JPH08502257A - Pp14に基づく治療 - Google Patents
Pp14に基づく治療Info
- Publication number
- JPH08502257A JPH08502257A JP6509255A JP50925594A JPH08502257A JP H08502257 A JPH08502257 A JP H08502257A JP 6509255 A JP6509255 A JP 6509255A JP 50925594 A JP50925594 A JP 50925594A JP H08502257 A JPH08502257 A JP H08502257A
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- receptor
- cells
- antibody
- binding
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 238000011282 treatment Methods 0.000 title description 18
- 238000000034 method Methods 0.000 claims abstract description 90
- 108010029485 Protein Isoforms Proteins 0.000 claims abstract description 53
- 102000001708 Protein Isoforms Human genes 0.000 claims abstract description 53
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 47
- 230000001506 immunosuppresive effect Effects 0.000 claims abstract description 37
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 30
- 206010062016 Immunosuppression Diseases 0.000 claims abstract description 24
- 239000003153 chemical reaction reagent Substances 0.000 claims abstract description 24
- 208000030507 AIDS Diseases 0.000 claims abstract description 10
- 230000004962 physiological condition Effects 0.000 claims abstract description 3
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 150
- 210000004027 cell Anatomy 0.000 claims description 143
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 136
- 229920001184 polypeptide Polymers 0.000 claims description 131
- 108020003175 receptors Proteins 0.000 claims description 107
- 102000005962 receptors Human genes 0.000 claims description 107
- 239000002299 complementary DNA Substances 0.000 claims description 28
- 230000027455 binding Effects 0.000 claims description 25
- 208000032839 leukemia Diseases 0.000 claims description 24
- 238000013518 transcription Methods 0.000 claims description 24
- 230000035897 transcription Effects 0.000 claims description 24
- 150000001413 amino acids Chemical class 0.000 claims description 23
- 238000004519 manufacturing process Methods 0.000 claims description 19
- 239000000203 mixture Substances 0.000 claims description 19
- 239000000523 sample Substances 0.000 claims description 19
- 108091034117 Oligonucleotide Proteins 0.000 claims description 13
- 210000003958 hematopoietic stem cell Anatomy 0.000 claims description 13
- 230000000694 effects Effects 0.000 claims description 12
- 238000010367 cloning Methods 0.000 claims description 11
- 239000000284 extract Substances 0.000 claims description 11
- 108020004707 nucleic acids Proteins 0.000 claims description 11
- 102000039446 nucleic acids Human genes 0.000 claims description 11
- 150000007523 nucleic acids Chemical class 0.000 claims description 11
- 108060003951 Immunoglobulin Proteins 0.000 claims description 10
- 102000018358 immunoglobulin Human genes 0.000 claims description 10
- 238000006243 chemical reaction Methods 0.000 claims description 9
- 238000012216 screening Methods 0.000 claims description 9
- 230000008685 targeting Effects 0.000 claims description 9
- 238000012546 transfer Methods 0.000 claims description 9
- 239000003795 chemical substances by application Substances 0.000 claims description 8
- 230000003302 anti-idiotype Effects 0.000 claims description 7
- 230000003053 immunization Effects 0.000 claims description 7
- 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 claims description 6
- 239000003814 drug Substances 0.000 claims description 6
- 238000013519 translation Methods 0.000 claims description 6
- 210000000612 antigen-presenting cell Anatomy 0.000 claims description 5
- 239000000074 antisense oligonucleotide Substances 0.000 claims description 5
- 238000012230 antisense oligonucleotides Methods 0.000 claims description 5
- 230000000903 blocking effect Effects 0.000 claims description 5
- 230000001413 cellular effect Effects 0.000 claims description 5
- 150000001875 compounds Chemical class 0.000 claims description 5
- 239000011159 matrix material Substances 0.000 claims description 5
- 239000008194 pharmaceutical composition Substances 0.000 claims description 5
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 5
