NZ264529A - Fibroblast growth factor analogues which have mutations at a heparin binding site - Google Patents
Fibroblast growth factor analogues which have mutations at a heparin binding siteInfo
- Publication number
- NZ264529A NZ264529A NZ264529A NZ26452994A NZ264529A NZ 264529 A NZ264529 A NZ 264529A NZ 264529 A NZ264529 A NZ 264529A NZ 26452994 A NZ26452994 A NZ 26452994A NZ 264529 A NZ264529 A NZ 264529A
- Authority
- NZ
- New Zealand
- Prior art keywords
- fgf
- analogues
- heparin
- growth factor
- seq
- Prior art date
Links
- 102000018233 Fibroblast Growth Factor Human genes 0.000 title abstract description 70
- 108050007372 Fibroblast Growth Factor Proteins 0.000 title abstract description 70
- 230000027455 binding Effects 0.000 title abstract description 61
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 title abstract description 60
- 229920000669 heparin Polymers 0.000 title abstract description 59
- 229960002897 heparin Drugs 0.000 title abstract description 59
- 230000035772 mutation Effects 0.000 title abstract description 19
- 229940126864 fibroblast growth factor Drugs 0.000 title description 60
- 108090000379 Fibroblast growth factor 2 Proteins 0.000 claims description 74
- 102000003974 Fibroblast growth factor 2 Human genes 0.000 claims description 74
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 16
- 230000004071 biological effect Effects 0.000 abstract description 18
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 abstract description 14
- 239000003102 growth factor Substances 0.000 abstract description 12
- 230000002378 acidificating effect Effects 0.000 abstract description 9
- 238000012217 deletion Methods 0.000 abstract description 9
- 230000037430 deletion Effects 0.000 abstract description 9
- 108010001857 Cell Surface Receptors Proteins 0.000 abstract description 8
- 230000007935 neutral effect Effects 0.000 abstract description 8
- 230000010556 Heparin Binding Activity Effects 0.000 abstract description 5
- 102000006240 membrane receptors Human genes 0.000 abstract description 2
- 210000004027 cell Anatomy 0.000 description 43
- 108020004414 DNA Proteins 0.000 description 34
- 108090000623 proteins and genes Proteins 0.000 description 22
- 108091034117 Oligonucleotide Proteins 0.000 description 19
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 17
- 239000012634 fragment Substances 0.000 description 17
- 230000000694 effects Effects 0.000 description 16
- 150000007523 nucleic acids Chemical group 0.000 description 15
- 108020004707 nucleic acids Proteins 0.000 description 14
- 102000039446 nucleic acids Human genes 0.000 description 14
- 102000004196 processed proteins & peptides Human genes 0.000 description 14
- 108090000765 processed proteins & peptides Proteins 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 14
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 13
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 13
- 235000018102 proteins Nutrition 0.000 description 13
- 239000013598 vector Substances 0.000 description 13
- 230000003247 decreasing effect Effects 0.000 description 12
- 229920001184 polypeptide Polymers 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 11
- 230000002829 reductive effect Effects 0.000 description 11
- 102000005962 receptors Human genes 0.000 description 10
- 108020003175 receptors Proteins 0.000 description 10
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 9
- 235000001014 amino acid Nutrition 0.000 description 9
- 229940024606 amino acid Drugs 0.000 description 9
- 230000002297 mitogenic effect Effects 0.000 description 9
- 101150021185 FGF gene Proteins 0.000 description 8
- 101001052035 Homo sapiens Fibroblast growth factor 2 Proteins 0.000 description 8
- 102000000844 Cell Surface Receptors Human genes 0.000 description 7
- 150000001413 amino acids Chemical class 0.000 description 7
- 239000005557 antagonist Substances 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 210000002889 endothelial cell Anatomy 0.000 description 7
- 210000002950 fibroblast Anatomy 0.000 description 7
- 239000003446 ligand Substances 0.000 description 7
- 238000004519 manufacturing process Methods 0.000 description 7
