrane Conductance Regulator Human genes 0.000 description 3
- 108010079245 Cystic Fibrosis Transmembrane Conductance Regulator Proteins 0.000 description 3
- 101700011961 DPOM Proteins 0.000 description 3
- 102100002070 FOS Human genes 0.000 description 3
- 230000035521 G2 Phase Effects 0.000 description 3
- 230000010337 G2 phase Effects 0.000 description 3
- 210000003494 Hepatocytes Anatomy 0.000 description 3
- 208000009889 Herpes Simplex Diseases 0.000 description 3
- 206010025650 Malignant melanoma Diseases 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 238000000636 Northern blotting Methods 0.000 description 3
- 101700061424 POLB Proteins 0.000 description 3
- 101700054624 RF1 Proteins 0.000 description 3
- 108050008067 Rad9 Proteins 0.000 description 3
- 108020004682 Single-Stranded DNA Proteins 0.000 description 3
- 238000002105 Southern blotting Methods 0.000 description 3
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 3
- 108010001801 Tumor Necrosis Factor-alpha Proteins 0.000 description 3
- 230000036462 Unbound Effects 0.000 description 3
- 210000002845 Virion Anatomy 0.000 description 3
- 239000008272 agar Substances 0.000 description 3
- 108010084541 asialoorosomucoid Proteins 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 3
- 229960002685 biotin Drugs 0.000 description 3
- 235000020958 biotin Nutrition 0.000 description 3
- 239000011616 biotin Substances 0.000 description 3
- UIIMBOGNXHQVGW-UHFFFAOYSA-M buffer Substances [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 3
- 230000025084 cell cycle arrest Effects 0.000 description 3
- 230000023359 cell cycle switching, meiotic to mitotic cell cycle Effects 0.000 description 3
- 230000004663 cell proliferation Effects 0.000 description 3
- 229960002424 collagenase Drugs 0.000 description 3
- 238000005520 cutting process Methods 0.000 description 3
- 125000004122 cyclic group Chemical group 0.000 description 3
- 230000001086 cytosolic Effects 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- 239000002612 dispersion media Substances 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 3
- 239000010931 gold Substances 0.000 description 3
- 229910052737 gold Inorganic materials 0.000 description 3
- 238000009396 hybridization Methods 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 238000003364 immunohistochemistry Methods 0.000 description 3
- 239000004615 ingredient Substances 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 230000002147 killing Effects 0.000 description 3
- 239000006193 liquid solution Substances 0.000 description 3
- 201000001441 melanoma Diseases 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000006011 modification reaction Methods 0.000 description 3
- 210000000056 organs Anatomy 0.000 description 3
- 238000007911 parenteral administration Methods 0.000 description 3
- 239000004033 plastic Substances 0.000 description 3
- 229920003023 plastic Polymers 0.000 description 3
- 229920000136 polysorbate Polymers 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 3
- 230000003362 replicative Effects 0.000 description 3
- 238000010839 reverse transcription Methods 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 230000011664 signaling Effects 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 108090000464 transcription factors Proteins 0.000 description 3
- 102000003995 transcription factors Human genes 0.000 description 3
- 239000002753 trypsin inhibitor Substances 0.000 description 3
- 238000004450 types of analysis Methods 0.000 description 3
- 238000011144 upstream manufacturing Methods 0.000 description 3
- UCSJYZPVAKXKNQ-HZYVHMACSA-N 1-[(1S,2R,3R,4S,5R,6R)-3-carbamimidamido-6-{[(2R,3R,4R,5S)-3-{[(2S,3S,4S,5R,6S)-4,5-dihydroxy-6-(hydroxymethyl)-3-(methylamino)oxan-2-yl]oxy}-4-formyl-4-hydroxy-5-methyloxolan-2-yl]oxy}-2,4,5-trihydroxycyclohexyl]guanidine Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 102100008450 AFP Human genes 0.000 description 2
- 229940100198 ALKYLATING AGENTS Drugs 0.000 description 2
- 206010001258 Adenoviral infection Diseases 0.000 description 2
- 102100000690 CHL1 Human genes 0.000 description 2
- 101710025159 CMPK1 Proteins 0.000 description 2
- 102000004040 Capsid Proteins Human genes 0.000 description 2
- 108090000565 Capsid Proteins Proteins 0.000 description 2
- 241000701022 Cytomegalovirus Species 0.000 description 2
- 108009000097 DNA Replication Proteins 0.000 description 2
- 230000004543 DNA replication Effects 0.000 description 2
- 102000016615 EC 2.7.7.49 Human genes 0.000 description 2
- 210000001161 Embryo, Mammalian Anatomy 0.000 description 2
- 210000000981 Epithelium Anatomy 0.000 description 2
- ZMMJGEGLRURXTF-UHFFFAOYSA-N Ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 2
- 206010073306 Exposure to radiation Diseases 0.000 description 2
- 108060001038 FOS Proteins 0.000 description 2
- 102000011422 GADD45 protein Human genes 0.000 description 2
- 108091007852 GADD45 protein Proteins 0.000 description 2
- 102000018898 GTPase-Activating Proteins Human genes 0.000 description 2
- 108091006078 GTPase-accelerating proteins Proteins 0.000 description 2
- 102000005720 Glutathione Transferase family Human genes 0.000 description 2
- 108010070675 Glutathione Transferase family Proteins 0.000 description 2
- 102100009498 HMGB1 Human genes 0.000 description 2
- 108010014739 HMGB1 Protein Proteins 0.000 description 2
- 241000700721 Hepatitis B virus Species 0.000 description 2
- 206010073071 Hepatocellular carcinoma Diseases 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 108090000745 Immune Sera Proteins 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 231100000002 MTT assay Toxicity 0.000 description 2
- 238000000134 MTT assay Methods 0.000 description 2
- 210000003205 Muscles Anatomy 0.000 description 2
- 229920002957 Naked DNA Polymers 0.000 description 2
- 108010069196 Neural Cell Adhesion Molecules Proteins 0.000 description 2
- 239000000020 Nitrocellulose Substances 0.000 description 2
- 108010089610 Nuclear Proteins Proteins 0.000 description 2
- 102000007999 Nuclear Proteins Human genes 0.000 description 2
- 210000004940 Nucleus Anatomy 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 229940072417 Peroxidase Drugs 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 108090000437 Peroxidases Proteins 0.000 description 2
- 102000003993 Phosphatidylinositol 3-Kinases Human genes 0.000 description 2
- 108090000430 Phosphatidylinositol 3-Kinases Proteins 0.000 description 2
- 108010071690 Prealbumin Proteins 0.000 description 2
- 102000007584 Prealbumin Human genes 0.000 description 2
- 102000003923 Protein Kinase C Human genes 0.000 description 2
- 108090000315 Protein Kinase C Proteins 0.000 description 2
- 102000005663 Proto-Oncogene Proteins c-abl Human genes 0.000 description 2
- 108010045292 Proto-Oncogene Proteins c-abl Proteins 0.000 description 2
- 108050002653 Retinoblastoma Protein Proteins 0.000 description 2
- 241000700584 Simplexvirus Species 0.000 description 2
- QORWJWZARLRLPR-UHFFFAOYSA-H Tricalcium phosphate Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 108010026331 alpha-Fetoproteins Proteins 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 238000000137 annealing Methods 0.000 description 2
- 239000003429 antifungal agent Substances 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 239000001506 calcium phosphate Substances 0.000 description 2
- 229910000389 calcium phosphate Inorganic materials 0.000 description 2
- 235000011010 calcium phosphates Nutrition 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 230000030833 cell death Effects 0.000 description 2
- 230000022534 cell killing Effects 0.000 description 2
- 229920002083 cellular DNA Polymers 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000007795 chemical reaction product Substances 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 239000003593 chromogenic compound Substances 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000001351 cycling Effects 0.000 description 2
- 238000006073 displacement reaction Methods 0.000 description 2
- 239000003937 drug carrier Substances 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 230000001747 exhibiting Effects 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 2
- 238000002509 fluorescent in situ hybridization Methods 0.000 description 2
- 238000001476 gene delivery Methods 0.000 description 2
- 210000004602 germ cell Anatomy 0.000 description 2
- 239000001963 growth media Substances 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 230000003100 immobilizing Effects 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 230000002779 inactivation Effects 0.000 description 2
- 239000000411 inducer Substances 0.000 description 2
- 230000003834 intracellular Effects 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000010253 intravenous injection Methods 0.000 description 2
- 230000001678 irradiating Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 239000007951 isotonicity adjuster Substances 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000006210 lotion Substances 0.000 description 2
- 239000012139 lysis buffer Substances 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000011278 mitosis Effects 0.000 description 2
- 230000017066 negative regulation of growth Effects 0.000 description 2
- 230000001264 neutralization Effects 0.000 description 2
- 229920001220 nitrocellulos Polymers 0.000 description 2
- 230000000144 pharmacologic effect Effects 0.000 description 2
- 150000003904 phospholipids Chemical class 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 238000003752 polymerase chain reaction Methods 0.000 description 2
- 238000006116 polymerization reaction Methods 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 230000002285 radioactive Effects 0.000 description 2
- 230000010837 receptor-mediated endocytosis Effects 0.000 description 2
- 230000002829 reduced Effects 0.000 description 2
- 238000001228 spectrum Methods 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 230000037327 stress response Effects 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 230000000576 supplementary Effects 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 230000000699 topical Effects 0.000 description 2
- 230000002588 toxic Effects 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000001052 transient Effects 0.000 description 2
- 239000001226 triphosphate Substances 0.000 description 2
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- JLPULHDHAOZNQI-ZTIMHPMXSA-N 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCC\C=C/C\C=C/CCCCC JLPULHDHAOZNQI-ZTIMHPMXSA-N 0.000 description 1
- 101710025088 66 Proteins 0.000 description 1
- ZTOJFFHGPLIVKC-CLFAGFIQSA-N ABTS Chemical compound S/1C2=CC(S(O)(=O)=O)=CC=C2N(CC)C\1=N\N=C1/SC2=CC(S(O)(=O)=O)=CC=C2N1CC ZTOJFFHGPLIVKC-CLFAGFIQSA-N 0.000 description 1
- 101700033661 ACTB Proteins 0.000 description 1
- 102100011550 ACTB Human genes 0.000 description 1
- 101710032514 ACTI Proteins 0.000 description 1
- 102100001249 ALB Human genes 0.000 description 1
- 101710027066 ALB Proteins 0.000 description 1
- 101710028063 APCS Proteins 0.000 description 1
- 102100003659 APCS Human genes 0.000 description 1
- 206010069754 Acquired gene mutation Diseases 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 108020005544 Antisense RNA Proteins 0.000 description 1
- NOFOAYPPHIUXJR-APNQCZIXSA-N Aphidicolin Chemical compound C1[C@@]23[C@@]4(C)CC[C@@H](O)[C@@](C)(CO)[C@@H]4CC[C@H]3C[C@H]1[C@](CO)(O)CC2 NOFOAYPPHIUXJR-APNQCZIXSA-N 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 210000003719 B-Lymphocytes Anatomy 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 210000001772 Blood Platelets Anatomy 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 208000003174 Brain Neoplasms Diseases 0.000 description 1
- ABIUHPWEYMSGSR-UHFFFAOYSA-N Bromocresol purple Chemical compound BrC1=C(O)C(C)=CC(C2(C3=CC=CC=C3S(=O)(=O)O2)C=2C=C(Br)C(O)=C(C)C=2)=C1 ABIUHPWEYMSGSR-UHFFFAOYSA-N 0.000 description 1
- 210000003771 C cell Anatomy 0.000 description 1
- 102100000189 CD22 Human genes 0.000 description 1
- 101700020617 CD22 Proteins 0.000 description 1
- 101700024634 CDK16 Proteins 0.000 description 1
- 206010057248 Cell death Diseases 0.000 description 1
- 210000003837 Chick Embryo Anatomy 0.000 description 1
- 229960004926 Chlorobutanol Drugs 0.000 description 1
- OSASVXMJTNOKOY-UHFFFAOYSA-N Chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 1
- 108010077544 Chromatin Proteins 0.000 description 1
- 210000003483 Chromatin Anatomy 0.000 description 1
- 102000012422 Collagen Type I Human genes 0.000 description 1
- 108010022452 Collagen Type I Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 229940109239 Creatinine Drugs 0.000 description 1
- 102000003903 Cyclin-Dependent Kinases Human genes 0.000 description 1
- 108090000266 Cyclin-Dependent Kinases Proteins 0.000 description 1
- 210000000805 Cytoplasm Anatomy 0.000 description 1
- UHDGCWIWMRVCDJ-CCXZUQQUSA-N Cytosar Chemical compound O=C1N=C(N)C=CN1[C@H]1[C@@H](O)[C@H](O)[C@@H](CO)O1 UHDGCWIWMRVCDJ-CCXZUQQUSA-N 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N D-Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- 101710007887 DHFR Proteins 0.000 description 1
- 102100005838 DHFR Human genes 0.000 description 1
- 108010017826 DNA Polymerase I Proteins 0.000 description 1
- 102000004594 DNA Polymerase I Human genes 0.000 description 1
