CZ300710B6 - Použití blokující monoklonální protilátky proti VLA-1 pro výrobu farmaceutického prípravku k lécení zánetlivých onemocnení - Google Patents
Použití blokující monoklonální protilátky proti VLA-1 pro výrobu farmaceutického prípravku k lécení zánetlivých onemocnení Download PDFInfo
- Publication number
- CZ300710B6 CZ300710B6 CZ20014249A CZ20014249A CZ300710B6 CZ 300710 B6 CZ300710 B6 CZ 300710B6 CZ 20014249 A CZ20014249 A CZ 20014249A CZ 20014249 A CZ20014249 A CZ 20014249A CZ 300710 B6 CZ300710 B6 CZ 300710B6
- Authority
- CZ
- Czechia
- Prior art keywords
- antibody
- integrin
- monoclonal antibodies
- mice
- human
- Prior art date
Links
- 230000000903 blocking effect Effects 0.000 title claims abstract description 34
- 108010041341 Integrin alpha1 Proteins 0.000 title claims abstract description 32
- 108010055795 Integrin alpha1beta1 Proteins 0.000 title claims abstract description 14
- 239000008194 pharmaceutical composition Substances 0.000 title claims abstract description 12
- 102100025323 Integrin alpha-1 Human genes 0.000 title claims abstract description 10
- 208000027866 inflammatory disease Diseases 0.000 title abstract description 7
- 206010003246 arthritis Diseases 0.000 claims abstract description 64
- 238000011282 treatment Methods 0.000 claims abstract description 31
- 239000012634 fragment Substances 0.000 claims abstract description 24
- 125000000539 amino acid group Chemical group 0.000 claims description 21
- 239000000203 mixture Substances 0.000 claims description 10
- 238000004519 manufacturing process Methods 0.000 claims description 6
- 238000007920 subcutaneous administration Methods 0.000 claims description 4
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 2
- 238000009472 formulation Methods 0.000 claims 1
- 241000282414 Homo sapiens Species 0.000 abstract description 99
- 102000006495 integrins Human genes 0.000 abstract description 96
- 108010044426 integrins Proteins 0.000 abstract description 96
- 241001465754 Metazoa Species 0.000 abstract description 19
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 6
- 230000002757 inflammatory effect Effects 0.000 abstract description 6
- 210000003423 ankle Anatomy 0.000 abstract description 4
- 201000010099 disease Diseases 0.000 abstract description 4
- 241000282412 Homo Species 0.000 abstract description 3
- 150000001408 amides Chemical class 0.000 abstract description 2
- 239000002253 acid Substances 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 95
- 241000699670 Mus sp. Species 0.000 description 93
- 238000000034 method Methods 0.000 description 46
- 239000000427 antigen Substances 0.000 description 36
- 108091007433 antigens Proteins 0.000 description 35
- 102000036639 antigens Human genes 0.000 description 35
- 238000002474 experimental method Methods 0.000 description 29
- 241000699666 Mus <mouse, genus> Species 0.000 description 27
- 241000700159 Rattus Species 0.000 description 25
- 230000027455 binding Effects 0.000 description 25
- 230000005764 inhibitory process Effects 0.000 description 24
- 102000008186 Collagen Human genes 0.000 description 22
- 108010035532 Collagen Proteins 0.000 description 22
- 229920001436 collagen Polymers 0.000 description 22
- 230000002917 arthritic effect Effects 0.000 description 21
- 230000000694 effects Effects 0.000 description 21
- 230000004054 inflammatory process Effects 0.000 description 20
- 230000004044 response Effects 0.000 description 20
- 108060003951 Immunoglobulin Proteins 0.000 description 19
- 102100024952 Protein CBFA2T1 Human genes 0.000 description 19
- 210000002683 foot Anatomy 0.000 description 19
- 102000018358 immunoglobulin Human genes 0.000 description 19
- 239000002953 phosphate buffered saline Substances 0.000 description 18
- 241000699800 Cricetinae Species 0.000 description 17
- 241001494479 Pecora Species 0.000 description 17
- 239000012636 effector Substances 0.000 description 17
- 208000010247 contact dermatitis Diseases 0.000 description 16
- 239000002158 endotoxin Substances 0.000 description 16
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 15
- 210000004408 hybridoma Anatomy 0.000 description 15
- 108010048623 Collagen Receptors Proteins 0.000 description 14
- 102000000507 Integrin alpha2 Human genes 0.000 description 14
- 230000002950 deficient Effects 0.000 description 14
- 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 14
- 108020001507 fusion proteins Proteins 0.000 description 14
- 102000037865 fusion proteins Human genes 0.000 description 14
- 210000000265 leukocyte Anatomy 0.000 description 14
- 108090000623 proteins and genes Proteins 0.000 description 14
- 210000001519 tissue Anatomy 0.000 description 14
- 102000004266 Collagen Type IV Human genes 0.000 description 13
- 108010042086 Collagen Type IV Proteins 0.000 description 13
- 241001529936 Murinae Species 0.000 description 13
- 229940098773 bovine serum albumin Drugs 0.000 description 13
- 239000006228 supernatant Substances 0.000 description 13
- 230000008961 swelling Effects 0.000 description 13
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 12
- 210000003414 extremity Anatomy 0.000 description 12
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 11
- 206010061218 Inflammation Diseases 0.000 description 11
- 150000001413 amino acids Chemical group 0.000 description 11
- 230000001965 increasing effect Effects 0.000 description 11
- 238000002360 preparation method Methods 0.000 description 11
- 230000003367 anti-collagen effect Effects 0.000 description 10
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
- 210000001744 T-lymphocyte Anatomy 0.000 description 9
- 239000000872 buffer Substances 0.000 description 9
- 230000001419 dependent effect Effects 0.000 description 9
- 230000018109 developmental process Effects 0.000 description 9
- 210000000624 ear auricle Anatomy 0.000 description 9
- 210000004698 lymphocyte Anatomy 0.000 description 9
- 102000012422 Collagen Type I Human genes 0.000 description 8
- 108010022452 Collagen Type I Proteins 0.000 description 8
- 108020004414 DNA Proteins 0.000 description 8
- 102000005720 Glutathione transferase Human genes 0.000 description 8
- 108010070675 Glutathione transferase Proteins 0.000 description 8
- 229940024606 amino acid Drugs 0.000 description 8
- 238000010367 cloning Methods 0.000 description 8
- 229940117173 croton oil Drugs 0.000 description 8
- 238000011161 development Methods 0.000 description 8
- 210000003743 erythrocyte Anatomy 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 230000037396 body weight Effects 0.000 description 7
- 239000003795 chemical substances by application Substances 0.000 description 7
- 229940072221 immunoglobulins Drugs 0.000 description 7
- 230000009467 reduction Effects 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 210000004988 splenocyte Anatomy 0.000 description 7
- 102100039793 E3 ubiquitin-protein ligase RAG1 Human genes 0.000 description 6
- 101000744443 Homo sapiens E3 ubiquitin-protein ligase RAG1 Proteins 0.000 description 6
- 206010035226 Plasma cell myeloma Diseases 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 201000000050 myeloid neoplasm Diseases 0.000 description 6
- 210000000440 neutrophil Anatomy 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 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 5
- 102000000588 Interleukin-2 Human genes 0.000 description 5
- 108010002350 Interleukin-2 Proteins 0.000 description 5
- 210000003719 b-lymphocyte Anatomy 0.000 description 5
- 238000002649 immunization Methods 0.000 description 5
- 230000003053 immunization Effects 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 230000003993 interaction Effects 0.000 description 5
- 238000007912 intraperitoneal administration Methods 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 108090000765 processed proteins & peptides Proteins 0.000 description 5