- 239000013612 plasmid Substances 0.000 description 7
- 239000000126 substance Substances 0.000 description 7
- 241000283690 Bos taurus Species 0.000 description 6
- XZMCDFZZKTWFGF-UHFFFAOYSA-N Cyanamide Chemical compound NC#N XZMCDFZZKTWFGF-UHFFFAOYSA-N 0.000 description 6
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 6
- 238000007792 addition Methods 0.000 description 6
- 125000000539 amino acid group Chemical group 0.000 description 6
- 230000008859 change Effects 0.000 description 6
- 239000002299 complementary DNA Substances 0.000 description 6
- 238000010494 dissociation reaction Methods 0.000 description 6
- 230000005593 dissociations Effects 0.000 description 6
- 238000000338 in vitro Methods 0.000 description 6
- 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 6
- 108020004705 Codon Proteins 0.000 description 5
- 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 5
- 230000033115 angiogenesis Effects 0.000 description 5
- 230000004663 cell proliferation Effects 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 4
- 239000004475 Arginine Substances 0.000 description 4
- 241000699800 Cricetinae Species 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical group NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 229920002971 Heparan sulfate Polymers 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 4
- 239000000556 agonist Substances 0.000 description 4
- 125000003275 alpha amino acid group Chemical group 0.000 description 4
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 4
- 238000010276 construction Methods 0.000 description 4
- 230000006698 induction Effects 0.000 description 4
- 210000003734 kidney Anatomy 0.000 description 4
- 238000002703 mutagenesis Methods 0.000 description 4
- 231100000350 mutagenesis Toxicity 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 3
- 101100215647 Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) aflR gene Proteins 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- 108091008794 FGF receptors Proteins 0.000 description 3
- 102000044168 Fibroblast Growth Factor Receptor Human genes 0.000 description 3
- 229930182816 L-glutamine Natural products 0.000 description 3
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 108010021466 Mutant Proteins Proteins 0.000 description 3
- 102000008300 Mutant Proteins Human genes 0.000 description 3
- 229930182555 Penicillin Natural products 0.000 description 3
- 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 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 3
- 206010052428 Wound Diseases 0.000 description 3
- 208000027418 Wounds and injury Diseases 0.000 description 3
- 230000002491 angiogenic effect Effects 0.000 description 3
- 244000309466 calf Species 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 239000000512 collagen gel Substances 0.000 description 3
- 230000007423 decrease Effects 0.000 description 3
- 230000003511 endothelial effect Effects 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 230000003278 mimic effect Effects 0.000 description 3
- 125000001483 monosaccharide substituent group Chemical group 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 150000002482 oligosaccharides Polymers 0.000 description 3
- 229940049954 penicillin Drugs 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 230000035755 proliferation Effects 0.000 description 3
- 238000010791 quenching Methods 0.000 description 3
- 230000000171 quenching effect Effects 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 229960005322 streptomycin Drugs 0.000 description 3
- 230000004083 survival effect Effects 0.000 description 3
- -1 tral amino acid Chemical group 0.000 description 3
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 3
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 229940123256 Fibroblast growth factor antagonist Drugs 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Chemical group 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical group OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 102000016611 Proteoglycans Human genes 0.000 description 2
