Activation of pro-(matrix metalloproteinase-2) (pro-MMP-2) by thrombin is membrane-type-MMP-dependent in human umbilical vein endothelial cells and generates a distinct 63 kDa active species

Thrombin, a critical enzyme in the coagulation cascade, has also been associated with angiogenesis and activation of the zymogen form of matrix metalloproteinase-2 (MMP-2 or gelatinase-A). We show that thrombin activated pro-MMP-2 in a dose- and time-dependent manner in cultured human umbilical-vein...

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Veröffentlicht in:	Biochemical journal 2001-07, Vol.357 (Pt 1), p.107-115
Hauptverfasser:	Lafleur, M A, Hollenberg, M D, Atkinson, S J, Knäuper, V, Murphy, G, Edwards, D R
Format:	Artikel
Sprache:	eng
Schlagworte:	Cells, Cultured Endothelium, Vascular - enzymology Enzyme Activation Enzyme Precursors - metabolism Gelatinases - metabolism Gene Expression Regulation, Enzymologic Humans Kinetics Matrix Metalloproteinases, Membrane-Associated Metalloendopeptidases - genetics Metalloendopeptidases - metabolism Molecular Weight Oligopeptides - pharmacology Protease Inhibitors - pharmacology Receptors, Thrombin - antagonists & inhibitors Receptors, Thrombin - physiology Recombinant Proteins - metabolism Reverse Transcriptase Polymerase Chain Reaction Tetradecanoylphorbol Acetate - pharmacology Thrombin - metabolism Time Factors Transcription, Genetic Umbilical Veins
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