NO333085B1 - Opploselig CRAM-1 polypeptid antistoff rettet mot CRAM-1 og som modulerer transendotelial migrering av leukocytter, samt anvendelse derav for fremstilling av medikamenter for inhibering av angiogenese i tumorer. - Google Patents
Opploselig CRAM-1 polypeptid antistoff rettet mot CRAM-1 og som modulerer transendotelial migrering av leukocytter, samt anvendelse derav for fremstilling av medikamenter for inhibering av angiogenese i tumorer.Info
- Publication number
- NO333085B1 NO333085B1 NO20014417A NO20014417A NO333085B1 NO 333085 B1 NO333085 B1 NO 333085B1 NO 20014417 A NO20014417 A NO 20014417A NO 20014417 A NO20014417 A NO 20014417A NO 333085 B1 NO333085 B1 NO 333085B1
- Authority
- NO
- Norway
- Prior art keywords
- cram
- jam
- cells
- cell
- endothelial
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 26
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 24
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 22
- 206010028980 Neoplasm Diseases 0.000 title claims abstract description 20
- 210000000265 leukocyte Anatomy 0.000 title claims description 21
- 230000005012 migration Effects 0.000 title claims description 12
- 238000013508 migration Methods 0.000 title claims description 12
- 229940079593 drug Drugs 0.000 title claims description 9
- 239000003814 drug Substances 0.000 title claims description 9
- 230000033115 angiogenesis Effects 0.000 title claims description 8
- 230000002401 inhibitory effect Effects 0.000 title claims description 3
- 238000002360 preparation method Methods 0.000 title description 2
- 230000001105 regulatory effect Effects 0.000 claims abstract description 18
- 241001529936 Murinae Species 0.000 claims abstract description 12
- 108060003951 Immunoglobulin Proteins 0.000 claims abstract description 9
- 102000018358 immunoglobulin Human genes 0.000 claims abstract description 9
- 206010061218 Inflammation Diseases 0.000 claims abstract description 8
- 230000004054 inflammatory process Effects 0.000 claims abstract description 8
- KZMAWJRXKGLWGS-UHFFFAOYSA-N 2-chloro-n-[4-(4-methoxyphenyl)-1,3-thiazol-2-yl]-n-(3-methoxypropyl)acetamide Chemical compound S1C(N(C(=O)CCl)CCCOC)=NC(C=2C=CC(OC)=CC=2)=C1 KZMAWJRXKGLWGS-UHFFFAOYSA-N 0.000 claims abstract description 6
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 4
- 210000004027 cell Anatomy 0.000 claims description 148
- 150000001413 amino acids Chemical class 0.000 claims description 31
- 102000002110 C2 domains Human genes 0.000 claims description 11
- 108050009459 C2 domains Proteins 0.000 claims description 11
- 238000004519 manufacturing process Methods 0.000 claims description 7
- 230000002285 radioactive effect Effects 0.000 claims description 4
- 239000003053 toxin Substances 0.000 claims description 3
- 231100000765 toxin Toxicity 0.000 claims description 3
- 108700012359 toxins Proteins 0.000 claims description 3
- 230000000903 blocking effect Effects 0.000 claims description 2
- 230000002255 enzymatic effect Effects 0.000 claims description 2
- 239000002502 liposome Substances 0.000 claims description 2
- 108010040135 Junctional Adhesion Molecule C Proteins 0.000 description 66
- 102100023429 Junctional adhesion molecule C Human genes 0.000 description 66
- 108010040149 Junctional Adhesion Molecule B Proteins 0.000 description 62
- 210000002889 endothelial cell Anatomy 0.000 description 56
- 239000000047 product Substances 0.000 description 50
- 238000013518 transcription Methods 0.000 description 30
- 230000035897 transcription Effects 0.000 description 30
- 108090000623 proteins and genes Proteins 0.000 description 27
- 230000014509 gene expression Effects 0.000 description 25
- 108010040082 Junctional Adhesion Molecule A Proteins 0.000 description 24
- 102100022304 Junctional adhesion molecule A Human genes 0.000 description 24
- 239000002299 complementary DNA Substances 0.000 description 23
- 238000003752 polymerase chain reaction Methods 0.000 description 23
- 235000018102 proteins Nutrition 0.000 description 21
- 102000004169 proteins and genes Human genes 0.000 description 21
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 19
- 238000000034 method Methods 0.000 description 19
- 210000001519 tissue Anatomy 0.000 description 18
- 108010048367 enhanced green fluorescent protein Proteins 0.000 description 17
- 238000010186 staining Methods 0.000 description 16
- 102100024441 Dihydropyrimidinase-related protein 5 Human genes 0.000 description 15