- 230000007118 DNA alkylation Effects 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 108091000102 DNA-Binding Proteins Proteins 0.000 description 1
- 102000031025 DNA-Binding Proteins Human genes 0.000 description 1
- 101710028159 DNTT Proteins 0.000 description 1
- 102100002445 DNTT Human genes 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 206010013801 Duchenne muscular dystrophy Diseases 0.000 description 1
- 241000725618 Duck hepatitis B virus Species 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 108010015776 EC 1.1.3.4 Proteins 0.000 description 1
- 102000003425 EC 1.14.18.1 Human genes 0.000 description 1
- 108060008724 EC 1.14.18.1 Proteins 0.000 description 1
- 102100010813 EGF Human genes 0.000 description 1
- 101700033006 EGF Proteins 0.000 description 1
- 102000001301 EGF receptors Human genes 0.000 description 1
- 108060006698 EGF receptors Proteins 0.000 description 1
- 101700036757 ERN1 Proteins 0.000 description 1
- 102100016655 ERN1 Human genes 0.000 description 1
- 101700014948 ERN2 Proteins 0.000 description 1
- 102000033180 ERVK-6 Human genes 0.000 description 1
- 101710027967 ERVW-1 Proteins 0.000 description 1
- 229940116977 Epidermal Growth Factor Drugs 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 229920001272 Exogenous DNA Polymers 0.000 description 1
- 102100016764 FYN Human genes 0.000 description 1
- 101700037202 FYN Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 230000004668 G2/M phase Effects 0.000 description 1
- 102100008842 GH1 Human genes 0.000 description 1
- 229940116332 GLUCOSE OXIDASE Drugs 0.000 description 1
- IRSCQMHQWWYFCW-UHFFFAOYSA-N Ganciclovir Chemical compound O=C1NC(N)=NC2=C1N=CN2COC(CO)CO IRSCQMHQWWYFCW-UHFFFAOYSA-N 0.000 description 1
- 229960002963 Ganciclovir Drugs 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 241000713813 Gibbon ape leukemia virus Species 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 229960002743 Glutamine Drugs 0.000 description 1
- 210000003714 Granulocytes Anatomy 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 206010053759 Growth retardation Diseases 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N Guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 102100019126 HBB Human genes 0.000 description 1
- 101710023137 HSP90B1 Proteins 0.000 description 1
- 102100009909 HSP90B1 Human genes 0.000 description 1
- 101710006403 HSPA5 Proteins 0.000 description 1
- 102100015710 HSPA5 Human genes 0.000 description 1
- 230000036499 Half live Effects 0.000 description 1
- 108091005902 Hemoglobin subunit beta Proteins 0.000 description 1
- 206010019695 Hepatic neoplasm Diseases 0.000 description 1
- 102000018713 Histocompatibility Antigens Class II Human genes 0.000 description 1
- 108010027412 Histocompatibility Antigens Class II Proteins 0.000 description 1
- 108090000246 Histone Acetyltransferases Proteins 0.000 description 1
- 102000003893 Histone Acetyltransferases Human genes 0.000 description 1
- 108010033040 Histones Proteins 0.000 description 1
- 102000006947 Histones Human genes 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 241000598171 Human adenovirus sp. Species 0.000 description 1
- 241000700588 Human alphaherpesvirus 1 Species 0.000 description 1
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 1
- 241000725303 Human immunodeficiency virus Species 0.000 description 1
- 241000701806 Human papillomavirus Species 0.000 description 1
- 229920002153 Hydroxypropyl cellulose Polymers 0.000 description 1
- 101700082799 IL2RA Proteins 0.000 description 1
- 101700085586 IRE1A Proteins 0.000 description 1
- 101700019719 IRE1B Proteins 0.000 description 1
- 101700015336 ISG20 Proteins 0.000 description 1
- 102100002950 ISG20 Human genes 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 1
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 1
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 1
- 102000003996 Interferon beta Human genes 0.000 description 1
- 108090000467 Interferon beta Proteins 0.000 description 1
- 102000000588 Interleukin-2 Human genes 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 1
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 1
- QWTDNUCVQCZILF-UHFFFAOYSA-N Isopentane Chemical compound CCC(C)C QWTDNUCVQCZILF-UHFFFAOYSA-N 0.000 description 1
- JJWLVOIRVHMVIS-UHFFFAOYSA-N Isopropylamine Chemical compound CC(C)N JJWLVOIRVHMVIS-UHFFFAOYSA-N 0.000 description 1
- 102000019145 JUN kinase activity proteins Human genes 0.000 description 1
- 108040008094 JUN kinase activity proteins Proteins 0.000 description 1
- 102100002583 KAT2B Human genes 0.000 description 1
- 101700083085 KAT2B Proteins 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- ZQISRDCJNBUVMM-YFKPBYRVSA-N L-histidinol Chemical compound OC[C@@H](N)CC1=CNC=N1 ZQISRDCJNBUVMM-YFKPBYRVSA-N 0.000 description 1
- 229940067606 Lecithin Drugs 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- 101710007526 MAP3K14 Proteins 0.000 description 1
- 101710029922 MAPK9 Proteins 0.000 description 1
- 102100005528 MAPK9 Human genes 0.000 description 1
- 102100019155 MDM2 Human genes 0.000 description 1
- 101700032565 MDM2 Proteins 0.000 description 1
- 108010059343 MM Form Creatine Kinase Proteins 0.000 description 1
- 102100015262 MYC Human genes 0.000 description 1
- 229920002521 Macromolecule Polymers 0.000 description 1
- 108090000157 Metallothionein Proteins 0.000 description 1
- 102000003792 Metallothionein Human genes 0.000 description 1
- 206010027476 Metastasis Diseases 0.000 description 1
- 210000004080 Milk Anatomy 0.000 description 1
- 101710017500 MitHPPK/DHPS Proteins 0.000 description 1
- 206010061309 Neoplasm progression Diseases 0.000 description 1
- 241001028048 Nicola Species 0.000 description 1
- 102000006570 Non-Histone Chromosomal Proteins Human genes 0.000 description 1
- 108010008964 Non-Histone Chromosomal Proteins Proteins 0.000 description 1
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 1
- 210000001623 Nucleosomes Anatomy 0.000 description 1
- 108010047956 Nucleosomes Proteins 0.000 description 1
- 206010025310 Other lymphomas Diseases 0.000 description 1
- XAPRFLSJBSXESP-UHFFFAOYSA-N Oxycinchophen Chemical compound N=1C2=CC=CC=C2C(C(=O)O)=C(O)C=1C1=CC=CC=C1 XAPRFLSJBSXESP-UHFFFAOYSA-N 0.000 description 1
- 101710016786 P/C Proteins 0.000 description 1
- 101700044505 PUB33 Proteins 0.000 description 1
- 101700045570 PUB34 Proteins 0.000 description 1
- 101700046887 PUB35 Proteins 0.000 description 1
- 101700066160 PUB51 Proteins 0.000 description 1
- 101700067511 PUB52 Proteins 0.000 description 1
- 101700068819 PUB53 Proteins 0.000 description 1
- 101700086326 PUB70 Proteins 0.000 description 1
- 229950010131 PUROMYCIN Drugs 0.000 description 1
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N PUROMYCIN Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 1
- 102000016387 Pancreatic Elastase Human genes 0.000 description 1
- 108010067372 Pancreatic Elastase Proteins 0.000 description 1
- 241001631646 Papillomaviridae Species 0.000 description 1
- 235000019483 Peanut oil Nutrition 0.000 description 1
- 229940049954 Penicillin Drugs 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- WGVWLKXZBUVUAM-UHFFFAOYSA-N Pentanochlor Chemical compound CCCC(C)C(=O)NC1=CC=C(C)C(Cl)=C1 WGVWLKXZBUVUAM-UHFFFAOYSA-N 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 229940067631 Phospholipids Drugs 0.000 description 1
- 102000007982 Phosphoproteins Human genes 0.000 description 1
- 235000008331 Pinus X rigitaeda Nutrition 0.000 description 1
- 235000011613 Pinus brutia Nutrition 0.000 description 1
- 241000018646 Pinus brutia Species 0.000 description 1
- 210000002381 Plasma Anatomy 0.000 description 1
- 108010022233 Plasminogen Activator Inhibitor 1 Proteins 0.000 description 1
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 1
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 1
- YJGVMLPVUAXIQN-XVVDYKMHSA-N Podophyllotoxin Chemical compound COC1=C(OC)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3[C@H](O)[C@@H]3[C@@H]2C(OC3)=O)=C1 YJGVMLPVUAXIQN-XVVDYKMHSA-N 0.000 description 1
- 208000000474 Poliomyelitis Diseases 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 241001505332 Polyomavirus sp. Species 0.000 description 1
- 241001272996 Polyphylla fullo Species 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- MFDFERRIHVXMIY-UHFFFAOYSA-N Procaine Chemical compound CCN(CC)CCOC(=O)C1=CC=C(N)C=C1 MFDFERRIHVXMIY-UHFFFAOYSA-N 0.000 description 1
- 102000007066 Prostate-Specific Antigen Human genes 0.000 description 1
- 108010072866 Prostate-Specific Antigen Proteins 0.000 description 1
- 208000008425 Protein Deficiency Diseases 0.000 description 1
- 102000012500 Proto-Oncogene Proteins c-crk Human genes 0.000 description 1
- 108010022955 Proto-Oncogene Proteins c-crk Proteins 0.000 description 1
- 108010066717 Q beta Replicase Proteins 0.000 description 1
- 108020004412 RNA 3' Polyadenylation Signals Proteins 0.000 description 1
- 108010009460 RNA Polymerase II Proteins 0.000 description 1
- 102000009572 RNA Polymerase II Human genes 0.000 description 1
- 241000282941 Rangifer tarandus Species 0.000 description 1
- 102000009661 Repressor Proteins Human genes 0.000 description 1
- 108010034634 Repressor Proteins Proteins 0.000 description 1
- 102000012121 Retinoblastoma Protein Human genes 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N Rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 210000003705 Ribosomes Anatomy 0.000 description 1
- 241000714474 Rous sarcoma virus Species 0.000 description 1
- 101710017605 Rv2228c Proteins 0.000 description 1
- 102100015622 SCGB1A1 Human genes 0.000 description 1
- 101710010598 SCGB1A1 Proteins 0.000 description 1
- 102100007015 SERPINE1 Human genes 0.000 description 1
- 101710009384 SRC Proteins 0.000 description 1
- 235000003534 Saccharomyces carlsbergensis Nutrition 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 1
- 229940081969 Saccharomyces cerevisiae Drugs 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 101710023234 Segment 5 Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 102000011763 Serum Amyloid A Protein Human genes 0.000 description 1
- 108010076895 Serum Amyloid A Protein Proteins 0.000 description 1
- 102000007365 Sialoglycoproteins Human genes 0.000 description 1
- 108010032838 Sialoglycoproteins Proteins 0.000 description 1
- 241000144282 Sigmodon Species 0.000 description 1
- 229940075582 Sorbic Acid Drugs 0.000 description 1
- 206010041823 Squamous cell carcinoma Diseases 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 241000521327 Streptomyces caespitosus Species 0.000 description 1
- 229960005322 Streptomycin Drugs 0.000 description 1
- 108091008153 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 208000000389 T-Cell Leukemia Diseases 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 229940033663 Thimerosal Drugs 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L Thiomersal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 230000036335 Tissue distribution Effects 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- GETQZCLCWQTVFV-UHFFFAOYSA-N Trimethylamine Chemical compound CN(C)C GETQZCLCWQTVFV-UHFFFAOYSA-N 0.000 description 1
- 102000013394 Troponin I Human genes 0.000 description 1
- 108010065729 Troponin I Proteins 0.000 description 1
- 102000015098 Tumor Suppressor Protein p53 Human genes 0.000 description 1
- 108010078814 Tumor Suppressor Protein p53 Proteins 0.000 description 1
- 206010053614 Type III immune complex mediated reaction Diseases 0.000 description 1
- 238000003302 UV-light treatment Methods 0.000 description 1
- 108010046334 Urease Proteins 0.000 description 1
- 101700021643 VP4A Proteins 0.000 description 1
- 101700028070 VPX Proteins 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- VBJHPXDIVMXHJU-UHFFFAOYSA-N Zeocin Chemical compound N=1C(C=2SC=C(N=2)C(=O)NCCCCN=C(N)N)CSC=1CCNC(=O)C(C(O)C)NC(=O)C(C)C(O)C(C)NC(=O)C(C(OC1C(C(O)C(O)C(CO)O1)OC1C(C(OC(N)=O)C(O)C(CO)O1)O)C=1[N]C=NC=1)NC(=O)C1=NC(C(CC(N)=O)NCC(N)C(N)=O)=NC(N)=C1C VBJHPXDIVMXHJU-UHFFFAOYSA-N 0.000 description 1
- 108010084455 Zeocin Proteins 0.000 description 1
- 239000003070 absorption delaying agent Substances 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000003213 activating Effects 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 230000001154 acute Effects 0.000 description 1
- 230000001058 adult Effects 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 229940050528 albumin Drugs 0.000 description 1
- 230000000172 allergic Effects 0.000 description 1
- 108010090535 alpha-albumin Proteins 0.000 description 1
- 150000001413 amino acids Chemical group 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000844 anti-bacterial Effects 0.000 description 1
- 230000000118 anti-eoplastic Effects 0.000 description 1
- 230000000340 anti-metabolite Effects 0.000 description 1
- 230000001028 anti-proliferant Effects 0.000 description 1
- 239000002256 antimetabolite Substances 0.000 description 1
- 239000003972 antineoplastic antibiotic Substances 0.000 description 1
- 229920002847 antisense RNA Polymers 0.000 description 1
- 239000003443 antiviral agent Substances 0.000 description 1
- 201000008937 atopic dermatitis Diseases 0.000 description 1
- 230000003190 augmentative Effects 0.000 description 1
- 230000001580 bacterial Effects 0.000 description 1
- 108010003152 bacteriophage T7 RNA polymerase Proteins 0.000 description 1
- 229960000626 benzylpenicillin Drugs 0.000 description 1
- 230000001588 bifunctional Effects 0.000 description 1