- 108010067787 Proteoglycans Proteins 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Chemical group CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 229920001586 anionic polysaccharide Polymers 0.000 description 2
- 150000004836 anionic polysaccharides Chemical class 0.000 description 2
- 230000001093 anti-cancer Effects 0.000 description 2
- 230000001028 anti-proliverative effect Effects 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Chemical group OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 2
- 230000008512 biological response Effects 0.000 description 2
- 210000004556 brain Anatomy 0.000 description 2
- 238000010804 cDNA synthesis Methods 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 238000012219 cassette mutagenesis Methods 0.000 description 2
- 230000024245 cell differentiation Effects 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 230000003292 diminished effect Effects 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- 230000001747 exhibiting effect Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 238000000099 in vitro assay Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 238000012417 linear regression Methods 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 210000005036 nerve Anatomy 0.000 description 2
- 229920001542 oligosaccharide Polymers 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- 230000001766 physiological effect Effects 0.000 description 2
- 230000001817 pituitary effect Effects 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- 230000008929 regeneration Effects 0.000 description 2
- 238000011069 regeneration method Methods 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 238000013207 serial dilution Methods 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 230000017423 tissue regeneration Effects 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- 238000000954 titration curve Methods 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 229960005356 urokinase Drugs 0.000 description 2
- 239000004474 valine Chemical group 0.000 description 2
- 230000007998 vessel formation Effects 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 208000010392 Bone Fractures Diseases 0.000 description 1
- 101001051969 Bos taurus Fibroblast growth factor 2 Proteins 0.000 description 1
- JBUMCIVFJKIQSM-KDYGOWAZSA-N C(C)(=O)O.[N+](=O)([O-])C1=CC=C(NC([C@@H](NC([C@@H](NC([C@H](N)CCCC)=O)CC2CCC(CC2)O)=O)CCCCN)=O)C=C1 Chemical compound C(C)(=O)O.[N+](=O)([O-])C1=CC=C(NC([C@@H](NC([C@@H](NC([C@H](N)CCCC)=O)CC2CCC(CC2)O)=O)CCCCN)=O)C=C1 JBUMCIVFJKIQSM-KDYGOWAZSA-N 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 102000012422 Collagen Type I Human genes 0.000 description 1
- 108010022452 Collagen Type I Proteins 0.000 description 1
- 102000030746 Collagen Type X Human genes 0.000 description 1
- 108010022510 Collagen Type X Proteins 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
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 241000672609 Escherichia coli BL21 Species 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 102000003973 Fibroblast growth factor 21 Human genes 0.000 description 1
- 108090000376 Fibroblast growth factor 21 Proteins 0.000 description 1
- 241000812584 Fictor Species 0.000 description 1
- IAJILQKETJEXLJ-UHFFFAOYSA-N Galacturonsaeure Natural products O=CC(O)C(O)C(O)C(O)C(O)=O IAJILQKETJEXLJ-UHFFFAOYSA-N 0.000 description 1
- 230000010558 Gene Alterations Effects 0.000 description 1
- 208000010412 Glaucoma Diseases 0.000 description 1
- 102100039064 Interleukin-3 Human genes 0.000 description 1
- 108010002386 Interleukin-3 Proteins 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical group NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 239000006137 Luria-Bertani broth Substances 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 229920002274 Nalgene Polymers 0.000 description 1
- 206010029113 Neovascularisation Diseases 0.000 description 1
- 108010025020 Nerve Growth Factor Proteins 0.000 description 1
- 102000015336 Nerve Growth Factor Human genes 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 1
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 206010038923 Retinopathy Diseases 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 240000003186 Stachytarpheta cayennensis Species 0.000 description 1