- 102000004169 proteins and genes Human genes 0.000 description 5
- 230000002829 reductive effect Effects 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- 201000004624 Dermatitis Diseases 0.000 description 4
- 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 4
- 206010014025 Ear swelling Diseases 0.000 description 4
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Chemical compound C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 241000700157 Rattus norvegicus Species 0.000 description 4
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 4
- 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 4
- 230000009471 action Effects 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000005784 autoimmunity Effects 0.000 description 4
- 239000012148 binding buffer Substances 0.000 description 4
- 210000000601 blood cell Anatomy 0.000 description 4
- -1 carboxyethyl Chemical group 0.000 description 4
- 210000005069 ears Anatomy 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 230000004927 fusion Effects 0.000 description 4
- 238000010353 genetic engineering Methods 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 229910052739 hydrogen Inorganic materials 0.000 description 4
- 238000003119 immunoblot Methods 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 230000028709 inflammatory response Effects 0.000 description 4
- 210000001616 monocyte Anatomy 0.000 description 4
- 238000002703 mutagenesis Methods 0.000 description 4
- 231100000350 mutagenesis Toxicity 0.000 description 4
- 230000035515 penetration Effects 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 238000012163 sequencing technique Methods 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 238000002560 therapeutic procedure Methods 0.000 description 4
- 238000012546 transfer Methods 0.000 description 4
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 4
- 238000011714 129 mouse Methods 0.000 description 3
- 101710122228 Epstein-Barr nuclear antigen 2 Proteins 0.000 description 3
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 3
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 3
- 108010017642 Integrin alpha2beta1 Proteins 0.000 description 3
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 3
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 3
- 208000012659 Joint disease Diseases 0.000 description 3
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- 239000002671 adjuvant Substances 0.000 description 3
- 238000010171 animal model Methods 0.000 description 3
- 125000004429 atom Chemical group 0.000 description 3
- 239000011230 binding agent Substances 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 150000001768 cations Chemical class 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 230000006378 damage Effects 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 3
- 210000003714 granulocyte Anatomy 0.000 description 3
- 230000009610 hypersensitivity Effects 0.000 description 3
- 229940127121 immunoconjugate Drugs 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 230000008595 infiltration Effects 0.000 description 3
- 238000001764 infiltration Methods 0.000 description 3
- 210000004969 inflammatory cell Anatomy 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 238000011081 inoculation Methods 0.000 description 3
- 238000007918 intramuscular administration Methods 0.000 description 3
- 150000002500 ions Chemical class 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 229910021645 metal ion Inorganic materials 0.000 description 3
- 230000000149 penetrating effect Effects 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 230000003449 preventive effect Effects 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 210000004989 spleen cell Anatomy 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 210000003371 toe Anatomy 0.000 description 3
- 230000009261 transgenic effect Effects 0.000 description 3
- 210000000707 wrist Anatomy 0.000 description 3
- SJHPCNCNNSSLPL-CSKARUKUSA-N (4e)-4-(ethoxymethylidene)-2-phenyl-1,3-oxazol-5-one Chemical compound O1C(=O)C(=C/OCC)\N=C1C1=CC=CC=C1 SJHPCNCNNSSLPL-CSKARUKUSA-N 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 2
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 2
- FJVAQLJNTSUQPY-CIUDSAMLSA-N Ala-Ala-Lys Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CCCCN FJVAQLJNTSUQPY-CIUDSAMLSA-N 0.000 description 2
- MNZHHDPWDWQJCQ-YUMQZZPRSA-N Ala-Leu-Gly Chemical compound C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)NCC(O)=O MNZHHDPWDWQJCQ-YUMQZZPRSA-N 0.000 description 2
- VCSABYLVNWQYQE-UHFFFAOYSA-N Ala-Lys-Lys Natural products NCCCCC(NC(=O)C(N)C)C(=O)NC(CCCCN)C(O)=O VCSABYLVNWQYQE-UHFFFAOYSA-N 0.000 description 2
- OFIYLHVAAJYRBC-HJWJTTGWSA-N Arg-Ile-Phe Chemical compound CC[C@H](C)[C@H](NC(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](Cc1ccccc1)C(O)=O OFIYLHVAAJYRBC-HJWJTTGWSA-N 0.000 description 2
- AOHKLEBWKMKITA-IHRRRGAJSA-N Arg-Phe-Ser Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CO)C(=O)O)NC(=O)[C@H](CCCN=C(N)N)N AOHKLEBWKMKITA-IHRRRGAJSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 206010003800 Auricular swelling Diseases 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 101100289995 Caenorhabditis elegans mac-1 gene Proteins 0.000 description 2
- 102000000503 Collagen Type II Human genes 0.000 description 2
- 108010041390 Collagen Type II Proteins 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- HVYWQYLBVXMXSV-GUBZILKMSA-N Glu-Leu-Ala Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(O)=O HVYWQYLBVXMXSV-GUBZILKMSA-N 0.000 description 2
- UERORLSAFUHDGU-AVGNSLFASA-N Glu-Phe-Asn Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)O)NC(=O)[C@H](CCC(=O)O)N UERORLSAFUHDGU-AVGNSLFASA-N 0.000 description 2
- 101710102075 Glutathione S-transferase 1 Proteins 0.000 description 2
- JLXVRFDTDUGQEE-YFKPBYRVSA-N Gly-Arg Chemical compound NCC(=O)N[C@H](C(O)=O)CCCN=C(N)N JLXVRFDTDUGQEE-YFKPBYRVSA-N 0.000 description 2
- XPJBQTCXPJNIFE-ZETCQYMHSA-N Gly-Gly-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)CNC(=O)CN XPJBQTCXPJNIFE-ZETCQYMHSA-N 0.000 description 2
- SGLXGEDPYJPGIQ-ACRUOGEOSA-N His-Phe-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CC2=CC=CC=C2)C(=O)O)NC(=O)[C@H](CC3=CN=CN3)N SGLXGEDPYJPGIQ-ACRUOGEOSA-N 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 2
- 206010020751 Hypersensitivity Diseases 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- 108010041014 Integrin alpha5 Proteins 0.000 description 2
- 108010064593 Intercellular Adhesion Molecule-1 Proteins 0.000 description 2
- 102100037877 Intercellular adhesion molecule 1 Human genes 0.000 description 2
- ULXYQAJWJGLCNR-YUMQZZPRSA-N Leu-Asp-Gly Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(O)=O ULXYQAJWJGLCNR-YUMQZZPRSA-N 0.000 description 2
- KTFHTMHHKXUYPW-ZPFDUUQYSA-N Leu-Asp-Ile Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O KTFHTMHHKXUYPW-ZPFDUUQYSA-N 0.000 description 2
- LXKNSJLSGPNHSK-KKUMJFAQSA-N Leu-Leu-Lys Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)O)N LXKNSJLSGPNHSK-KKUMJFAQSA-N 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 239000004698 Polyethylene Substances 0.000 description 2
- 108010067787 Proteoglycans Proteins 0.000 description 2
- 201000004681 Psoriasis Diseases 0.000 description 2
- SFTZTYBXIXLRGQ-JBDRJPRFSA-N Ser-Ile-Ala Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(O)=O SFTZTYBXIXLRGQ-JBDRJPRFSA-N 0.000 description 2
- 241000700584 Simplexvirus Species 0.000 description 2
- HJOSVGCWOTYJFG-WDCWCFNPSA-N Thr-Glu-Lys Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N)O HJOSVGCWOTYJFG-WDCWCFNPSA-N 0.000 description 2
