JP2011500005A - ヒト造血幹細胞の生着を増加させるためのSIRPα−CD47相互作用の調節およびそのための化合物 - Google Patents
ヒト造血幹細胞の生着を増加させるためのSIRPα−CD47相互作用の調節およびそのための化合物 Download PDFInfo
- Publication number
- JP2011500005A JP2011500005A JP2010528256A JP2010528256A JP2011500005A JP 2011500005 A JP2011500005 A JP 2011500005A JP 2010528256 A JP2010528256 A JP 2010528256A JP 2010528256 A JP2010528256 A JP 2010528256A JP 2011500005 A JP2011500005 A JP 2011500005A
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- human
- sirpα
- seq
- nod
- 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
- 210000003958 hematopoietic stem cell Anatomy 0.000 title claims abstract description 106
- 150000001875 compounds Chemical class 0.000 title claims abstract description 26
- 230000003993 interaction Effects 0.000 title claims abstract description 24
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 176
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 176
- 229920001184 polypeptide Polymers 0.000 claims abstract description 174
- 101000868279 Homo sapiens Leukocyte surface antigen CD47 Proteins 0.000 claims abstract description 94
- 238000000034 method Methods 0.000 claims abstract description 56
- 239000012634 fragment Substances 0.000 claims abstract description 41
- 102100032913 Leukocyte surface antigen CD47 Human genes 0.000 claims abstract description 33
- 230000001965 increasing effect Effects 0.000 claims abstract description 31
- 210000002540 macrophage Anatomy 0.000 claims description 115
- 210000004027 cell Anatomy 0.000 claims description 106
- 108090000623 proteins and genes Proteins 0.000 claims description 77
- 102000044459 human CD47 Human genes 0.000 claims description 61
- 150000001413 amino acids Chemical class 0.000 claims description 58
- 230000027455 binding Effects 0.000 claims description 52
- 102000004169 proteins and genes Human genes 0.000 claims description 40
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 28
- 230000014509 gene expression Effects 0.000 claims description 24
- 238000012217 deletion Methods 0.000 claims description 19
- 230000037430 deletion Effects 0.000 claims description 19
- 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 claims description 18
- 102000039446 nucleic acids Human genes 0.000 claims description 17
- 108020004707 nucleic acids Proteins 0.000 claims description 17
- 150000007523 nucleic acids Chemical class 0.000 claims description 17
- 238000012163 sequencing technique Methods 0.000 claims description 17
- 238000006467 substitution reaction Methods 0.000 claims description 17
- 238000002054 transplantation Methods 0.000 claims description 17
- 238000012360 testing method Methods 0.000 claims description 16
- 241000282412 Homo Species 0.000 claims description 15
- 241000124008 Mammalia Species 0.000 claims description 15
- 230000003394 haemopoietic effect Effects 0.000 claims description 14
- 125000003729 nucleotide group Chemical group 0.000 claims description 13
- 238000003780 insertion Methods 0.000 claims description 12
- 230000037431 insertion Effects 0.000 claims description 12
- 239000002773 nucleotide Substances 0.000 claims description 12
- 230000002401 inhibitory effect Effects 0.000 claims description 10
- 210000004748 cultured cell Anatomy 0.000 claims description 9
- 102000054765 polymorphisms of proteins Human genes 0.000 claims description 9
- 230000001629 suppression Effects 0.000 claims description 8
- 239000013598 vector Substances 0.000 claims description 8
- 239000003937 drug carrier Substances 0.000 claims description 7
- 239000003814 drug Substances 0.000 claims description 6
- 239000013604 expression vector Substances 0.000 claims description 6
- 238000012258 culturing Methods 0.000 claims description 5
- 239000008194 pharmaceutical composition Substances 0.000 claims description 4
- 206010071602 Genetic polymorphism Diseases 0.000 claims description 3
- 229940079593 drug Drugs 0.000 claims description 3
- 108091035707 Consensus sequence Proteins 0.000 claims 1
- 101000863873 Homo sapiens Tyrosine-protein phosphatase non-receptor type substrate 1 Proteins 0.000 abstract description 111
- 102100029948 Tyrosine-protein phosphatase non-receptor type substrate 1 Human genes 0.000 abstract description 111
- 108020001507 fusion proteins Proteins 0.000 abstract description 26
- 102000037865 fusion proteins Human genes 0.000 abstract description 26
- 230000002708 enhancing effect Effects 0.000 abstract description 2
- 241000699670 Mus sp. Species 0.000 description 51
- 210000001185 bone marrow Anatomy 0.000 description 49
- 241000699666 Mus <mouse, genus> Species 0.000 description 43
- 235000001014 amino acid Nutrition 0.000 description 40
- 229940024606 amino acid Drugs 0.000 description 38
- 230000011132 hemopoiesis Effects 0.000 description 28
- 235000018102 proteins Nutrition 0.000 description 28
- 238000003556 assay Methods 0.000 description 25
- 238000011579 SCID mouse model Methods 0.000 description 20
- 238000001727 in vivo Methods 0.000 description 19
- 210000004369 blood Anatomy 0.000 description 18
- 239000008280 blood Substances 0.000 description 18
- 230000000694 effects Effects 0.000 description 16
- 230000001404 mediated effect Effects 0.000 description 16
- 241000713666 Lentivirus Species 0.000 description 15
- 238000000338 in vitro Methods 0.000 description 15
- 108700028369 Alleles Proteins 0.000 description 14
- 239000013612 plasmid Substances 0.000 description 13
- 230000035772 mutation Effects 0.000 description 12
- 238000003119 immunoblot Methods 0.000 description 11
- 238000003752 polymerase chain reaction Methods 0.000 description 11
- 108091026890 Coding region Proteins 0.000 description 10
- 210000003995 blood forming stem cell Anatomy 0.000 description 10