- 101001053479 Homo sapiens Dihydropyrimidinase-related protein 5 Proteins 0.000 description 15
- 230000003511 endothelial effect Effects 0.000 description 14
- 230000006870 function Effects 0.000 description 14
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 13
- 238000004458 analytical method Methods 0.000 description 13
- 238000003556 assay Methods 0.000 description 13
- 230000035699 permeability Effects 0.000 description 12
- 235000001014 amino acid Nutrition 0.000 description 11
- 108020004999 messenger RNA Proteins 0.000 description 11
- 239000013598 vector Substances 0.000 description 11
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 10
- 230000000694 effects Effects 0.000 description 10
- 210000001165 lymph node Anatomy 0.000 description 10
- 230000033228 biological regulation Effects 0.000 description 9
- 210000003038 endothelium Anatomy 0.000 description 9
- 238000001114 immunoprecipitation Methods 0.000 description 9
- 238000001890 transfection Methods 0.000 description 9
- 210000004881 tumor cell Anatomy 0.000 description 9
- 102000003390 tumor necrosis factor Human genes 0.000 description 9
- 238000002474 experimental method Methods 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- 238000000636 Northern blotting Methods 0.000 description 7
- 238000009826 distribution Methods 0.000 description 7
- 238000012360 testing method Methods 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 6
- 239000013553 cell monolayer Substances 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- 238000010367 cloning Methods 0.000 description 6
- 238000009396 hybridization Methods 0.000 description 6
- 210000003734 kidney Anatomy 0.000 description 6
- 239000010410 layer Substances 0.000 description 6
- 239000003550 marker Substances 0.000 description 6
- 230000007246 mechanism Effects 0.000 description 6
- 239000002609 medium Substances 0.000 description 6
- 201000001441 melanoma Diseases 0.000 description 6
- 239000002773 nucleotide Substances 0.000 description 6
- 125000003729 nucleotide group Chemical group 0.000 description 6
- 238000003757 reverse transcription PCR Methods 0.000 description 6
- 230000008685 targeting Effects 0.000 description 6
- 201000009030 Carcinoma Diseases 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 101150044441 PECAM1 gene Proteins 0.000 description 5
- 102100024616 Platelet endothelial cell adhesion molecule Human genes 0.000 description 5
- 230000002491 angiogenic effect Effects 0.000 description 5
- 230000001086 cytosolic effect Effects 0.000 description 5
- 230000003993 interaction Effects 0.000 description 5
- 210000004698 lymphocyte Anatomy 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 210000001986 peyer's patch Anatomy 0.000 description 5
- 239000002356 single layer Substances 0.000 description 5
- 230000002792 vascular Effects 0.000 description 5
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 4
- 230000004988 N-glycosylation Effects 0.000 description 4
- 102000003940 Occludin Human genes 0.000 description 4
- 108090000304 Occludin Proteins 0.000 description 4
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 4
- 230000003321 amplification Effects 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 230000001351 cycling effect Effects 0.000 description 4
- 230000003247 decreasing effect Effects 0.000 description 4
- 230000013020 embryo development Effects 0.000 description 4
- 210000003989 endothelium vascular Anatomy 0.000 description 4
- 239000012634 fragment Substances 0.000 description 4
- 230000004807 localization Effects 0.000 description 4
- 238000012423 maintenance Methods 0.000 description 4
- 239000013642 negative control Substances 0.000 description 4
- 238000003199 nucleic acid amplification method Methods 0.000 description 4
- 210000000056 organ Anatomy 0.000 description 4
- 230000026731 phosphorylation Effects 0.000 description 4
- 238000006366 phosphorylation reaction Methods 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 108091026890 Coding region Proteins 0.000 description 3
- 102000029816 Collagenase Human genes 0.000 description 3
- 108060005980 Collagenase Proteins 0.000 description 3
- 229920002307 Dextran Polymers 0.000 description 3
- 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 3
- 208000001382 Experimental Melanoma Diseases 0.000 description 3
- 102000003974 Fibroblast growth factor 2 Human genes 0.000 description 3