- 239000003012 bilayer membrane Substances 0.000 description 1
- BPYKTIZUTYGOLE-IFADSCNNSA-N bilirubin Chemical compound N1C(=O)C(C)=C(C=C)\C1=C\C1=C(C)C(CCC(O)=O)=C(CC2=C(C(C)=C(\C=C/3C(=C(C=C)C(=O)N\3)C)N2)CCC(O)=O)N1 BPYKTIZUTYGOLE-IFADSCNNSA-N 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 230000000903 blocking Effects 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 230000036952 cancer formation Effects 0.000 description 1
- 230000000711 cancerogenic Effects 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 231100000504 carcinogenesis Toxicity 0.000 description 1
- 231100000315 carcinogenic Toxicity 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 238000002659 cell therapy Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 230000002759 chromosomal Effects 0.000 description 1
- 238000000749 co-immunoprecipitation Methods 0.000 description 1
- 201000011231 colorectal cancer Diseases 0.000 description 1
- 201000010989 colorectal carcinoma Diseases 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 239000003184 complementary RNA Substances 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 230000000875 corresponding Effects 0.000 description 1
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 230000002354 daily Effects 0.000 description 1
- 230000003247 decreasing Effects 0.000 description 1
- 230000004059 degradation Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000003935 denaturing gradient gel electrophoresis Methods 0.000 description 1
- 230000001687 destabilization Effects 0.000 description 1
- 230000000368 destabilizing Effects 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- UGMCXQCYOVCMTB-UHFFFAOYSA-K dihydroxy(stearato)aluminium Chemical compound CCCCCCCCCCCCCCCCCC(=O)O[Al](O)O UGMCXQCYOVCMTB-UHFFFAOYSA-K 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000003534 dna topoisomerase inhibitor Substances 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 241001493065 dsRNA viruses Species 0.000 description 1
- 210000002919 epithelial cells Anatomy 0.000 description 1
- 238000011124 ex vivo culture Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- WSFSSNUMVMOOMR-UHFFFAOYSA-N formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 1
- 231100000221 frame shift mutation induction Toxicity 0.000 description 1
- 239000012458 free base Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 102000037240 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 108010074605 gamma-Globulins Proteins 0.000 description 1
- 238000004817 gas chromatography Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000010363 gene targeting Methods 0.000 description 1
- 201000002406 genetic disease Diseases 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 108010017007 glucose-regulated proteins Proteins 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 239000003630 growth substance Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000003505 heat denaturation Methods 0.000 description 1
- 230000003067 hemagglutinative Effects 0.000 description 1
- 230000000493 homozygosity Effects 0.000 description 1
- 235000011167 hydrochloric acid Nutrition 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 125000004435 hydrogen atoms Chemical class [H]* 0.000 description 1
- 150000004679 hydroxides Chemical class 0.000 description 1
- TUJKJAMUKRIRHC-UHFFFAOYSA-N hydroxyl radical Chemical class [OH] TUJKJAMUKRIRHC-UHFFFAOYSA-N 0.000 description 1
- 239000001863 hydroxypropyl cellulose Substances 0.000 description 1
- 235000010977 hydroxypropyl cellulose Nutrition 0.000 description 1
- 229940071676 hydroxypropylcellulose Drugs 0.000 description 1
- 239000005457 ice water Substances 0.000 description 1
- 230000016178 immune complex formation Effects 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 238000003365 immunocytochemistry Methods 0.000 description 1
- 230000002055 immunohistochemical Effects 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 230000001771 impaired Effects 0.000 description 1
- 238000010249 in-situ analysis Methods 0.000 description 1
- 230000000415 inactivating Effects 0.000 description 1
- 230000002458 infectious Effects 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 150000007529 inorganic bases Chemical class 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 101700052395 ire-1 Proteins 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 230000003907 kidney function Effects 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N lactose group Chemical group OC1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@@H](O)[C@H](O2)CO)[C@H](O1)CO GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 101710017890 large T Proteins 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 230000003902 lesions Effects 0.000 description 1
- 231100000225 lethality Toxicity 0.000 description 1
- 238000007834 ligase chain reaction Methods 0.000 description 1
- 239000006194 liquid suspension Substances 0.000 description 1
- 230000003908 liver function Effects 0.000 description 1
- 238000003670 luciferase enzyme activity assay Methods 0.000 description 1
- 201000005202 lung cancer Diseases 0.000 description 1
- 201000005244 lung non-small cell carcinoma Diseases 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 108010031099 mannose receptor Proteins 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 210000004779 membrane envelope Anatomy 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 150000007522 mineralic acids Chemical class 0.000 description 1
- 239000003226 mitogen Substances 0.000 description 1
- 230000000394 mitotic Effects 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000020654 modulation by virus of host translation Effects 0.000 description 1
- 239000002991 molded plastic Substances 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 108010045030 monoclonal antibodies Proteins 0.000 description 1
- 102000005614 monoclonal antibodies Human genes 0.000 description 1
- 239000002324 mouth wash Substances 0.000 description 1
- 210000000663 muscle cells Anatomy 0.000 description 1
- 230000000869 mutational Effects 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 239000002853 nucleic acid probe Substances 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 231100000590 oncogenic Toxicity 0.000 description 1
- 230000002246 oncogenic Effects 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 150000007530 organic bases Chemical class 0.000 description 1
- 238000004816 paper chromatography Methods 0.000 description 1
- 239000012188 paraffin wax Substances 0.000 description 1
- 230000036961 partial Effects 0.000 description 1
- 238000005192 partition Methods 0.000 description 1
- 239000000312 peanut oil Substances 0.000 description 1
- 230000002093 peripheral Effects 0.000 description 1
- 230000002688 persistence Effects 0.000 description 1
- 230000002085 persistent Effects 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 229960003742 phenol Drugs 0.000 description 1
- 235000011007 phosphoric acid Nutrition 0.000 description 1
- 150000003016 phosphoric acids Chemical class 0.000 description 1
- 229960001237 podophyllotoxin Drugs 0.000 description 1
- 229930001140 podophyllotoxin Natural products 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 230000032029 positive regulation of DNA repair Effects 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 230000002335 preservative Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 229960004919 procaine Drugs 0.000 description 1
- 230000002035 prolonged Effects 0.000 description 1
- ZDWVWKDAWBGPDN-UHFFFAOYSA-O propidium Chemical compound C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 ZDWVWKDAWBGPDN-UHFFFAOYSA-O 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 238000009163 protein therapy Methods 0.000 description 1
- 230000002685 pulmonary Effects 0.000 description 1
- 238000003906 pulsed field gel electrophoresis Methods 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 230000003439 radiotherapeutic Effects 0.000 description 1
- 102000027656 receptor tyrosine kinases Human genes 0.000 description 1
- 108091007921 receptor tyrosine kinases Proteins 0.000 description 1
- 230000022983 regulation of cell cycle Effects 0.000 description 1
- 230000009703 regulation of cell differentiation Effects 0.000 description 1
- 230000021014 regulation of cell growth Effects 0.000 description 1
- 230000026267 regulation of growth Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000028617 response to DNA damage stimulus Effects 0.000 description 1
- 230000034408 response to ionizing radiation Effects 0.000 description 1
- 108091007521 restriction endonucleases Proteins 0.000 description 1
- 238000007894 restriction fragment length polymorphism technique Methods 0.000 description 1
- 230000000717 retained Effects 0.000 description 1
- 201000000582 retinoblastoma Diseases 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000005204 segregation Methods 0.000 description 1
- 239000008159 sesame oil Substances 0.000 description 1
- 235000011803 sesame oil Nutrition 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 231100000188 sister chromatid exchange Toxicity 0.000 description 1
- 230000001340 slower Effects 0.000 description 1
- KEAYESYHFKHZAL-UHFFFAOYSA-N sodium Chemical compound [Na] KEAYESYHFKHZAL-UHFFFAOYSA-N 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000000392 somatic Effects 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- WSWCOQWTEOXDQX-UHFFFAOYSA-N sorbic acid Chemical compound CC=CC=CC(O)=O WSWCOQWTEOXDQX-UHFFFAOYSA-N 0.000 description 1
- 235000010199 sorbic acid Nutrition 0.000 description 1
- 239000004334 sorbic acid Substances 0.000 description 1
- 102000009076 src-Family Kinases Human genes 0.000 description 1
- 108010087686 src-Family Kinases Proteins 0.000 description 1
- 230000001954 sterilising Effects 0.000 description 1
- 231100000803 sterility Toxicity 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 230000004936 stimulating Effects 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 230000020382 suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002459 sustained Effects 0.000 description 1
- 230000001360 synchronised Effects 0.000 description 1
- 230000002195 synergetic Effects 0.000 description 1
- 238000004809 thin layer chromatography Methods 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 108060008606 traP Proteins 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
- 238000003146 transient transfection Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 230000001960 triggered Effects 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- 125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 1
- WFKWXMTUELFFGS-UHFFFAOYSA-N tungsten Chemical compound [W] WFKWXMTUELFFGS-UHFFFAOYSA-N 0.000 description 1
- 229910052721 tungsten Inorganic materials 0.000 description 1
- 239000010937 tungsten Substances 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 230000003827 upregulation Effects 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 230000029812 viral genome replication Effects 0.000 description 1
- 238000001429 visible spectrum Methods 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 238000007794 visualization technique Methods 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N β-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
Definitions
- the present invention relates generally to the fields of cancer therapy and control of cell proliferation. More particularly, it concerns the use of the c-Abl and p300 genes, either alone or in combination with p53, to induce programmed cell death or decreased cell proliferation.
- Certain cancer treatment methods involve damaging the DNA of the cancer cell.
- the cellular response to DNA damage includes activation of DNA repair, cell cycle arrest and lethality (Hall, 1988).
- the signaling events responsible for the regulation of these events remain unclear.
- EGR early growth response
- Mitomycin C is an antitumor antibiotic isolated from Streptomyces caespitosus that covalently binds to DNA (Tomasz et al, 1988) This agent induces both monofunctional and bifunctional DNA lesions (Carrano et al, 1979) Other studies have demonstrated that MMC stimulates the formation of hydroxyl radicals (Dusre et al, 1989) Although the precise mechanism of action of this agent is unclear, MMC-induced cytotoxicity has been attributed to DNA alkylation and the formation of interstrand cross-links (Carrano et al. , 1979, Dusre et al. , 1989, Tomasz et al.
- Protein tyrosine kinases can be divided into receptor-type and nonreceptor- type (Src-like) kinases (Cantley et al, 1991; Hanks et al, 1988; Bonni et al, 1993; Larner et al, 1993; Ruff- Jamison et al, 1993).
- Several protein tyrosine kinases have been purified from the cytosolic fractions of various tissues (Nakamura et al, 1988; Wong & Goldberg, 1984;
- the Src-like kinases which can associate with receptors at the plasma membrane, induce rapid tyrosine phosphorylation and/or activation of effectors such as phospholipase C- ⁇ l (PLC ⁇ l) (Carter et al, 1991), PLC ⁇ 2 (Hempel et al, 1992), mitogen-activated protein
- MAP MAP kinase
- GAP GTPase activating protein
- PI3-K phosphatidylinositol 3 -kinase
- the present invention in one embodiment, provides a method for increasing p53-mediated apoptosis in a tumor cell comprising the step of increasing the activity level of at least one of c-Abl and p300 in said tumor cell.