- 238000002474 experimental method Methods 0.000 description 10
- 208000015181 infectious disease Diseases 0.000 description 10
- 108020004414 DNA Proteins 0.000 description 9
- 206010057249 Phagocytosis Diseases 0.000 description 9
- 241000700605 Viruses Species 0.000 description 9
- 238000004458 analytical method Methods 0.000 description 9
- 238000000684 flow cytometry Methods 0.000 description 9
- 230000008782 phagocytosis Effects 0.000 description 9
- 108091033319 polynucleotide Proteins 0.000 description 9
- 102000040430 polynucleotide Human genes 0.000 description 9
- 239000002157 polynucleotide Substances 0.000 description 9
- 210000000130 stem cell Anatomy 0.000 description 9
- 210000002536 stromal cell Anatomy 0.000 description 9
- 230000008093 supporting effect Effects 0.000 description 9
- 239000002299 complementary DNA Substances 0.000 description 8
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 7
- 101001046686 Homo sapiens Integrin alpha-M Proteins 0.000 description 7
- 102100022338 Integrin alpha-M Human genes 0.000 description 7
- 101100477532 Mus musculus Sirpa gene Proteins 0.000 description 7
- 230000001086 cytosolic effect Effects 0.000 description 7
- 230000006870 function Effects 0.000 description 7
- 230000005764 inhibitory process Effects 0.000 description 7
- 239000006166 lysate Substances 0.000 description 7
- 108010093459 tubulin-specific chaperone C Proteins 0.000 description 7
- 101000738771 Homo sapiens Receptor-type tyrosine-protein phosphatase C Proteins 0.000 description 6
- 108091092878 Microsatellite Proteins 0.000 description 6
- 102100037422 Receptor-type tyrosine-protein phosphatase C Human genes 0.000 description 6
- 210000000349 chromosome Anatomy 0.000 description 6
- 230000001419 dependent effect Effects 0.000 description 6
- 210000005260 human cell Anatomy 0.000 description 6
- 230000001105 regulatory effect Effects 0.000 description 6
- 230000011664 signaling Effects 0.000 description 6
- 239000006228 supernatant Substances 0.000 description 6
- 230000004083 survival effect Effects 0.000 description 6
- 230000014616 translation Effects 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 5
- 230000009471 action Effects 0.000 description 5
- 238000013459 approach Methods 0.000 description 5
- 230000001413 cellular effect Effects 0.000 description 5
- 239000003446 ligand Substances 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 238000011282 treatment Methods 0.000 description 5
- 238000002689 xenotransplantation Methods 0.000 description 5
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 4
- 101000891634 Homo sapiens Tubulin-specific chaperone C Proteins 0.000 description 4
- 238000012408 PCR amplification Methods 0.000 description 4
- 102000000447 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Human genes 0.000 description 4
- 108010055817 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Proteins 0.000 description 4
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 4
- 101710120037 Toxin CcdB Proteins 0.000 description 4
- 239000012228 culture supernatant Substances 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 230000018109 developmental process Effects 0.000 description 4
- 239000010432 diamond Substances 0.000 description 4
- 239000000284 extract Substances 0.000 description 4
- 210000000265 leukocyte Anatomy 0.000 description 4
- 230000007774 longterm Effects 0.000 description 4
- 230000007246 mechanism Effects 0.000 description 4
- 229920000609 methyl cellulose Polymers 0.000 description 4
- 239000001923 methylcellulose Substances 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 244000052769 pathogen Species 0.000 description 4
- 210000003024 peritoneal macrophage Anatomy 0.000 description 4
- 239000002831 pharmacologic agent Substances 0.000 description 4
- 238000010186 staining Methods 0.000 description 4
- 238000012546 transfer Methods 0.000 description 4
- 101100193633 Danio rerio rag2 gene Proteins 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102100031573 Hematopoietic progenitor cell antigen CD34 Human genes 0.000 description 3
- 101000777663 Homo sapiens Hematopoietic progenitor cell antigen CD34 Proteins 0.000 description 3
- 101000781942 Homo sapiens Zinc finger CCCH domain-containing protein 8 Proteins 0.000 description 3
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 3
- 206010061598 Immunodeficiency Diseases 0.000 description 3
- 208000029462 Immunodeficiency disease Diseases 0.000 description 3
- 101100193635 Mus musculus Rag2 gene Proteins 0.000 description 3
- 108010004729 Phycoerythrin Proteins 0.000 description 3
- 210000001744 T-lymphocyte Anatomy 0.000 description 3
- 206010052779 Transplant rejections Diseases 0.000 description 3
- 102100036580 Zinc finger CCCH domain-containing protein 8 Human genes 0.000 description 3
- 210000000601 blood cell Anatomy 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 239000007975 buffered saline Substances 0.000 description 3
- 238000012790 confirmation Methods 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 231100000673 dose–response relationship Toxicity 0.000 description 3
- 210000004700 fetal blood Anatomy 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 230000013595 glycosylation Effects 0.000 description 3
- 238000006206 glycosylation reaction Methods 0.000 description 3
- 230000007813 immunodeficiency Effects 0.000 description 3
- 238000001114 immunoprecipitation Methods 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- 230000003834 intracellular effect Effects 0.000 description 3
- 208000032839 leukemia Diseases 0.000 description 3
- 210000004185 liver Anatomy 0.000 description 3
- 238000013507 mapping Methods 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 210000000066 myeloid cell Anatomy 0.000 description 3