- 208000023275 Autoimmune disease Diseases 0.000 claims description 4
- 208000026935 allergic disease Diseases 0.000 claims description 4
- 230000001086 cytosolic effect Effects 0.000 claims description 4
- 229940079593 drug Drugs 0.000 claims description 4
- 230000003278 mimic effect Effects 0.000 claims description 4
- 230000008569 process Effects 0.000 claims description 4
- 102000053642 Catalytic RNA Human genes 0.000 claims description 3
- 108090000994 Catalytic RNA Proteins 0.000 claims description 3
- 108091026890 Coding region Proteins 0.000 claims description 3
- 108700008625 Reporter Genes Proteins 0.000 claims description 3
- 230000000890 antigenic effect Effects 0.000 claims description 3
- 229960002685 biotin Drugs 0.000 claims description 3
- 235000020958 biotin Nutrition 0.000 claims description 3
- 239000011616 biotin Substances 0.000 claims description 3
- 230000007812 deficiency Effects 0.000 claims description 3
- 239000012634 fragment Substances 0.000 claims description 3
- 210000000822 natural killer cell Anatomy 0.000 claims description 3
- 108091092562 ribozyme Proteins 0.000 claims description 3
- 108020000948 Antisense Oligonucleotides Proteins 0.000 claims description 2
- 108090001008 Avidin Proteins 0.000 claims description 2
- 108020004635 Complementary DNA Proteins 0.000 claims description 2
- 238000010804 cDNA synthesis Methods 0.000 claims description 2
- 239000011248 coating agent Substances 0.000 claims description 2
- 238000000576 coating method Methods 0.000 claims description 2
- 238000002360 preparation method Methods 0.000 claims description 2
- 238000012360 testing method Methods 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 5
- 230000000593 degrading effect Effects 0.000 claims 2
- 208000009329 Graft vs Host Disease Diseases 0.000 claims 1
- 108010090804 Streptavidin Proteins 0.000 claims 1
- 208000007536 Thrombosis Diseases 0.000 claims 1
- CESGKXMBHGUQTB-VONOSFMSSA-N [(1S,2S,6R,10S,11R,13S,14R,15R)-1,6,14-trihydroxy-8-(hydroxymethyl)-4,12,12,15-tetramethyl-5-oxo-13-tetracyclo[8.5.0.02,6.011,13]pentadeca-3,8-dienyl] tetradecanoate Chemical compound C1=C(CO)C[C@]2(O)C(=O)C(C)=C[C@H]2[C@@]2(O)[C@H](C)[C@@H](O)[C@@]3(OC(=O)CCCCCCCCCCCCC)C(C)(C)[C@H]3[C@@H]21 CESGKXMBHGUQTB-VONOSFMSSA-N 0.000 claims 1
- 230000001464 adherent effect Effects 0.000 claims 1
- 239000000853 adhesive Substances 0.000 claims 1
- 230000001070 adhesive effect Effects 0.000 claims 1
- 208000009190 disseminated intravascular coagulation Diseases 0.000 claims 1
- 208000024908 graft versus host disease Diseases 0.000 claims 1
- 230000001376 precipitating effect Effects 0.000 claims 1
- 230000036961 partial effect Effects 0.000 abstract description 2
- 238000010586 diagram Methods 0.000 abstract 1
- 108020004999 messenger RNA Proteins 0.000 description 44
- 210000001772 blood platelet Anatomy 0.000 description 41
- PHEDXBVPIONUQT-RGYGYFBISA-N phorbol 13-acetate 12-myristate Chemical compound C([C@]1(O)C(=O)C(C)=C[C@H]1[C@@]1(O)[C@H](C)[C@H]2OC(=O)CCCCCCCCCCCCC)C(CO)=C[C@H]1[C@H]1[C@]2(OC(C)=O)C1(C)C PHEDXBVPIONUQT-RGYGYFBISA-N 0.000 description 41
- PHEDXBVPIONUQT-UHFFFAOYSA-N Cocarcinogen A1 Natural products CCCCCCCCCCCCCC(=O)OC1C(C)C2(O)C3C=C(C)C(=O)C3(O)CC(CO)=CC2C2C1(OC(C)=O)C2(C)C PHEDXBVPIONUQT-UHFFFAOYSA-N 0.000 description 40
- 201000008752 progressive muscular atrophy Diseases 0.000 description 40
- 235000018102 proteins Nutrition 0.000 description 28
- 210000003593 megakaryocyte Anatomy 0.000 description 22
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 20
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 19
- 230000014509 gene expression Effects 0.000 description 17
- 230000001225 therapeutic effect Effects 0.000 description 17
- 238000002560 therapeutic procedure Methods 0.000 description 17
- 201000010099 disease Diseases 0.000 description 16
- 239000003636 conditioned culture medium Substances 0.000 description 15
- 238000004458 analytical method Methods 0.000 description 13
- 210000004369 blood Anatomy 0.000 description 13
- 239000008280 blood Substances 0.000 description 13
- 229930004094 glycosylphosphatidylinositol Natural products 0.000 description 13