- the tumor cell may be derived from various tissues including brain, lung, liver, spleen, kidney, lymph node, small intestine, blood cells, pancreas, colon, stomach, breast, endometrium, prostate, testicle, ovary, skin, head and neck, esophagus, bone marrow and blood tissue
- the activity levels of both c-Abl and p300 are increased in said tumor cell
- Increasing activities may be accomplished (i) by providing at least one of a c-Abl polypeptide and a p300 polypeptide to said tumor cell in an amount effective to increase p53-mediated apoptosis, (ii) by providing at least one of a nucleic acid encoding c-Abl and a nucleic acid encoding p300 to said tumor cell, wherein said nucleic acid is operably linked to a promoter active in eukaryotic cells in an amount effective to increase p53-mediated apoptosis, or (iii) by providing an agent to said cell that increases the expression or stability of at least one of c-Abl and p300 in an amount effective to increase p53-mediated apoptosis
- nucleic acids contained in viral expression vectors, via infection of target cells by encapsulated viral vectors also is contemplated
- viral vectors include herpesvirus, adenovirus, vaccinia virus, retrovirus and adeno-associated virus
- the method may further comprise determining the p53 activity of the target cell Where the target cell is defective in p53, and the method further comprises providing to said tumor cell a nucleic acid encoding a wild-type p53 operably linked to a promoter active in eukaryotic cells
- the p53 nucleic acid preferably is contained in an expression vector, and more preferably in a viral vector
- target cells may be subjected, either before or after the methods described above, to ionizing radiation or to a chemotherapeutic agent
- the ionizing radiation may be x-irradiation or ⁇ -irradiation
- the chemotherapeutic agent may be mitomycin C, etoposide, genistin, cisplatin, 5-FU, adriamycin, doxorubicin, actinomycin D, verapamil, nitrosourea, ara-C and camptothecin
- a method for treating a patient having a tumor comprising the step of increasing the activity level of at least one of c-Abl and p300 in cells of said tumor Again, the activity level may be increased by providing at least one of a c-Abl polypeptide and a p300 polypeptide to said tumor in an amount effective to increase p53-mediated apoptosis in cells thereof
- the method may further comprising screening the tumor cells to determine the p53 status thereof
- the method may further comprise providing to said tumor cells a nucleic acid encoding a wild-type p53 operably linked to a promoter active in eukaryotic cells
- the method may further take advantage of combined therapies, for example, by additionally treating the tumor with ionizing radiation or a chemotherapeutic agent
- a method of screening a candidate substance for p53 -stimulatory activity comprising the steps of (i) providing a eukaryotic cell expressing a functional p300 polypeptide, (ii) contacting said cell with said candidate substance, and (iii) determining the effect of said candidate substance on the p300 level of said cell, wherein an increase in the p300 level in said cell, as compared to an untreated cell, indicates that said candidate substance increases p53 activity
- a similar method is provided where the effect of the candidate substance on c-Abl is determined
- the p300 or c-Abl level may be measured by Western blot or ELISA
- contacting comprises transferring said nucleic acid into said cell
- Methods of transferring include transfection, lipofection, protoplast fusion, bombardment, electroporation or viral infection
- a use of at least one of a p300 and a c-Abl polypeptide for the preparation of a pharmaceutical composition effective to increase p53-mediated apoptosis in a cell (ii) a use of at least one of a nucleic acid encoding a p300 polypeptide and a nucleic acid encoding a c-Abl polypeptide for the preparation of a pharmaceutical composition effective to increase apoptosis in a cell, (iii) a use of a p300 polypeptide or gene coding therefor for the preparation of a pharmaceutical composition for the treatment of cancer, and (iv) a use of a p300 polypeptide or gene coding therefor for the preparation of a pharmaceutical composition for the treatment of cancer
- kits for use in killing malignant cells or reducing their growth are kits for use in cancer treatment
- the kits of the invention will generally comprise, in suitable container means, pharmaceutical formulations of a p53 polypeptides or gene construct, c-Abl polypeptides or gene constructs and p300 polypeptides or gene constructs
- p53 polypeptides or gene construct a p53 polypeptides or gene construct
- c-Abl polypeptides or gene constructs p300 polypeptides or gene constructs
- kits for use in killing malignant cells or reducing their growth will generally comprise, in suitable container means, pharmaceutical formulations of a p53 polypeptides or gene construct, c-Abl polypeptides or gene constructs and p300 polypeptides or gene constructs
- These agents may be present within a single container, or these components may be provided in distinct or separate container means
- Classical chemotherapeutic pharmaceutical preparations also are contemplated for use with the therapeutic compositions of the present invention
- FIGS. lA-C Overexpression of kinase active c-Abl downregulates Cdk activity
- FIG 1A MCF-7 cells were transfected with 2 ⁇ g p53-enhancer-luciferase plasmid (mdm2NA-Luc) and, (1) 8 ⁇ g control vector pSRaMSVtkNeo, (2) 5 and 8 ⁇ g c-abl vector, (3) 5 and 8 ⁇ g c-Aabl (K-R) vector, and (4) 5 and 8 ⁇ g c-abl ⁇ Pro 4 vector
- Cells were also transfected with 2 ⁇ g SV40-promoter-luciferase plasmid (pGL2-control vector, Promega) and 8 ⁇ g c-Abl vector Luciferase activity was measured and normalized for protein concentration to that for control vector, D, MCF-7 cells were transfected with 8 ⁇ g control, c-abl, c-abl (K-R) of c-abl ⁇
- FIGS. 2A-D c-Abl kinase activity regulates irradiation (IR)-induced inhibition of Cdk2
- FIG 2A MCF-7 cells stably transfected with null pSR vector or c-abl (K-R) were treated with 5 Gy IR and collected after 3h Nuclei were isolated and nuclear proteins immunoprecipitated with anti-Abl (Ab-3, Oncogene Science) as described Immune- complex kinase was analyzed using a glutathione S transferase (GST)-Crk (120-225) fusion protein as substrate (top) And Abl immunoprecipitates were also analyzed by immunoblotting with anti-Abl (bottom)
- FIG 2B Lysates were immunoblotted with anti- Abl, anti-p53 (Ab-6, Oncogene Science), anti-p21, anti-GADD45 (AT-26, Santa Cruz Biotechnology) and anti-c-Myc (9E10, Santa Cruz Biotechnology)
- FIG 2C Lys
- FIGS. 3A-D c-Abl kinase activity regulates IR-induced growth arrest
- FIG 3 A Representative two-dimensional FACS analysis of MCF-7/pSR and MCF-7/c-Abl (K-R) cells after exposure to 0 or 5 Gy IR Synchronized cells were irradiated and percentage of cells in S phase was assessed at 24h Boxes labeled Rl, R2 and R3 represent S, Gl and G2/M phase cells, respectively
- FIG 3B Percentage of cells entering S phase after IR relative to control unirradiated cells Results are expressed as the mean ⁇ s e of 6 experiments for each of two (a,b) independently selected clones
- FIG 3C C57BL6 wild- type (ab h ) and abl' MEFs were exposed to 0 or 5 Gy and collected at 3 h Cell lysates were immunoblotted with anti-Abl and anti-PCNA antibodies
- FIGS. 4A-D c-Abl kinase downregulates Cdk2 activity by a p53-dependent. p21 -independent mechanism
- FIG 4A Lysates were immunoprecipitated with anti-Abl (left) or anti-p53 (right) and the precipitates analyzed by immunoblotting with the indicated antibodies
- FIG 4B MEFs (p59 7 , p53 +/+ ) n were transfected with the c-abl or c-abl (K-R) vectors and collected at 48 h
- FIG 4C MEFs (abt' ab ' ) 11 were exposed to D or 5 Gy and collected at the indicated times
- FIG 4D MEFs (p2T , p21 +/+ were transfected with the c-Abl or c-Abl (K-R) vectors and collected at 48 h
- Cell lysates were immunoprecipitated with anti-Cdk2 and the precipitates assayed for histone HI
- the c-Abl protein tyrosine kinase is activated by certain DNA-damaging agents, and its overexpression causes arrest in the Gl phase of the cell cycle by the tumor- suppressor protein p53 (Sawyers et al, 1994, Mattioni et al., 1995, Goga et al, 1995)
- the present investigators studied the role of c-Abl in growth arrest induced by DNA damage Transient transfection experiments using wild-type or inactivated c-Abl show that both induce expression of p21, an effector of p53, but only wild-type c-Abl down regulates the activity of the cyclin-dependent kinase Cdk2 and causes growth arrest
- Exposure to ionizing radiation of cells that stably express active or inactive c-Abl is associated with induction of c-Abl/p53 complexes and p21 expression.
- cells expressing the dominant-negative c-Abl mutant and cells lacking the c-abl gene are impaired in their ability to down-regulate Cdk2 or undergo Gl arrest in response to ionizing radiation.
- p300 is a nuclear protein originally identified for its ability to interact with adenovirus El A protein It is a regulator of transcription and interacts with a variety of cellular as well as viral proteins p300 possesses histone acetyltransferase activity resulting from either intrinsic activity and/or from an assocaited protein, P/CAF Bannister et al, 1996, Ogryzko et al, 1996, Yang et al, 1996 The acetylation of histones in thought to be involved in destabilization and restructuring of nucleosomes, which is likely a crucial event for accessibility of transcription factors to DNA templates
- p300 A role for p300 in control of cellular growth has been proposed on the basis of the functional behavior of adenovirus El A and SV40 Tag proteins, which lose the ability to bind p300 Moran, 1993, Avantaggiati et al, 1996, Eckner et al, 1996a Such mutants are defective in the induction of cellular DNA synthesis and, in several instances, of transformation
- p300 is required for the activation of muscle-specific genes and for cell cycle arrest during differentiation of muscle cells. Eckner et al, 1996b, Puri et al, 1997.
- mutations or translocation of the p300 gene has been described in human tumors.
- p300 mutations in colorectal carcinomas are somatic and coupled to deletion of the second allele of the gene, suggesting that p300 is consequently inactivated It also is induced upon a cell's exposure to radiation On the basis of this evidence, p300 is envisioned to be a negative regulator of cell growth
- p300 apparently is responsible for several p53-mediated functions, such as inhibition of API -regulated enhancers, transcriptional activation, apoptosis and cell cycle progression
- the present inventors have determined that p300 is activated by c-Abl More specifically, p300 is phosphorylated by a tyrosine kinase function of c-Abl This phosphorylation causes p300 interaction with p53, and the aforementioned activities
- the present invention exploits signaling pathways that are involved in the correction of DNA damage, in cell cycle progression and in apoptosis
- the methods involve the use of the c-Abl, p300 and p53 gene products to effect cellular responses to various external stimuli
- the present invention provides a means of increasing the levels of wild-type p53 expression in tumor cells, thereby allowing for an increased apoptosis or reduction in cellular proliferation
- c-Abl and p300 can increase the expression of wild-type p53
- cancers that express normal p53 can be treated with c-Abl genes or the c-Abl gene product, or with p300 or the corresponding p300 gene
- the compositions of the present invention can be used to augment conventional gene therapy, where wild- type p53 is introduced into tumor cells concomitantly with c-Abl and/or p300 to increase the level of p53 so that programmed cell death is triggered
- the present application is drawn, in one embodiment, to methods of screening cells for their ability to express wild-type p53 protein expression of cancer cells and to concomitantly induce apoptosis in said cells
- To augment the expression of p53 one would then add the c-Abl gene product and/or p300 to a cell If wild-type p53 is lacking in a cell, wild-type p53 and c-Abl are administered to a cell in combination to induce the apoptotic response
- Effective amounts are those amounts of compositions effective at reproducibly increasing wild-type p53 expression in cancer cells in comparison to their normal levels Compounds that achieve significant appropriate changes in activity will be used A significant increase in wild-type p53 expression, e.g., as measured using for example,
- Western blot analysis are represented by an increase in wild-type p53 levels of at least about 30%-40%, and most preferably, by increases of at least about 50%, with higher values of course being possible Assays that measure p53 content and expression in cells are well known in the art and may be conducted in vitro or in vivo
- MTT assay it may be desirable simply to measure inhibition of growth of cancer cells, for example, by measuring growth according to the MTT assay
- a significant inhibition in growth is represented by decreases of at least about 30%-40% as compared to uninhibited, and most preferably, of at least about 50%, with more significant decreases also being possible.
- Growth assays as measured by the MTT assay are well known in the art Assays may be conducted as described by Mosmann et al, 1983; Rubinstein et al, 1990 (incorporated herein by reference) Therefore, if a candidate substance exhibited inhibition of growth of cancer cells in this type of study, it would likely be a suitable compound for use in the present invention.
- vectors that incorporate nucleic acid sequences that encode the c-Abl and p300 sequences It is contemplated that these vectors may either be transiently incorporated into the host cell, or may be stably integrated into the host cell genome This expression preferably occurs in a mammalian cell, and even more preferably, the mammalian cell is a human cell.
- suitable vectors for use within the scope of the present invention include, but are not limited to, adenovirus, adeno-associated virus, retrovirus or herpes simplex virus 1.
- the present invention contemplates the preparation of nucleic acid molecules that comprise a coding region that contains regions complementary to and capable of hybridizing with a c-Abl gene sequence.
- the preferred nucleic acid molecules will be DNA sequences arranged in a vector, such as a virus or plasmid, and positioned under the control of an appropriate promoter.
- the antisense RNA molecule may itself be an appropriate nucleic acid, such as retrovirus RNA into which the appropriate coding sequences have been incorporated.
- the nucleic acids may be introduced into cells by means of liposomes, or the like.
- a target cell with a c-Abl and/or p300 construct in a combined amount effective to kill the cell. This process may involve contacting the cells with the p53 construct and c-Abl/p300 construct(s) at the same time.
- compositions or pharmacological formulations that includes both agents, or by contacting the cell with two distinct compositions or formulations, at the same time, wherein one composition includes the p53 construct and the other composition includes the c-Abl construct
- target cell where lacking a functional p53 molecule, may be first exposed to a p53 expression construct and then contacted with a c-Abl or p300 construct, or vice versa
- contacted and “exposed”, when applied to a cell are used herein to describe the process by which a p53 or c-Abl construct are delivered to a target cell or are placed in direct juxtaposition with the target cell
- either one or both agents are delivered to a cell in a combined amount effective to kill the cell, i.e , to induce programmed cell death or apoptosis
- killing i.e , to induce programmed cell death or apoptosis
- apoptosis are used interchangeably in the present text to describe a series of intracellular events that lead to target cell death Reduced cell growth refers to a lower rate of cellular proliferation than observed for the untreated cells
- p53 As a Tumor Suppressor p53 is currently recognized as a tumor suppressor gene (Montenarh, 1992) High levels have been found in many cells transformed by chemical carcinogenesis, ultraviolet radiation, and several viruses, including SV40 The p53 gene is a frequent target of mutational inactivation in a wide variety of human tumors and is already documented to be the most frequently-mutated gene in common human cancers (Mercer, 1992) It is mutated in over 50% of human NSCLC (Hollestein et al, 1991) and in a wide spectrum of other tumors
- the p53 gene encodes a 393-amino-acid phosphoprotein that can form complexes with host proteins such as large-T antigen and E1B
- the protein is found in normal tissues and cells, but at concentrations which are minute by comparison with transformed cells or tumor tissue Interestingly, wild-type p53 appears to be important in regulating cell growth and division Overexpression of wild-type p53 has been shown in some cases to be anti-proliferative in human tumor cell lines Thus p53 can act as a negative regulator of cell growth (Weinberg, 1991) and may directly suppress uncontrolled cell growth or indirectly activate genes that suppress this growth Thus, absence or inactivation of wild type p53 may contribute to transformation However, some studies indicate that the presence of mutant p53 may be necessary for full expression of the transforming potential of the gene
- Wild-type p53 is recognized as an important growth regulator in many cell types Mis-sense mutations are common for the p53 gene and are essential for the transforming ability of the oncogene
- a single genetic change prompted by point mutations can create carcinogenic p53 Unlike other oncogenes, however, p53 point mutations are known to occur in at least 30 distinct codons, often creating dominant alleles that produce shifts in cell phenotype without a reduction to homozygosity Additionally, many of these dominant negative alleles appear to be tolerated in the organism and passed on in the germ line Various mutant alleles appear to range from minimally dysfunctional to strongly penetrant, dominant negative alleles (Weinberg, 1991)
- a patient presenting a p53-positive tumor that expresses wild-type p53 will be treated with c-Abl and/or p300 based therapies
- the p53 status of the tumor cells will be determined using any conventional methods, examples of which are described below
- Patients may, but need not, have received previous chemo-, radio- or gene therapies
- patients will have adequate bone marrow function (defined as peripheral absolute granulocyte count of > 2,000/mm 3 and platelet count of 100,000/mm 3 ), adequate liver function (bilirubin ⁇ 1 5 mg/dl) and adequate renal function (creatinine ⁇ 1 5 mg/dl)
- the patient will be treated with a pharmaceutically acceptable form of the c-Abl and/or p300 gene products, or will be treated by gene therapy techniques that will allow the in vivo expression of the c-Abl or p300 gene products Alternatively, the patient may be treated with a substance that augments the expressionon c-Abl or p300 normally produced by the target cell Treatment regimens normally last between about 3 and 6 weeks, and involve repeat dosings In order to know whether a cell will respond to provision of c-Abl and/or p300, it must first be determined whether the cell expresses an active p53 molecule Thus, screening for p53 expression is an important first step
- detection methods can be employed in the present invention to detect the p53 status of a cell
- any assay that utilizes antibodies for detection for example, ELISAs, Western Blotting, immunoassay techniques etc
- assays that employ nucleotide probes may be used to identify the presence/absence/status of p53, for example, Southern blotting,
- Immunoassays encompassed by the present invention include, but are not limited to those described in U S Patent No 4,367,110 (double monoclonal antibody sandwich assay) and U S Patent No 4,452,901 (Western blot) Other assays include immunoprecipitation of labeled ligands and immunocytochemistry, both in vitro and in vivo
- Immunoassays in their most simple and direct sense, are binding assays. Certain preferred immunoassays are the various types of enzyme linked immunosorbent assays (ELISAs) and radioimmunoassays (RIA) known in the art Immunohistochemical detection using tissue sections is also particularly useful.