- 210000000822 natural killer cell Anatomy 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 239000003531 protein hydrolysate Substances 0.000 description 3
- 238000001273 protein sequence alignment Methods 0.000 description 3
- 238000003753 real-time PCR Methods 0.000 description 3
- 230000019491 signal transduction Effects 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 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 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 108091093088 Amplicon Proteins 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108010067770 Endopeptidase K Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 2
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- MWUXSHHQAYIFBG-UHFFFAOYSA-N Nitric oxide Chemical compound O=[N] MWUXSHHQAYIFBG-UHFFFAOYSA-N 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 238000002105 Southern blotting Methods 0.000 description 2
- 108010006785 Taq Polymerase Proteins 0.000 description 2
- 102100033019 Tyrosine-protein phosphatase non-receptor type 11 Human genes 0.000 description 2
- 101710116241 Tyrosine-protein phosphatase non-receptor type 11 Proteins 0.000 description 2
- 102100021657 Tyrosine-protein phosphatase non-receptor type 6 Human genes 0.000 description 2
- 101710128901 Tyrosine-protein phosphatase non-receptor type 6 Proteins 0.000 description 2
- 125000001931 aliphatic group Chemical group 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 210000002798 bone marrow cell Anatomy 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 230000001332 colony forming effect Effects 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 210000005220 cytoplasmic tail Anatomy 0.000 description 2
- 230000007812 deficiency Effects 0.000 description 2
- 206010012601 diabetes mellitus Diseases 0.000 description 2
- 229910003460 diamond Inorganic materials 0.000 description 2
- 230000004069 differentiation Effects 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 2
- 238000012252 genetic analysis Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 238000003205 genotyping method Methods 0.000 description 2
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 2
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- JYGXADMDTFJGBT-VWUMJDOOSA-N hydrocortisone Chemical compound O=C1CC[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 JYGXADMDTFJGBT-VWUMJDOOSA-N 0.000 description 2
- 239000012133 immunoprecipitate Substances 0.000 description 2
- 230000002757 inflammatory effect Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 239000007951 isotonicity adjuster Substances 0.000 description 2
- 230000005012 migration Effects 0.000 description 2
- 238000013508 migration Methods 0.000 description 2
- 210000005087 mononuclear cell Anatomy 0.000 description 2
- 210000002569 neuron Anatomy 0.000 description 2
- 238000005457 optimization Methods 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 210000005259 peripheral blood Anatomy 0.000 description 2
- 239000011886 peripheral blood Substances 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- 238000007747 plating Methods 0.000 description 2
- 230000001323 posttranslational effect Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 230000002269 spontaneous effect Effects 0.000 description 2
- 238000007619 statistical method Methods 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin 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
- 230000003319 supportive effect Effects 0.000 description 2
- 210000002303 tibia Anatomy 0.000 description 2
- 230000006433 tumor necrosis factor production Effects 0.000 description 2
- 210000000689 upper leg Anatomy 0.000 description 2
- 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
- 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 1
- 108020003589 5' Untranslated Regions Proteins 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 102000009410 Chemokine receptor Human genes 0.000 description 1
- 108050000299 Chemokine receptor Proteins 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 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 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 101000835928 Homo sapiens Signal-regulatory protein gamma Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 208000026350 Inborn Genetic disease Diseases 0.000 description 1
- 102100037850 Interferon gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 108700018351 Major Histocompatibility Complex Proteins 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 102000012750 Membrane Glycoproteins Human genes 0.000 description 1
- 108010090054 Membrane Glycoproteins Proteins 0.000 description 1
- 108700005084 Multigene Family Proteins 0.000 description 1
- 101000746372 Mus musculus Granulocyte-macrophage colony-stimulating factor Proteins 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 229930182555 Penicillin Natural products 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
- KHGNFPUMBJSZSM-UHFFFAOYSA-N Perforine Natural products COC1=C2CCC(O)C(CCC(C)(C)O)(OC)C2=NC2=C1C=CO2 KHGNFPUMBJSZSM-UHFFFAOYSA-N 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 102000002727 Protein Tyrosine Phosphatase Human genes 0.000 description 1
- 102000001183 RAG-1 Human genes 0.000 description 1
- 108060006897 RAG1 Proteins 0.000 description 1
- 108020005067 RNA Splice Sites Proteins 0.000 description 1
- 102000018120 Recombinases Human genes 0.000 description 1
- 108010091086 Recombinases Proteins 0.000 description 1
- 101150036449 SIRPA gene Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 102100025795 Signal-regulatory protein gamma Human genes 0.000 description 1
- 208000002903 Thalassemia Diseases 0.000 description 1