- KPNSNVTUVKSBFL-ZJDVBMNYSA-N Thr-Met-Thr Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H]([C@@H](C)O)C(=O)O)N)O KPNSNVTUVKSBFL-ZJDVBMNYSA-N 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 108090000190 Thrombin Proteins 0.000 description 2
- 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 2
- 229920004890 Triton X-100 Polymers 0.000 description 2
- CKKFTIQYURNSEI-IHRRRGAJSA-N Tyr-Asn-Arg Chemical compound NC(N)=NCCC[C@@H](C(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 CKKFTIQYURNSEI-IHRRRGAJSA-N 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 230000006978 adaptation Effects 0.000 description 2
- 239000000853 adhesive Substances 0.000 description 2
- 230000001070 adhesive effect Effects 0.000 description 2
- 208000026935 allergic disease Diseases 0.000 description 2
- 239000005557 antagonist Substances 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 210000000845 cartilage Anatomy 0.000 description 2
- 229940096422 collagen type i Drugs 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 230000003111 delayed effect Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- DOIRQSBPFJWKBE-UHFFFAOYSA-N dibutyl phthalate Chemical compound CCCCOC(=O)C1=CC=CC=C1C(=O)OCCCC DOIRQSBPFJWKBE-UHFFFAOYSA-N 0.000 description 2
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 2
- 210000003989 endothelium vascular Anatomy 0.000 description 2
- YQGOJNYOYNNSMM-UHFFFAOYSA-N eosin Chemical compound [Na+].OC(=O)C1=CC=CC=C1C1=C2C=C(Br)C(=O)C(Br)=C2OC2=C(Br)C(O)=C(Br)C=C21 YQGOJNYOYNNSMM-UHFFFAOYSA-N 0.000 description 2
- 238000000684 flow cytometry Methods 0.000 description 2
- 108010026364 glycyl-glycyl-leucine Proteins 0.000 description 2
- 108010050848 glycylleucine Proteins 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 238000002991 immunohistochemical analysis Methods 0.000 description 2
- 238000011532 immunohistochemical staining Methods 0.000 description 2
- 208000032839 leukemia Diseases 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 210000001165 lymph node Anatomy 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 210000004379 membrane Anatomy 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 239000003068 molecular probe Substances 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 210000002464 muscle smooth vascular Anatomy 0.000 description 2
- 230000009871 nonspecific binding Effects 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 230000002085 persistent effect Effects 0.000 description 2
- 230000035790 physiological processes and functions Effects 0.000 description 2
- 230000008092 positive effect Effects 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000000750 progressive effect Effects 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 108010005652 splenotritin Proteins 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 208000011580 syndromic disease Diseases 0.000 description 2
- 229960004072 thrombin Drugs 0.000 description 2
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 2
- 230000002792 vascular Effects 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- IITIZHOBOIBGBW-UHFFFAOYSA-N 3-ethyl-2h-1,3-benzothiazole Chemical compound C1=CC=C2N(CC)CSC2=C1 IITIZHOBOIBGBW-UHFFFAOYSA-N 0.000 description 1
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- BZTDTCNHAFUJOG-UHFFFAOYSA-N 6-carboxyfluorescein Chemical compound C12=CC=C(O)C=C2OC2=CC(O)=CC=C2C11OC(=O)C2=CC=C(C(=O)O)C=C21 BZTDTCNHAFUJOG-UHFFFAOYSA-N 0.000 description 1
- LWUWMHIOBPTZBA-DCAQKATOSA-N Ala-Arg-Lys Chemical compound NC(=N)NCCC[C@H](NC(=O)[C@@H](N)C)C(=O)N[C@@H](CCCCN)C(O)=O LWUWMHIOBPTZBA-DCAQKATOSA-N 0.000 description 1
- TZDNWXDLYFIFPT-BJDJZHNGSA-N Ala-Ile-Leu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(O)=O TZDNWXDLYFIFPT-BJDJZHNGSA-N 0.000 description 1
- CCDFBRZVTDDJNM-GUBZILKMSA-N Ala-Leu-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O CCDFBRZVTDDJNM-GUBZILKMSA-N 0.000 description 1
- ZBLQIYPCUWZSRZ-QEJZJMRPSA-N Ala-Phe-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](C)N)CC1=CC=CC=C1 ZBLQIYPCUWZSRZ-QEJZJMRPSA-N 0.000 description 1
- CYBJZLQSUJEMAS-LFSVMHDDSA-N Ala-Phe-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)[C@H](C)N)O CYBJZLQSUJEMAS-LFSVMHDDSA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 206010002199 Anaphylactic shock Diseases 0.000 description 1
- 208000032467 Aplastic anaemia Diseases 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- 101100338021 Arabidopsis thaliana GSTU7 gene Proteins 0.000 description 1
- IASNWHAGGYTEKX-IUCAKERBSA-N Arg-Arg-Gly Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(O)=O IASNWHAGGYTEKX-IUCAKERBSA-N 0.000 description 1
- CYXCAHZVPFREJD-LURJTMIESA-N Arg-Gly-Gly Chemical compound NC(=N)NCCC[C@H](N)C(=O)NCC(=O)NCC(O)=O CYXCAHZVPFREJD-LURJTMIESA-N 0.000 description 1
- NKNILFJYKKHBKE-WPRPVWTQSA-N Arg-Gly-Val Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](C(C)C)C(O)=O NKNILFJYKKHBKE-WPRPVWTQSA-N 0.000 description 1
- AFNHFVVOJZBIJD-GUBZILKMSA-N Arg-Met-Asp Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(O)=O AFNHFVVOJZBIJD-GUBZILKMSA-N 0.000 description 1
- 206010003210 Arteriosclerosis Diseases 0.000 description 1
- ZKDGORKGHPCZOV-DCAQKATOSA-N Asn-His-Arg Chemical compound C1=C(NC=N1)C[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)NC(=O)[C@H](CC(=O)N)N ZKDGORKGHPCZOV-DCAQKATOSA-N 0.000 description 1
- SONUFGRSSMFHFN-IMJSIDKUSA-N Asn-Ser Chemical compound NC(=O)C[C@H](N)C(=O)N[C@@H](CO)C(O)=O SONUFGRSSMFHFN-IMJSIDKUSA-N 0.000 description 1
- NPZJLGMWMDNQDD-GHCJXIJMSA-N Asn-Ser-Ile Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O NPZJLGMWMDNQDD-GHCJXIJMSA-N 0.000 description 1
- PQKSVQSMTHPRIB-ZKWXMUAHSA-N Asn-Val-Ser Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CO)C(O)=O PQKSVQSMTHPRIB-ZKWXMUAHSA-N 0.000 description 1
- FKBFDTRILNZGAI-IMJSIDKUSA-N Asp-Cys Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H](CS)C(O)=O FKBFDTRILNZGAI-IMJSIDKUSA-N 0.000 description 1
- VIRHEUMYXXLCBF-WDSKDSINSA-N Asp-Gly-Glu Chemical compound [H]N[C@@H](CC(O)=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(O)=O VIRHEUMYXXLCBF-WDSKDSINSA-N 0.000 description 1
- SEMWSADZTMJELF-BYULHYEWSA-N Asp-Ile-Gly Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(O)=O SEMWSADZTMJELF-BYULHYEWSA-N 0.000 description 1
- JSHWXQIZOCVWIA-ZKWXMUAHSA-N Asp-Ser-Val Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(O)=O JSHWXQIZOCVWIA-ZKWXMUAHSA-N 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 102100032912 CD44 antigen Human genes 0.000 description 1
- 101100177112 Caenorhabditis elegans his-70 gene Proteins 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 206010007710 Cartilage injury Diseases 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 206010010904 Convulsion Diseases 0.000 description 1
- 208000011231 Crohn disease Diseases 0.000 description 1
- VBPGTULCFGKGTF-ACZMJKKPSA-N Cys-Glu-Asp Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O VBPGTULCFGKGTF-ACZMJKKPSA-N 0.000 description 1
- DQGIAOGALAQBGK-BWBBJGPYSA-N Cys-Ser-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CS)N)O DQGIAOGALAQBGK-BWBBJGPYSA-N 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 206010013935 Dysmenorrhoea Diseases 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
- 241000283086 Equidae Species 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 102000016359 Fibronectins Human genes 0.000 description 1
- 208000007882 Gastritis Diseases 0.000 description 1
- 208000018522 Gastrointestinal disease Diseases 0.000 description 1
- ATRHMOJQJWPVBQ-DRZSPHRISA-N Glu-Ala-Phe Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O ATRHMOJQJWPVBQ-DRZSPHRISA-N 0.000 description 1
- TUTIHHSZKFBMHM-WHFBIAKZSA-N Glu-Asn Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CC(N)=O)C(O)=O TUTIHHSZKFBMHM-WHFBIAKZSA-N 0.000 description 1
- AFODTOLGSZQDSL-PEFMBERDSA-N Glu-Asn-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CCC(=O)O)N AFODTOLGSZQDSL-PEFMBERDSA-N 0.000 description 1