- 230000006698 induction Effects 0.000 description 13
- 239000012528 membrane Substances 0.000 description 13
- 210000004698 lymphocyte Anatomy 0.000 description 12
- 210000002966 serum Anatomy 0.000 description 12
- 241000894007 species Species 0.000 description 11
- 230000008901 benefit Effects 0.000 description 10
- 230000004069 differentiation Effects 0.000 description 10
- 239000000047 product Substances 0.000 description 10
- 210000001519 tissue Anatomy 0.000 description 10
- 239000000872 buffer Substances 0.000 description 9
- 210000004696 endometrium Anatomy 0.000 description 9
- 108020004414 DNA Proteins 0.000 description 8
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 238000012217 deletion Methods 0.000 description 8
- 230000037430 deletion Effects 0.000 description 8
- 230000002401 inhibitory effect Effects 0.000 description 8
- 239000000126 substance Substances 0.000 description 8
- 102100032420 Protein S100-A9 Human genes 0.000 description 7
- 230000002357 endometrial effect Effects 0.000 description 7
- 230000006870 function Effects 0.000 description 7
- 239000002773 nucleotide Substances 0.000 description 7
- 125000003729 nucleotide group Chemical group 0.000 description 7
- 238000010240 RT-PCR analysis Methods 0.000 description 6
- 235000001014 amino acid Nutrition 0.000 description 6
- 238000001514 detection method Methods 0.000 description 6
- 238000001727 in vivo Methods 0.000 description 6
- 230000005764 inhibitory process Effects 0.000 description 6
- 108010076504 Protein Sorting Signals Proteins 0.000 description 5
- 108091034057 RNA (poly(A)) Proteins 0.000 description 5
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 230000015271 coagulation Effects 0.000 description 5
- 238000005345 coagulation Methods 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 230000003993 interaction Effects 0.000 description 5
- 239000003550 marker Substances 0.000 description 5
- 230000035755 proliferation Effects 0.000 description 5
- 230000010076 replication Effects 0.000 description 5
- 238000011160 research Methods 0.000 description 5
- 230000002441 reversible effect Effects 0.000 description 5
- 238000010561 standard procedure Methods 0.000 description 5
- 230000009885 systemic effect Effects 0.000 description 5
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 4
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 4
- 206010053567 Coagulopathies Diseases 0.000 description 4
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 4
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 4
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 4
- 208000010668 atopic eczema Diseases 0.000 description 4
- 238000002405 diagnostic procedure Methods 0.000 description 4
- 239000000539 dimer Substances 0.000 description 4
- 208000035475 disorder Diseases 0.000 description 4
- 210000002950 fibroblast Anatomy 0.000 description 4
- 230000003394 haemopoietic effect Effects 0.000 description 4
- 210000000777 hematopoietic system Anatomy 0.000 description 4
- 239000000833 heterodimer Substances 0.000 description 4
- 239000000710 homodimer Substances 0.000 description 4
- 210000000987 immune system Anatomy 0.000 description 4
- 238000001114 immunoprecipitation Methods 0.000 description 4
- 239000003018 immunosuppressive agent Substances 0.000 description 4
- 239000000411 inducer Substances 0.000 description 4
- 239000003446 ligand Substances 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 208000025113 myeloid leukemia Diseases 0.000 description 4
- 210000002826 placenta Anatomy 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 206010012434 Dermatitis allergic Diseases 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
- OWXMKDGYPWMGEB-UHFFFAOYSA-N HEPPS Chemical compound OCCN1CCN(CCCS(O)(=O)=O)CC1 OWXMKDGYPWMGEB-UHFFFAOYSA-N 0.000 description 3
- 101000585553 Homo sapiens Glycodelin Proteins 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 101710120037 Toxin CcdB Proteins 0.000 description 3
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
- 230000000692 anti-sense effect Effects 0.000 description 3
- 201000008937 atopic dermatitis Diseases 0.000 description 3