- 102100023935 Transmembrane glycoprotein NMB Human genes 0.000 description 1
- 206010060872 Transplant failure Diseases 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 108010084455 Zeocin Proteins 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- 230000000735 allogeneic effect Effects 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 229940121375 antifungal agent Drugs 0.000 description 1
- 239000003429 antifungal agent Substances 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-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
- 238000012742 biochemical analysis Methods 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 239000006172 buffering agent Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 238000009104 chemotherapy regimen Methods 0.000 description 1
- 230000003021 clonogenic effect Effects 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- -1 coatings Substances 0.000 description 1
- 238000007398 colorimetric assay Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000009402 cross-breeding Methods 0.000 description 1
- 230000016396 cytokine production Effects 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 210000004443 dendritic cell Anatomy 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 239000002612 dispersion medium Substances 0.000 description 1
- 230000004064 dysfunction Effects 0.000 description 1
- 230000005014 ectopic expression Effects 0.000 description 1
- 230000009982 effect on human Effects 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 238000002825 functional assay Methods 0.000 description 1
- 102000034356 gene-regulatory proteins Human genes 0.000 description 1
- 108091006104 gene-regulatory proteins Proteins 0.000 description 1
- 208000016361 genetic disease Diseases 0.000 description 1
- 102000054766 genetic haplotypes Human genes 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 208000024200 hematopoietic and lymphoid system neoplasm Diseases 0.000 description 1
- 238000011134 hematopoietic stem cell transplantation Methods 0.000 description 1
- 210000000777 hematopoietic system Anatomy 0.000 description 1
- 210000003630 histaminocyte Anatomy 0.000 description 1
- 229960000890 hydrocortisone Drugs 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 108091008915 immune receptors Proteins 0.000 description 1
- 102000027596 immune receptors Human genes 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000002458 infectious effect Effects 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
- 210000005007 innate immune system Anatomy 0.000 description 1
- 102000006495 integrins Human genes 0.000 description 1
- 108010044426 integrins Proteins 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 230000023404 leukocyte cell-cell adhesion Effects 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 239000011325 microbead Substances 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000003032 molecular docking Methods 0.000 description 1
- 230000009456 molecular mechanism Effects 0.000 description 1
- 239000003068 molecular probe Substances 0.000 description 1
- 230000001400 myeloablative effect Effects 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000001613 neoplastic effect Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
- 238000010899 nucleation Methods 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 238000001216 nucleic acid method Methods 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 238000001543 one-way ANOVA Methods 0.000 description 1
- 210000000963 osteoblast Anatomy 0.000 description 1
- 210000002997 osteoclast Anatomy 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 229930192851 perforin Natural products 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- CWCMIVBLVUHDHK-ZSNHEYEWSA-N phleomycin D1 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC[C@@H](N=1)C=1SC=C(N=1)C(=O)NCCCCNC(N)=N)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C CWCMIVBLVUHDHK-ZSNHEYEWSA-N 0.000 description 1
- 230000010118 platelet activation Effects 0.000 description 1
- 230000004983 pleiotropic effect Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- XJMOSONTPMZWPB-UHFFFAOYSA-M propidium iodide Chemical compound [I-].[I-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 XJMOSONTPMZWPB-UHFFFAOYSA-M 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 108020000494 protein-tyrosine phosphatase Proteins 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000004043 responsiveness Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 238000007790 scraping Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 208000002491 severe combined immunodeficiency Diseases 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- CMZUMMUJMWNLFH-UHFFFAOYSA-N sodium metavanadate Chemical compound [Na+].[O-][V](=O)=O CMZUMMUJMWNLFH-UHFFFAOYSA-N 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 238000007801 sublethal irradiation Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000005846 sugar alcohols Polymers 0.000 description 1
- 150000008163 sugars Chemical class 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
- 208000011580 syndromic disease Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000009897 systematic effect Effects 0.000 description 1
- 238000011287 therapeutic dose Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 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
- 201000002341 thymus lymphoma Diseases 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000003146 transient transfection Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 108091007466 transmembrane glycoproteins Proteins 0.000 description 1
- 108091005703 transmembrane proteins Proteins 0.000 description 1