- XXCDTYBVGMPIOA-FXQIFTODSA-N Glu-Asp-Glu Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O XXCDTYBVGMPIOA-FXQIFTODSA-N 0.000 description 1
- KVBPDJIFRQUQFY-ACZMJKKPSA-N Glu-Cys-Ser Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CO)C(O)=O KVBPDJIFRQUQFY-ACZMJKKPSA-N 0.000 description 1
- KOSRFJWDECSPRO-WDSKDSINSA-N Glu-Glu Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(O)=O KOSRFJWDECSPRO-WDSKDSINSA-N 0.000 description 1
- AUTNXSQEVVHSJK-YVNDNENWSA-N Glu-Glu-Ile Chemical compound CC[C@H](C)[C@@H](C(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CCC(O)=O AUTNXSQEVVHSJK-YVNDNENWSA-N 0.000 description 1
- QJCKNLPMTPXXEM-AUTRQRHGSA-N Glu-Glu-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CCC(O)=O QJCKNLPMTPXXEM-AUTRQRHGSA-N 0.000 description 1
- XTZDZAXYPDISRR-MNXVOIDGSA-N Glu-Ile-Lys Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CCC(=O)O)N XTZDZAXYPDISRR-MNXVOIDGSA-N 0.000 description 1
- ZAPFAWQHBOHWLL-GUBZILKMSA-N Glu-Ser-His Chemical compound C1=C(NC=N1)C[C@@H](C(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(=O)O)N ZAPFAWQHBOHWLL-GUBZILKMSA-N 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
- 108010024636 Glutathione Proteins 0.000 description 1
- JVWPPCWUDRJGAE-YUMQZZPRSA-N Gly-Asn-Leu Chemical compound [H]NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(O)=O JVWPPCWUDRJGAE-YUMQZZPRSA-N 0.000 description 1
- HDNXXTBKOJKWNN-WDSKDSINSA-N Gly-Glu-Asn Chemical compound NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O HDNXXTBKOJKWNN-WDSKDSINSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 208000017604 Hodgkin disease Diseases 0.000 description 1
- 208000010747 Hodgkins lymphoma Diseases 0.000 description 1
- 101000868273 Homo sapiens CD44 antigen Proteins 0.000 description 1
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 1
- QICVAHODWHIWIS-HTFCKZLJSA-N Ile-Ala-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)O)N QICVAHODWHIWIS-HTFCKZLJSA-N 0.000 description 1
- NJGXXYLPDMMFJB-XUXIUFHCSA-N Ile-Val-Lys Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)O)N NJGXXYLPDMMFJB-XUXIUFHCSA-N 0.000 description 1
- APQYGMBHIVXFML-OSUNSFLBSA-N Ile-Val-Thr Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)O)N APQYGMBHIVXFML-OSUNSFLBSA-N 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 1
- 208000022559 Inflammatory bowel disease Diseases 0.000 description 1
- 108010041012 Integrin alpha4 Proteins 0.000 description 1
- 108010008212 Integrin alpha4beta1 Proteins 0.000 description 1
- 108010041100 Integrin alpha6 Proteins 0.000 description 1
- 102000000426 Integrin alpha6 Human genes 0.000 description 1
- 102000000924 Integrin beta subunit Human genes 0.000 description 1
- 108050007872 Integrin beta subunit Proteins 0.000 description 1
- 108010022222 Integrin beta1 Proteins 0.000 description 1
- 102000012355 Integrin beta1 Human genes 0.000 description 1
- 102000007547 Laminin Human genes 0.000 description 1
- 108010085895 Laminin Proteins 0.000 description 1
- 206010023799 Large intestinal ulcer Diseases 0.000 description 1
- VCSBGUACOYUIGD-CIUDSAMLSA-N Leu-Asn-Asp Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O VCSBGUACOYUIGD-CIUDSAMLSA-N 0.000 description 1
- POJPZSMTTMLSTG-SRVKXCTJSA-N Leu-Asn-Lys Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CCCCN)C(=O)O)N POJPZSMTTMLSTG-SRVKXCTJSA-N 0.000 description 1
- VGPCJSXPPOQPBK-YUMQZZPRSA-N Leu-Gly-Ser Chemical compound CC(C)C[C@H](N)C(=O)NCC(=O)N[C@@H](CO)C(O)=O VGPCJSXPPOQPBK-YUMQZZPRSA-N 0.000 description 1
- KPYAOIVPJKPIOU-KKUMJFAQSA-N Leu-Lys-Lys Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(O)=O KPYAOIVPJKPIOU-KKUMJFAQSA-N 0.000 description 1
- PPGBXYKMUMHFBF-KATARQTJSA-N Leu-Ser-Thr Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(O)=O PPGBXYKMUMHFBF-KATARQTJSA-N 0.000 description 1
- QESXLSQLQHHTIX-RHYQMDGZSA-N Leu-Val-Thr Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O QESXLSQLQHHTIX-RHYQMDGZSA-N 0.000 description 1
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 1
- KCXUCYYZNZFGLL-SRVKXCTJSA-N Lys-Ala-Leu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(O)=O KCXUCYYZNZFGLL-SRVKXCTJSA-N 0.000 description 1
- WAIHHELKYSFIQN-XUXIUFHCSA-N Lys-Ile-Val Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C(C)C)C(O)=O WAIHHELKYSFIQN-XUXIUFHCSA-N 0.000 description 1
- NVGBPTNZLWRQSY-UWVGGRQHSA-N Lys-Lys Chemical compound NCCCC[C@H](N)C(=O)N[C@H](C(O)=O)CCCCN NVGBPTNZLWRQSY-UWVGGRQHSA-N 0.000 description 1
- QQPSCXKFDSORFT-IHRRRGAJSA-N Lys-Lys-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCCCN QQPSCXKFDSORFT-IHRRRGAJSA-N 0.000 description 1
- WLXGMVVHTIUPHE-ULQDDVLXSA-N Lys-Phe-Val Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](C(C)C)C(O)=O WLXGMVVHTIUPHE-ULQDDVLXSA-N 0.000 description 1
- JOSAKOKSPXROGQ-BJDJZHNGSA-N Lys-Ser-Ile Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O JOSAKOKSPXROGQ-BJDJZHNGSA-N 0.000 description 1
- SQRLLZAQNOQCEG-KKUMJFAQSA-N Lys-Tyr-Ser Chemical compound NCCCC[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](CO)C(O)=O)CC1=CC=C(O)C=C1 SQRLLZAQNOQCEG-KKUMJFAQSA-N 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 208000019695 Migraine disease Diseases 0.000 description 1
- 241000357437 Mola Species 0.000 description 1
- 108010085220 Multiprotein Complexes Proteins 0.000 description 1
- 102000007474 Multiprotein Complexes Human genes 0.000 description 1
- 206010029164 Nephrotic syndrome Diseases 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 206010030113 Oedema Diseases 0.000 description 1
- 208000002193 Pain Diseases 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 229920002535 Polyethylene Glycol 1500 Polymers 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 241001430696 Protis Species 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 239000012564 Q sepharose fast flow resin Substances 0.000 description 1
- 108700025866 RAG-1 Genes Proteins 0.000 description 1
- 239000012979 RPMI medium Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 208000015634 Rectal Neoplasms Diseases 0.000 description 1
- 206010038687 Respiratory distress Diseases 0.000 description 1
- 206010039085 Rhinitis allergic Diseases 0.000 description 1
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 1
- 206010070834 Sensitisation Diseases 0.000 description 1
- RDFQNDHEHVSONI-ZLUOBGJFSA-N Ser-Asn-Ser Chemical compound OC[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(O)=O RDFQNDHEHVSONI-ZLUOBGJFSA-N 0.000 description 1
- FTVRVZNYIYWJGB-ACZMJKKPSA-N Ser-Asp-Glu Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O FTVRVZNYIYWJGB-ACZMJKKPSA-N 0.000 description 1
- XERQKTRGJIKTRB-CIUDSAMLSA-N Ser-His-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CO)N)CC1=CN=CN1 XERQKTRGJIKTRB-CIUDSAMLSA-N 0.000 description 1
- KKKVOZNCLALMPV-XKBZYTNZSA-N Ser-Thr-Glu Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(O)=O KKKVOZNCLALMPV-XKBZYTNZSA-N 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 208000000491 Tendinopathy Diseases 0.000 description 1
- 206010043255 Tendonitis Diseases 0.000 description 1
- MQCPGOZXFSYJPS-KZVJFYERSA-N Thr-Ala-Arg Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O MQCPGOZXFSYJPS-KZVJFYERSA-N 0.000 description 1
- KEGBFULVYKYJRD-LFSVMHDDSA-N Thr-Ala-Phe Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 KEGBFULVYKYJRD-LFSVMHDDSA-N 0.000 description 1
- JEDIEMIJYSRUBB-FOHZUACHSA-N Thr-Asp-Gly Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(O)=O JEDIEMIJYSRUBB-FOHZUACHSA-N 0.000 description 1
- XDARBNMYXKUFOJ-GSSVUCPTSA-N Thr-Asp-Thr Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O XDARBNMYXKUFOJ-GSSVUCPTSA-N 0.000 description 1
- FHDLKMFZKRUQCE-HJGDQZAQSA-N Thr-Glu-Arg Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O FHDLKMFZKRUQCE-HJGDQZAQSA-N 0.000 description 1
