NO324725B1 - MORT-1-protein, DNA-sekvens som koder for MORT-1 og antistoffer spesifikke for MORT-1, samt fremgangsmate for fremstilling, farmasoytiske sammensetninger og anvendelser. - Google Patents
MORT-1-protein, DNA-sekvens som koder for MORT-1 og antistoffer spesifikke for MORT-1, samt fremgangsmate for fremstilling, farmasoytiske sammensetninger og anvendelser. Download PDFInfo
- Publication number
- NO324725B1 NO324725B1 NO19972716A NO972716A NO324725B1 NO 324725 B1 NO324725 B1 NO 324725B1 NO 19972716 A NO19972716 A NO 19972716A NO 972716 A NO972716 A NO 972716A NO 324725 B1 NO324725 B1 NO 324725B1
- Authority
- NO
- Norway
- Prior art keywords
- protein
- mort
- fas
- cells
- proteins
- Prior art date
Links
- 108010077716 Fas-Associated Death Domain Protein Proteins 0.000 title claims description 70
- 102000010579 Fas-Associated Death Domain Protein Human genes 0.000 title claims description 69
- 238000000034 method Methods 0.000 title claims description 60
- 108091028043 Nucleic acid sequence Proteins 0.000 title claims description 16
- 239000008194 pharmaceutical composition Substances 0.000 title claims description 8
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 137
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 132
- 239000013598 vector Substances 0.000 claims abstract description 51
- 238000012258 culturing Methods 0.000 claims abstract description 3
- 210000004027 cell Anatomy 0.000 claims description 172
- 102000005962 receptors Human genes 0.000 claims description 57
- 230000027455 binding Effects 0.000 claims description 44
- 230000003834 intracellular effect Effects 0.000 claims description 43
- 239000002299 complementary DNA Substances 0.000 claims description 42
- 239000003446 ligand Substances 0.000 claims description 40
- 230000014509 gene expression Effects 0.000 claims description 28
- 239000012634 fragment Substances 0.000 claims description 20
- 241000700605 Viruses Species 0.000 claims description 17
- 239000000284 extract Substances 0.000 claims description 17
- 239000000523 sample Substances 0.000 claims description 16
- 108020004414 DNA Proteins 0.000 claims description 15
- 241001465754 Metazoa Species 0.000 claims description 15
- 238000004519 manufacturing process Methods 0.000 claims description 14
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 13
- 230000008569 process Effects 0.000 claims description 13
- 210000004881 tumor cell Anatomy 0.000 claims description 13
- 230000002900 effect on cell Effects 0.000 claims description 11
- 238000000338 in vitro Methods 0.000 claims description 10
- 238000002955 isolation Methods 0.000 claims description 10
- 238000010367 cloning Methods 0.000 claims description 9
- 102000000844 Cell Surface Receptors Human genes 0.000 claims description 8
- 108010001857 Cell Surface Receptors Proteins 0.000 claims description 8
- 238000001042 affinity chromatography Methods 0.000 claims description 8
- 102100031988 Tumor necrosis factor ligand superfamily member 6 Human genes 0.000 claims description 7
- 108050002568 Tumor necrosis factor ligand superfamily member 6 Proteins 0.000 claims description 7
- 238000001086 yeast two-hybrid system Methods 0.000 claims description 7
- 102000018697 Membrane Proteins Human genes 0.000 claims description 6
- 108010052285 Membrane Proteins Proteins 0.000 claims description 6
- 206010028980 Neoplasm Diseases 0.000 claims description 6
- 238000002105 Southern blotting Methods 0.000 claims description 4
- 230000036961 partial effect Effects 0.000 claims description 4
- 239000004480 active ingredient Substances 0.000 claims description 2
- 239000012504 chromatography matrix Substances 0.000 claims description 2
- 238000000605 extraction Methods 0.000 claims description 2
- 239000000825 pharmaceutical preparation Substances 0.000 claims description 2
- 230000004481 post-translational protein modification Effects 0.000 claims description 2
- 230000003612 virological effect Effects 0.000 claims description 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 claims 1
- 101150028668 APO1 gene Proteins 0.000 abstract description 3
- 108010052621 fas Receptor Proteins 0.000 description 132
- 102000018823 fas Receptor Human genes 0.000 description 131
- 235000018102 proteins Nutrition 0.000 description 108
- 108020003175 receptors Proteins 0.000 description 52
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 45
- 230000000694 effects Effects 0.000 description 45
- 102000003390 tumor necrosis factor Human genes 0.000 description 40