- 235000009233 Stachytarpheta cayennensis Nutrition 0.000 description 1
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- 238000005299 abrasion Methods 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 210000002556 adrenal cortex cell Anatomy 0.000 description 1
- 230000008484 agonism Effects 0.000 description 1
- AEMOLEFTQBMNLQ-WAXACMCWSA-N alpha-D-glucuronic acid Chemical compound O[C@H]1O[C@H](C(O)=O)[C@@H](O)[C@H](O)[C@H]1O AEMOLEFTQBMNLQ-WAXACMCWSA-N 0.000 description 1
- BWZOPYPOZJBVLQ-UHFFFAOYSA-K aluminium glycinate Chemical compound O[Al+]O.NCC([O-])=O BWZOPYPOZJBVLQ-UHFFFAOYSA-K 0.000 description 1
- 230000006229 amino acid addition Effects 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000013103 analytical ultracentrifugation Methods 0.000 description 1
- 230000006427 angiogenic response Effects 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 230000008485 antagonism Effects 0.000 description 1
- 230000003527 anti-angiogenesis Effects 0.000 description 1
- 230000002429 anti-coagulating effect Effects 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 210000002376 aorta thoracic Anatomy 0.000 description 1
- 238000000149 argon plasma sintering Methods 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 210000001130 astrocyte Anatomy 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 1
- MSWZFWKMSRAUBD-QZABAPFNSA-N beta-D-glucosamine Chemical compound N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-QZABAPFNSA-N 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000012292 cell migration Effects 0.000 description 1
- 230000003399 chemotactic effect Effects 0.000 description 1
- 230000035605 chemotaxis Effects 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 238000013375 chromatographic separation Methods 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 230000006020 chronic inflammation Effects 0.000 description 1
- 208000037976 chronic inflammation Diseases 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000002447 crystallographic data Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 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
- 230000002500 effect on skin Effects 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 230000007368 endocrine function Effects 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 1
- 230000035876 healing Effects 0.000 description 1
- 208000019622 heart disease Diseases 0.000 description 1
- 230000003054 hormonal effect Effects 0.000 description 1
- 238000010191 image analysis Methods 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 208000028867 ischemia Diseases 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 108020004084 membrane receptors Proteins 0.000 description 1
- 210000003716 mesoderm Anatomy 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 239000003226 mitogen Substances 0.000 description 1
- 230000008747 mitogenic response Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000004001 molecular interaction Effects 0.000 description 1
- 210000003098 myoblast Anatomy 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 210000004165 myocardium Anatomy 0.000 description 1
- 230000014508 negative regulation of coagulation Effects 0.000 description 1
- 201000003142 neovascular glaucoma Diseases 0.000 description 1
- 229940053128 nerve growth factor Drugs 0.000 description 1
- 210000001020 neural plate Anatomy 0.000 description 1
- 230000005257 nucleotidylation Effects 0.000 description 1
- 210000004248 oligodendroglia Anatomy 0.000 description 1
- 210000000963 osteoblast Anatomy 0.000 description 1
- 239000004031 partial agonist Substances 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000035778 pathophysiological process Effects 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 230000003169 placental effect Effects 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 208000017520 skin disease Diseases 0.000 description 1