- 108090000379 Fibroblast growth factor 2 Proteins 0.000 description 3
- 125000002842 L-seryl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])O[H] 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- 108700026244 Open Reading Frames Proteins 0.000 description 3
- 102100021669 Stromal cell-derived factor 1 Human genes 0.000 description 3
- 101710088580 Stromal cell-derived factor 1 Proteins 0.000 description 3
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
- 108010022164 acetyl-LDL Proteins 0.000 description 3
- 230000004888 barrier function Effects 0.000 description 3
- 239000011324 bead Substances 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 229960002424 collagenase Drugs 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 108010007093 dispase Proteins 0.000 description 3
- 230000003828 downregulation Effects 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 108020001507 fusion proteins Proteins 0.000 description 3
- 102000037865 fusion proteins Human genes 0.000 description 3
- 238000003364 immunohistochemistry Methods 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 3
- 239000004417 polycarbonate Substances 0.000 description 3
- 239000011148 porous material Substances 0.000 description 3
- 230000000284 resting effect Effects 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 210000004988 splenocyte Anatomy 0.000 description 3
- 238000010865 video microscopy Methods 0.000 description 3
- 102000007469 Actins Human genes 0.000 description 2
- 108010085238 Actins Proteins 0.000 description 2
- 240000006108 Allium ampeloprasum Species 0.000 description 2
- 235000005254 Allium ampeloprasum Nutrition 0.000 description 2
- 108010012236 Chemokines Proteins 0.000 description 2
- 102000019034 Chemokines Human genes 0.000 description 2
- 241001301450 Crocidium multicaule Species 0.000 description 2
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 2
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 2
- 108010010803 Gelatin Proteins 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 102000018251 Hypoxanthine Phosphoribosyltransferase Human genes 0.000 description 2
- 108010091358 Hypoxanthine Phosphoribosyltransferase Proteins 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 108090000184 Selectins Proteins 0.000 description 2
- 102000003800 Selectins Human genes 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 108010090804 Streptavidin Proteins 0.000 description 2
- 210000001744 T-lymphocyte Anatomy 0.000 description 2
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 2
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 2
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 2
- 206010052428 Wound Diseases 0.000 description 2
- 208000027418 Wounds and injury Diseases 0.000 description 2
- 230000006287 biotinylation Effects 0.000 description 2
- 238000007413 biotinylation Methods 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000004204 blood vessel Anatomy 0.000 description 2
- 230000023402 cell communication Effects 0.000 description 2
- 230000022131 cell cycle Effects 0.000 description 2
- 230000008614 cellular interaction Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 230000001054 cortical effect Effects 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 238000010494 dissociation reaction Methods 0.000 description 2
- 230000005593 dissociations Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 210000002919 epithelial cell Anatomy 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 210000002744 extracellular matrix Anatomy 0.000 description 2
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 239000008273 gelatin Substances 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 235000011852 gelatine desserts Nutrition 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 238000010185 immunofluorescence analysis Methods 0.000 description 2
- 102000006495 integrins Human genes 0.000 description 2
- 108010044426 integrins Proteins 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 238000010232 migration assay Methods 0.000 description 2
- 210000000066 myeloid cell Anatomy 0.000 description 2
- 150000007523 nucleic acids Chemical group 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 229920000515 polycarbonate Polymers 0.000 description 2
- 108091033319 polynucleotide Proteins 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000003753 real-time PCR Methods 0.000 description 2