- 102000037865 fusion proteins Human genes 0.000 description 28
- 108020001507 fusion proteins Proteins 0.000 description 28
- 102000010170 Death domains Human genes 0.000 description 24
- 108050001718 Death domains Proteins 0.000 description 24
- 150000001413 amino acids Chemical class 0.000 description 22
- 239000000427 antigen Substances 0.000 description 22
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 20
- 108091007433 antigens Proteins 0.000 description 20
- 102000036639 antigens Human genes 0.000 description 20
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 20
- 102100039556 Galectin-4 Human genes 0.000 description 19
- 101000608765 Homo sapiens Galectin-4 Proteins 0.000 description 19
- 102100033732 Tumor necrosis factor receptor superfamily member 1A Human genes 0.000 description 19
- 230000011664 signaling Effects 0.000 description 19
- 230000004068 intracellular signaling Effects 0.000 description 18
- 238000003556 assay Methods 0.000 description 17
- 235000001014 amino acid Nutrition 0.000 description 16
- 230000003993 interaction Effects 0.000 description 15
- 230000001404 mediated effect Effects 0.000 description 15
- 238000011534 incubation Methods 0.000 description 14
- 239000007790 solid phase Substances 0.000 description 14
- 239000002773 nucleotide Substances 0.000 description 13
- 125000003729 nucleotide group Chemical group 0.000 description 13
- 230000004568 DNA-binding Effects 0.000 description 12
- 239000004098 Tetracycline Substances 0.000 description 12
- 229960002180 tetracycline Drugs 0.000 description 12
- 229930101283 tetracycline Natural products 0.000 description 12
- 235000019364 tetracycline Nutrition 0.000 description 12
- 150000003522 tetracyclines Chemical class 0.000 description 12
- 102000014914 Carrier Proteins Human genes 0.000 description 11
- 241000699666 Mus <mouse, genus> Species 0.000 description 11
- 238000000211 autoradiogram Methods 0.000 description 11
- 108091008324 binding proteins Proteins 0.000 description 11
- 230000030833 cell death Effects 0.000 description 11
- 230000001472 cytotoxic effect Effects 0.000 description 11
- 239000000463 material Substances 0.000 description 11
- 230000035772 mutation Effects 0.000 description 11
- 102000004196 processed proteins & peptides Human genes 0.000 description 11
- 108090000765 processed proteins & peptides Proteins 0.000 description 11
- 101150064015 FAS gene Proteins 0.000 description 10
- 101000611023 Homo sapiens Tumor necrosis factor receptor superfamily member 6 Proteins 0.000 description 10
- 230000001413 cellular effect Effects 0.000 description 10
- 239000013604 expression vector Substances 0.000 description 10
- 230000006870 function Effects 0.000 description 10
- 238000001114 immunoprecipitation Methods 0.000 description 10
- 210000001519 tissue Anatomy 0.000 description 10
- 238000010396 two-hybrid screening Methods 0.000 description 10
- 102000053642 Catalytic RNA Human genes 0.000 description 9
- 108090000994 Catalytic RNA Proteins 0.000 description 9
- 230000004913 activation Effects 0.000 description 9
- 230000000445 cytocidal effect Effects 0.000 description 9
- 231100000433 cytotoxic Toxicity 0.000 description 9
- 230000003013 cytotoxicity Effects 0.000 description 9
- 231100000135 cytotoxicity Toxicity 0.000 description 9
- 238000001514 detection method Methods 0.000 description 9
- 229960004452 methionine Drugs 0.000 description 9
- 230000033458 reproduction Effects 0.000 description 9
- 108091092562 ribozyme Proteins 0.000 description 9
- 102100022089 Acyl-[acyl-carrier-protein] hydrolase Human genes 0.000 description 8
- 108060001084 Luciferase Proteins 0.000 description 8
- 239000005089 Luciferase Substances 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 8
- 239000011324 bead Substances 0.000 description 8
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 8
- 238000013519 translation Methods 0.000 description 8
- 102100023995 Beta-nerve growth factor Human genes 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- 102000005720 Glutathione transferase Human genes 0.000 description 7
- 108010070675 Glutathione transferase Proteins 0.000 description 7
- 108010025020 Nerve Growth Factor Proteins 0.000 description 7
- 210000004899 c-terminal region Anatomy 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 238000002474 experimental method Methods 0.000 description 7
- 230000004927 fusion Effects 0.000 description 7