- WXVIGTAUZBUDPZ-DTLFHODZSA-N Thr-His Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@H](C(O)=O)CC1=CN=CN1 WXVIGTAUZBUDPZ-DTLFHODZSA-N 0.000 description 1
- LUMXICQAOKVQOB-YWIQKCBGSA-N Thr-Ile Chemical compound CC[C@H](C)[C@@H](C(O)=O)NC(=O)[C@@H](N)[C@@H](C)O LUMXICQAOKVQOB-YWIQKCBGSA-N 0.000 description 1
- RFKVQLIXNVEOMB-WEDXCCLWSA-N Thr-Leu-Gly Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)O)N)O RFKVQLIXNVEOMB-WEDXCCLWSA-N 0.000 description 1
- IQHUITKNHOKGFC-MIMYLULJSA-N Thr-Phe Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 IQHUITKNHOKGFC-MIMYLULJSA-N 0.000 description 1
- 108700019146 Transgenes Proteins 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- UDCHKDYNMRJYMI-QEJZJMRPSA-N Trp-Glu-Ser Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(O)=O UDCHKDYNMRJYMI-QEJZJMRPSA-N 0.000 description 1
- 102100040247 Tumor necrosis factor Human genes 0.000 description 1
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 1
- ADBDQGBDNUTRDB-ULQDDVLXSA-N Tyr-Arg-Leu Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(O)=O ADBDQGBDNUTRDB-ULQDDVLXSA-N 0.000 description 1
- FRMFMFNMGQGMNB-BVSLBCMMSA-N Tyr-Pro-Trp Chemical compound C([C@H](N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(O)=O)C1=CC=C(O)C=C1 FRMFMFNMGQGMNB-BVSLBCMMSA-N 0.000 description 1
- UMSZZGTXGKHTFJ-SRVKXCTJSA-N Tyr-Ser-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 UMSZZGTXGKHTFJ-SRVKXCTJSA-N 0.000 description 1
- XXROXFHCMVXETG-UWVGGRQHSA-N Val-Gly-Val Chemical compound CC(C)[C@H](N)C(=O)NCC(=O)N[C@@H](C(C)C)C(O)=O XXROXFHCMVXETG-UWVGGRQHSA-N 0.000 description 1
- DJQIUOKSNRBTSV-CYDGBPFRSA-N Val-Ile-Val Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](C(C)C)C(=O)O)NC(=O)[C@H](C(C)C)N DJQIUOKSNRBTSV-CYDGBPFRSA-N 0.000 description 1
- GBIUHAYJGWVNLN-AEJSXWLSSA-N Val-Ser-Pro Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CO)C(=O)N1CCC[C@@H]1C(=O)O)N GBIUHAYJGWVNLN-AEJSXWLSSA-N 0.000 description 1
- GBIUHAYJGWVNLN-UHFFFAOYSA-N Val-Ser-Pro Natural products CC(C)C(N)C(=O)NC(CO)C(=O)N1CCCC1C(O)=O GBIUHAYJGWVNLN-UHFFFAOYSA-N 0.000 description 1
- TVGWMCTYUFBXAP-QTKMDUPCSA-N Val-Thr-His Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)NC(=O)[C@H](C(C)C)N)O TVGWMCTYUFBXAP-QTKMDUPCSA-N 0.000 description 1
- DFQZDQPLWBSFEJ-LSJOCFKGSA-N Val-Val-Asn Chemical compound CC(C)[C@@H](C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(=O)N)C(=O)O)N DFQZDQPLWBSFEJ-LSJOCFKGSA-N 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 238000002441 X-ray diffraction Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 108010087924 alanylproline Proteins 0.000 description 1
- 201000010105 allergic rhinitis Diseases 0.000 description 1
- KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 208000003455 anaphylaxis Diseases 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 230000001754 anti-pyretic effect Effects 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000002221 antipyretic Substances 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 239000007900 aqueous suspension Substances 0.000 description 1
- 108010068380 arginylarginine Proteins 0.000 description 1
- 208000011775 arteriosclerosis disease Diseases 0.000 description 1
- 210000003567 ascitic fluid Anatomy 0.000 description 1
- 208000006673 asthma Diseases 0.000 description 1
- 208000010668 atopic eczema Diseases 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 239000005441 aurora Substances 0.000 description 1
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
- 150000001540 azides Chemical class 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 238000004159 blood analysis Methods 0.000 description 1
- 206010006451 bronchitis Diseases 0.000 description 1
- 238000013276 bronchoscopy Methods 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000020411 cell activation Effects 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 238000010366 cell biology technique Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000012292 cell migration Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000011976 chest X-ray Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 210000001072 colon Anatomy 0.000 description 1
- 208000029742 colonic neoplasm Diseases 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 238000013170 computed tomography imaging Methods 0.000 description 1
- 238000005094 computer simulation Methods 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 210000001526 defensive cell Anatomy 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 239000010432 diamond Substances 0.000 description 1
- 230000004069 differentiation 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
- BFMYDTVEBKDAKJ-UHFFFAOYSA-L disodium;(2',7'-dibromo-3',6'-dioxido-3-oxospiro[2-benzofuran-1,9'-xanthene]-4'-yl)mercury;hydrate Chemical compound O.[Na+].[Na+].O1C(=O)C2=CC=CC=C2C21C1=CC(Br)=C([O-])C([Hg])=C1OC1=C2C=C(Br)C([O-])=C1 BFMYDTVEBKDAKJ-UHFFFAOYSA-L 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 239000002270 dispersing agent Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 210000003038 endothelium Anatomy 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 210000000981 epithelium Anatomy 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 210000001723 extracellular space Anatomy 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 238000010230 functional analysis Methods 0.000 description 1
- 208000007565 gingivitis Diseases 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 108010055341 glutamyl-glutamic acid Proteins 0.000 description 1
- 108010049041 glutamylalanine Proteins 0.000 description 1
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 1
- 108010062266 glycyl-glycyl-argininal Proteins 0.000 description 1
- 210000003780 hair follicle Anatomy 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 210000005104 human peripheral blood lymphocyte Anatomy 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 210000001822 immobilized cell Anatomy 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 238000003125 immunofluorescent labeling Methods 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000001939 inductive 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
- 230000000977 initiatory effect Effects 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000007919 intrasynovial administration Methods 0.000 description 1
- 238000007913 intrathecal administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 208000002551 irritable bowel syndrome Diseases 0.000 description 1
- 239000002085 irritant Substances 0.000 description 1
- 231100000021 irritant Toxicity 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- 208000028867 ischemia Diseases 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 108010044374 isoleucyl-tyrosine Proteins 0.000 description 1
- 230000002045 lasting effect Effects 0.000 description 1
- 108010034529 leucyl-lysine Proteins 0.000 description 1
- 230000023404 leukocyte cell-cell adhesion Effects 0.000 description 1
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 1
- 108010052968 leupeptin Proteins 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 210000003141 lower extremity Anatomy 0.000 description 1
- 108010054155 lysyllysine Proteins 0.000 description 1
- 108010017391 lysylvaline Proteins 0.000 description 1
- 238000010841 mRNA extraction Methods 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 206010027599 migraine Diseases 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 206010028417 myasthenia gravis Diseases 0.000 description 1
- 210000004165 myocardium Anatomy 0.000 description 1
- 239000007922 nasal spray Substances 0.000 description 1
- 239000006199 nebulizer Substances 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 125000000449 nitro group Chemical group [O-][N+](*)=O 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000007899 nucleic acid hybridization Methods 0.000 description 1