- ELISAs enzyme linked immunosorbent assays
- RIA radioimmunoassays
- anti-p53 antibodies are immobilized onto a selected surface exhibiting protein affinity, such as a well in a polystyrene microtiter plate Then, a test composition suspected of containing the desired antigen, such as a clinical sample, is added to the wells After binding and washing to remove non-specifically bound immune complexes, the bound antigen may be detected Detection is generally achieved by the addition of another antibody, specific for the desired antigen, that is linked to a detectable label This type of ELISA is a simple "sandwich ELISA" Detection may also be achieved by the addition of a second antibody specific for the desired antigen, followed by the addition of a third antibody that has binding affinity for the second antibody, with the third antibody being linked to a detectable label
- Varaitions of ELISA techniques are know to those of skill in the art
- the samples suspected of containing the desired antigen are immobilized onto the well surface and then contacted with the antibodies of the invention After binding and appropriate washing, the bound immune complexes are detected
- the immune complexes may be detected directly
- the immune complexes may be detected using a second antibody that has binding affinity for the first antigen specific antibody, with the second antibody being linked to a detectable label
- Competition ELISAs are also possible in which test samples compete for binding with known amounts of labeled antigens or antibodies
- the amount of reactive species in the unknown sample is determined by mixing the sample with the known labeled species before or during incubation ⁇ with coated wells
- the presence of reactive species in the sample acts to reduce the amount of labeled species available for binding to the well and thus reduces the ultimate signal
- ELISAs have certain features in common, such as coating, incubating or binding, washing to remove non-specifically bound species, and detecting the bound immune complexes These are described as below
- Antigen or antibodies may also be linked to a solid support, such as in the form of plate, beads, dipstick, membrane or column matrix, and the sample to be analyzed applied to the immobilized antigen or antibody
- a solid support such as in the form of plate, beads, dipstick, membrane or column matrix
- the sample to be analyzed applied to the immobilized antigen or antibody
- a plate with either antigen or antibody one will generally incubate the wells of the plate with a solution of the antigen or antibody, either overnight or for a specified period The wells of the plate will then be washed to remove incompletely adsorbed material Any remaining available surfaces of the wells are then "coated" with a nonspecific protein that is antigenically neutral with regard to the test antisera These include bovine serum albumin (BSA), casein and solutions of milk powder
- BSA bovine serum albumin
- casein casein
- the coating allows for blocking of nonspecific adsorption sites on the immobilizing surface and thus reduces the background caused by nonspecific binding of anti
- the immobilizing surface is contacted with the clinical or biological sample to be tested under conditions effective to allow immune complex
- Under conditions effective to allow immune complex (antigen/antibody) formation means that the conditions preferably include diluting the antigens and antibodies with solutions such as BSA, bovine gamma globulin (BGG) and phosphate buffered saline (PBS)/Tween These added agents also tend to assist in the reduction of nonspecific background
- the suitable conditions also mean that the incubation is at a temperature and for a period of time sufficient to allow effective binding Incubation steps are typically from about 1 to 2 to 4 hours, at temperatures preferably on the order of 25° to 27°C, or may be overnight at about 4°C or so
- washing often includes washing with a solution of
- the second or third antibody will have an associated label to allow detection
- this will be an enzyme that will generate color development upon incubating with an appropriate chromogenic substrate
- a urease, glucose oxidase, alkaline phosphatase or hydrogen peroxidase-conjugated antibody for a period of time and under conditions that favor the development of further immune complex formation, e.g., incubation for 2 hours at room temperature in a PBS-containing solution such as PBS-Tween.
- the amount of label is quantified, e.g., by incubation with a chromogenic substrate such as urea and bromocresol purple or 2,2'-azino-di-(3-ethyl-benzthiazoline-6-sulfonic acid [ABTS] and H 2 O , in the case of peroxidase as the enzyme label. Quantification is then achieved by measuring the degree of color generation, e.g., using a visible spectra spectrophotometer
- the label may be a chemiluminescent one.
- Assays for the p53 radiation status of the cell can determine normal/abnormal tissue distribution for diagnostic purposes
- Methods for in vitro and in situ analysis are well known and involve assessing binding of antigen-specific antibodies to tissues, cells or cell extracts These are conventional techniques well within the grasp of those skilled in the art
- the antibodies to p53 may be used in conjunction with both fresh-frozen and formalin-fixed, paraffin-embedded tissue blocks prepared for study by immunohistochemistry (IHC) Each tissue block may consist of 50 mg of residual "pulverized" tumor
- IHC immunohistochemistry
- frozen-sections may be prepared by rehydrating 50 ng of frozen pulverized tumor at room temperature in PBS in small plastic capsules, pelleting the particles by centrifugation, resuspending them in a viscous embedding medium (OCT), inverting the capsule and pelleting again by centrifugation, snap-freezing in -70°C isopentane, cutting the plastic capsule and removing the frozen cylinder of tissue, securing the tissue cylinder on a cryostat microtome chuck, and cutting 25-50 serial sections containing an average of about 500 remarkably intact tumor cells
- OCT viscous embedding medium
- Permanent-sections may be prepared by a similar method involving rehydration of the 50 mg sample in a plastic microfuge tube, pelleting, resuspending in 10% formalin for 4 hours fixation, washing/pelleting; resuspending in warm 2 5% agar, pelleting, cooling in ice water to harden the agar; removing the tissue/agar block from the tube, infiltrating and embedding the block in paraffin, and cutting up to 50 serial permanent sections
- nucleic acids may be isolated from cells according to standard methodologies (Sambrook et al, 1989)
- the nucleic acid may be genomic DNA or fractionated or whole cell RNA Where mRNA is used, it may be desired to convert the mRNA to a complementary DNA
- the RNA is whole cell RNA, in another, it is poly-A RNA Normally, the nucleic acid is amplified
- the specific nucleic acid of interest is identified in the sample directly using amplification or with a second, known nucleic acid following amplification
- the identified product is detected
- the detection may be performed by visual means (e.g., ethidium bromide staining of a gel)
- the detection may involve indirect identification of the product via chemiluminescence, radioactive scintigraphy of radiolabel or fluorescent label or even via a system using electrical or thermal impulse signals
- alterations should be read as including deletions, insertions, point mutations and duplications
- Point mutations result in stop codons, frameshift mutations or amino acid substitutions
- Somatic mutations are those occurring in non-germline tissues
- Germ-line tissue can occur in any tissue and are inherited Mutations in and outside the coding region also may affect the amount of p53 produced, both by altering the transcription of the gene or in destabilizing or otherwise altering the processing of either the transcript (mRNA) or protein
- FISH fluorescent in situ hybridization
- PFGE direct DNA sequencing
- SSCA single-stranded conformation analysis
- ASO allele-specific oligonucleotide
- dot blot analysis denaturing gradient gel electrophoresis, RFLP and PCR-SSCP
- primer as defined herein, is meant to encompass any nucleic acid that is capable of priming the synthesis of a nascent nucleic acid in a template-dependent process
- primers are oligonucleotides from ten to twenty base pairs in length, but longer sequences can be employed
- Primers may be provided in double-stranded or single-stranded form, although the single-stranded form is preferred
- Probes are defined differently, although they may act as primers
- Probes while perhaps capable of priming, are designed to binding to the target DNA or RNA and need not be used in an amplification process
- the probes or primers are labeled with radioactive species ( 32 P, 14 C, 35 S, 3 H, or other label), with a fluorophore (rhodamine, fluorescein) or a chemillumiscent (luciferase)
- radioactive species 32 P, 14 C, 35 S, 3 H, or other label
- fluorophore rhodamine, fluorescein
- chemillumiscent luciferase
- PCRTM polymerase chain reaction
- PCR two primer sequences are prepared that are complementary to regions on opposite complementary strands of the marker sequence
- An excess of deoxynucleoside triphosphates are added to a reaction mixture along with a DNA polymerase, e.g. , Taq polymerase
- a DNA polymerase e.g. , Taq polymerase
- the primers will bind to the marker and the polymerase will cause the primers to be extended along the marker sequence by adding on nucleotides
- the extended primers will dissociate from the marker to form reaction products, excess primers will bind to the marker and to the reaction products and the process is repeated
- a reverse transcriptase PCR amplification procedure may be performed in order to quantify the amount of mRNA amplified
- Methods of reverse transcribing RNA into cDNA are well known and described in Sambrook et al, 1989
- Alternative methods for reverse transcription utilize thermostable, RNA-dependent DNA polymerases These methods are described in WO 90/07641 filed December 21, 1990 Polymerase chain reaction methodologies are well known in the art
- LCR ligase chain reaction
- Qbeta Replicase described in PCT Application No PCT US87/00880, may also be used as still another amplification method in the present invention
- a replicative sequence of RNA that has a region complementary to that of a target is added to a sample in the presence of an RNA polymerase The polymerase will copy the replicative sequence that can then be detected
- restriction endonucleases and ligases are used to achieve the amplification of target molecules that contain nucleotide 5'-[alpha- thio]-triphosphates in one strand of a restriction site may also be useful in the amplification of nucleic acids in the present invention, Walker et al, (1992)
- SDA Strand Displacement Amplification
- RCR cyclic probe reaction
- DNA and a middle sequence of specific RNA is hybridized to DNA that is present in a sample Upon hybridization, the reaction is treated with RNase H, and the products of the probe identified as distinctive products that are released after digestion The original template is annealed to another cycling probe and the reaction is repeated Still another amplification methods described in GB Application No 2 202 328, and in PCT Application No PCT/US89/01025, each of which is incorporated herein by reference in its entirety, may be used in accordance with the present invention In the former application, "modified" primers are used in a PCR-like, template- and enzyme- dependent synthesis The primers may be modified by labeling with a capture moiety
- an excess of labeled probes are added to a sample
- the probe binds and is cleaved catalytically After cleavage, the target sequence is released intact to be bound by excess probe Cleavage of the labeled probe signals the presence of the target sequence
- nucleic acid amplification procedures include transcription-based amplification systems (TAS), including nucleic acid sequence based amplification (NASBA) and 3SR (Kwoh et al, 1989, Gingeras et al, PCT Application WO 88/10315, incorporated herein by reference in their entirety)
- TAS transcription-based amplification systems
- NASBA nucleic acid sequence based amplification
- 3SR 3SR
- the nucleic acids can be prepared for amplification by standard phenol/chloroform extraction, heat denaturation of a clinical sample, treatment with lysis buffer and minispin columns for isolation of DNA and RNA or guanidinium chloride extraction of RNA
- amplification techniques involve annealing a primer which has target specific sequences Following polymerization, DNA/RNA hybrids are digested with RNase H while double stranded
- DNA molecules are heat denatured again In either case the single stranded DNA is made fully double stranded by addition of second target specific primer, followed by polymerization
- the double-stranded DNA molecules are then multiply transcribed by an RNA polymerase such as T7 or SP6 In an isothermal cyclic reaction, the RNA's are reverse transcribed into single stranded DNA, which is then converted to double stranded
- RNA polymerase such as T7 or SP6
- ssRNA single- stranded RNA
- dsDNA double-stranded DNA
- the ssRNA is a template for a first primer oligonucleotide, which is elongated by reverse transcriptase (RNA-dependent DNA polymerase)
- RNA-dependent DNA polymerase reverse transcriptase
- the RNA is then removed from the resulting DNA RNA duplex by the action of ribonuclease H (RNase H, an RNase specific for RNA in duplex with either DNA or RNA)
- RNase H an RNase specific for RNA in duplex with either DNA or RNA
- the resultant ssDNA is a template for a second primer, which also includes the sequences of an RNA polymerase promoter (exemplified by T7 RNA polymerase) 5' to its homology to the template This primer is then extended by DNA polymerase (exemplified by the large "K
- dsDNA double-stranded DNA
- dsDNA double-stranded DNA
- This promoter sequence can be used by the appropriate RNA polymerase to make many RNA copies of the DNA These copies can then re-enter the cycle leading to very swift amplification With proper choice of enzymes, this amplification can be done isothermally without addition of enzymes at each cycle Because of the cyclical nature of this process, the starting sequence can be chosen to be in the form of either DNA or RNA
- a probe is used to target a DNA or RNA species that has been immobilized on a suitable matrix, often a filter of nitrocellulose
- the different species should be spatially separated to facilitate analysis This often is accomplished by gel electrophoresis of nucleic acid species followed by "blotting" on to the filter
- the blotted target is incubated with a probe (usually labeled) under conditions that promote denaturation and rehybridization Because the probe is designed to base pair with the target, the probe will binding a portion of the target sequence under renaturing conditions Unbound probe is then removed, and detection is accomplished as described above
- amplification products are separated by agarose, agarose-acrylamide or polyacrylamide gel electrophoresis using standard methods See Sambrook et al, 1989
- chromatographic techniques may be employed to effect separation
- adsorption, partition, ion-exchange and molecular sieve, and many specialized techniques for using them including column, paper, thin-layer and gas chromatography
- Products may be visualized in order to confirm amplification of the marker sequences
- One typical visualization method involves staining of a gel with ethidium bromide and visualization under UV light
- the amplification products can then be exposed to x-ray film or visualized under the appropriate stimulating spectra, following separation
- ⁇ visualization is achieved indirectly
- a labeled nucleic acid probe is brought into contact with the amplified marker sequence
- the probe preferably is conjugated to a chromophore but may be radiolabeled
- the probe is conjugated to a binding partner, such as an antibody or biotin, and the other member of the binding pair carries a detectable moiety
- detection is by a labeled probe
- chromophore or radiolabel probes or primers identify the target during or following amplification
- oligonucleotide primers may be designed to permit the amplification of sequences throughout the p53 gene that may then be analyzed by direct sequencing
- kits This generally will comprise preselected primers and probes Also included may be enzymes suitable for amplifying nucleic acids including various polymerases (RT, Taq, SequenaseTM, etc ), deoxynucleotides and buffers to provide the necessary reaction mixture for amplification
- enzymes suitable for amplifying nucleic acids including various polymerases (RT, Taq, SequenaseTM, etc ), deoxynucleotides and buffers to provide the necessary reaction mixture for amplification
- kits also generally will comprise, in suitable means, distinct containers for each individual reagent and enzyme as well as for each primer or probe
- chip-based DNA technologies such as those described by Hacia et al. (1996) and Shoemaker et al. (1996)
- a c-Abl and optionally or alternatively, p300 polypeptide or a gene construct that comprises a c-Abl sequence, and optionally or alternatively, a p300 sequence are used in combination with a recombinant vector that comprises a nucleic acid sequence capable of expressing the desired gene sequence in the cell.