- 238000001727 in vivo Methods 0.000 description 7
- 101150066555 lacZ gene Proteins 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 239000007787 solid Substances 0.000 description 7
- 238000001890 transfection Methods 0.000 description 7
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 6
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 6
- 101710187830 Tumor necrosis factor receptor superfamily member 1B Proteins 0.000 description 6
- 238000013459 approach Methods 0.000 description 6
- YPHMISFOHDHNIV-FSZOTQKASA-N cycloheximide Chemical compound C1[C@@H](C)C[C@H](C)C(=O)[C@@H]1[C@H](O)CC1CC(=O)NC(=O)C1 YPHMISFOHDHNIV-FSZOTQKASA-N 0.000 description 6
- -1 factors Proteins 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 108020003519 protein disulfide isomerase Proteins 0.000 description 6
- 230000001105 regulatory effect Effects 0.000 description 6
- 102100024321 Alkaline phosphatase, placental type Human genes 0.000 description 5
- 108020004705 Codon Proteins 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 238000010276 construction Methods 0.000 description 5
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 5
- 230000005764 inhibitory process Effects 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 108020004999 messenger RNA Proteins 0.000 description 5
- 229930182817 methionine Natural products 0.000 description 5
- 108010031345 placental alkaline phosphatase Proteins 0.000 description 5
- 238000010561 standard procedure Methods 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 230000035899 viability Effects 0.000 description 5
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 108700008625 Reporter Genes Proteins 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 230000006907 apoptotic process Effects 0.000 description 4
- 230000003833 cell viability Effects 0.000 description 4
- 230000004186 co-expression Effects 0.000 description 4
- 230000006378 damage Effects 0.000 description 4
- 230000034994 death Effects 0.000 description 4
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical group OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 4
- 239000012133 immunoprecipitate Substances 0.000 description 4
- 230000000977 initiatory effect Effects 0.000 description 4
- 239000013642 negative control Substances 0.000 description 4
- PGSADBUBUOPOJS-UHFFFAOYSA-N neutral red Chemical compound Cl.C1=C(C)C(N)=CC2=NC3=CC(N(C)C)=CC=C3N=C21 PGSADBUBUOPOJS-UHFFFAOYSA-N 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 3
- 108091026890 Coding region Proteins 0.000 description 3
- 102100026693 FAS-associated death domain protein Human genes 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 210000001744 T-lymphocyte Anatomy 0.000 description 3
- 108091023040 Transcription factor Proteins 0.000 description 3
- 102000040945 Transcription factor Human genes 0.000 description 3
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 3
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
- 231100000354 acute hepatitis Toxicity 0.000 description 3
- 230000002776 aggregation Effects 0.000 description 3
- 238000004220 aggregation Methods 0.000 description 3
- 238000000376 autoradiography Methods 0.000 description 3
- 239000012472 biological sample Substances 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 239000012636 effector Substances 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 238000001415 gene therapy Methods 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 208000006454 hepatitis Diseases 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 238000013198 immunometric assay Methods 0.000 description 3
- 238000011065 in-situ storage Methods 0.000 description 3
- 238000002372 labelling Methods 0.000 description 3
- 238000001466 metabolic labeling Methods 0.000 description 3
- 229910052751 metal Inorganic materials 0.000 description 3
- 239000002184 metal Substances 0.000 description 3
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 3
- 238000003127 radioimmunoassay Methods 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 230000009870 specific binding Effects 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 230000000451 tissue damage Effects 0.000 description 3
- 231100000827 tissue damage Toxicity 0.000 description 3
- 108091006106 transcriptional activators Proteins 0.000 description 3
- 238000011144 upstream manufacturing Methods 0.000 description 3
- 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 2
- 102100032303 26S proteasome non-ATPase regulatory subunit 2 Human genes 0.000 description 2
- OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 101000835846 Arabidopsis thaliana Sucrose nonfermenting 4-like protein Proteins 0.000 description 2
- 238000011725 BALB/c mouse Methods 0.000 description 2
- 102100026189 Beta-galactosidase Human genes 0.000 description 2
- 101710127053 FAS-associated death domain protein Proteins 0.000 description 2
- 108010024636 Glutathione Proteins 0.000 description 2
- 101150009006 HIS3 gene Proteins 0.000 description 2
- 101000590272 Homo sapiens 26S proteasome non-ATPase regulatory subunit 2 Proteins 0.000 description 2
- 238000000636 Northern blotting Methods 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 239000004793 Polystyrene Substances 0.000 description 2
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 206010040070 Septic Shock Diseases 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- 101710120037 Toxin CcdB Proteins 0.000 description 2
- 206010046865 Vaccinia virus infection Diseases 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 239000005557 antagonist Substances 0.000 description 2
- DZBUGLKDJFMEHC-UHFFFAOYSA-N benzoquinolinylidene Natural products C1=CC=CC2=CC3=CC=CC=C3N=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-N 0.000 description 2
- 108010005774 beta-Galactosidase Proteins 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 208000035475 disorder Diseases 0.000 description 2
- 239000007850 fluorescent dye Substances 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 229960003180 glutathione Drugs 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 230000009931 harmful effect Effects 0.000 description 2
- 102000047715 human FAS Human genes 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 238000010166 immunofluorescence Methods 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 2
- 238000004020 luminiscence type Methods 0.000 description 2
- 210000004698 lymphocyte Anatomy 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 150000002739 metals Chemical class 0.000 description 2
- 230000000869 mutational effect Effects 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 229920002223 polystyrene Polymers 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 230000036303 septic shock Effects 0.000 description 2
- 230000019491 signal transduction Effects 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- PUZPDOWCWNUUKD-UHFFFAOYSA-M sodium fluoride Chemical compound [F-].[Na+] PUZPDOWCWNUUKD-UHFFFAOYSA-M 0.000 description 2
- 201000000596 systemic lupus erythematosus Diseases 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 230000010474 transient expression Effects 0.000 description 2
- 102000035160 transmembrane proteins Human genes 0.000 description 2
- 108091005703 transmembrane proteins Proteins 0.000 description 2
- 230000001960 triggered effect Effects 0.000 description 2
- 208000007089 vaccinia Diseases 0.000 description 2
- 230000000007 visual effect Effects 0.000 description 2
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- KTPDNYVWXJTUKG-UHFFFAOYSA-O 1-methyl-2-[2-(2-phenyl-1h-indol-3-yl)ethenyl]quinolin-1-ium Chemical compound C1=CC2=CC=CC=C2[N+](C)=C1\C=C\C(C1=CC=CC=C1N1)=C1C1=CC=CC=C1 KTPDNYVWXJTUKG-UHFFFAOYSA-O 0.000 description 1
- HUDPLKWXRLNSPC-UHFFFAOYSA-N 4-aminophthalhydrazide Chemical compound O=C1NNC(=O)C=2C1=CC(N)=CC=2 HUDPLKWXRLNSPC-UHFFFAOYSA-N 0.000 description 1
- 102100031126 6-phosphogluconolactonase Human genes 0.000 description 1
- 108010029731 6-phosphogluconolactonase Proteins 0.000 description 1
- 102000012440 Acetylcholinesterase Human genes 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 108010000239 Aequorin Proteins 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 1
- KLSJWNVTNUYHDU-UHFFFAOYSA-N Amitrole Chemical compound NC1=NC=NN1 KLSJWNVTNUYHDU-UHFFFAOYSA-N 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 108010024976 Asparaginase Proteins 0.000 description 1
- 102000015790 Asparaginase Human genes 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- LZJRNLRASBVRRX-ZDUSSCGKSA-N Boldine Chemical compound CN1CCC2=CC(O)=C(OC)C3=C2[C@@H]1CC1=C3C=C(OC)C(O)=C1 LZJRNLRASBVRRX-ZDUSSCGKSA-N 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 101150013553 CD40 gene Proteins 0.000 description 1
- 210000001239 CD8-positive, alpha-beta cytotoxic T lymphocyte Anatomy 0.000 description 1
- 101710180366 CDP-L-myo-inositol myo-inositolphosphotransferase Proteins 0.000 description 1