- 102000035160 transmembrane proteins Human genes 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 108700001624 vesicular stomatitis virus G Proteins 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 229910000166 zirconium phosphate Inorganic materials 0.000 description 1
Classifications
-
- 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
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/3955—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against proteinaceous materials, e.g. enzymes, hormones, lymphokines
-
- 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
- C07K14/70596—Molecules with a "CD"-designation not provided for elsewhere
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- 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
- A61K47/68—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 an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6801—Drug-antibody or immunoglobulin conjugates defined by the pharmacologically or therapeutically active agent
- A61K47/6803—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates
- A61K47/6811—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates the drug being a protein or peptide, e.g. transferrin or bleomycin
-
- 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
- A61K47/68—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 an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6835—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 an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- 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
-
- 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
- A61P7/06—Antianaemics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/32—Fusion polypeptide fusions with soluble part of a cell surface receptor, "decoy receptors"
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Immunology (AREA)
- Organic Chemistry (AREA)
- Epidemiology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Molecular Biology (AREA)
- Marine Sciences & Fisheries (AREA)
- Cell Biology (AREA)
- Biochemistry (AREA)
- Diabetes (AREA)
- Genetics & Genomics (AREA)
- Hematology (AREA)
- Biophysics (AREA)
- Toxicology (AREA)
- Microbiology (AREA)
- Endocrinology (AREA)
- Mycology (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US96072407P | 2007-10-11 | 2007-10-11 | |
| PCT/CA2008/001814 WO2009046541A1 (en) | 2007-10-11 | 2008-10-10 | MODULATION OF SIRPα - CD47 INTERACTION FOR INCREASING HUMAN HEMATOPOIETIC STEM CELL ENGRAFTMENT AND COMPOUNDS THEREFOR |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2011500005A true JP2011500005A (ja) | 2011-01-06 |
| JP2011500005A5 JP2011500005A5 (enExample) | 2011-11-24 |
Family
ID=40548916
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2010528256A Pending JP2011500005A (ja) | 2007-10-11 | 2008-10-10 | ヒト造血幹細胞の生着を増加させるためのSIRPα−CD47相互作用の調節およびそのための化合物 |
Country Status (7)
| Country | Link |
|---|---|
| US (2) | US20100239578A1 (enExample) |
| EP (3) | EP2207797A4 (enExample) |
| JP (1) | JP2011500005A (enExample) |
| CN (2) | CN103242444A (enExample) |
| AU (1) | AU2008310263B2 (enExample) |
| CA (1) | CA2702217A1 (enExample) |
| WO (1) | WO2009046541A1 (enExample) |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2015504899A (ja) * | 2012-01-17 | 2015-02-16 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | 高親和性sirp−アルファ試薬 |
| JP2016501896A (ja) * | 2012-12-17 | 2016-01-21 | トリリアム・セラピューティクス・インコーポレイテッドTrillium Therapeutics Inc. | SIRPアルファ−Fc融合体でのCD47+疾患細胞の治療 |
| JP2016537015A (ja) * | 2013-09-23 | 2016-12-01 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドRegeneron Pharmaceuticals, Inc. | ヒト化シグナル調節タンパク質遺伝子を有する非ヒト動物 |
| US10259859B2 (en) | 2015-08-07 | 2019-04-16 | ALX Oncology Inc. | Constructs having a SIRP-α domain or variant thereof |
| US11613564B2 (en) | 2019-05-31 | 2023-03-28 | ALX Oncology Inc. | Methods of treating cancer |
| US12098214B2 (en) | 2021-05-13 | 2024-09-24 | ALX Oncology Inc. | Combination therapies for treating cancer |
Families Citing this family (85)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| HUE037173T2 (hu) | 2006-08-08 | 2018-08-28 | Univ Bonn Rheinische Friedrich Wilhelms | 5'-Foszfát-oligonukleotidok szerkezete és alkalmazása |
| EP3722317B1 (en) | 2008-01-15 | 2024-08-07 | The Board of Trustees of the Leland Stanford Junior University | Markers of acute myeloid leukemia stem cells |
| US11072655B2 (en) | 2008-01-15 | 2021-07-27 | The Board Of Trustees Of The Leland Stanford Junior University | Markers of acute myeloid leukemia stem cells |
| AU2016203572A1 (en) * | 2008-01-15 | 2016-06-16 | The Board Of Trustees Of The Leland Stanford Junior University | Methods for manipulating phagocytosis mediated by CD47 |
| ES2735144T3 (es) | 2008-01-15 | 2019-12-16 | Univ Leland Stanford Junior | Métodos para manipular fagocitosis mediada por CD47 |
| AU2014201010B2 (en) * | 2008-01-15 | 2016-03-03 | The Board Of Trustees Of The Leland Stanford Junior University | Methods for manipulating phagocytosis mediated by CD47 |
| US9738680B2 (en) | 2008-05-21 | 2017-08-22 | Rheinische Friedrich-Wilhelms-Universität Bonn | 5′ triphosphate oligonucleotide with blunt end and uses thereof |
| EA201100947A1 (ru) * | 2008-12-19 | 2012-02-28 | Новартис Аг | Растворимые полипептиды, предназначенные для применения при лечении аутоиммунных и воспалительных нарушений |
| CA2761438C (en) * | 2009-05-15 | 2017-12-12 | University Health Network | Compositions and methods for treating hematologic cancers targeting the sirp.alpha.-cd47 interaction |
| CA2785139A1 (en) | 2009-12-22 | 2011-06-30 | Novartis Ag | Tetravalent cd47-antibody constant region fusion protein for use in therapy |