- 238000007789 sealing Methods 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 206010041823 squamous cell carcinoma Diseases 0.000 description 2
- 230000004936 stimulating effect Effects 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- MPLHNVLQVRSVEE-UHFFFAOYSA-N texas red Chemical compound [O-]S(=O)(=O)C1=CC(S(Cl)(=O)=O)=CC=C1C(C1=CC=2CCCN3CCCC(C=23)=C1O1)=C2C1=C(CCC1)C3=[N+]1CCCC3=C2 MPLHNVLQVRSVEE-UHFFFAOYSA-N 0.000 description 2
- 210000001578 tight junction Anatomy 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 230000008728 vascular permeability Effects 0.000 description 2
- 210000005166 vasculature Anatomy 0.000 description 2
- 210000000264 venule Anatomy 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 108020005544 Antisense RNA Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 238000011537 Coomassie blue staining Methods 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 101100364969 Dictyostelium discoideum scai gene Proteins 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 1
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 1
- 101000996823 Homo sapiens Cell surface A33 antigen Proteins 0.000 description 1
- 101001055144 Homo sapiens Interleukin-2 receptor subunit alpha Proteins 0.000 description 1
- 101150003028 Hprt1 gene Proteins 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 102100026878 Interleukin-2 receptor subunit alpha Human genes 0.000 description 1
- 108090001007 Interleukin-8 Proteins 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 125000000769 L-threonyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])[C@](O[H])(C([H])([H])[H])[H] 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 108010007622 LDL Lipoproteins Proteins 0.000 description 1
- 101001050319 Mus musculus Junctional adhesion molecule B Proteins 0.000 description 1
- 101001050316 Mus musculus Junctional adhesion molecule C Proteins 0.000 description 1
- 101100364971 Mus musculus Scai gene Proteins 0.000 description 1
- 108010069196 Neural Cell Adhesion Molecules Proteins 0.000 description 1
- 102100023616 Neural cell adhesion molecule L1-like protein Human genes 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 108010002747 Pfu DNA polymerase Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 102000003923 Protein Kinase C Human genes 0.000 description 1
- 108090000315 Protein Kinase C Proteins 0.000 description 1
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 1
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 238000000692 Student's t-test Methods 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 108091036066 Three prime untranslated region Proteins 0.000 description 1
- 108010002321 Tight Junction Proteins Proteins 0.000 description 1
- 102000000591 Tight Junction Proteins Human genes 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- GLNADSQYFUSGOU-GPTZEZBUSA-J Trypan blue Chemical compound [Na+].[Na+].[Na+].[Na+].C1=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(/N=N/C3=CC=C(C=C3C)C=3C=C(C(=CC=3)\N=N\C=3C(=CC4=CC(=CC(N)=C4C=3O)S([O-])(=O)=O)S([O-])(=O)=O)C)=C(O)C2=C1N GLNADSQYFUSGOU-GPTZEZBUSA-J 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 102000008790 VE-cadherin Human genes 0.000 description 1
- 108010000134 Vascular Cell Adhesion Molecule-1 Proteins 0.000 description 1
- 102100023543 Vascular cell adhesion protein 1 Human genes 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 230000001464 adherent effect Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000003277 amino acid sequence analysis Methods 0.000 description 1
- 230000003698 anagen phase Effects 0.000 description 1
- 239000002870 angiogenesis inducing agent Substances 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 108091006004 biotinylated proteins Proteins 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 108010018828 cadherin 5 Proteins 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 208000037976 chronic inflammation Diseases 0.000 description 1
- 230000006020 chronic inflammation Effects 0.000 description 1
- 238000003501 co-culture Methods 0.000 description 1
- 230000008045 co-localization Effects 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000003184 complementary RNA Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 108091036078 conserved sequence Proteins 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 230000000212 effect on lymphocytes Effects 0.000 description 1