- 208000015294 blood coagulation disease Diseases 0.000 description 3
- 210000001185 bone marrow Anatomy 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 210000004556 brain Anatomy 0.000 description 3
- 238000004113 cell culture Methods 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 3
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 3
- HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 3
- 210000003785 decidua Anatomy 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- 239000008121 dextrose Substances 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 210000005001 male reproductive tract Anatomy 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 108091033319 polynucleotide Proteins 0.000 description 3
- 102000040430 polynucleotide Human genes 0.000 description 3
- 239000002157 polynucleotide Substances 0.000 description 3
- 230000035935 pregnancy Effects 0.000 description 3
- -1 rephozymes Proteins 0.000 description 3
- 238000010839 reverse transcription Methods 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 238000011144 upstream manufacturing Methods 0.000 description 3
- 229930024421 Adenine Natural products 0.000 description 2
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 2
- BZUNJUAMQZRJIP-UHFFFAOYSA-N CPDA Natural products OCCCCCCCCCCCCCCC(O)=O BZUNJUAMQZRJIP-UHFFFAOYSA-N 0.000 description 2
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 2
- 102000000589 Interleukin-1 Human genes 0.000 description 2
- 108010002352 Interleukin-1 Proteins 0.000 description 2
- 238000010222 PCR analysis Methods 0.000 description 2
- 241000282320 Panthera leo Species 0.000 description 2
- 208000013544 Platelet disease Diseases 0.000 description 2
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 2
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 206010040047 Sepsis Diseases 0.000 description 2
- 206010052779 Transplant rejections Diseases 0.000 description 2
- 229920004890 Triton X-100 Polymers 0.000 description 2
- 239000013504 Triton X-100 Substances 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 229960000643 adenine Drugs 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 230000001028 anti-proliverative effect Effects 0.000 description 2
- 230000002457 bidirectional effect Effects 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 210000000988 bone and bone Anatomy 0.000 description 2
- 239000013592 cell lysate Substances 0.000 description 2
- 108091092328 cellular RNA Proteins 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 238000012790 confirmation Methods 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 210000005168 endometrial cell Anatomy 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 229940025294 hemin Drugs 0.000 description 2
- BTIJJDXEELBZFS-QDUVMHSLSA-K hemin Chemical compound CC1=C(CCC(O)=O)C(C=C2C(CCC(O)=O)=C(C)\C(N2[Fe](Cl)N23)=C\4)=N\C1=C/C2=C(C)C(C=C)=C3\C=C/1C(C)=C(C=C)C/4=N\1 BTIJJDXEELBZFS-QDUVMHSLSA-K 0.000 description 2
- 102000048444 human PAEP Human genes 0.000 description 2
- 230000008629 immune suppression Effects 0.000 description 2
- 208000026278 immune system disease Diseases 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 239000012133 immunoprecipitate Substances 0.000 description 2
- 229940125721 immunosuppressive agent Drugs 0.000 description 2
- 208000027866 inflammatory disease Diseases 0.000 description 2
- 230000004054 inflammatory process Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 210000000265 leukocyte Anatomy 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 210000002418 meninge Anatomy 0.000 description 2
- WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 2
- 230000008450 motivation Effects 0.000 description 2
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 2
- GISJHCLTIVIGLX-UHFFFAOYSA-N n-[4-[(4-chlorophenyl)methoxy]pyridin-2-yl]-2-(2,6-difluorophenyl)acetamide Chemical compound FC1=CC=CC(F)=C1CC(=O)NC1=CC(OCC=2C=CC(Cl)=CC=2)=CC=N1 GISJHCLTIVIGLX-UHFFFAOYSA-N 0.000 description 2
- 210000000440 neutrophil Anatomy 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- 230000001991 pathophysiological effect Effects 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 230000003169 placental effect Effects 0.000 description 2