- 206010006895 Cachexia Diseases 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- 102100035882 Catalase Human genes 0.000 description 1
- 101710104316 Cell surface-binding protein Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 102000003910 Cyclin D Human genes 0.000 description 1
- 108090000259 Cyclin D Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 206010011953 Decreased activity Diseases 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 description 1
- 102000000587 Glycerolphosphate Dehydrogenase Human genes 0.000 description 1
- 108010041921 Glycerolphosphate Dehydrogenase Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101100099884 Homo sapiens CD40 gene Proteins 0.000 description 1
- 101000801228 Homo sapiens Tumor necrosis factor receptor superfamily member 1A Proteins 0.000 description 1
- 101000801232 Homo sapiens Tumor necrosis factor receptor superfamily member 1B Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000004195 Isomerases Human genes 0.000 description 1
- 108090000769 Isomerases Proteins 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- 108010047294 Lamins Proteins 0.000 description 1
- 102000006835 Lamins Human genes 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
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- 108010047357 Luminescent Proteins Proteins 0.000 description 1
- 102000006830 Luminescent Proteins Human genes 0.000 description 1
- 208000030289 Lymphoproliferative disease Diseases 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 102000013460 Malate Dehydrogenase Human genes 0.000 description 1
- 108010026217 Malate Dehydrogenase Proteins 0.000 description 1
- 108010059724 Micrococcal Nuclease Proteins 0.000 description 1
- QPCDCPDFJACHGM-UHFFFAOYSA-N N,N-bis{2-[bis(carboxymethyl)amino]ethyl}glycine Chemical group OC(=O)CN(CC(O)=O)CCN(CC(=O)O)CCN(CC(O)=O)CC(O)=O QPCDCPDFJACHGM-UHFFFAOYSA-N 0.000 description 1
- 108091008604 NGF receptors Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 108010053210 Phycocyanin Proteins 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 1
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 1
- 239000012083 RIPA buffer Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 208000025747 Rheumatic disease Diseases 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 101150055709 SNF1 gene Proteins 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- 102000005924 Triose-Phosphate Isomerase Human genes 0.000 description 1
- 108700015934 Triose-phosphate isomerases Proteins 0.000 description 1
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 1
- 108010046334 Urease Proteins 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000007488 abnormal function Effects 0.000 description 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- 230000002730 additional effect Effects 0.000 description 1
- 210000001789 adipocyte Anatomy 0.000 description 1
- 108010004469 allophycocyanin Proteins 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 208000022531 anorexia Diseases 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000036436 anti-hiv Effects 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 229960005475 antiinfective agent Drugs 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 229960003272 asparaginase Drugs 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 239000013060 biological fluid Substances 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 238000005415 bioluminescence Methods 0.000 description 1
- 230000029918 bioluminescence Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 239000012876 carrier material Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000007248 cellular mechanism Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 230000005754 cellular signaling Effects 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 235000010980 cellulose Nutrition 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 238000012761 co-transfection Methods 0.000 description 1
- 238000004737 colorimetric analysis Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 206010061428 decreased appetite Diseases 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 229940009976 deoxycholate Drugs 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 230000001066 destructive effect Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- ZFKJVJIDPQDDFY-UHFFFAOYSA-N fluorescamine Chemical compound C12=CC=CC=C2C(=O)OC1(C1=O)OC=C1C1=CC=CC=C1 ZFKJVJIDPQDDFY-UHFFFAOYSA-N 0.000 description 1