- 230000010595 endothelial cell migration Effects 0.000 description 1
- 210000004407 endothelial cell of postcapillary venule of lymph node Anatomy 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 210000003386 epithelial cell of thymus gland Anatomy 0.000 description 1
- 210000000981 epithelium Anatomy 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 230000020764 fibrinolysis Effects 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 238000002073 fluorescence micrograph Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 239000005090 green fluorescent protein Substances 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 230000013632 homeostatic process Effects 0.000 description 1
- 102000054366 human GPA33 Human genes 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000003365 immunocytochemistry Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 238000002991 immunohistochemical analysis Methods 0.000 description 1
- 239000012133 immunoprecipitate Substances 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000003455 independent Effects 0.000 description 1
- 230000028709 inflammatory response Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 210000004692 intercellular junction Anatomy 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 230000009545 invasion Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 230000001926 lymphatic effect Effects 0.000 description 1
- 210000001365 lymphatic vessel Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 239000003068 molecular probe Substances 0.000 description 1
- 238000010172 mouse model Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 238000007857 nested PCR Methods 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000008288 physiological mechanism Effects 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 230000007542 postnatal development Effects 0.000 description 1
- 239000013615 primer Substances 0.000 description 1
- 239000002987 primer (paints) Substances 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 238000003153 stable transfection Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000012353 t test Methods 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- 230000002992 thymic effect Effects 0.000 description 1
- 210000001541 thymus gland Anatomy 0.000 description 1
- 230000030968 tissue homeostasis Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 238000003146 transient transfection Methods 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 210000004926 tubular epithelial cell Anatomy 0.000 description 1
- 230000005748 tumor development Effects 0.000 description 1
- 230000004614 tumor growth Effects 0.000 description 1
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
- 210000004291 uterus Anatomy 0.000 description 1
- 210000005167 vascular cell Anatomy 0.000 description 1
- 230000037197 vascular physiology Effects 0.000 description 1
- 230000004862 vasculogenesis Effects 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70503—Immunoglobulin superfamily
-
- 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
- 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
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/582—Recycling of unreacted starting or intermediate materials
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Cell Biology (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Cardiology (AREA)
- Rheumatology (AREA)
- Heart & Thoracic Surgery (AREA)
- Pain & Pain Management (AREA)
- Transplantation (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Materials For Medical Uses (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP99200746 | 1999-03-11 | ||
| PCT/EP2000/002219 WO2000053749A2 (fr) | 1999-03-11 | 2000-03-13 | Molecules d'adhesion vasculaire et modulation de leur fonction |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO20014417D0 NO20014417D0 (no) | 2001-09-11 |
| NO20014417L NO20014417L (no) | 2001-11-12 |
| NO333085B1 true NO333085B1 (no) | 2013-02-25 |
Family
ID=8239973
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO20014417A NO333085B1 (no) | 1999-03-11 | 2001-09-11 | Opploselig CRAM-1 polypeptid antistoff rettet mot CRAM-1 og som modulerer transendotelial migrering av leukocytter, samt anvendelse derav for fremstilling av medikamenter for inhibering av angiogenese i tumorer. |