- the vector typically is introduced into the cell in a manner that allows expression of the encoded gene sequence at a level sufficient to effect cell function and cause an apoptotic response or to reduce cell proliferation.
- expression construct is meant to include any type of genetic construct containing a nucleic acid coding for a gene product in which part or all of the nucleic acid encoding sequence is capable of being transcribed
- the transcript may be translated into a protein, but it need not be
- expression includes both transcription of a p53, p300 or c-Abl gene and translation of p53, p300 or c-Abl mRNA into the proper protein product
- promoter refers to a DNA sequence recognized by the synthetic machinery of the host cell, or introduced synthetic machinery, that is required to initiate the specific transcription of a gene
- under transcriptional control means that the promoter is in the correct location in relation to the polynucleotide to control RNA polymerase initiation and expression of the polynucleotide
- promoter will be used here to refer to a group of transcriptional control modules that are clustered around the initiation site for RNA polymerase II
- Much of the thinking about how promoters are organized derives from analyses of several viral promoters, including those for the HSV thymidine kinase (tk) and SV40 early transcription units
- At least one module in each promoter functions to position the start site for RNA synthesis
- the best known example of this is the TATA box, but in some promoters lacking a TATA box, such as the promoter for the mammalian terminal deoxynucleotidyl transferase gene and the promoter for the SV40 late genes, a discrete element overlying the start site itself helps to fix the place of initiation
- promoter elements regulate the frequency of transcriptional initiation Typically, these are located in the region 30-1 10 bp upstream of the start site, although a number of promoters have recently been shown to contain functional elements downstream of the start site as well
- the spacing between promoter elements frequently is flexible, so that promoter function is preserved when elements are inverted or moved relative to one another
- the spacing between promoter elements can be increased to 50 bp apart before activity begins to decline Depending on the promoter, it appears that individual elements can function either cooperatively or independently to activate transcription
- the particular promoter that is employed to control the expression of ap53 or c- Abl polynucleotide is not believed to be critical, so long as it is capable of expressing the polynucleotide in the targeted cell
- a promoter that is capable of being expressed in a human cell
- such a promoter might include either a human or viral promoter
- the human cytomegalovirus (CMV) immediate early gene promoter, the SV40 early promoter and the Rous sarcoma virus long terminal repeat can be used to obtain high-level expression of the p53 or c-Abl polynucleotide
- CMV cytomegalovirus
- the use of other viral or mammalian cellular or bacterial phage promoters which are well-known in the art to achieve expression of polynucleotides is contemplated as well, provided that the levels of expression are sufficient to produce a growth inhibitory effect
- a promoter which is active in specific cells, such as tyrosinase (melanoma), alpha-fetoprotein and albumin (liver tumors), CC10 (lung tumor) and prostate-specific antigen (prostate tumor) will permit tissue-specific expression of p53 or c-Abl constructs
- Table 1 lists several elements/promoters which may be employed, in the context of the present invention, to regulate the expression o ⁇ p53 or c-Abl constructs This list is not intended to be exhaustive of all the possible elements involved in the promotion of p53 or c-Abl expression but, merely, to be exemplary thereof
- Enhancers were originally detected as genetic elements that increased transcription from a promoter located at a distant position on the same molecule of DNA This ability to act over a large distance had little precedent in classic studies of prokaryotic transcriptional regulation Subsequent work showed that regions of DNA with enhancer activity are organized much like promoters That is, they are composed of many individual elements, each of which binds to one or more transcriptional proteins
- enhancers are operational An enhancer region as a whole must be able to stimulate transcription at a distance, this need not be true of a promoter region or its component elements On the other hand, a promoter must have one or. more elements that direct initiation of RNA synthesis at a particular site and in a particular orientation, whereas enhancers lack these specificities Promoters and enhancers are often overlapping and contiguous, often seeming to have a very similar modular organization
- Eukaryotic Promoter Data Base EPDB any promoter/enhancer combination (as per the Eukaryotic Promoter Data Base EPDB) could also be used to drive expression of a p53, p300 or c-Abl construct
- a T3, T7 or SP6 cytoplasmic expression system Use of a T3, T7 or SP6 cytoplasmic expression system is another possible embodiment Eukaryotic cells can support cytoplasmic transcription from certain bacteriophage promoters if the appropriate bacteriophage polymerase is provided, either as part of the delivery complex or as an additional genetic expression vector
- NCAM Neural Cell Adhesion Molecule
- SAA Human Serum Amyloid A
- a promoter that is regulated in response to specific physiologic signals can permit inducible expression of the p53 construct.
- expression is inducible by tumor necrosis factor.
- Table 2 illustrates several promoter/inducer combinations:
- the delivery of an expression vector in a cell may be identified in vitro or in vivo by including a marker in the expression vector
- the marker would result in an identifiable change to the transfected cell permitting easy identification of expression
- a drug selection marker aids in cloning and in the selection of transformants
- enzymes such as herpes simplex virus thymidine kinase (tk) (eukaryotic) or chloramphenicol acetyltransferase (CAT) (prokaryotic)
- CAT chloramphenicol acetyltransferase
- Immunologic markers also can be employed
- the selectable marker employed is not believed to be important, so long as it is capable of being expressed along with the polynucleotide encoding p53 Further examples of selectable markers are well known to one of skill in the art
- polyadenylation signal to effect proper polyadenylation of the transcript
- the nature of the polyadenylation signal is not believed to be crucial to the successful practice of the invention, and any such sequence may be employed
- the inventor has employed the SV40 polyadenylation signal in that it was convenient and known to function well in the target cells employed Also contemplated as an element of the expression construct is a terminator These elements can serve to enhance message levels and to minimize read through from the construct into other sequences
- the cells contain nucleic acid constructs of the present invention
- a cell may be identified in vitro or in vivo by including a marker in the expression construct
- markers would confer an identifiable change to the cell permitting easy identification of cells containing the expression construct
- a drug selection marker aids in cloning and in the selection of transformants, for example, genes that confer resistance to neomycin, puromycin, hygromycin, DHFR, GPT, zeocin and histidinol are useful selectable markers
- enzymes such as herpes simplex virus thymidine kinase (tk) or chloramphenicol acetyltransferase (CAT) may be employed
- Immunologic markers also can be employed The selectable marker employed is not believed to be important, so long as it is capable of being expressed simultaneously with the nucleic acid encoding a gene product Further examples of selectable markers are well known to one of skill in the art
- IRES elements internal ribosome binding sites
- IRES elements are able to bypass the ribosome scanning model of 5' methylated Cap dependent translation and begin translation at internal sites
- IRES elements from two members of the picanovirus family polio and encephalomyocarditis
- IRES elements from two members of the picanovirus family Polio and encephalomyocarditis
- IRES elements can be linked to heterologous open reading frames
- Multiple open reading frames can be transcribed together, each separated by an IRES, creating polycistronic messages
- each open reading frame is accessible to ribosomes for efficient translation
- Multiple genes can be efficiently expressed using a single promoter/enhancer to transcribe a single message
- Any heterologous open reading frame can be linked to IRES elements This includes genes for secreted proteins, multi-subunit proteins, encoded by independent genes, intracellular or membrane-bound proteins and selectable markers In this way, expression of several proteins can be simultaneously engineered into a cell with a single construct and a single selectable marker
- the expression construct comprises a virus or engineered construct derived from a viral genome
- a virus or engineered construct derived from a viral genome
- expression vectors need not be viral but, instead, may be any plasmid, cosmid or phage construct that is capable of supporting expression of encoded genes in mammalian cells, such as pUC or BluescriptTM plasmid series
- the retroviruses are a group of single-stranded RNA viruses characterized by an ability to convert their RNA to double-stranded DNA in infected cells by a process of reverse-transcription (Coffin, 1990)
- the resulting DNA then stably integrates into cellular chromosomes as a provirus and directs synthesis of viral proteins
- the integration results in the retention of the viral gene sequences in the recipient cell and its descendants
- the retroviral genome contains three genes - gag, pol, and env - that code for capsid proteins, polymerase enzyme, and envelope components, respectively
- a sequence found upstream from the gag gene, termed ⁇ functions as a signal for packaging of the genome into virions
- Two long terminal repeat (LTR) sequences are present at the 5' and 3' ends of the viral genome These contain strong promoter and enhancer sequences and are also required for integration in the host cell genome (Coffin, 1990)
- a nucleic acid encoding a p53 is inserted into the viral genome in the place of certain viral sequences to produce a virus that is replication-defective
- a packaging cell line containing the gag, pol and env genes but without the LTR and ⁇ components is constructed (Mann et al, 1983)
- the ⁇ sequence allows the RNA transcript of the recombinant plasmid to be packaged into viral particles, which are then secreted into the culture media (Nicolas and Rubenstein, 1988, Temin, 1986, Mann et al, 1983)
- the media containing the recombinant retroviruses is then collected, optionally concentrated, and used for gene transfer Retroviral vectors are able to infect a broad variety of cell types
- Retroviral vectors are able to infect a broad variety of cell types
- adenoviruses are double-stranded DNA tumor viruses with genome sizes of approximate 36 kb (Tooza, 1981)
- adenoviruses As a model system for eukaryotic gene expression, adenoviruses have been widely studied and well characterized, which makes them an attractive system for development of adenovirus as a gene transfer system
- This group of viruses is easy to grow and manipulate, and exhibit a broad host range in vitro and in vivo
- adenoviruses are capable of shutting off host protein synthesis, directing cellular machineries to synthesize large quantities of viral proteins, and producing copious amounts of virus
- the El region of the genome includes El A and E1B which encode proteins responsible for transcription regulation of the viral genome, as well as a few cellular genes E2 expression, including E2A and E2B, allows synthesis of viral replicative functions, e.g. DNA-binding protein, DNA polymerase, and a terminal protein that primes replication E3 gene products prevent cytolysis by cytotoxic T cells and tumor necrosis factor and appear to be important for viral propagation Functions associated with the E4 proteins include DNA replication, late gene expression, and host cell shutoff
- the late gene products include most of the virion capsid proteins, and these are expressed only after most of the processing of a single primary transcript from the major late promoter has occurred
- the major late promoter exhibits high efficiency during the late phase of the infection (Stratford-Perricaudet and Perricaudet, 1991)
- adenovirus-derived vectors offer excellent potential for the substitution of large DNA fragments when used in connection with cell lines such as 293 cells
- Ad 5 -transformed human embryonic kidney cell lines have been developed to provide the essential viral proteins in trans. The inventor thus reasoned that the characteristics of adenoviruses rendered them good candidates for use in targeting cancer cells in vivo (Grunhaus & Horwitz, 1992)
- an adenovirus system for delivering foreign proteins to a cell include (i) the ability to substitute relatively large pieces of viral DNA by foreign DNA, (ii) the structural stability of recombinant adenoviruses, (iii) the safety of adenoviral administration to humans, £nd (iv) lack of any known association of adenoviral infection with cancer or malignancies, (v) the ability to obtain high titers of the recombinant virus, and (vi) the high infectivity of Adenovirus
- adenovirus vectors over retroviruses include the higher levels of gene expression Additionally, adenovirus replication is independent of host gene replication, unlike retroviral sequences Because adenovirus transforming genes in the El region can be readily deleted and still provide efficient expression vectors, oncogenic risk from adenovirus vectors is thought to be negligible (Grunhaus & Horwitz, 1992)
- adenovirus gene transfer systems are based upon recombinant, engineered adenovirus which is rendered replication-incompetent by deletion of a portion of its genome, such as El, and yet still retains its competency for infection Sequences encoding relatively large foreign proteins can be expressed when additional deletions are made in the adenovirus genome For example, adenoviruses deleted in both El and E3 regions are capable of carrying up to 10 Kb of foreign DNA and can be grown to high titers in 293 cells (Stratford-Perricaudet and Perricaudet, 1991) Surprisingly persistent expression of transgenes following adenoviral infection has also been reported
- Adenovirus-mediated gene transfer has recently been investigated as a means of mediating gene transfer into eukaryotic cells and into whole animals
- OTC rare recessive genetic disorder ornithine transcarbamylase
- viral vectors may be employed as expression constructs in the present invention.