- GMVPRGQOIOIIMI-DWKJAMRDSA-N prostaglandin E1 Chemical compound CCCCC[C@H](O)\C=C\[C@H]1[C@H](O)CC(=O)[C@@H]1CCCCCCC(O)=O GMVPRGQOIOIIMI-DWKJAMRDSA-N 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 238000006722 reduction reaction Methods 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 210000000582 semen Anatomy 0.000 description 2
- 210000000813 small intestine Anatomy 0.000 description 2
- 239000001509 sodium citrate Substances 0.000 description 2
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 229940104230 thymidine Drugs 0.000 description 2
- 230000001988 toxicity Effects 0.000 description 2
- 231100000419 toxicity Toxicity 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- QGVLYPPODPLXMB-UBTYZVCOSA-N (1aR,1bS,4aR,7aS,7bS,8R,9R,9aS)-4a,7b,9,9a-tetrahydroxy-3-(hydroxymethyl)-1,1,6,8-tetramethyl-1,1a,1b,4,4a,7a,7b,8,9,9a-decahydro-5H-cyclopropa[3,4]benzo[1,2-e]azulen-5-one Chemical compound C1=C(CO)C[C@]2(O)C(=O)C(C)=C[C@H]2[C@@]2(O)[C@H](C)[C@@H](O)[C@@]3(O)C(C)(C)[C@H]3[C@@H]21 QGVLYPPODPLXMB-UBTYZVCOSA-N 0.000 description 1
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- WFCSWCVEJLETKA-UHFFFAOYSA-N 2-piperazin-1-ylethanol Chemical compound OCCN1CCNCC1 WFCSWCVEJLETKA-UHFFFAOYSA-N 0.000 description 1
- 206010000234 Abortion spontaneous Diseases 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 description 1
- 108091032955 Bacterial small RNA Proteins 0.000 description 1
- 102000000119 Beta-lactoglobulin Human genes 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 241000251204 Chimaeridae Species 0.000 description 1
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 1
- 208000010833 Chronic myeloid leukaemia Diseases 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 101710160621 Fusion glycoprotein F0 Proteins 0.000 description 1
- 102100029880 Glycodelin Human genes 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 208000017604 Hodgkin disease Diseases 0.000 description 1
- 208000010747 Hodgkins lymphoma Diseases 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 1
- 238000012404 In vitro experiment Methods 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 208000022559 Inflammatory bowel disease Diseases 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 102000019223 Interleukin-1 receptor Human genes 0.000 description 1
- 108050006617 Interleukin-1 receptor 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
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 108010060630 Lactoglobulins Proteins 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- 208000030289 Lymphoproliferative disease Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 208000033761 Myelogenous Chronic BCR-ABL Positive Leukemia Diseases 0.000 description 1
- 208000015914 Non-Hodgkin lymphomas Diseases 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 101710158668 Placental protein Proteins 0.000 description 1
- 102000008217 Pregnancy Proteins Human genes 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 208000012287 Prolapse Diseases 0.000 description 1
- 201000004681 Psoriasis Diseases 0.000 description 1
- 108020005067 RNA Splice Sites Proteins 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 239000012979 RPMI medium Substances 0.000 description 1
- 230000010799 Receptor Interactions Effects 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 235000013290 Sagittaria latifolia Nutrition 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 201000001880 Sexual dysfunction Diseases 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 208000018359 Systemic autoimmune disease Diseases 0.000 description 1
- 230000005867 T cell response Effects 0.000 description 1
- 208000005485 Thrombocytosis Diseases 0.000 description 1
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 1
- 108010009583 Transforming Growth Factors Proteins 0.000 description 1
- 102000009618 Transforming Growth Factors Human genes 0.000 description 1