Country Status (23)
| Country | Link |
|---|---|
| US (3) | US7393651B2 (fr) |
| EP (2) | EP1163337B1 (fr) |
| JP (2) | JP4836329B2 (fr) |
| CN (2) | CN1637019A (fr) |
| AT (1) | ATE500328T1 (fr) |
| AU (1) | AU782139B2 (fr) |
| BR (1) | BR0008915A (fr) |
| CA (1) | CA2362896C (fr) |
| CZ (1) | CZ303128B6 (fr) |
| DE (1) | DE60045681D1 (fr) |
| EE (1) | EE05497B1 (fr) |
| ES (1) | ES2361905T3 (fr) |
| HK (1) | HK1044169A1 (fr) |
| HU (1) | HU229376B1 (fr) |
| IL (1) | IL145310A0 (fr) |
| IS (1) | IS2819B (fr) |
| MX (1) | MXPA01009110A (fr) |
| NO (1) | NO333085B1 (fr) |
| NZ (1) | NZ514091A (fr) |
| PL (1) | PL207994B1 (fr) |
| RU (1) | RU2244748C2 (fr) |
| WO (1) | WO2000053749A2 (fr) |
| ZA (1) | ZA200107283B (fr) |
Families Citing this family (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8088386B2 (en) | 1998-03-20 | 2012-01-03 | Genentech, Inc. | Treatment of complement-associated disorders |
| US8007798B2 (en) | 1997-11-21 | 2011-08-30 | Genentech, Inc. | Treatment of complement-associated disorders |
| EE05497B1 (et) * | 1999-03-11 | 2011-12-15 | Rmf Dictagene S.A. | Polüpeptiid, lahustuv CRAM-1 polüpeptiid, polünukleotiid ja antikeha |
| GB0100750D0 (en) * | 2001-01-11 | 2001-02-21 | Inpharmatica Ltd | Novel proteins |
| WO2003006673A2 (fr) * | 2001-07-11 | 2003-01-23 | Texas Biotechnology Corporation | Acide nucleique codant une proteine d'adhesion jonctionnelle humaine (jam3) |
| US7642341B2 (en) | 2003-12-18 | 2010-01-05 | Merck Serono S.A. | Angiogenesis inhibiting molecules, their selection, production and their use in the treatment of cancer |
| EP1533617A1 (fr) * | 2003-11-19 | 2005-05-25 | RMF Dictagene S.A. | Molécules inhibant l'angiogénèse, leur sélection, production et utilisation pour le traitement et diagnose du cancer |
| CN107929731A (zh) | 2005-11-04 | 2018-04-20 | 健泰科生物技术公司 | 利用补体途径抑制剂治疗眼部疾病 |
| RU2464030C2 (ru) * | 2006-05-26 | 2012-10-20 | Регадо Байосайенсиз, Инк. | Введение противосвертывающей системы reg1 |
| US8007797B2 (en) | 2006-09-28 | 2011-08-30 | Merck Serono S.A. | Junctional adhesion molecule-C (JAM-C) binding compounds and methods of their use |
| ES2700609T3 (es) | 2006-11-02 | 2019-02-18 | Genentech Inc | Anticuerpos anti-factor D humanizados y sus usos |
| FR2909092B1 (fr) * | 2006-11-24 | 2012-10-19 | Pf Medicament | Nouveaux anticorps anti-proliferation |
| AR066660A1 (es) | 2007-05-23 | 2009-09-02 | Genentech Inc | Prevencion y tratamiento de condiciones del ojo asociadas con su complemento |
| PL2190991T3 (pl) * | 2007-08-06 | 2020-05-18 | Noxxon Pharma Ag | Kwasy nukleinowe wiążące sdf-1 i ich zastosowanie |
| CR20170001A (es) | 2008-04-28 | 2017-08-10 | Genentech Inc | Anticuerpos anti factor d humanizados |
| KR20180021234A (ko) | 2013-08-12 | 2018-02-28 | 제넨테크, 인크. | 보체-연관 상태의 치료를 위한 조성물 및 방법 |
| WO2015168468A1 (fr) | 2014-05-01 | 2015-11-05 | Genentech, Inc. | Variants d'anticorps anti-facteur d et leurs utilisations |
| EP3368090A1 (fr) | 2015-10-30 | 2018-09-05 | H. Hoffnabb-La Roche Ag | Conjugués de variants d'anticorps anti-facteur d et leurs utilisations |
| JP2018534930A (ja) | 2015-10-30 | 2018-11-29 | ジェネンテック， インコーポレイテッド | 抗ｄ因子抗体及びコンジュゲート |
Family Cites Families (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2000053753A2 (fr) * | 1999-03-08 | 2000-09-14 | Genentech, Inc. | Activation ou inhibition de l'angiogenese et de la cardiovascularisation |
| US20030170864A1 (en) * | 2000-05-30 | 2003-09-11 | Genentech, Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| WO2000036102A2 (fr) * | 1998-12-16 | 2000-06-22 | Genentech, Inc. | Polypeptides secretes et transmembranaires et acides nucleiques codant pour ceux-ci |
| SE9604470D0 (sv) * | 1996-12-04 | 1996-12-04 | Tamas Bartfai Konsulting Ab | Transmembrane component of tight junction |
| JP2001524814A (ja) * | 1997-03-14 | 2001-12-04 | ヒューマン・ジェノム・サイエンシズ・インコーポレイテッド | ２８種類のヒト分泌タンパク質 |
| WO1998042739A2 (fr) * | 1997-03-21 | 1998-10-01 | Genetics Institute, Inc. | Proteines secretees et polynucleotides les codant |
| WO1999006551A2 (fr) | 1997-08-01 | 1999-02-11 | Genset | Est 5' pour proteines secretees identifiees dans le tissu cerebral |
| US20030092002A1 (en) * | 1997-09-17 | 2003-05-15 | Genentech, Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| EP1002864A1 (fr) * | 1998-11-10 | 2000-05-24 | Universita' degli studi di Bologna | HIgR et domaine V relié pour la préparation d'un médicament pour la prévention et le traitement des infections de HSV-1, HSV-2 et BHV |