- 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 1
- 238000001215 fluorescent labelling Methods 0.000 description 1
- 238000005558 fluorometry Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 125000003712 glycosamine group Chemical group 0.000 description 1
- 208000024908 graft versus host disease Diseases 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 230000031146 intracellular signal transduction Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- SZVJSHCCFOBDDC-UHFFFAOYSA-N iron(II,III) oxide Inorganic materials O=[Fe]O[Fe]O[Fe]=O SZVJSHCCFOBDDC-UHFFFAOYSA-N 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 210000005053 lamin Anatomy 0.000 description 1
- 229910052747 lanthanoid Inorganic materials 0.000 description 1
- 150000002602 lanthanoids Chemical class 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 210000000265 leukocyte Anatomy 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
- 108020001756 ligand binding domains Proteins 0.000 description 1
- 238000009630 liquid culture Methods 0.000 description 1
- 210000005229 liver cell Anatomy 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 201000001268 lymphoproliferative syndrome Diseases 0.000 description 1
- 230000035800 maturation Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 238000003032 molecular docking Methods 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 229960003330 pentetic acid Drugs 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- ZWLUXSQADUDCSB-UHFFFAOYSA-N phthalaldehyde Chemical compound O=CC1=CC=CC=C1C=O ZWLUXSQADUDCSB-UHFFFAOYSA-N 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 244000062804 prey Species 0.000 description 1
- 230000000770 proinflammatory effect Effects 0.000 description 1
- 238000000751 protein extraction Methods 0.000 description 1
- 230000004850 protein–protein interaction Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 102000037983 regulatory factors Human genes 0.000 description 1
- 108091008025 regulatory factors Proteins 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 235000013024 sodium fluoride Nutrition 0.000 description 1
- 239000011775 sodium fluoride Substances 0.000 description 1
- CMZUMMUJMWNLFH-UHFFFAOYSA-N sodium metavanadate Chemical compound [Na+].[O-][V](=O)=O CMZUMMUJMWNLFH-UHFFFAOYSA-N 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 210000005166 vasculature Anatomy 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 208000016261 weight loss Diseases 0.000 description 1
- 230000004580 weight loss Effects 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
- 238000003158 yeast two-hybrid assay Methods 0.000 description 1
- 229910000166 zirconium phosphate Inorganic materials 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6402—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
- C12N9/6405—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals not being snakes
- C12N9/641—Cysteine endopeptidases (3.4.22)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70578—NGF-receptor/TNF-receptor superfamily, e.g. CD27, CD30, CD40, CD95
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/715—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons
-
- 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
- C07K16/2866—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for cytokines, lymphokines, interferons
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6472—Cysteine endopeptidases (3.4.22)
- C12N9/6475—Interleukin 1-beta convertase-like enzymes (3.4.22.10; 3.4.22.36; 3.4.22.63)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Wood Science & Technology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- General Engineering & Computer Science (AREA)
- Virology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Transmitters (AREA)
- Peptides Or Proteins (AREA)
- Steroid Compounds (AREA)
- Radar Systems Or Details Thereof (AREA)
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
IL11200294A IL112002A0 (en) | 1994-05-11 | 1994-12-15 | Modulatiors of tnf/ngf superfamily receptors, their preparation and use |
IL112692A IL112692A (en) | 1995-02-19 | 1995-02-19 | ANTIBODIES TO PROTEIN WHICH BINDS TO Fas-R |
IL11461595A IL114615A0 (en) | 1995-07-16 | 1995-07-16 | Modulators of the function of fas receptors and other proteins |
PCT/US1995/016542 WO1996018641A1 (en) | 1994-12-15 | 1995-12-14 | Modulators of the function of fas/apo1 receptors |
Publications (3)
Publication Number | Publication Date |
---|---|
NO972716D0 NO972716D0 (no) | 1997-06-12 |