- 208000034953 Twin anemia-polycythemia sequence Diseases 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000012042 active reagent Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 230000000172 allergic effect Effects 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 230000000961 alloantigen Effects 0.000 description 1
- 230000000735 allogeneic effect Effects 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 210000003484 anatomy Anatomy 0.000 description 1
- 230000001621 anti-mitogenic effect Effects 0.000 description 1
- 230000002927 anti-mitotic effect Effects 0.000 description 1
- 230000000417 anti-transforming effect Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- 230000005975 antitumor immune response Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 208000006673 asthma Diseases 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 230000005784 autoimmunity Effects 0.000 description 1
- VJBCNMFKFZIXHC-UHFFFAOYSA-N azanium;2-(4-methyl-5-oxo-4-propan-2-yl-1h-imidazol-2-yl)quinoline-3-carboxylate Chemical class N.N1C(=O)C(C(C)C)(C)N=C1C1=NC2=CC=CC=C2C=C1C(O)=O VJBCNMFKFZIXHC-UHFFFAOYSA-N 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 239000002981 blocking agent Substances 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 210000004271 bone marrow stromal cell Anatomy 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000015861 cell surface binding Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- VYLVYHXQOHJDJL-UHFFFAOYSA-K cerium trichloride Chemical compound Cl[Ce](Cl)Cl VYLVYHXQOHJDJL-UHFFFAOYSA-K 0.000 description 1
- 239000013043 chemical agent Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 150000001860 citric acid derivatives Chemical class 0.000 description 1
- 210000000078 claw Anatomy 0.000 description 1
- 238000003501 co-culture Methods 0.000 description 1
- 238000012761 co-transfection Methods 0.000 description 1
- 230000009852 coagulant defect Effects 0.000 description 1
- 238000004581 coalescence Methods 0.000 description 1
- 235000015246 common arrowhead Nutrition 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000001461 cytolytic effect Effects 0.000 description 1
- RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 238000005034 decoration Methods 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- UREBDLICKHMUKA-CXSFZGCWSA-N dexamethasone Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@@H](C)[C@@](C(=O)CO)(O)[C@@]1(C)C[C@@H]2O UREBDLICKHMUKA-CXSFZGCWSA-N 0.000 description 1
- 229960003957 dexamethasone Drugs 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 230000000431 effect on proliferation Effects 0.000 description 1
- 230000002500 effect on skin Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000000925 erythroid effect Effects 0.000 description 1
- 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 1
- 239000013604 expression vector Substances 0.000 description 1
- 210000005002 female reproductive tract Anatomy 0.000 description 1
- 230000008175 fetal development Effects 0.000 description 1
- 210000003754 fetus Anatomy 0.000 description 1
- 239000012997 ficoll-paque Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 230000009036 growth inhibition Effects 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- ZJYYHGLJYGJLLN-UHFFFAOYSA-N guanidinium thiocyanate Chemical compound SC#N.NC(N)=N ZJYYHGLJYGJLLN-UHFFFAOYSA-N 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 108010055756 hemalin Proteins 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 210000003701 histiocyte Anatomy 0.000 description 1
- 238000011577 humanized mouse model Methods 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 229940027941 immunoglobulin g Drugs 0.000 description 1
- 239000002955 immunomodulating agent Substances 0.000 description 1
- 230000002584 immunomodulator Effects 0.000 description 1
- 229940121354 immunomodulator Drugs 0.000 description 1
- 230000004957 immunoregulator effect Effects 0.000 description 1
- 229960003444 immunosuppressant agent Drugs 0.000 description 1
- 229940124589 immunosuppressive drug Drugs 0.000 description 1
- 230000001024 immunotherapeutic effect Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 208000000509 infertility Diseases 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 231100000535 infertility Toxicity 0.000 description 1