| EP2508530A1 (en) | 2011-03-28 | 2012-10-10 | Rheinische Friedrich-Wilhelms-Universität Bonn | Purification of triphosphorylated oligonucleotides using capture tags |
| MX2013014789A (es) * | 2011-06-16 | 2014-01-20 | Novartis Ag | Proteinas solubles para utilizarse como productos terapeuticos. |
| KR102473555B1 (ko) * | 2012-09-07 | 2022-12-05 | 예일 유니버시티 | 유전적으로 변형된 비-인간 동물 및 이것들의 사용 방법 |
| EP2712870A1 (en) | 2012-09-27 | 2014-04-02 | Rheinische Friedrich-Wilhelms-Universität Bonn | Novel RIG-I ligands and methods for producing them |
| CN105121467B (zh) | 2012-12-03 | 2019-07-05 | 诺夫免疫股份有限公司 | 抗cd47抗体及其使用方法 |
| US9873747B2 (en) | 2013-01-31 | 2018-01-23 | Thomas Jefferson University | Fusion proteins that facilitate cancer cell destruction |
| ES2728066T3 (es) * | 2013-03-15 | 2019-10-22 | Univ Leland Stanford Junior | Métodos para la obtención de dosis terapéuticamente eficaces de agentes anti-CD47 |
| CN103665165B (zh) * | 2013-08-28 | 2016-02-24 | 江苏匡亚生物医药科技有限公司 | 一种靶向人CD47-SIRPα信号通路的双特异性抗体及其制备方法和用途 |
| EP3116544A4 (en) | 2014-03-11 | 2017-08-23 | The Board of Trustees of the Leland Stanford Junior University | Anti sirp-alpha antibodies and bi-specific macrophage enhancing antibodies |
| EP3643727A1 (en) | 2014-08-15 | 2020-04-29 | Merck Patent GmbH | Sirp-alpha immunoglobulin fusion proteins |
| US10358472B2 (en) | 2015-05-06 | 2019-07-23 | The Board Of Trustees Of The Leland Stanford Junior University | High affinity CD47 analogs |
| ES2796378T3 (es) * | 2016-01-11 | 2020-11-26 | Forty Seven Inc | Anticuerpos monoclonales anti-cd47 humanizados, de ratón o químicos |
| ES2990971T3 (es) | 2016-04-14 | 2024-12-02 | Ose Immunotherapeutics | Nuevos anticuerpos anti-SIRPa y sus aplicaciones terapéuticas |
| EP3443010B1 (en) * | 2016-04-14 | 2024-08-07 | Ose Immunotherapeutics | New anti-sirpa antibodies and their therapeutic applications |
| US11649284B2 (en) | 2016-04-18 | 2023-05-16 | Baylor College Of Medicine | Cancer gene therapy targeting CD47 |
| JP7461741B2 (ja) | 2016-06-20 | 2024-04-04 | カイマブ・リミテッド | 抗pd-l1およびil-2サイトカイン |
| US10148939B2 (en) | 2016-07-19 | 2018-12-04 | Gopro, Inc. | Mapping of spherical image data into rectangular faces for transport and decoding across networks |
| JOP20190009A1 (ar) | 2016-09-21 | 2019-01-27 | Alx Oncology Inc | أجسام مضادة ضد بروتين ألفا منظم للإشارات وطرق استخدامها |
| CA3042581A1 (en) | 2016-11-03 | 2018-05-11 | Trillium Therapeutics Inc. | Enhancement of cd47 blockade therapy by proteasome inhibitors |
| US11779642B2 (en) | 2016-12-09 | 2023-10-10 | Alector Llc | Anti-SIRP-alpha antibodies and methods of use thereof |
| JP7321934B2 (ja) | 2017-01-30 | 2023-08-07 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | 幹細胞移植のための非遺伝毒性移植前処置レジメン |
| AU2018308364C1 (en) | 2017-07-26 | 2023-02-16 | Forty Seven, LLC | Anti-SIRP-alpha antibodies and related methods |
| EP3661965A4 (en) | 2017-08-02 | 2022-07-13 | Phanes Therapeutics, Inc. | ANTI-CD47 ANTIBODIES AND USES THEREOF |
| US11708418B2 (en) * | 2017-08-10 | 2023-07-25 | Grifols Diagnostic Solutions Inc. | Compositions, methods and/or kits comprising a recombinant human CD38- extracellular domain |
| US11713356B2 (en) | 2017-10-13 | 2023-08-01 | Ose Immunotherapeutics | Modified bifunctional anti-human signal regulatory protein alpha (SIRPa) antibody and method of use thereof for treating cancer |
| US11180552B2 (en) | 2017-12-01 | 2021-11-23 | Seagen Inc. | CD47 antibodies and uses thereof for treating cancer |
| WO2019129054A1 (zh) | 2017-12-27 | 2019-07-04 | 信达生物制药(苏州)有限公司 | 三链抗体、其制备方法及其用途 |
| CN108484774B (zh) * | 2018-03-09 | 2021-11-05 | 上海高菲生物科技有限公司 | 一种SIRPα融合蛋白及其制备方法和用途 |
| WO2019175218A1 (en) | 2018-03-13 | 2019-09-19 | Ose Immunotherapeutics | Use of anti-human sirpa v1 antibodies and method for producing anti-sirpa v1 antibodies |
| US11292850B2 (en) | 2018-03-21 | 2022-04-05 | ALX Oncology Inc. | Antibodies against signal-regulatory protein α and methods of use |
| JP7337099B2 (ja) | 2018-05-25 | 2023-09-01 | アレクトル エルエルシー | 抗sirpa抗体およびその使用法 |
| WO2020033646A1 (en) * | 2018-08-08 | 2020-02-13 | Orionis Biosciences, Inc. | SIRP1α TARGETED CHIMERIC PROTEINS AND USES THEREOF |
| WO2020068431A1 (en) * | 2018-09-28 | 2020-04-02 | The Board Of Trustees Of The Leland Stanford Junior University | Analysis of polymorphisms in sirp-alpha for evaluating response to immunotherapy |
| JP7295283B2 (ja) | 2019-06-25 | 2023-06-20 | ギリアード サイエンシーズ, インコーポレイテッド | Flt3l-fc融合タンパク質及び使用方法 |
| CA3144244A1 (en) | 2019-06-25 | 2020-12-30 | Innovent Biologics (Suzhou) Co., Ltd. | Formulation comprising anti-cd47/pd-l1 bispecific antibody, method for preparing same and use thereof |
| JP7454645B2 (ja) | 2019-07-16 | 2024-03-22 | ギリアード サイエンシーズ, インコーポレイテッド | Hivワクチン並びにその作製方法及び使用方法 |
| EP4045083B1 (en) | 2019-10-18 | 2024-01-10 | Forty Seven, Inc. | Combination therapies for treating myelodysplastic syndromes and acute myeloid leukemia |
| NZ786589A (en) | 2019-10-31 | 2025-03-28 | Forty Seven Llc | Anti-cd47 and anti-cd20 based treatment of blood cancer |
| CN117736207A (zh) | 2019-12-24 | 2024-03-22 | 卡尔那生物科学株式会社 | 二酰基甘油激酶调节化合物 |
| TWI832035B (zh) | 2020-02-14 | 2024-02-11 | 美商基利科學股份有限公司 | 結合ccr8之抗體及融合蛋白及其用途 |
| CA3172449A1 (en) | 2020-03-27 | 2021-09-30 | Erik Hans MANTING | Ex vivo use of modified cells of leukemic origin for enhancing the efficacy of adoptive cell therapy |
| CN116133679A (zh) | 2020-06-30 | 2023-05-16 | 门德斯有限公司 | 白血病衍生细胞在卵巢癌疫苗中的用途 |
| WO2022190058A1 (en) | 2021-03-12 | 2022-09-15 | Dcprime B.V. | Methods of vaccination and use of cd47 blockade |
| TW202302145A (zh) | 2021-04-14 | 2023-01-16 | 美商基利科學股份有限公司 | CD47/SIRPα結合及NEDD8活化酶E1調節次單元之共抑制以用於治療癌症 |
| WO2022245671A1 (en) | 2021-05-18 | 2022-11-24 | Gilead Sciences, Inc. | Methods of using flt3l-fc fusion proteins |
| CN117480155A (zh) | 2021-06-23 | 2024-01-30 | 吉利德科学公司 | 二酰基甘油激酶调节化合物 |