- QYSGYZVSCZSLHT-UHFFFAOYSA-N octafluoropropane Chemical compound FC(F)(F)C(F)(F)C(F)(F)F QYSGYZVSCZSLHT-UHFFFAOYSA-N 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 201000008482 osteoarthritis Diseases 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 210000003200 peritoneal cavity Anatomy 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 206010038038 rectal cancer Diseases 0.000 description 1
- 201000001275 rectum cancer Diseases 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000004202 respiratory function Effects 0.000 description 1
- 208000030925 respiratory syncytial virus infectious disease Diseases 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 201000003068 rheumatic fever Diseases 0.000 description 1
- 206010039083 rhinitis Diseases 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 201000000306 sarcoidosis Diseases 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 230000008313 sensitization Effects 0.000 description 1
- 230000001235 sensitizing effect Effects 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 208000017520 skin disease Diseases 0.000 description 1
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- OBTWBSRJZRCYQV-UHFFFAOYSA-N sulfuryl difluoride Chemical compound FS(F)(=O)=O OBTWBSRJZRCYQV-UHFFFAOYSA-N 0.000 description 1
- 239000000375 suspending agent Substances 0.000 description 1
- 210000001258 synovial membrane Anatomy 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 201000004415 tendinitis Diseases 0.000 description 1
- VUYXVWGKCKTUMF-UHFFFAOYSA-N tetratriacontaethylene glycol monomethyl ether Chemical compound COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO VUYXVWGKCKTUMF-UHFFFAOYSA-N 0.000 description 1
- 238000011287 therapeutic dose Methods 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 229950003937 tolonium Drugs 0.000 description 1
- HNONEKILPDHFOL-UHFFFAOYSA-M tolonium chloride Chemical compound [Cl-].C1=C(C)C(N)=CC2=[S+]C3=CC(N(C)C)=CC=C3N=C21 HNONEKILPDHFOL-UHFFFAOYSA-M 0.000 description 1
- 238000003325 tomography Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 208000019553 vascular disease Diseases 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
Classifications
-
- 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
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2839—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily
- C07K16/2842—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily against integrin beta1-subunit-containing molecules, e.g. CD29, CD49
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/02—Stomatological preparations, e.g. drugs for caries, aphtae, periodontitis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/04—Drugs for disorders of the alimentary tract or the digestive system for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of acid secretion, mucosal protectants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/06—Anti-spasmodics, e.g. drugs for colics, esophagic dyskinesia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/02—Nasal agents, e.g. decongestants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/06—Antiasthmatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P15/00—Drugs for genital or sexual disorders; Contraceptives
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/04—Antipruritics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/06—Antipsoriatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/04—Drugs for skeletal disorders for non-specific disorders of the connective tissue
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P21/00—Drugs for disorders of the muscular or neuromuscular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P21/00—Drugs for disorders of the muscular or neuromuscular system
- A61P21/04—Drugs for disorders of the muscular or neuromuscular system for myasthenia gravis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/06—Antimigraine agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/16—Otologicals
-
- 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
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- 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
- 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
- A61P39/00—General protective or antinoxious agents
- A61P39/02—Antidotes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
- A61P5/14—Drugs for disorders of the endocrine system of the thyroid hormones, e.g. T3, T4
-
- 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
- A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
-
- 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
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- 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
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
- C07K16/2821—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily against ICAM molecules, e.g. CD50, CD54, CD102
-
- 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
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2839—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily
-
- 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
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- 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
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
-
- 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
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Animal Behavior & Ethology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Immunology (AREA)
- Diabetes (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Neurology (AREA)
- Pulmonology (AREA)
- Biomedical Technology (AREA)
- Hematology (AREA)
- Neurosurgery (AREA)
- Dermatology (AREA)
- Physical Education & Sports Medicine (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Endocrinology (AREA)
- Cardiology (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Heart & Thoracic Surgery (AREA)
- Ophthalmology & Optometry (AREA)
- Urology & Nephrology (AREA)
- Vascular Medicine (AREA)
- Transplantation (AREA)
- Otolaryngology (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US13703899P | 1999-06-01 | 1999-06-01 | |
| US18533600P | 2000-02-29 | 2000-02-29 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CZ20014249A3 CZ20014249A3 (cs) | 2002-06-12 |
| CZ300710B6 true CZ300710B6 (cs) | 2009-07-22 |
Family
ID=26834850
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CZ20014249A CZ300710B6 (cs) | 1999-06-01 | 2000-06-01 | Použití blokující monoklonální protilátky proti VLA-1 pro výrobu farmaceutického prípravku k lécení zánetlivých onemocnení |
Country Status (28)
| Country | Link |
|---|---|
| US (5) | US6955810B2 (enExample) |
| EP (3) | EP1488806B1 (enExample) |
| JP (6) | JP4817503B2 (enExample) |
| CN (1) | CN1309419C (enExample) |
| AU (2) | AU783989B2 (enExample) |
| BG (1) | BG65579B1 (enExample) |
| BR (1) | BR0011250A (enExample) |
| CA (1) | CA2375827C (enExample) |
| CY (1) | CY1116042T1 (enExample) |
| CZ (1) | CZ300710B6 (enExample) |
| DK (2) | DK2314315T3 (enExample) |
| EA (1) | EA011384B1 (enExample) |
| EE (1) | EE200100651A (enExample) |
| ES (2) | ES2529706T3 (enExample) |
| GE (1) | GEP20063774B (enExample) |
| HK (1) | HK1043320A1 (enExample) |
| HU (1) | HUP0202568A3 (enExample) |
| IL (2) | IL146508A0 (enExample) |
| IS (1) | IS6179A (enExample) |
| MX (1) | MXPA01012388A (enExample) |
| NO (1) | NO20015864L (enExample) |
| NZ (1) | NZ515686A (enExample) |
| PT (2) | PT1488806E (enExample) |
| SI (2) | SI2314315T1 (enExample) |
| SK (1) | SK17232001A3 (enExample) |
| TR (1) | TR200103432T2 (enExample) |
| WO (1) | WO2000072881A1 (enExample) |
| YU (1) | YU85501A (enExample) |