- 230000002757 inflammatory effect Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 239000002932 luster Substances 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L magnesium chloride Substances [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 229960004452 methionine Drugs 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 238000004242 micellar liquid chromatography Methods 0.000 description 1
- 208000015994 miscarriage Diseases 0.000 description 1
- 230000000394 mitotic effect Effects 0.000 description 1
- 230000037230 mobility Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 229940045641 monobasic sodium phosphate Drugs 0.000 description 1
- 210000005087 mononuclear cell Anatomy 0.000 description 1
- 229910000403 monosodium phosphate Inorganic materials 0.000 description 1
- 235000019799 monosodium phosphate Nutrition 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 210000000066 myeloid cell Anatomy 0.000 description 1
- 229940105132 myristate Drugs 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000006213 negative regulation of lymphocyte proliferation Effects 0.000 description 1
- 230000001613 neoplastic effect Effects 0.000 description 1
- 238000010899 nucleation Methods 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 201000008482 osteoarthritis Diseases 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000007310 pathophysiology Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 1
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- QGVLYPPODPLXMB-QXYKVGAMSA-N phorbol Natural products C[C@@H]1[C@@H](O)[C@]2(O)[C@H]([C@H]3C=C(CO)C[C@@]4(O)[C@H](C=C(C)C4=O)[C@@]13O)C2(C)C QGVLYPPODPLXMB-QXYKVGAMSA-N 0.000 description 1
- 239000002644 phorbol ester Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 210000005059 placental tissue Anatomy 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000001124 posttranscriptional effect Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 238000000730 protein immunoprecipitation Methods 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 210000003370 receptor cell Anatomy 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000006485 reductive methylation reaction Methods 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 230000001850 reproductive effect Effects 0.000 description 1
- 210000004994 reproductive system Anatomy 0.000 description 1
- 210000005000 reproductive tract Anatomy 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 108090000064 retinoic acid receptors Proteins 0.000 description 1
- 102000003702 retinoic acid receptors Human genes 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 229940110622 rovera Drugs 0.000 description 1
- 102220201851 rs143406017 Human genes 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 231100000872 sexual dysfunction Toxicity 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N sodium azide Substances [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 1
- UIIMBOGNXHQVGW-UHFFFAOYSA-M sodium bicarbonate Substances [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 235000011008 sodium phosphates Nutrition 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 208000000995 spontaneous abortion Diseases 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 201000000596 systemic lupus erythematosus Diseases 0.000 description 1
- 230000002381 testicular Effects 0.000 description 1
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000004797 therapeutic response Effects 0.000 description 1
- ANRHNWWPFJCPAZ-UHFFFAOYSA-M thionine Chemical compound [Cl-].C1=CC(N)=CC2=[S+]C3=CC(N)=CC=C3N=C21 ANRHNWWPFJCPAZ-UHFFFAOYSA-M 0.000 description 1
- KUAZQDVKQLNFPE-UHFFFAOYSA-N thiram Chemical compound CN(C)C(=S)SSC(=S)N(C)C KUAZQDVKQLNFPE-UHFFFAOYSA-N 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 230000005945 translocation Effects 0.000 description 1
- 238000011277 treatment modality Methods 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 230000009278 visceral effect Effects 0.000 description 1