| EE05497B1 (et) * | 1999-03-11 | 2011-12-15 | Rmf Dictagene S.A. | Polüpeptiid, lahustuv CRAM-1 polüpeptiid, polünukleotiid ja antikeha |
| EP1533617A1 (fr) | 2003-11-19 | 2005-05-25 | RMF Dictagene S.A. | Molécules inhibant l'angiogénèse, leur sélection, production et utilisation pour le traitement et diagnose du cancer |
| US7642341B2 (en) * | 2003-12-18 | 2010-01-05 | Merck Serono S.A. | Angiogenesis inhibiting molecules, their selection, production and their use in the treatment of cancer |
-
2000
- 2000-03-13 EE EEP200100472A patent/EE05497B1/xx not_active IP Right Cessation
- 2000-03-13 ES ES00920497T patent/ES2361905T3/es not_active Expired - Lifetime
- 2000-03-13 EP EP00920497A patent/EP1163337B1/fr not_active Expired - Lifetime
- 2000-03-13 WO PCT/EP2000/002219 patent/WO2000053749A2/fr active Application Filing
- 2000-03-13 AT AT00920497T patent/ATE500328T1/de not_active IP Right Cessation
- 2000-03-13 RU RU2001127668/13A patent/RU2244748C2/ru not_active IP Right Cessation
- 2000-03-13 AU AU41051/00A patent/AU782139B2/en not_active Expired
- 2000-03-13 EP EP10181055A patent/EP2292761A1/fr not_active Withdrawn
- 2000-03-13 CZ CZ20013267A patent/CZ303128B6/cs not_active IP Right Cessation
- 2000-03-13 CN CNA2004100952754A patent/CN1637019A/zh active Pending
- 2000-03-13 PL PL350417A patent/PL207994B1/pl not_active IP Right Cessation
- 2000-03-13 IL IL14531000A patent/IL145310A0/xx unknown
- 2000-03-13 JP JP2000603370A patent/JP4836329B2/ja not_active Expired - Lifetime
- 2000-03-13 HU HU0200606A patent/HU229376B1/hu not_active IP Right Cessation
- 2000-03-13 BR BR0008915-0A patent/BR0008915A/pt not_active Application Discontinuation
- 2000-03-13 DE DE60045681T patent/DE60045681D1/de not_active Expired - Lifetime
- 2000-03-13 CN CNB008063206A patent/CN100469878C/zh not_active Expired - Lifetime
- 2000-03-13 CA CA2362896A patent/CA2362896C/fr not_active Expired - Lifetime
- 2000-03-13 MX MXPA01009110A patent/MXPA01009110A/es active IP Right Grant
- 2000-03-13 NZ NZ514091A patent/NZ514091A/xx not_active IP Right Cessation
-
2001
- 2001-09-03 ZA ZA200107283A patent/ZA200107283B/xx unknown
- 2001-09-10 IS IS6072A patent/IS2819B/is unknown
- 2001-09-11 NO NO20014417A patent/NO333085B1/no not_active IP Right Cessation
-
2002
- 2002-06-19 HK HK02104558.4A patent/HK1044169A1/xx not_active IP Right Cessation
-
2004
- 2004-12-30 US US11/025,834 patent/US7393651B2/en not_active Expired - Fee Related
-
2008
- 2008-06-12 US US12/137,898 patent/US7670826B2/en not_active Expired - Fee Related
-
2010
- 2010-02-10 US US12/703,439 patent/US8143056B2/en not_active Expired - Fee Related
- 2010-05-06 JP JP2010106164A patent/JP2010233572A/ja active Pending
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US7670826B2 (en) | Confluence regulated adhesion molecules useful in modulating vascular permeability | |
| US6379925B1 (en) | Angiogenic modulation by notch signal transduction | |
| US5597725A (en) | Cadherin-specific antibodies and hybridoma cell lines | |
| WO1998057621A1 (fr) | Modulation angiogenique par transduction du signal de notch | |
| EP1074618A2 (fr) | Eléments et procédés permettant la production de cadherines | |
| CA2542171A1 (fr) | Modulateurs et modulation de l'interaction entre les rgm et la neogenine | |
| JP4326944B2 (ja) | ナチュラルキラー細胞活性に関与する表面分子ｎｔｂ−ａ | |
| EP1187917B1 (fr) | Variante d'epissage de cd44 associee a la polyarthrite rhumatoide | |
| WO2018138185A1 (fr) | Nouveaux récepteurs de lymphocytes t et thérapie immunitaire les utilisant pour le traitement du cancer et de maladies infectieuses | |
| EP2006299A1 (fr) | Identification de nouveaux isoformes du récepteur CD160 spécifique de classe I MHC et utilisations associées | |
| US6447776B1 (en) | Mutations of E cadherin as a basis for the diagnosis and therapy of human malignant tumors | |
| EP1646657B1 (fr) | Anticorps anti-cd44vra et leurs procedes d'utilisation | |
| AU2005202246B8 (en) | Vascular adhesion molecules and modulation of their function | |
| AU2008201101B2 (en) | Vascular adhesion molecules and modulation of their function | |
| WO1998004697A9 (fr) | Proteine et gene suppresseur de tumeur cdo | |
| WO1998004697A1 (fr) | Proteine et gene suppresseur de tumeur cdo | |
| ZA200109315B (en) | OX2 receptor homologs. |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM1K | Lapsed by not paying the annual fees |