Families Citing this family (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CZ300710B6 (cs) * | 1999-06-01 | 2009-07-22 | Biogen Idec Ma Inc. | Použití blokující monoklonální protilátky proti VLA-1 pro výrobu farmaceutického prípravku k lécení zánetlivých onemocnení |
| UA83791C2 (ru) | 2001-04-13 | 2008-08-26 | Байоджен Айдек Ма Инк. | Антитело против vla-1, фармацевтическая композиция, которая его содержит, и из применение для лечения индивидуума с иммунологическим расстройством, опосредованным vla-1 |
| WO2003068262A1 (en) * | 2002-02-14 | 2003-08-21 | Biogen, Inc. | Alpha1beta1 antagonists for treatment of atherosclerosis |
| US7348002B2 (en) * | 2002-11-01 | 2008-03-25 | Boys Town National Research Hospital | Inducible ligand for α1β1 integrin and uses |
| WO2005004800A2 (en) * | 2003-06-20 | 2005-01-20 | Morehouse School Of Medicine | Trypanosome derived apoptotic factors (taf) |
| US20080093950A1 (en) * | 2003-12-09 | 2008-04-24 | Electrotechnologies Selem. Inc | Polyphase Claw-Pole Machines With a Segmented Magnetic Circuit |
| US20050136055A1 (en) * | 2003-12-22 | 2005-06-23 | Pfizer Inc | CD40 antibody formulation and methods |
| WO2006124269A2 (en) * | 2005-05-16 | 2006-11-23 | Amgen Fremont Inc. | Human monoclonal antibodies that bind to very late antigen-1 for the treatment of inflammation and other disorders |
| WO2006133286A2 (en) * | 2005-06-07 | 2006-12-14 | Tel Hashomer Medical Research Infrastructure And Services Ltd. | Treatment of tnf antagonist-resistant inflammatory disorders and related methods |
| US10119979B2 (en) * | 2006-05-25 | 2018-11-06 | Biogen Ma Inc. | Methods of treating stroke and traumatic brain injury using humanized AQC2 anti-VLA-1 antibodies |
| WO2009135953A2 (en) * | 2008-05-09 | 2009-11-12 | Ablynx Nv | Amino acid sequences directed against integrins and uses thereof |
| JP6324720B2 (ja) * | 2010-06-18 | 2018-05-16 | エックスバイオテク, インコーポレイテッドXbiotech, Inc. | 関節炎治療 |
| US20140017261A1 (en) * | 2011-02-03 | 2014-01-16 | Mark Totoritis | Selection and treatment of subjects |
| NZ629204A (en) | 2012-02-16 | 2016-09-30 | Santarus Inc | Anti-vla1 (cd49a) antibody pharmaceutical compositions |
| EP3655011A4 (en) * | 2017-07-20 | 2021-03-31 | University Of Virginia Patent Foundation | PROCEDURES FOR THE TREATMENT OR PREVENTION OF A NEUROLOGICAL DISORDER OF THE IMMUNE SYSTEM |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5788966A (en) * | 1990-08-31 | 1998-08-04 | The Trustees Of Columbia University In The City Of New York | Antibody which is directed against and inhibits collagen binding to a VLA-1 epitope and uses thereof |
Family Cites Families (67)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| AU600575B2 (en) | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
| IL162181A (en) | 1988-12-28 | 2006-04-10 | Pdl Biopharma Inc | A method of producing humanized immunoglubulin, and polynucleotides encoding the same |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5859205A (en) | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| WO1991010737A1 (en) | 1990-01-11 | 1991-07-25 | Molecular Affinities Corporation | Production of antibodies using gene libraries |
| US6673986B1 (en) | 1990-01-12 | 2004-01-06 | Abgenix, Inc. | Generation of xenogeneic antibodies |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5789650A (en) | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| DE69230142T2 (de) | 1991-05-15 | 2000-03-09 | Cambridge Antibody Technology Ltd. | Verfahren zur herstellung von spezifischen bindungspaargliedern |
| EP0590058B1 (en) | 1991-06-14 | 2003-11-26 | Genentech, Inc. | HUMANIZED Heregulin ANTIBODy |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| DK0626861T4 (da) | 1992-01-13 | 2004-08-16 | Biogen Inc | Behandling af astma. |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US6307026B1 (en) | 1992-12-10 | 2001-10-23 | Celltech Limited | Humanized antibodies directed against A33 antigen |
| DK0678122T3 (da) | 1993-01-12 | 2000-03-06 | Biogen Inc | Rekombinante anti-VLA4 antistofmolekyler |
| WO1994017828A2 (en) | 1993-02-09 | 1994-08-18 | Biogen, Inc. | Treatment for insulin dependent diabetes |
| US6111598A (en) | 1993-11-12 | 2000-08-29 | Peveo, Inc. | System and method for producing and displaying spectrally-multiplexed images of three-dimensional imagery for use in flicker-free stereoscopic viewing thereof |
| US5827690A (en) | 1993-12-20 | 1998-10-27 | Genzyme Transgenics Corporatiion | Transgenic production of antibodies in milk |
| JP4115517B2 (ja) | 1994-01-25 | 2008-07-09 | エラン ファーマシューティカルズ, インコーポレイテッド | 白血球付着分子 vla−4に対するヒト化抗体 |
| US5840299A (en) * | 1994-01-25 | 1998-11-24 | Athena Neurosciences, Inc. | Humanized antibodies against leukocyte adhesion molecule VLA-4 |
| ATE195428T1 (de) | 1994-04-26 | 2000-09-15 | Kanebo Ltd | Arznei für rheumatoide arthritis |
| JPH08131185A (ja) * | 1994-11-14 | 1996-05-28 | Sumitomo Electric Ind Ltd | マウスvla−1分子に対するモノクローナル抗体 |
| JPH08160972A (ja) | 1994-12-01 | 1996-06-21 | Sega Enterp Ltd | エフェクト制御方法、制御装置およびこれを利用したカラオケ装置 |
| EP0823941A4 (en) | 1995-04-28 | 2001-09-19 | Abgenix Inc | HUMAN ANTIBODIES DERIVED FROM IMMUNIZED XENO MOUSES |
| GB9516399D0 (en) | 1995-08-10 | 1995-10-11 | Camelot Superabsorbents Ltd | Process for the production of water-absorbing compositions |
| CA2229043C (en) | 1995-08-18 | 2016-06-07 | Morphosys Gesellschaft Fur Proteinoptimierung Mbh | Protein/(poly)peptide libraries |
| CA2230759C (en) | 1995-08-29 | 2012-02-21 | Kirin Beer Kabushiki Kaisha | Chimeric animal and method for producing the same |
| DE19534177A1 (de) | 1995-09-15 | 1997-03-20 | Merck Patent Gmbh | Cyclische Adhäsionsinhibitoren |
| GB9519667D0 (en) | 1995-09-27 | 1995-11-29 | Univ Manchester | Pharmaceutical composition |
| DE19541844C1 (de) | 1995-11-09 | 1997-07-24 | Gsf Forschungszentrum Umwelt | Verfahren zur Herstellung von menschlichen Antikörpern und deren Verwendung |
| FR2745912B1 (fr) * | 1996-03-08 | 1998-05-29 | Lorraine Laminage | Procede et dispositif de controle de la soudabilite de toles sandwich |
| US6127524A (en) | 1996-10-18 | 2000-10-03 | Dade Behring Inc. | Binding molecules and computer-based methods of increasing the binding affinity thereof |
| DE69738539T2 (de) | 1996-12-03 | 2009-03-26 | Amgen Fremont Inc. | Vollkommen humane Antikörper die EGFR binden |
| DK0999853T3 (da) | 1997-06-13 | 2003-04-22 | Genentech Inc | Stabiliseret antostofformulering |
| SI1079843T1 (sl) | 1998-05-22 | 2007-10-31 | Bpys Town Nat Res Hospital | Uporaba inhibitorjev receptorja alfa1beta1-integrina in inhibitorjev TGF-beta1 pri zdravljenju ledvične bolezni |
| DE19831710A1 (de) | 1998-07-15 | 2000-01-20 | Merck Patent Gmbh | Diacylhydrazinderivate |
| WO2000020459A1 (en) | 1998-10-06 | 2000-04-13 | Biogen, Inc. | Crystals of the alpha 1 beta 1 integrin i-domain and their use |
| HK1041452B (en) * | 1999-04-22 | 2005-10-14 | Biogen Idec Ma Inc. | Method for the treatment of fibrosis using an antagonist of the integrin alpha-4 subunit |
| CZ300710B6 (cs) * | 1999-06-01 | 2009-07-22 | Biogen Idec Ma Inc. | Použití blokující monoklonální protilátky proti VLA-1 pro výrobu farmaceutického prípravku k lécení zánetlivých onemocnení |
| US7601125B1 (en) | 1999-06-17 | 2009-10-13 | Desinger Kai | Surgical, grooved director for collecting tissue in a minimally invasive manner |
| WO2001073444A2 (en) | 2000-03-28 | 2001-10-04 | Cambridge University Technical Services Limited | Receptor/peptide crystal structure for identification of inhibitors |
| US8288322B2 (en) | 2000-04-17 | 2012-10-16 | Dyax Corp. | Methods of constructing libraries comprising displayed and/or expressed members of a diverse family of peptides, polypeptides or proteins and the novel libraries |
| DE10028402A1 (de) | 2000-06-13 | 2001-12-20 | Merck Patent Gmbh | Pyridin-2-yl-aminoalkycarbonylglycyl-beta-alanin und Derivate |
| US7153944B2 (en) | 2000-07-31 | 2006-12-26 | The General Hospital Corporation | High affinity integrin polypeptides and uses thereof |