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000003595 spectral effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 230000019635 sulfation Effects 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 239000010414 supernatant solution Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000002463 transducing effect Effects 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 230000001173 tumoral effect Effects 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 210000003556 vascular endothelial cell Anatomy 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 230000037314 wound repair Effects 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
- C07K14/475—Growth factors; Growth regulators
- C07K14/50—Fibroblast growth factor [FGF]
- C07K14/503—Fibroblast growth factor [FGF] basic FGF [bFGF]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Toxicology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Materials For Medical Uses (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US12697493A | 1993-09-24 | 1993-09-24 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NZ264529A true NZ264529A (en) | 1997-06-24 |
Family
ID=22427669
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NZ264529A NZ264529A (en) | 1993-09-24 | 1994-09-23 | Fibroblast growth factor analogues which have mutations at a heparin binding site |
Country Status (13)
| Country | Link |
|---|---|
| EP (1) | EP0645451B1 (enExample) |
| JP (1) | JPH07149797A (enExample) |
| KR (1) | KR100320803B1 (enExample) |
| AT (1) | ATE204604T1 (enExample) |
| AU (1) | AU680533B2 (enExample) |
| CA (1) | CA2132668A1 (enExample) |
| DE (1) | DE69428013T2 (enExample) |
| DK (1) | DK0645451T3 (enExample) |
| ES (1) | ES2161233T3 (enExample) |
| NZ (1) | NZ264529A (enExample) |
| PT (1) | PT645451E (enExample) |
| TW (1) | TW275068B (enExample) |
| ZA (1) | ZA947454B (enExample) |
Families Citing this family (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6127116A (en) * | 1995-08-29 | 2000-10-03 | Washington University | Functional DNA clone for hepatitis C virus (HCV) and uses thereof |
| US5874565A (en) * | 1995-08-29 | 1999-02-23 | Washington University | Nucleic acids comprising a highly conserved novel 3 terminal sequence element of the hepatitis C virus |
| US7049428B1 (en) | 1998-03-04 | 2006-05-23 | Washington University | HCV variants |
| US7338759B1 (en) | 1997-03-04 | 2008-03-04 | Washington University | HCV variants |
| WO1999055861A2 (en) * | 1998-04-28 | 1999-11-04 | Eisai Co., Ltd. | Fibroblast growth factor mutein compositions and methods of use therefor |
| JP5767314B2 (ja) | 2010-04-16 | 2015-08-19 | ソーク インスティチュート フォー バイオロジカル スタディーズ | Fgfを用いて代謝障害を処置するための方法 |
| US9475856B2 (en) | 2012-03-02 | 2016-10-25 | New York University | Chimeric FGF21 proteins with enhanced binding affinity for β-klotho for the treatment of type II diabetes, obesity, and related metabolic disorders |
| US9464126B2 (en) | 2012-06-07 | 2016-10-11 | New York University | Chimeric fibroblast growth factor 21 proteins and methods of use |
| US9474785B2 (en) | 2012-06-07 | 2016-10-25 | New York University | Chimeric fibroblast growth factor 19 proteins and methods of use |
| US9657075B2 (en) * | 2012-06-07 | 2017-05-23 | New York University | Chimeric fibroblast growth factor 23 proteins and methods of use |
| US9550820B2 (en) | 2013-02-22 | 2017-01-24 | New York University | Chimeric fibroblast growth factor 23/fibroblast growth factor 19 proteins and methods of use |
| JP6621752B2 (ja) | 2013-10-21 | 2019-12-18 | ソーク インスティテュート フォー バイオロジカル スタディーズ | 変異した線維芽細胞増殖因子(fgf)1および使用方法 |
| WO2015061331A1 (en) | 2013-10-21 | 2015-04-30 | Salk Institute For Biological Studies | Chimeric fibroblast growth factor (fgf) 2/fgf1 peptides and methods of use |
| EP3368059A4 (en) | 2015-10-30 | 2019-03-27 | Salk Institute for Biological Studies | TREATMENT OF STEROID-INDUCED HYPERGLYCEMIA WITH FIBROBLAST GROWTH FACTOR (FGF) -1 ANALOGUE |
| KR20170109207A (ko) * | 2016-03-17 | 2017-09-28 | 중앙대학교 산학협력단 | 화학반응을 통하여 결합된 섬유아세포 증식인자-헤파린 복합체 및 이의 제조 방법 |
| US11229681B2 (en) * | 2017-07-14 | 2022-01-25 | The Regents Of The University Of California | Dominant-negative FGF2 antagonists |
| US11542309B2 (en) | 2019-07-31 | 2023-01-03 | Salk Institute For Biological Studies | Fibroblast growth factor 1 (FGF1) mutant proteins that selectively activate FGFR1B to reduce blood glucose |