- 230000002747 voluntary effect Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 210000004885 white matter Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4715—Pregnancy proteins, e.g. placenta proteins, alpha-feto-protein, pregnancy specific beta glycoprotein
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/62—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being a protein, peptide or polyamino acid
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/08—Antiallergic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/74—Inducing cell proliferation
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US95480292A | 1992-09-30 | 1992-09-30 | |
US07/954,802 | 1992-09-30 | ||
PCT/US1993/009216 WO1994007366A1 (en) | 1992-09-30 | 1993-09-28 | Pp14-based therapy |
Publications (1)
Publication Number | Publication Date |
---|---|
JPH08502257A true JPH08502257A (ja) | 1996-03-12 |
Family
ID=25495948
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP6509255A Pending JPH08502257A (ja) | 1992-09-30 | 1993-09-28 | Pp14に基づく治療 |
Country Status (5)
Country | Link |
---|---|
EP (1) | EP0662782A4 (de) |
JP (1) | JPH08502257A (de) |
AU (1) | AU5165993A (de) |
CA (1) | CA2145762A1 (de) |
WO (1) | WO1994007366A1 (de) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2003519162A (ja) * | 2000-01-03 | 2003-06-17 | ティーアール アソシエイツ,エル.エル.シー. | Pp14融合蛋白質並びに該蛋白質の製造及び使用方法 |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
IL111743A0 (en) * | 1993-12-08 | 1995-01-24 | Intermune Life Sciences Inc | Recombinant genes expressing pp14 |
WO2004093907A2 (en) * | 2003-04-23 | 2004-11-04 | Tomoaki Hoshino | Therapeutic agents for treating dermatitis, alopecia and itching and transgenic animals for evaluating such therapeutic agents |
Family Cites Families (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5039521A (en) * | 1989-01-11 | 1991-08-13 | Hyal Pharmaceutical Corporation | Immune cell proliferation inhibitors |
-
1993
- 1993-09-28 WO PCT/US1993/009216 patent/WO1994007366A1/en not_active Application Discontinuation
- 1993-09-28 AU AU51659/93A patent/AU5165993A/en not_active Abandoned
- 1993-09-28 JP JP6509255A patent/JPH08502257A/ja active Pending
- 1993-09-28 EP EP93922763A patent/EP0662782A4/de not_active Withdrawn
- 1993-09-28 CA CA002145762A patent/CA2145762A1/en not_active Abandoned
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2003519162A (ja) * | 2000-01-03 | 2003-06-17 | ティーアール アソシエイツ,エル.エル.シー. | Pp14融合蛋白質並びに該蛋白質の製造及び使用方法 |
Also Published As
Publication number | Publication date |
---|---|
WO1994007366A1 (en) | 1994-04-14 |
EP0662782A1 (de) | 1995-07-19 |
CA2145762A1 (en) | 1994-04-14 |
AU5165993A (en) | 1994-04-26 |
EP0662782A4 (de) | 1995-10-25 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Weis et al. | Structure of the human B lymphocyte receptor for C3d and the Epstein-Barr virus and relatedness to other members of the family of C3/C4 binding proteins. | |
US7939640B2 (en) | Antibodies that bind B7L-1 | |
JP4426724B2 (ja) | Ldcamと称される分子 | |
JP2008131944A (ja) | 白血球免疫グロブリン様受容体(lir)と命名される免疫調節剤ファミリー | |
JP2010155846A (ja) | 免疫調節のための方法および組成物 | |
JP2001517425A (ja) | T細胞共同刺激性ポリペプチド、モノクローナル抗体、ならびにその製法および使用 | |
JP2002504818A (ja) | リガンドファミリーのntn−2メンバー | |
JP2002543787A (ja) | 白血球免疫グロブリン様受容体(lir)と命名された免疫調節因子のファミリー | |
JP2930713B2 (ja) | タンパク質ホルモン形成の抑制用の組成物およびその使用法 | |
JPH06506596A (ja) | インターロイキン−8受容体及び関連分子及び方法 | |
JP2002532061A (ja) | Apj受容体とhivウイルスとの相互作用を調節するための方法及び組成物 | |
JP2718827B2 (ja) | 分泌Mac−2結合糖タンパク質 | |
JP2001519656A (ja) | Tnf/ngfレセプターファミリーのレセプター機能モジュレーター | |
JP2000510709A (ja) | 少なくとも1種のhla―gイソ型をその表面で発現する真核細胞、およびその使用 | |
AU762392B2 (en) | Methods and materials relating to novel CD39-like polypeptides | |
JPH08502257A (ja) | Pp14に基づく治療 | |
JP2001500013A (ja) | HT▲下m4▼、治療およびアッセイ方法、アゴニストおよびアンタゴニスト | |
JP2005519590A (ja) | 免疫関連疾患の治療のための組成物及び方法 | |
JPWO2003031620A1 (ja) | 新規クラスiiサイトカイン受容体 | |
WO2001096564A2 (fr) | Isoforme d'hla-g (hla-g7) et ses applications | |
JPH02481A (ja) | 可溶性t4の精製方法 | |
US6447771B1 (en) | Methods and materials relating to novel CD39-like polypeptides | |
US6670135B1 (en) | Semaphorin polypeptides | |
US5837495A (en) | DNA encoding interleukin-1 antagonist | |
JP2004208583A (ja) | 新規免疫抑制性受容体 |