| JP7686091B2 (ja) | 2021-06-23 | 2025-05-30 | ギリアード サイエンシーズ, インコーポレイテッド | ジアシルグリセロールキナーゼ調節化合物 |
| CN117377671A (zh) | 2021-06-23 | 2024-01-09 | 吉利德科学公司 | 二酰基甘油激酶调节化合物 |
| EP4359415A1 (en) | 2021-06-23 | 2024-05-01 | Gilead Sciences, Inc. | Diacylglyercol kinase modulating compounds |
| TW202317190A (zh) | 2021-06-29 | 2023-05-01 | 美商思進公司 | 以非岩藻糖基化抗cd70抗體及cd47拮抗劑之組合治療癌症之方法 |
| EP4389767A1 (en) | 2021-08-17 | 2024-06-26 | Hangzhou Jiuyuan Gene Engineering Co., Ltd | Monoclonal antibody targeting sirp? and use thereof |
| WO2023076983A1 (en) | 2021-10-28 | 2023-05-04 | Gilead Sciences, Inc. | Pyridizin-3(2h)-one derivatives |
| JP7787991B2 (ja) | 2021-10-29 | 2025-12-17 | ギリアード サイエンシーズ, インコーポレイテッド | Cd73化合物 |
| WO2023122615A1 (en) | 2021-12-22 | 2023-06-29 | Gilead Sciences, Inc. | Ikaros zinc finger family degraders and uses thereof |
| AU2022419982A1 (en) | 2021-12-22 | 2024-06-06 | Gilead Sciences, Inc. | Ikaros zinc finger family degraders and uses thereof |
| TW202340168A (zh) | 2022-01-28 | 2023-10-16 | 美商基利科學股份有限公司 | Parp7抑制劑 |
| TW202346277A (zh) | 2022-03-17 | 2023-12-01 | 美商基利科學股份有限公司 | Ikaros鋅指家族降解劑及其用途 |
| AU2023240346A1 (en) | 2022-03-24 | 2024-09-19 | Gilead Sciences, Inc. | Combination therapy for treating trop-2 expressing cancers |
| TWI876305B (zh) | 2022-04-05 | 2025-03-11 | 美商基利科學股份有限公司 | 用於治療結腸直腸癌之組合療法 |
| PE20250157A1 (es) | 2022-04-21 | 2025-01-22 | Gilead Sciences Inc | Compuestos de modulacion de kras g12d |
| CN119384415A (zh) | 2022-07-01 | 2025-01-28 | 吉利德科学公司 | Cd73化合物 |
| EP4554628A1 (en) | 2022-07-12 | 2025-05-21 | Gilead Sciences, Inc. | Hiv immunogenic polypeptides and vaccines and uses thereof |
| WO2024064668A1 (en) | 2022-09-21 | 2024-03-28 | Gilead Sciences, Inc. | FOCAL IONIZING RADIATION AND CD47/SIRPα DISRUPTION ANTICANCER COMBINATION THERAPY |
| WO2024008979A1 (en) * | 2022-09-30 | 2024-01-11 | Novo Nordisk A/S | A sirp-alpha binding chimeric protein |
| US20240254118A1 (en) | 2022-12-22 | 2024-08-01 | Gilead Sciences, Inc. | Prmt5 inhibitors and uses thereof |
| KR20250167002A (ko) | 2023-04-11 | 2025-11-28 | 길리애드 사이언시즈, 인코포레이티드 | Kras 조절 화합물 |
| CN121079300A (zh) | 2023-04-21 | 2025-12-05 | 吉利德科学公司 | Prmt5抑制剂及其用途 |
| US20250042922A1 (en) | 2023-06-30 | 2025-02-06 | Gilead Sciences, Inc. | Kras modulating compounds |
| US20250066328A1 (en) | 2023-07-26 | 2025-02-27 | Gilead Sciences, Inc. | Parp7 inhibitors |
| WO2025024811A1 (en) | 2023-07-26 | 2025-01-30 | Gilead Sciences, Inc. | Parp7 inhibitors |
| US20250101042A1 (en) | 2023-09-08 | 2025-03-27 | Gilead Sciences, Inc. | Kras g12d modulating compounds |
| WO2025054530A1 (en) | 2023-09-08 | 2025-03-13 | Gilead Sciences, Inc. | Pyrimidine-containing polycyclic derivatives as kras g12d modulating compounds |
| WO2025096589A1 (en) | 2023-11-03 | 2025-05-08 | Gilead Sciences, Inc. | Prmt5 inhibitors and uses thereof |
| WO2025137640A1 (en) | 2023-12-22 | 2025-06-26 | Gilead Sciences, Inc. | Azaspiro wrn inhibitors |
| WO2025245003A1 (en) | 2024-05-21 | 2025-11-27 | Gilead Sciences, Inc. | Prmt5 inhibitors and uses thereof |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20070113297A1 (en) * | 2005-09-13 | 2007-05-17 | Yongguang Yang | Methods and compositions for inhibition of immune responses |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5116964A (en) | 1989-02-23 | 1992-05-26 | Genentech, Inc. | Hybrid immunoglobulins |
| US5580756A (en) | 1990-03-26 | 1996-12-03 | Bristol-Myers Squibb Co. | B7Ig fusion protein |
| US5844095A (en) | 1991-06-27 | 1998-12-01 | Bristol-Myers Squibb Company | CTLA4 Ig fusion proteins |
| CA2259122A1 (en) | 1996-06-17 | 1997-12-24 | Max Planck Gesellschaft Zur Forderung Der Wissenschaften E.V. | Novel ptp-20, pcp-2, bdp1, clk and sirp proteins and related products and methods |
| US6541615B1 (en) * | 1996-11-15 | 2003-04-01 | Max-Planck-Gellschaft Zur Foderung Der Wissenschaften E.V. | SIRP proteins and uses thereof |
| CA2226962A1 (en) * | 1998-02-16 | 1999-08-16 | Marie Sarfati | Use of binding agents to cd47 and its ligands in the treatment or the prophylaxis of various inflammatory, autoimmune and allergic diseases and in the treatment of graft rejection |
| GB9825555D0 (en) | 1998-11-20 | 1999-01-13 | Imp College Innovations Ltd | Suppression of xenotransplant rejection |
| WO2001040307A1 (de) | 1999-11-30 | 2001-06-07 | Eberhard-Karls-Universität Tübingen Universitätsklinikum | Antikörper gegen signal-regulator-proteine |
| GB9930706D0 (en) | 1999-12-24 | 2000-02-16 | Medical Res Council | Composition for inhibiting macrophage activity |
| WO2003036264A2 (en) * | 2001-10-26 | 2003-05-01 | Immunex Corporation | Treating diseases mediated by metalloprotease-shed proteins |
| WO2004011618A2 (en) * | 2002-07-29 | 2004-02-05 | Hmgene, Inc. | Methods of identifying adipocyte specific genes, the genes identified, and their uses |
| JP3936673B2 (ja) | 2003-06-02 | 2007-06-27 | 国立大学法人群馬大学 | Cd47部分ペプチドと抗shps−1モノクロナール抗体 |
| WO2007133811A2 (en) * | 2006-05-15 | 2007-11-22 | Viral Logic Systems Technology Corp. | Cd47 related compositions and methods for treating immunological diseases and disorders |
-
2008
- 2008-10-10 JP JP2010528256A patent/JP2011500005A/ja active Pending
- 2008-10-10 US US12/682,307 patent/US20100239578A1/en not_active Abandoned
- 2008-10-10 AU AU2008310263A patent/AU2008310263B2/en not_active Expired - Fee Related
- 2008-10-10 WO PCT/CA2008/001814 patent/WO2009046541A1/en not_active Ceased
- 2008-10-10 CA CA2702217A patent/CA2702217A1/en not_active Abandoned
- 2008-10-10 EP EP08838285A patent/EP2207797A4/en not_active Withdrawn
- 2008-10-10 EP EP11169933A patent/EP2388270A3/en not_active Withdrawn
- 2008-10-10 CN CN2013101029534A patent/CN103242444A/zh active Pending
