Huet et al., 2004 - Google Patents
Inhibition of plasmin-mediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5Huet et al., 2004
- Document ID
- 18021698338329894044
- Author
- Huet E
- Cauchard J
- Berton A
- Robinet A
- Decarme M
- Hornebeck W
- Bellon G
- Publication year
- Publication venue
- Biochemical pharmacology
External Links
Snippet
C18 unsaturated fatty acids were here found to inhibit proMMP (matrix metalloproteinase)-3 activation by plasmin. This effect was suppressed by lysine ligand competitors, indicating that it was mediated by binding to kringle domains. Surface plasmon resonance analysis …
- 108010088842 Fibrinolysin 0 title abstract description 133
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; 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 Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6437—Coagulation factor VIIa (3.4.21.21)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; 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 Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; 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 Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6427—Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; 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 Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6489—Metalloendopeptidases (3.4.24)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
- A61K38/482—Serine endopeptidases (3.4.21)
- A61K38/484—Plasmin (3.4.21.7)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/55—Protease inhibitors
- A61K38/57—Protease inhibitors from animals; from humans
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21007—Plasmin (3.4.21.7), i.e. fibrinolysin
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Maquart et al. | Matrikines in the regulation of extracellular matrix degradation | |
| He et al. | Tissue cooperation in a proteolytic cascade activating human interstitial collagenase. | |
| Davies et al. | Proteinases and glomerular matrix turnover | |
| Legrand et al. | uPA/plasmin system-mediated MMP-9 activation is implicated in bronchial epithelial cell migration | |
| Kucukguven et al. | Matrix metalloproteinases as potential targets in the venous dilation associated with varicose veins | |
| Michael et al. | Biochemical and enzymatic characterization of human kallikrein 5 (hK5), a novel serine protease potentially involved in cancer progression | |
| Radisky et al. | Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer | |
| Van Hinsbergh et al. | Endothelial sprouting and angiogenesis: matrix metalloproteinases in the lead | |
| Mazzieri et al. | Control of type IV collagenase activity by components of the urokinase–plasmin system: a regulatory mechanism with cell‐bound reactants | |
| Mignatti et al. | Plasminogen activators and matrix metalloproteinases in angiogenesis | |
| DeCarlo Jr et al. | Activation and novel processing of matrix metalloproteinases by a thiol-proteinase from the oral anaerobe Porphyromonas gingivalis | |
| Nagase | Matrix metalloproteinases | |
| Okada et al. | Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties. | |
| Kähäri et al. | Matrix metalloproteinases in skin | |
| Raza et al. | Matrix metalloproteinases: pro-and anti-angiogenic activities | |
| Tyagi | Proteinases and myocardial extracellular matrix turnover | |
| Song et al. | Matrix metalloproteinase dependent and independent collagen degradation | |
| Reunanen et al. | Matrix metalloproteinases in cancer cell invasion | |
| Huet et al. | Inhibition of plasmin-mediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5 | |
| Kobayashi et al. | Inhibition of the soluble and the tumor cell receptor-bound plasmin by urinary trypsin inhibitor and subsequent effects on tumor cell invasion and metastasis | |
| Tortorella et al. | ADAMTS-4 (aggrecanase-1): N-terminal activation mechanisms | |
| Sorsa et al. | Collagenase in synovitis of rheumatoid arthritis | |
| Van Hinsbergh et al. | Regulation of plasminogen activator production by endothelial cells: role in fibrinolysis and local proteolysis | |
| Kroon et al. | Collagen type 1 retards tube formation by human microvascular endothelial cells in a fibrin matrix | |
| Higashi et al. | Molecular design of a highly selective and strong protein inhibitor against matrix metalloproteinase-2 (MMP-2) |