- Vectors derived from viruses such as vaccinia virus (Ridgeway, 1988; Baichwal and Sugden, 1986; Coupar et al, 1988) adeno-associated virus (AAV) (Ridgeway, 1988; Baichwal and Sugden, 1986; Hermonat and Muzycska, 1984) and herpes viruses may be employed. These viruses offer several attractive features for various mammalian cells (Friedmann, 1989; Ridgeway, 1988; Baichwal and Sugden,
- CAT chloramphenicol acetyltransferase
- the expression vector In order to effect expression of therapeutic constructs according to the present invention, the expression vector must be delivered into a cell As described above, one mechanism for delivery is via viral infection where the expression vector is encapsidated in an infectious virus particle
- Another embodiment of the invention for transferring a naked DNA expression vector into cells may involve particle bombardment This method depends on the ability to accelerate DNA coated microprojectiles to a high velocity allowing them to pierce cell membranes and enter cells without killing them (Klein et al, 1987) Several devices for accelerating small particles have been developed One such device relies on a high voltage discharge to generate an electrical current, which in turn provides the motive force (Yang et al, 1990) The microprojectiles used have consisted of biologically inert substances such as tungsten or gold beads
- Selected organs including the liver, skin, and muscle tissue of rats and mice have been bombarded in vivo (Yang et al, 1990, Zelenin et al, 1991) This may require surgical exposure of the tissue or cells, to eliminate any intervening tissue between the gun and the target organ DNA encoding a p53, p300 or c-Abl construct may be delivered via this method
- the expression vector may be entrapped in a liposome
- Liposomes are vesicular structures characterized by a phospholipid bilayer membrane and an inner aqueous medium Multilamellar liposomes have multiple lipid layers separated by aqueous medium Liposomes form spontaneously when phospholipids are suspended in an excess of aqueous solution The lipid components undergo self-rearrangement before the formation of closed structures and entrap water and dissolved solutes between the lipid bilayers (Ghosh and Bachhawat, 1991) Also contemplated are lipofectamine-DNA complexes
- Liposome-mediated polynucleotide delivery and expression of foreign DNA in vitro has been very successful Wong et al. (1980) demonstrated the feasibility of liposome-mediated delivery and expression of foreign DNA in cultured chick embryo,
- the liposome may be complexed with a hemagglutinating virus (HVJ) This has been shown to facilitate fusion with the cell membrane and promote cell entry of liposome-encapsulated DNA (Kaneda et al, 1989)
- the liposome may be complexed or employed in conjunction with nuclear non-histone chromosomal proteins (HMG-1) (Kato et al, 1991)
- HMG-1 nuclear non-histone chromosomal proteins
- the liposome may be complexed or employed in conjunction with both HVJ and HMG-1
- expression vectors have been successfully employed in transfer and expression of a polynucleotide in vitro and in vivo, then they are applicable for the present invention
- a bacteriophage promoter is employed in the DNA construct, it also will be desirable to include within the liposome an appropriate bacteriophage polymerase
- Receptor-mediated gene targeting vehicles generally consist of two components a cell receptor-specific ligand and a DNA-binding agent Several ligands have been used for receptor-mediated gene transfer The most extensively characterized ligands are asialoorosomucoid (ASOR) (Wu and Wu, 1987) and transferrin (Wagner et al, 1993) Recently, a synthetic neoglycoprotein, which recognizes the same receptor as ASOR, has been used as a gene delivery vehicle (Ferkol et al, 1993, Perales et al, 1994) and epidermaj growth factor (EGF) has also been used to deliver genes to squamous carcinoma cells (Myers, EPO 0273085)
- the delivery vehicle may comprise a ligand and a liposome
- a ligand and a liposome For example, Nicolau et al. (1987) employed lactosyl-ceramide, a galactose-terminal asialganglioside, incorporated into liposomes and observed an increase in the uptake of the insulin gene by hepatocytes
- an adenoviral expression vector also may be specifically delivered into a cell type such as lung, epithelial or tumor cells, by any number of receptor-ligand systems, with or without liposomes
- epidermal growth factor (EGF) may be used as the receptor for mediated delivery of p53, p300 or cAbl construct in many tumor cells that exhibit upregulation of EGF receptor Mannose can be used to target the mannose receptor on liver cells
- antibodies to CD 5 (CLL), CD22 (lymphoma), CD25 (T-cell leukemia) and MAA (melanoma) can similarly be used as targeting moieties
- gene transfer may more easily be performed under ex vivo conditions
- Ex vivo gene therapy refers to the isolation of cells from an animal, the delivery of a polynucleotide into the cells, in vitro, and then the return of the modified cells back into an animal This may involve the surgical removal of tissue/organs from an animal or the primary culture of cells and tissues Anderson et al. , U S Patent 5,399,346, and incorporated herein in its entirety, disclose ex vivo therapeutic methods During ex vivo culture, the expression vector can express the p53 construct Finally, the cells may be reintroduced into the original animal, or administered into a distinct animal, in a pharmaceutically acceptable form by any of the means described below
- a patient presenting a tumor that does not express wild-type p53 will be treated with a combination of p53 and c-Abl and/or p300
- the patient will be treated with a pharmaceutically acceptable form of the c-Abl and/or p300 genes or gene products, as described above, and in addition, will be treated with a p53 gene or gene product
- a typical treatment regimen will involve repeated administrations over a six week period During this time, the tumor will be monitored for absence of tumor progression, response or toxicity and the doses adjusted accordingly
- compositions of the present invention To kill tumor cells or reduce their proliferation, using the methods and compositions of the present invention, one would generally contact a "target" cell with (i) radiation or a chemotherapeutic and (ii) a therapeutic protein or gene These compositions would be provided in a combined amount effective to kill or inhibit proliferation of the cell
- This process may involve contacting the cells with c-Abl, p300 and p53 protein or gene, at the same time This may be achieved by contacting the cell with a single composition or pharmacological formulation that includes both agents, or by contacting the cell with two distinct compositions or formulations, at the same time, wherein one composition includes c-Abl protein or gene and/or p300, and the other includes the p53 protein or gene
- the protein or gene therapy treatment may precede or follow the standard chemo- or radiotherapy treatment by intervals ranging from minutes to weeks
- the other agent and an expression construct are applied separately to the cell, one generally would ensure that a significant period of time did not expire between the time of each delivery, such that the agent and expression construct would still be able to exert an advantageously combined effect on the cell
- both agents are delivered to a cell in a combined amount effective to kill the cell
- Agents or factors suitable for use in a combined therapy are any chemical compound or treatment method that induces DNA damage when applied to a cell
- Such agents and factors include radiation and waves that induce DNA damage such as, ⁇ -irradiation, X-rays, UV-irradiation, microwaves, electronic emissions, and the like
- chemotherapeutic agents function to induce DNA damage, all of which are intended to be of use in the combined treatment methods disclosed herein
- Chemotherapeutic agents contemplated to be of use include, e.g., adriamycin, 5-fluorouracil (5FU), etoposide (VP-16), camptothecin, actinomycin-D, mitomycin C, cisplatin (CDDP) and even hydrogen peroxide
- the invention also encompasses the use of a combination of one or more DNA damaging agents, whether radiation-based or actual compounds, such as the use of X-rays with cisplatin or the use of cisplatin with etoposide
- the use of cisplatin in combination with a c-Abl or p300 expression construct is particularly preferred as this compound
- the tumor cells In treating cancer according to the invention, one would contact the tumor cells with an agent in addition to the expression construct This may be achieved by irradiating the localized tumor site with radiation such as X-rays, UV-light, ⁇ -rays or even microwaves Alternatively, the tumor cells may be contacted with the agent by administering to the subject a therapeutically effective amount of a pharmaceutical composition comprising a compound such as, adriamycin, 5-fluorouracil, etoposide, camptothecin, actinomycin-D, mitomycin C, or more preferably, cisplatin
- the agent may be prepared and used as a combined therapeutic composition, or kit, by combining it with an expression construct, as described above
- Cisplatin has been widely used to treat cancer, with efficacious doses used in clinical applications of 20 mg/m 2 for 5 days every three weeks for a total of three courses Cisplatin is not absorbed orally and must therefore be delivered via injection intravenously, subcutaneously, intratumorally or intraperitoneally
- chemotherapeutic compounds include adriamycin, also known as doxorubicin, etoposide, verapamil, podophyllotoxin, and the like Widely used in a clinical setting for the treatment of neoplasms, these compounds are administered through bolus injections intravenously at doses ranging from 25-75 mg/m 2 at 21 day intervals for adriamycin, to 35-50 mg/m 2 for etoposide intravenously or double the intravenous dose orally
- agents that have undergone extensive testing and are readily available
- agents such as 5-fluorouracil (5-FU)
- 5-FU 5-fluorouracil
- 5- FU is preferentially used by neoplastic tissue, making this agent particularly useful for targeting to neoplastic cells
- 5- FU is applicable in a wide range of carriers, including topical, however intravenous administration with doses ranging from 3 to 15 mg/kg/day being commonly used
- ⁇ -rays X-rays
- UV-irradiation UV-irradiation
- Dosage ranges for X-rays range from daily doses of 50 to 200 roentgens for prolonged periods of time (3 to 4 weeks), to single doses of 2000 to 6000 roentgens
- Dosage ranges for radioisotopes vary widely, and depend on the half-life of the isotope, the strength and type of radiation emitted, and the uptake by the neoplastic cells
- Aqueous compositions of the present invention will have an effective amount of a compound that increases the expression of wild-type p53, for example p300 or c-Abl gene products or p300 or c-Abl gene constructs. Such compositions will generally be dissolved or dispersed in a pharmaceutically acceptable carrier or aqueous medium. Also included in various embodiments of the present invention are standard chemotherapeutics in their various pharmaceutical forms.
- phrases "pharmaceutically or pharmacologically acceptable” refer to molecular entities and compositions that do not produce an adverse, allergic or other untoward reaction when administered to an animal, or human, as appropriate.
- pharmaceutically acceptable carrier includes any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents and the like. The use of such media and agents for pharmaceutical active substances is well known in the art. Except insofar as any conventional media or agent is incompatible with the active ingredients, its use in the therapeutic compositions is contemplated. Supplementary active ingredients, such as other anti-cancer agents, can also be incorporated into the compositions.
- other pharmaceutically acceptable forms include, e.g. , tablets or other solids for oral administration; time release capsules; and any other form currently used, including cremes, lotions, mouthwashes, inhalants and the like.
- the active compounds of the present invention will often be formulated for parenteral administration, e.g., formulated for injection via the intravenous, intramuscular, sub-cutaneous, or even intraperitoneal routes.
- parenteral administration e.g., formulated for injection via the intravenous, intramuscular, sub-cutaneous, or even intraperitoneal routes.
- the preparation of an aqueous composition that contains a compound or compounds that increase the expression of wild-type p53 will be known to those of skill in the art in light of the present disclosure.
- such compositions can be prepared as injectables, either as liquid solutions or suspensions; solid forms suitable for using to prepare solutions or suspensions upon the addition of a liquid prior to injection can also be prepared, and the preparations can also be emulsified
- compounds may be injected directly into a tumor
- the route of delivery is by a slow drip into the circulatory system of the patient
- Solutions of the active compounds as free base or pharmacologically acceptable salts can be prepared in water suitably mixed with a surfactant, such as hydroxypropylcellulose Dispersions can also be prepared in glycerol, liquid polyethylene glycols, and mixtures thereof and in oils Under ordinary conditions of storage and use, these preparations contain a preservative to prevent the growth of microorganisms
- the pharmaceutical forms suitable for injectable use include sterile aqueous solutions or dispersions, formulations including sesame oil, peanut oil or aqueous propylene glycol, and sterile powders for the extemporaneous preparation of sterile injectable solutions or dispersions
- the form must be sterile and must be fluid to the extent that easy syringability exists It must be stable under the conditions of manufacture and storage and must be preserved against the contaminating action of microorganisms, such as bacteria and fungi
- the active compounds may be formulated into a composition in a neutral or salt form
- Pharmaceutically acceptable salts include the acid addition salts (formed with the free amino groups of the protein) and which are formed with inorganic acids such as, for example, hydrochloric or phosphoric acids, or such organic acids as acetic, oxalic, tartaric, mandelic, and the like
- Salts formed with the free carboxyl groups can also be derived from inorganic bases such as, for example, sodium, potassium, ammonium, calcium, or ferric hydroxides, and such organic bases as isopropylamine, trimethylamine, histidine, procaine and the like
- the carrier can also be a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol, and liquid polyethylene glycol, and the like), suitable mixtures thereof, and vegetable oils
- a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol, and liquid polyethylene glycol, and the like), suitable mixtures thereof, and vegetable oils
- the proper fluidity can be maintained, for example, by the use of a coating, such as lecithin, by the maintenance of the required particle size in the case of dispersion and by the use of surfactants.
- the prevention of the action of microorganisms can be brought about by various antibacterial ad antifungal agents, for example, parabens, chlorobutanol, phenol, sorbic acid, thimerosal, and the like.
- isotonic agents for example, sugars or sodium chloride.
- Prolonged absorption of the injectable compositions can be brought about by the use in the compositions of agents delaying absorption, for example, aluminum monostearate and gelatin.
- Sterile injectable solutions are prepared by incorporating the active compounds in the required amount in the appropriate solvent with various of the other ingredients enumerated above, as required, followed by filtered sterilization.
- dispersions are prepared by incorporating the various sterilized active ingredients into a sterile vehicle which contains the basic dispersion medium and the required other ingredients from those enumerated above.
- the preferred methods of preparation are vacuum-drying and freeze-drying techniques which yield a powder of the active ingredient plus any additional desired ingredient from a previously sterile-filtered solution thereof.
- the therapeutic formulations of the invention could also be prepared in forms suitable for topical administration, such as in cremes and lotions. These forms may be used for treating skin-associated diseases, such as various sarcomas.
- solutions Upon formulation, solutions will be administered in a manner compatible with the dosage formulation and in such amount as is therapeutically effective.
- the formulations are easily administered in a variety of dosage forms, such as the type of injectable solutions described above, with even drug release capsules and the like being employable.
- aqueous solutions For parenteral administration in an aqueous solution, for example, the solution should be suitably buffered if necessary and the liquid diluent first rendered isotonic with sufficient saline or glucose.