- 2008-10-10 EP EP12189613A patent/EP2573112A1/en not_active Withdrawn
- 2008-10-10 CN CN2008801197876A patent/CN101970478A/zh active Pending
-
2012
- 2012-10-30 US US13/663,801 patent/US20130189253A1/en not_active Abandoned
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20070113297A1 (en) * | 2005-09-13 | 2007-05-17 | Yongguang Yang | Methods and compositions for inhibition of immune responses |
Non-Patent Citations (1)
| Title |
|---|
| JPN6014021176; J.Exp.Med.,2001 Aug 20,194(4),p.541-9 * |
Cited By (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2020007329A (ja) * | 2012-01-17 | 2020-01-16 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | 高親和性sirp−アルファ試薬 |
| US12195532B2 (en) | 2012-01-17 | 2025-01-14 | The Board Of Trustees Of The Leland Stanford Junior University | High affinity SIRP-alpha reagents and methods of using |
| JP2015504899A (ja) * | 2012-01-17 | 2015-02-16 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | 高親和性sirp−アルファ試薬 |
| JP2018021016A (ja) * | 2012-01-17 | 2018-02-08 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | 高親和性sirp−アルファ試薬 |
| US9944911B2 (en) | 2012-01-17 | 2018-04-17 | The Board Of Trustees Of The Leland Stanford Junior University | High affinity Sirp-alpha reagents and methods of using |
| US11208481B2 (en) | 2012-01-17 | 2021-12-28 | The Board Of Trustees Of The Leland Stanford Junior University | High affinity SIRP-alpha reagents and methods of using |
| JP2021176873A (ja) * | 2012-01-17 | 2021-11-11 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | 高親和性sirp−アルファ試薬 |
| JP2020143104A (ja) * | 2012-01-17 | 2020-09-10 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | 高親和性sirp−アルファ試薬 |
| JP7149450B2 (ja) | 2012-12-17 | 2022-10-07 | ピーエフ アージェンタム アイピー ホールディングズ エルエルシー | SIRPアルファ-Fc融合体でのCD47+疾患細胞の治療 |
| JP2018148897A (ja) * | 2012-12-17 | 2018-09-27 | トリリアム・セラピューティクス・インコーポレイテッドTrillium Therapeutics Inc. | SIRPアルファ−Fc融合体でのCD47+疾患細胞の治療 |
| JP2016501896A (ja) * | 2012-12-17 | 2016-01-21 | トリリアム・セラピューティクス・インコーポレイテッドTrillium Therapeutics Inc. | SIRPアルファ−Fc融合体でのCD47+疾患細胞の治療 |
| JP2020089387A (ja) * | 2012-12-17 | 2020-06-11 | トリリアム・セラピューティクス・インコーポレイテッドTrillium Therapeutics Inc. | SIRPアルファ−Fc融合体でのCD47+疾患細胞の治療 |
| JP2016537015A (ja) * | 2013-09-23 | 2016-12-01 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドRegeneron Pharmaceuticals, Inc. | ヒト化シグナル調節タンパク質遺伝子を有する非ヒト動物 |
| JP2021104064A (ja) * | 2013-09-23 | 2021-07-26 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドRegeneron Pharmaceuticals, Inc. | ヒト化シグナル調節タンパク質遺伝子を有する非ヒト動物 |
| JP2019047818A (ja) * | 2013-09-23 | 2019-03-28 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドRegeneron Pharmaceuticals, Inc. | ヒト化シグナル調節タンパク質遺伝子を有する非ヒト動物 |
| JP7149370B2 (ja) | 2013-09-23 | 2022-10-06 | リジェネロン・ファーマシューティカルズ・インコーポレイテッド | ヒト化シグナル調節タンパク質遺伝子を有する非ヒト動物 |
| JP2020114209A (ja) * | 2013-09-23 | 2020-07-30 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドRegeneron Pharmaceuticals, Inc. | ヒト化シグナル調節タンパク質遺伝子を有する非ヒト動物 |
| US12161097B2 (en) | 2013-09-23 | 2024-12-10 | Regeneron Pharmaceuticals, Inc. | Non-human animals having a humanized signal-regulatory protein gene |
| US10259859B2 (en) | 2015-08-07 | 2019-04-16 | ALX Oncology Inc. | Constructs having a SIRP-α domain or variant thereof |
| US11208459B2 (en) | 2015-08-07 | 2021-12-28 | ALX Oncology Inc. | Constructs having a SIRP-alpha domain or variant thereof |
| US11639376B2 (en) | 2015-08-07 | 2023-05-02 | ALX Oncology Inc. | Constructs having a SIRP-α domain or variant thereof |
| US10696730B2 (en) | 2015-08-07 | 2020-06-30 | ALX Oncology Inc. | Constructs having a SIRP-alpha domain or variant thereof |
| US11613564B2 (en) | 2019-05-31 | 2023-03-28 | ALX Oncology Inc. | Methods of treating cancer |
| US12098214B2 (en) | 2021-05-13 | 2024-09-24 | ALX Oncology Inc. | Combination therapies for treating cancer |
Also Published As
| Publication number | Publication date |
|---|---|
| EP2388270A3 (en) | 2012-04-25 |
| EP2207797A4 (en) | 2010-12-22 |
| EP2388270A2 (en) | 2011-11-23 |
| CN103242444A (zh) | 2013-08-14 |
| AU2008310263B2 (en) | 2014-09-11 |
| WO2009046541A1 (en) | 2009-04-16 |
| EP2573112A1 (en) | 2013-03-27 |
| US20130189253A1 (en) | 2013-07-25 |
| US20100239578A1 (en) | 2010-09-23 |
| CA2702217A1 (en) | 2009-04-16 |
| AU2008310263A1 (en) | 2009-04-16 |
| CN101970478A (zh) | 2011-02-09 |
| EP2207797A1 (en) | 2010-07-21 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2011500005A (ja) | ヒト造血幹細胞の生着を増加させるためのSIRPα−CD47相互作用の調節およびそのための化合物 | |
| US20240084399A1 (en) | Compositions and methods for treating hematological cancers targeting the sirpalpha - cd47 interaction | |
| Takenaka et al. | Polymorphism in Sirpa modulates engraftment of human hematopoietic stem cells | |
| JP5603145B2 (ja) | 疾患のイメージング、診断、及び治療 | |
| JP2011500005A5 (enExample) | ||
| KR20210089712A (ko) | 항-cd33 면역세포 암 치료법 | |
| JP2022510634A (ja) | 除去レジメンに抵抗性の遺伝的に改変されたhspc | |
| KR20220003586A (ko) | Cd19를 표적화하는 유전공학적으로 조작된 t 세포를 사용한 b 세포 악성종양의 동종이계 세포 요법 | |
| AU2022256193A1 (en) | Compositions and methods for treating hematologic cancers targeting the SIRPa-CD47 interaction | |
| HK40068210A (en) | Allogeneic cell therapy of b cell malignancies using genetically engineered t cells targeting cd19 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20100910 |
|
| A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A711 Effective date: 20101116 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20101116 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20111006 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20111006 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20130709 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20131008 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20140527 |