| CN116042681A (zh) * | 2022-08-01 | 2023-05-02 | 普纳思细胞(厦门)生物科技有限公司 | 一种bFGF热稳定性改造的方法 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1989000198A1 (en) * | 1987-07-07 | 1989-01-12 | Biotechnology Research Associates, J.V. | Recombinant fibroblast growth factors |
| AU638402B2 (en) * | 1987-11-24 | 1993-07-01 | Amgen, Inc. | Analogs of fibroblast growth factor |
| GB8821795D0 (en) * | 1988-09-16 | 1988-10-19 | Erba Carlo Spa | New derivatives of human/bovine basic fibroplast growth factor |
-
1993
- 1993-12-01 TW TW082110137A patent/TW275068B/zh active
-
1994
- 1994-09-09 EP EP94114212A patent/EP0645451B1/en not_active Expired - Lifetime
- 1994-09-09 AT AT94114212T patent/ATE204604T1/de not_active IP Right Cessation
- 1994-09-09 ES ES94114212T patent/ES2161233T3/es not_active Expired - Lifetime
- 1994-09-09 PT PT94114212T patent/PT645451E/pt unknown
- 1994-09-09 DK DK94114212T patent/DK0645451T3/da active
- 1994-09-09 DE DE69428013T patent/DE69428013T2/de not_active Expired - Fee Related
- 1994-09-22 JP JP6252766A patent/JPH07149797A/ja active Pending
- 1994-09-22 CA CA002132668A patent/CA2132668A1/en not_active Abandoned
- 1994-09-23 NZ NZ264529A patent/NZ264529A/en unknown
- 1994-09-23 ZA ZA947454A patent/ZA947454B/xx unknown
- 1994-09-23 AU AU74185/94A patent/AU680533B2/en not_active Ceased
- 1994-09-23 KR KR1019940024025A patent/KR100320803B1/ko not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| DK0645451T3 (da) | 2001-10-08 |
| DE69428013D1 (de) | 2001-09-27 |
| EP0645451B1 (en) | 2001-08-22 |
| CA2132668A1 (en) | 1995-03-25 |
| JPH07149797A (ja) | 1995-06-13 |
| ES2161233T3 (es) | 2001-12-01 |
| TW275068B (enExample) | 1996-05-01 |
| AU680533B2 (en) | 1997-07-31 |
| KR100320803B1 (ko) | 2002-06-20 |
| ATE204604T1 (de) | 2001-09-15 |
| AU7418594A (en) | 1995-04-06 |
| PT645451E (pt) | 2001-12-28 |
| EP0645451A1 (en) | 1995-03-29 |
| ZA947454B (en) | 1995-05-15 |
| DE69428013T2 (de) | 2002-05-29 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EP0645451B1 (en) | Heparin binding site structural analogues of fibroblast growth factors | |
| US5491220A (en) | Surface loop structural analogues of fibroblast growth factors | |
| Thompson et al. | Characterization of sequences within heparin-binding EGF-like growth factor that mediate interaction with heparin. | |
| EP0399806B1 (en) | Fibronectin derivative | |
| KR100205078B1 (ko) | 염기성 섬유 아세포 성장인자 및 이의 생산방법 | |
| AU654302B2 (en) | Novel neurothrophic factor | |
| Li et al. | Diminished heparin binding of a basic fibroblast growth factor mutant is associated with reduced receptor binding, mitogenesis, plasminogen activator induction, and in vitro angiogenesis | |
| Gualandris et al. | Interaction of high‐molecular‐weight basic fibroblast growth factor with endothelium: biological activity and intracellular fate of human recombinant Mr 24,000 bFGF | |
| US5332804A (en) | High molecular weight human angiogenic basic fibroblast growth factors | |
| AU647547B2 (en) | Active fragments of fibroblast growth factor | |
| CN109535243B (zh) | 人肝细胞生长因子突变体及其应用 | |
| JP4345077B2 (ja) | 有利なグリコシル化プロフィルを有する組換えヒトエリスロポエチン | |
| JP2829405B2 (ja) | 機能性ポリペプチド | |
| AU620925B2 (en) | New derivatives of human/bovine basic fibroblast growth factor | |
| HUT61047A (en) | Process for producing genetic structures for the expression of nerve cell growth factor in eucaryotic cells | |
| AU687455B2 (en) | Surface loop structural analogues of fibroblast growth factors | |
| Brigstock et al. | Subcellular distribution of basic fibroblast growth factor in human hepatoma cells | |
| DE69424747T2 (de) | Pharmazeutische Zusammensetzung zur Vorbeugung oder Behandlung von Knochenbrüchen | |
| JPH07103156B2 (ja) | 再生骨髄から同定された骨形成成長ポリペプチド | |
| US6399744B1 (en) | TCF mutant | |
| CA2079290A1 (en) | Activities of mk protein | |
| AU726538B2 (en) | Pharmaceutical composition for increasing differentiation of osteoblasts | |
| KR100481206B1 (ko) | 신규한 신생혈관생성 저해제 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| RENW | Renewal (renewal fees accepted) | ||
| RENW | Renewal (renewal fees accepted) |