- aqueous solutions are especially suitable for intravenous, intramuscular, subcutaneous and intraperitoneal administration
- sterile aqueous media which can be employed will be known to those of skill in the art in light of the present disclosure
- one dosage could be dissolved in 1 mL of isotonic NaCl solution and either added to 1000 mL of hypodermoclysis fluid or injected at the proposed site of infusion, (see for example, "Remington's Pharmaceutical Sciences" 15th Edition, pages 1035-1038 and 1570-1580)
- kits All the essential materials and reagents required for determining wild-type p53 in a sample or for increasing the expression of wild-type p53 using c-Abl and p300 in tumor cells may be assembled together in a kit
- the liquid solution preferably is an aqueous solution, with a sterile aqueous solution being particularly preferred
- the kit may contain materials for PCR analyses, such primers, buffers and appropriate solvents Alternatively, if the detection is via immunologic means, the kit may contain antibodies directed to the p53, secondary antibodies that binding primary antibodies, labels or signal generating compounds (either conjugated or unconjugated) and various reagents for the generation and detection of signals
- an inducer of wild-type p53 expression alone or in combination with, a expression vectors may be formulated into a single or separate pharmaceutically acceptable syringeable composition
- the container means may itself be an inhalant, syringe, pipette, eye dropper, or other such like apparatus, from which the formulation may be applied to an infected area of the body, such as the lungs, injected into an animal, or even applied to and mixed with the other components of the kit
- the components of these kits may also be provided in dried or lyophilized forms When reagents or components are provided as a dried form, reconstitution generally is by the addition of a suitable solvent It is envisioned that the solvent also may be provided in another container means
- the kits of the invention may also include an instruction sheet defining administration of wild-type p53 and c-Abl gene therapy agents, or explaining the assays for determining p53 levels in samples
- kits of the present invention also will typically include a means for containing the vials in close confinement for commercial sale such as, e.g., injection or blow-molded plastic containers into which the desired vials are retained Irrespective of the number or type of containers, the kits of the invention also may comprise, or be packaged with, an instrument for assisting with the injection/administration or placement of the ultimate complex composition within the body of an animal
- an instrument may be an inhalant, syringe, pipette, forceps, measured spoon, eye dropper or any such medically approved delivery vehicle
- Other instrumentation includes devices that permit the reading or monitoring of reactions in vitro
- c-Abl The product of the c-Abl gene is a non-receptor tyrosine kinase that is localized to the nucleus and cytoplasm Ionizing radiation (IR) activates c-Abl Similar results were obtained with the alkylating agents cisplatinum and mitomycin C Cells deficient in c-Abl fail to activate Jun kinase (JNK/SAP kinase) following IR or alkylating agent exposure and that reconstitution of c-Abl in these cells restores that response In contrast, the stress response to tumor necrosis factor is stimulated by a c-Abl-independent mechanism
- c-Abl contains actin binding and DNA binding domains
- Rh retinoblastoma
- MCF-7 cells were co- transfected with a construct containing the luciferase gene driven by a p53 enhancer from the MDM2 promoter (Barak et al, 1994), and vectors expressing wild-type c-Abl, a kinase-inactive K(290)R mutant (Sawyers et al, 1994), or a kinase-active mutant, designated ⁇ Pro 4 which is deleted at the p53-binding domain (Goga et al, 1995)
- Co- transfections of the reporter with wild-type or kinase-inactive c-Abl (K-R), but not c- Abl ⁇ Pro 4 resulted in induction of luciferase activity (FIG 1A)
- c-Abl expression had no detectable effect on activation of an SV40-luciferase construct (FIG la) As transcription of p21 is regulated by
- MCF-7 cells were prepared to stably express the dominant-negative c-Abl (K-R) 2 , which effectively inhibits the increase in c-Abl kinase activity induced by ionizing radiation control cells (FIG 2A)
- Irradiation of MCF-7/pSR or MCF-7/c-Abl (K-R) cells caused an increase in p53, p21 and GADD45, but not in c-Myc (which is not dependent on p53) (FIG 2B)
- FIG 2B Irradiation of MCF-7/pSR or MCF-7/c-Abl (K-R) cells caused an increase in p53, p21 and GADD45, but not in c-Myc (which is not dependent on p53) (FIG 2B)
- FIG. 3C Wild-type MEFs after 5 Gy radiation had an S-phase population that was 45% of that for untreated cells (FIG 3D) By contrast, irradiated abl ' MEFs had more than 70%> of cells in S phase compared with controls (FIG 3D) Exposure of the wild-type and abl' ' MEFs to 20 Gy radiation partially inhibited arrest in Gl in the abl ' cells, indicating that the c-Abl kinase function is necessary for radiation-induced Gl arrest
- mutant c-Abl may prevent Gl arrest in response to DNA damage by inactivating Rb But as irradiated cells expressing c-Abl (K-R) do not arrest in Gl because Cdk2 is not inhibited, the effect probably occurs upstream of Rb
- K-R irradiated cells expressing c-Abl
- the present inventors have demonstrated that c-Abl functions in the cellular response to DNA damage through p53-dependent pathways, confirmed by the failure of the c-Abl ⁇ Pro 4 mutant to bind p53 and downregulate Cdk2 and arrest growth It has also been shown that the kinase-defective c-Abl (K-R) mutant induces p53 transactivation but no Gl arrest although
- RESULTS Cell Culture - MCF-7 cells were cultured in Dulbecco's modified Eagle's medium (Sigma) containing 10%> heat-inactivated fetal bovine serum (Sigma), 2 mM L-glutamine, 100 units/ml penicillin, and 100 ⁇ g/ml streptomycin Null pSR ⁇ MSVtKneo, pSR MSVc-AblK(290)-RtKNeo (Sawyers et al, 1994), or E6Neo (Scheffner et al, 1990) vectors were stably introduced into cells by LipofectAMINE (Life
- Immunoprec ⁇ itations and Immunoblot Analysis were prepared as described (Yuan et al, 1996) and incubated with rabbit anti-Cdk2 (sc-163, Santa Cruz Biotechnology, San Diego, CA), mouse anti-c-Abl (Ab-3, Oncogene Science, Cambridge, MA), mouse anti-p53 (Ab-6, Oncogene Science) antibodies for 6-12 h at 4°C and then for 60 min with protein A-Sepharose
- 10 ⁇ g/sample of rabbit anti-mouse IgG was added and incubated for 60 min before the addition of protein A beads
- the immune complexes were resolved by SDS-polyacrylamide gel electrophoresis, transferred to nitrocellulose filters and analyzed by immunoblotting using an ECL (Amersham Corp ) detection system
- recombinant SHPTP1 protein 100 ⁇ g/ml was used as substrate (Kharbanda et al, 1996), and the reaction was incubated for 30 min at 30°C
- ara-C induces an interaction between c-Abl and p53 in vivo
- the inventors also prepared cells that express the human papillomavirus E6 protein to promote degradation of p53 (Scheffner et al, 1990)
- the MCF-7/E6 cells responded to ara-C with induction of c-Abl activity
- MMS exposure resulted in increased c-Abl activity in the MCF-7/pSR and MCF-7/E6 cells, but not the MCF-7/c-Abl(K-R) cells
- MMS increased binding of c-Abl and p53 in MCF-7/pSR and MCF-7/c-Abl(K-R), but not MCF-7/E6, cells
- MMS also induced the expression of p53 and p21 in only the MCF-7/pSR and MCF-7/c-Abl(K-R) cells
- the MMS-induced increases in p21 levels were associated with binding of p21 to Cdk2
- Cdk2 activity was down-regulated in MMS-treated MCF-7/pSR cells, there was little effect of MMS on Cdk2 activity in the MCF-7/c-Abl(K-R) cells
- compositions and/or methods disclosed and claimed herein can be made and executed without undue experimentation in light of the present disclosure. While the compositions and methods of this invention have been described in terms of preferred embodiments, it will be apparent to those of skill in the art that variations may be applied to the compositions and/or methods and in the steps or in the sequence of steps of the method described herein without departing from the concept, spirit and scope of the invention. More specifically, it will be apparent that certain agents which are both chemically and physiologically related may be substituted for the agents described herein while the same or similar results would be achieved. All such similar substitutes and modifications apparent to those skilled in the art are deemed to be within the spirit, scope and concept of the invention.
- Gazit, A Yaish, P , etal, JMedChem, 32(10) 2344-52, 1989
- Temin "Retrovirus vectors for gene transfer Efficient integration into and expression of exogenous DNA in vertebrate cell genome," In. Kucherlapati R, ed Gene transfer
Abstract
La présente invention, qui concerne des thérapies anticancéreuses, concerne plus particulièrement l'induction d'une apoptose des cellules cancéreuses à la suite d'une thérapie par c-Abl et p300 permettant de contrôler le niveau des p53 de type sauvage. L'invention concerne également un traitement associé consistant à apporter, aux cellules déficientes en p53, des c-Abl, p300 et p53 de type sauvage de façon à induire des réponses apoptotiques.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
AU37313/97A AU3731397A (en) | 1996-07-18 | 1997-07-18 | Methods and compositions for modulation of growth response |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US2212496P | 1996-07-18 | 1996-07-18 | |
US60/022,124 | 1996-07-18 |
Publications (2)
Publication Number | Publication Date |
---|---|
WO1998003195A1 WO1998003195A1 (fr) | 1998-01-29 |
WO1998003195A9 true WO1998003195A9 (fr) | 1998-06-04 |
Family
ID=21807939
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/US1997/012498 WO1998003195A1 (fr) | 1996-07-18 | 1997-07-18 | Procedes et compositions de modulation du taux de croissance |
Country Status (2)
Country | Link |
---|---|
AU (1) | AU3731397A (fr) |
WO (1) | WO1998003195A1 (fr) |
Families Citing this family (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US7927612B2 (en) | 2000-01-19 | 2011-04-19 | Baofa Yu | Combinations and methods for treating neoplasms |
US6811788B2 (en) | 2000-01-19 | 2004-11-02 | Baofa Yu | Combinations and methods for treating neoplasms |
AU2002303390A1 (en) | 2001-04-18 | 2002-11-05 | Dana-Farber Cancer Institute, Inc. | Induction of apoptosis by cellular stress |
CN101138634A (zh) | 2006-09-07 | 2008-03-12 | 于保法 | 用于治疗肿瘤的组合物 |
CA2968853A1 (fr) | 2014-11-26 | 2016-06-02 | Baofa Yu | Chimio-immunotherapie haptene-amelioree par chimio-immunotherapie intratumorale personnalisee par incision ultra-minimale |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5747469A (en) * | 1991-03-06 | 1998-05-05 | Board Of Regents, The University Of Texas System | Methods and compositions comprising DNA damaging agents and p53 |
US5658784A (en) * | 1994-04-14 | 1997-08-19 | Dana-Farber Cancer Institute, Inc. | Nucleic acid encoding transcription factor p300 and uses of p300 |
-
1997
- 1997-07-18 WO PCT/US1997/012498 patent/WO1998003195A1/fr active Application Filing
- 1997-07-18 AU AU37313/97A patent/AU3731397A/en not_active Abandoned
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US5958892A (en) | 2-methoxyestradiol-induced apoptosis in cancer cells | |
AU724212B2 (en) | Down-regulation of DNA repair to enhance sensitivity to P53-mediated suppression | |
Mercier et al. | Characterization of DOK1, a candidate tumor suppressor gene, in epithelial ovarian cancer | |
Nanos-Webb et al. | Targeting low molecular weight cyclin E (LMW-E) in breast cancer | |
WO2009102986A1 (fr) | Traitement de l'adénocarcinome exprimant lkb1 avec l'inhibiteur mtor en combinaison avec l'inhibiteur cox1 | |
Ferrer et al. | Spinophilin acts as a tumor suppressor by regulating Rb phosphorylation | |
Delia et al. | Dissociation between cell cycle arrest and apoptosis can occur in Li-Fraumeni cells heterozygous for p53 gene mutations | |
Hall et al. | A brief staurosporine treatment of mitotic cells triggers premature exit from mitosis and polyploid cell formation | |
Truong et al. | Direct transcriptional regulation of MDM2 by Fli-1 | |
Sionov et al. | Apoptosis by p53: mechanisms, regulation, and clinical implications | |
WO1998003195A9 (fr) | Procedes et compositions de modulation du taux de croissance | |
WO1998003195A1 (fr) | Procedes et compositions de modulation du taux de croissance | |
Qi et al. | Expression of the cyclin-dependent kinase inhibitor p27 and its deregulation in mouse B cell lymphomas | |
WO1997008184A1 (fr) | Procedes et compositions comprenant des agents alterant l'adn et des inhibiteurs ou des activateurs de la tyrosine kinase | |
Kudoh et al. | Protein expression of cell cycle regulator, p27Kip1, correlates with histopathological grade of non‐Hodgkin's lymphoma | |
CA2471967A1 (fr) | Oligonucleotides antisens wt1 inhibant le cancer du sein | |
Lukošiūtė-Urbonienė | Effects of Epigenetic Alterations on the Apoptosis Regulating Proteins in Pancreatic Cancer | |
Ling | Role of 14-3-3τ in autophagy and role of EDD in p53 regulation | |
Moncunill Massaguer | Molecular mechanisms of apoptosis induction by AICAR and the new prohibitin-binding compound fluorizoline | |
Ramesh et al. | Retroviral Transfer of the Herpes Simplex Virus-Thymidine Kinase (HSV-tK) Gene for the Treatment of Cancer | |
Fan et al. | Item Type Article | |
Flatt | Analysis of p53 signaling pathways after cell stress: A role for p53 in G2 cell cycle checkpoint response | |
Mihich et al. | Eleventh Annual Pezcoller Symposium: Molecular Horizons in Cancer Therapeutics | |
Schavolt | Identification and regulation of p53 target genes in primary human epidermal keratinocytes | |
Sun | Regulation of the P53-MDM2 feedback loop by nucleostemin and ribosomal proteins |