NO972716L NO972716L (no) | 1997-07-11 |
NO324725B1 true NO324725B1 (no) | 2007-12-03 |
Family
ID=27271687
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO19972716A NO324725B1 (no) | 1994-12-15 | 1997-06-12 | MORT-1-protein, DNA-sekvens som koder for MORT-1 og antistoffer spesifikke for MORT-1, samt fremgangsmate for fremstilling, farmasoytiske sammensetninger og anvendelser. |
Country Status (18)
Country | Link |
---|---|
EP (1) | EP0871645B1 (fi) |
JP (1) | JP3787355B2 (fi) |
KR (1) | KR100536394B1 (fi) |
CN (1) | CN1105725C (fi) |
AT (1) | ATE377073T1 (fi) |
AU (1) | AU706401B2 (fi) |
CA (1) | CA2207815C (fi) |
CY (1) | CY2586B2 (fi) |
DE (1) | DE69535634T2 (fi) |
DK (1) | DK0871645T3 (fi) |
ES (1) | ES2292172T3 (fi) |
FI (1) | FI121273B (fi) |
HK (1) | HK1007248A1 (fi) |
MX (1) | MX9704501A (fi) |
NO (1) | NO324725B1 (fi) |
PT (1) | PT871645E (fi) |
UA (1) | UA58489C2 (fi) |
WO (1) | WO1996018641A1 (fi) |
Families Citing this family (21)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
IL114615A0 (en) * | 1995-07-16 | 1995-11-27 | Yeda Res & Dev | Modulators of the function of fas receptors and other proteins |
US6060238A (en) * | 1995-02-13 | 2000-05-09 | The Regents Of The University Of Michigan | Method and composition for regulating apoptosis |
US7097972B1 (en) | 1995-02-13 | 2006-08-29 | Regents Of The University Of Michigan | Method and composition for regulating apoptosis |
US6015665A (en) * | 1995-02-13 | 2000-01-18 | The Regents Of The University Of Michigan | Method and composition for regulating apoptosis |
AU755662B2 (en) * | 1995-02-22 | 2002-12-19 | Yeda Research And Development Co. Ltd. | Modulators of regulatory proteins |
EP0813419B8 (en) * | 1995-02-22 | 2005-08-24 | Yeda Research & Development Company, Ltd. | Modulators of regulatory proteins |
US6747138B1 (en) | 1995-04-03 | 2004-06-08 | Regents Of The University Of Michigan | Methods and compositions for regulating Fas-associated apoptosis |
US7807783B1 (en) | 1995-04-03 | 2010-10-05 | The Regents Of The University Of Michigan | Methods and compositions for regulating FAS-associated apoptosis |
US6399327B1 (en) | 1995-07-16 | 2002-06-04 | Yeda Research And Development Co. Ltd. | Modulators of the function of FAS receptors and other proteins |
US6911526B2 (en) * | 1996-07-22 | 2005-06-28 | The Trustees Of Columbia University In The City Of New York | Compounds that inhibit the interaction between signal-transducing proteins and the GLGF (PDZ/DHR) domain and uses thereof |
EP0842665A3 (en) * | 1996-11-14 | 2002-12-18 | Smithkline Beecham Corporation | Interleukin-1 beta converting enzyme like apoptotic proteases and their agonists |
US5969102A (en) * | 1997-03-03 | 1999-10-19 | St. Jude Children's Research Hospital | Lymphocyte surface receptor that binds CAML, nucleic acids encoding the same and methods of use thereof |
JP2001522247A (ja) * | 1997-04-25 | 2001-11-13 | アメリカン・ホーム・プロダクツ・コーポレイション | ニューロンmort1イソ形態 |
WO1999000499A1 (en) * | 1997-06-26 | 1999-01-07 | Chiron Corporation | Human fadd-interacting protein (fip) |
US7833529B1 (en) | 1999-01-07 | 2010-11-16 | Zymogenetics, Inc. | Methods for inhibiting B lymphocyte proliferation with soluble ztnf4 receptor |
US6015712A (en) * | 1999-07-19 | 2000-01-18 | Isis Pharmaceuticals Inc. | Antisense modulation of FADD expression |
EA010594B1 (ru) | 2001-05-24 | 2008-10-30 | Займодженетикс, Инк. | Слитые белки taci-иммуноглобулина |
US6743630B2 (en) | 2002-03-06 | 2004-06-01 | The Trustees Of Columbia University In The City Of New York | Method of preparing a protein array based on biochemical protein-protein interaction |
AU2006278227B2 (en) | 2005-08-09 | 2011-10-20 | Ares Trading S.A. | Methods for the treatment and prevention of abnormal cell proliferation using TACI-fusion molecules |
CA2618765A1 (en) | 2005-08-09 | 2007-02-15 | Zymogenetics, Inc. | Methods for treating b-cell malignancies using taci-ig fusion molecule |
UA98462C2 (ru) | 2006-05-15 | 2012-05-25 | Арес Трейдинг С.А. | Способы лечения аутоиммунных заболеваний с использованием слитой молекулы taci-ig |
Family Cites Families (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
NO178777C (no) * | 1994-05-09 | 1996-05-29 | Kvaerner Eng | Varmeveksler |
US7807783B1 (en) * | 1995-04-03 | 2010-10-05 | The Regents Of The University Of Michigan | Methods and compositions for regulating FAS-associated apoptosis |
US5674734A (en) * | 1995-05-18 | 1997-10-07 | President And Fellows Of Harvard College | Cell death protein |