| UA83791C2 (ru) | 2001-04-13 | 2008-08-26 | Байоджен Айдек Ма Инк. | Антитело против vla-1, фармацевтическая композиция, которая его содержит, и из применение для лечения индивидуума с иммунологическим расстройством, опосредованным vla-1 |
| WO2003068262A1 (en) | 2002-02-14 | 2003-08-21 | Biogen, Inc. | Alpha1beta1 antagonists for treatment of atherosclerosis |
| KR101115797B1 (ko) | 2002-08-01 | 2012-07-27 | 이뮤노메딕스, 인코오포레이티드 | 알파 태아 단백질 Immu31 항체 및 융합단백질, 및이들의 이용 방법 |
| US20040208870A1 (en) | 2003-01-30 | 2004-10-21 | Medimmune, Inc. | Stabilized high concentration anti-integrin alphanubeta3 antibody formulations |
| WO2005019200A2 (en) | 2003-08-14 | 2005-03-03 | Icos Corporation | Aryl piperidine derivatives as vla-1 integrin antagonists and uses thereof |
| WO2005016883A2 (en) | 2003-08-14 | 2005-02-24 | Icos Corporation | Acrylamide derivatives as vla-1 integrin antagonists and uses thereof |
| US7285530B2 (en) | 2004-10-21 | 2007-10-23 | Viron Therapeutics, Inc. | Use of SERP-1 as an antiplatelet agent |
| WO2006124269A2 (en) | 2005-05-16 | 2006-11-23 | Amgen Fremont Inc. | Human monoclonal antibodies that bind to very late antigen-1 for the treatment of inflammation and other disorders |
| WO2006133286A2 (en) | 2005-06-07 | 2006-12-14 | Tel Hashomer Medical Research Infrastructure And Services Ltd. | Treatment of tnf antagonist-resistant inflammatory disorders and related methods |
| US7612181B2 (en) | 2005-08-19 | 2009-11-03 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| MY149159A (en) | 2005-11-15 | 2013-07-31 | Hoffmann La Roche | Method for treating joint damage |
| US20080118496A1 (en) | 2006-04-10 | 2008-05-22 | Medich John R | Uses and compositions for treatment of juvenile rheumatoid arthritis |
| JO3324B1 (ar) | 2006-04-21 | 2019-03-13 | Amgen Inc | مركبات علاجية مجففة بالتبريد تتعلق بالعصارة الهضمية |
| US10119979B2 (en) | 2006-05-25 | 2018-11-06 | Biogen Ma Inc. | Methods of treating stroke and traumatic brain injury using humanized AQC2 anti-VLA-1 antibodies |
| JP4951596B2 (ja) | 2008-07-31 | 2012-06-13 | 株式会社日立製作所 | 冷却システム及び電子装置 |
| CA2754528A1 (en) | 2009-03-06 | 2010-09-10 | Genetech, Inc. | Antibody formulation |
| ES2765657T3 (es) | 2009-12-21 | 2020-06-10 | Hoffmann La Roche | Formulación farmacéutica de bevacizumab |
| US20140017261A1 (en) | 2011-02-03 | 2014-01-16 | Mark Totoritis | Selection and treatment of subjects |
| JP5662565B2 (ja) | 2012-01-11 | 2015-02-04 | パナソニックIpマネジメント株式会社 | 圧接型半導体装置及びその製造方法 |
| NZ629204A (en) | 2012-02-16 | 2016-09-30 | Santarus Inc | Anti-vla1 (cd49a) antibody pharmaceutical compositions |
-
2000
- 2000-06-01 CZ CZ20014249A patent/CZ300710B6/cs not_active IP Right Cessation
- 2000-06-01 SI SI200031087T patent/SI2314315T1/sl unknown
- 2000-06-01 CA CA2375827A patent/CA2375827C/en not_active Expired - Lifetime
- 2000-06-01 TR TR2001/03432T patent/TR200103432T2/xx unknown
- 2000-06-01 JP JP2000620987A patent/JP4817503B2/ja not_active Expired - Lifetime
- 2000-06-01 HU HU0202568A patent/HUP0202568A3/hu unknown
- 2000-06-01 SI SI200031089T patent/SI1488806T1/sl unknown
- 2000-06-01 GE GE5125A patent/GEP20063774B/en unknown
- 2000-06-01 IL IL14650800A patent/IL146508A0/xx active IP Right Grant
- 2000-06-01 DK DK10185467.7T patent/DK2314315T3/en active
- 2000-06-01 ES ES10185467.7T patent/ES2529706T3/es not_active Expired - Lifetime
- 2000-06-01 AU AU57248/00A patent/AU783989B2/en not_active Expired
- 2000-06-01 NZ NZ515686A patent/NZ515686A/en unknown
- 2000-06-01 SK SK1723-2001A patent/SK17232001A3/sk unknown
- 2000-06-01 MX MXPA01012388A patent/MXPA01012388A/es active IP Right Grant
- 2000-06-01 YU YU85501A patent/YU85501A/sh unknown
- 2000-06-01 BR BR0011250-0A patent/BR0011250A/pt not_active Application Discontinuation
- 2000-06-01 ES ES04018151.3T patent/ES2557768T3/es not_active Expired - Lifetime
- 2000-06-01 PT PT40181513T patent/PT1488806E/pt unknown
- 2000-06-01 DK DK04018151.3T patent/DK1488806T3/en active
- 2000-06-01 EP EP04018151.3A patent/EP1488806B1/en not_active Expired - Lifetime
- 2000-06-01 PT PT10185467T patent/PT2314315E/pt unknown
- 2000-06-01 HK HK02105185.2A patent/HK1043320A1/zh unknown
- 2000-06-01 EA EA200400930A patent/EA011384B1/ru not_active IP Right Cessation
- 2000-06-01 EP EP10185467.7A patent/EP2314315B1/en not_active Expired - Lifetime
- 2000-06-01 WO PCT/US2000/015004 patent/WO2000072881A1/en not_active Ceased
- 2000-06-01 EE EEP200100651A patent/EE200100651A/xx unknown
- 2000-06-01 CN CNB008084289A patent/CN1309419C/zh not_active Expired - Lifetime
- 2000-06-01 EP EP00942654A patent/EP1181054A1/en not_active Withdrawn
-
2001
- 2001-11-15 IL IL146508A patent/IL146508A/en not_active IP Right Cessation
- 2001-11-28 IS IS6179A patent/IS6179A/is unknown
- 2001-11-30 NO NO20015864A patent/NO20015864L/no not_active Application Discontinuation
- 2001-11-30 US US09/996,738 patent/US6955810B2/en not_active Expired - Lifetime
- 2001-12-17 BG BG106226A patent/BG65579B1/bg unknown
-
2005
- 2005-04-18 US US11/108,581 patent/US7462353B2/en not_active Expired - Lifetime
-
2006
- 2006-04-12 AU AU2006201540A patent/AU2006201540A1/en not_active Abandoned
-
2007
- 2007-05-22 JP JP2007136041A patent/JP2007277253A/ja active Pending
-
2008
- 2008-11-11 US US12/268,459 patent/US8084031B2/en not_active Expired - Fee Related
-
2011
- 2011-05-24 JP JP2011116366A patent/JP5623335B2/ja not_active Expired - Lifetime
- 2011-11-15 US US13/296,778 patent/US8557240B2/en not_active Expired - Fee Related
-
2012
- 2012-06-07 JP JP2012130177A patent/JP2012176983A/ja active Pending
-
2013
- 2013-09-09 US US14/021,547 patent/US9902774B2/en not_active Expired - Fee Related
-
2014
- 2014-08-18 JP JP2014165702A patent/JP5960762B2/ja not_active Expired - Lifetime
-
2015
- 2015-02-20 CY CY20151100186T patent/CY1116042T1/el unknown
-
2016
- 2016-03-24 JP JP2016060029A patent/JP2016121184A/ja not_active Withdrawn
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5788966A (en) * | 1990-08-31 | 1998-08-04 | The Trustees Of Columbia University In The City Of New York | Antibody which is directed against and inhibits collagen binding to a VLA-1 epitope and uses thereof |
Non-Patent Citations (2)
| Title |
|---|
| Fabbri M. et al.: "A functional monoclonal antibody recognizing the human alpha 1 integrin I-domain", Tissue Antigens, vol. 48(1), 47-51, 1996 * |
| Laffon A. et al.: "Very late activation antigen on synovial fluid T cells from patients with rheumatoid arthritis and other rheumatic diseases", Arthritis Rheum., Vol. 32(4):386-92, 1989 * |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US8084031B2 (en) | Method for the treatment of inflammatory disorders | |
| CZ303450B6 (cs) | Protilátky k VLA-1, kompozice je obsahující a nukleové kyseliny, které je kódují, zpusob stanovení hladiny VLA-1 a použití pri lécení imunologického onemocnení | |
| PL203114B1 (pl) | Zastosowania przeciwciała przeciw VLA-4 lub jego fragmentu wiążącego antygen, przeciwciała przeciw integrynie alfa-4/beta7 lub jego fragmentu wiążącego antygen lub przeciwciała przeciw VCAM-1 lub jego fragmentu wiążącego antygen, zastosowania rozpuszczalnych polipeptydów VLA-4 lub VCAM-1, które antagonizują interakcję VLA-4/VCAM-1 | |
| HK1112193A (en) | A blocking monoclonal antibody to vla-1 and its use for the treatment of inflammatory disorders | |
| HK1154352B (en) | A blocking monoclonal antibody to the human alpha1 i-domain of vla-1, and its use for the treatment of inflammatory disorders | |
| EA005242B1 (ru) | Способ лечения артрита при использовании блокирующего моноклонального антитела к интегрину vla-1 или его фрагмента | |
| ZA200308568B (en) | Antibodies to VLA-1. |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | Patent lapsed due to non-payment of fee |
Effective date: 20000601 |