-
1995
- 1995-12-14 AU AU46022/96A patent/AU706401B2/en not_active Expired
- 1995-12-14 UA UA97063391A patent/UA58489C2/uk unknown
- 1995-12-14 PT PT95944148T patent/PT871645E/pt unknown
- 1995-12-14 JP JP51932496A patent/JP3787355B2/ja not_active Expired - Lifetime
- 1995-12-14 EP EP95944148A patent/EP0871645B1/en not_active Expired - Lifetime
- 1995-12-14 KR KR1019970703992A patent/KR100536394B1/ko not_active IP Right Cessation
- 1995-12-14 CN CN95196789A patent/CN1105725C/zh not_active Expired - Lifetime
- 1995-12-14 ES ES95944148T patent/ES2292172T3/es not_active Expired - Lifetime
- 1995-12-14 WO PCT/US1995/016542 patent/WO1996018641A1/en active IP Right Grant
- 1995-12-14 AT AT95944148T patent/ATE377073T1/de active
- 1995-12-14 DE DE69535634T patent/DE69535634T2/de not_active Expired - Lifetime
- 1995-12-14 CA CA2207815A patent/CA2207815C/en not_active Expired - Lifetime
- 1995-12-14 DK DK95944148T patent/DK0871645T3/da active
- 1995-12-14 MX MX9704501A patent/MX9704501A/es active IP Right Grant
-
1997
- 1997-06-10 FI FI972457A patent/FI121273B/fi not_active IP Right Cessation
- 1997-06-12 NO NO19972716A patent/NO324725B1/no not_active IP Right Cessation
-
1998
- 1998-06-24 HK HK98106458A patent/HK1007248A1/xx not_active IP Right Cessation
-
2007
- 2007-11-20 CY CY0700017A patent/CY2586B2/xx unknown
Also Published As
Publication number | Publication date |
---|---|
JP3787355B2 (ja) | 2006-06-21 |
NO972716D0 (no) | 1997-06-12 |
PT871645E (pt) | 2007-11-14 |
UA58489C2 (uk) | 2003-08-15 |
EP0871645A1 (en) | 1998-10-21 |
EP0871645B1 (en) | 2007-10-31 |
DE69535634T2 (de) | 2008-08-28 |
KR100536394B1 (ko) | 2006-04-21 |
FI972457A (fi) | 1997-06-10 |
CY2586B2 (en) | 2009-11-04 |
FI121273B (fi) | 2010-09-15 |
CA2207815C (en) | 2011-03-29 |
NO972716L (no) | 1997-07-11 |
AU4602296A (en) | 1996-07-03 |
CA2207815A1 (en) | 1996-06-20 |
AU706401B2 (en) | 1999-06-17 |
MX9704501A (es) | 1997-10-31 |
DK0871645T3 (da) | 2007-12-03 |
ATE377073T1 (de) | 2007-11-15 |
ES2292172T3 (es) | 2008-03-01 |
WO1996018641A1 (en) | 1996-06-20 |
FI972457A0 (fi) | 1997-06-10 |
EP0871645A4 (en) | 1999-11-24 |
DE69535634D1 (de) | 2007-12-13 |
JPH10510712A (ja) | 1998-10-20 |
CN1105725C (zh) | 2003-04-16 |
CN1169729A (zh) | 1998-01-07 |
HK1007248A1 (en) | 1999-04-09 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US20070166787A1 (en) | Modulators of regulatory proteins | |
NO324725B1 (no) | MORT-1-protein, DNA-sekvens som koder for MORT-1 og antistoffer spesifikke for MORT-1, samt fremgangsmate for fremstilling, farmasoytiske sammensetninger og anvendelser. | |
JP3980641B2 (ja) | Fas受容体およびほかのタンパク質の機能のモジュレーター | |
NO321514B1 (no) | DNA-sekvens som koder for modulatorer for TNF/NGF superfamiliereseptorer, samt protein, farmasoytisk sammensetning, vektor, fremgangsmater og anvendelser derav. | |
JP3860608B2 (ja) | 調節タンパク質のモジュレーター | |
NO327054B1 (no) | Polypeptid som bindes til TRAF2, samt fremgangsmate for fremstilling og isolering og identifisering derav og DNA-sekvens, vektor, transformerte eukaryote eller prokariote vertsceller, antistoffer, farmasoytisk sammensetning anvendelse derav. | |
WO1996018641A9 (en) | Modulators of the function of fas/apo1 receptors | |
IL109632A (en) | Modulators of the function of tnf receptors | |
JP4351389B2 (ja) | Tnf/ngfレセプターファミリーおよびほかのタンパク質のレセプター機能調節物質 | |
EP1058691A1 (en) | Caspase-8 interacting proteins | |
US7323548B2 (en) | Modulators of the function of FAS/APO1 receptors | |
US7108999B1 (en) | Modulators of the function of FAS/AP01 receptors | |
AU755662B2 (en) | Modulators of regulatory proteins | |
RU2241747C2 (ru) | Молекула днк, кодирующая полипептид, способный связываться с внутриклеточным доменом рецептора лиганда fas(fas-ic), полипептид, способ его получения, вектор, способ модуляции действия лиганда fas-r на клетки (варианты), фармацевтическая композиция (варианты), спрособ выделения и идентификации белка | |
AU2003200969B2 (en) | Modulators of the function of receptors of the TNF/NGF receptor family and other proteins | |
AU5133296A (en) | Modulators of regulatory proteins | |
IL112692A (en) | ANTIBODIES TO PROTEIN WHICH BINDS TO Fas-R | |
EP1454985A2 (en) | Modulators of receptors of the tnf/ngf receptor family | |
IL126428A (en) | Modulators of tnf receptor associated factor (traf), their preparation and use | |
AU3508101A (en) | Modulators of TNF receptor associated factor (TRAF), their preparation and use |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
MK1K | Patent expired |