title: Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases.
abstract: The degradation of tenascin purified from human melanoma cells was examined by treatment with matrix metalloproteinases (MMPs) and serine proteinases. Among eight different types of proteinases examined, MMP-1, -3, and -7, cathepsin G and leukocyte elastase could digest tenascin, but MMP-2, MMP-9 and thrombin did not. This suggests that tenascin may be readily catabolized by extracellular matrix-degrading proteinases found in the pathophysiological conditions.
authors.affiliation: Department of Pathology, School of Medicine, Kanazawa University, Ishikawa, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Imai
authors.forename: M
authors.initials: M
authors.lastname: Kusakabe
authors.forename: T
authors.initials: T
authors.lastname: Sakakura
authors.forename: I
authors.initials: I
authors.lastname: Nakanishi
authors.forename: Y
authors.initials: Y
authors.lastname: Okada
mesh_terms: D056649:Cathepsin G; D002403:Cathepsins / Q000378:metabolism; D015816:Cell Adhesion Molecules, Neuronal / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006801:Humans; D019272:Leukocyte Elastase; D008545:Melanoma / Q000737:chemistry; D008666:Metalloendopeptidases / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000378:metabolism*; D010196:Pancreatic Elastase / Q000378:metabolism*; D012697:Serine Endopeptidases; D019063:Tenascin; D014407:Tumor Cells, Cultured
chemical_list: D015816:Cell Adhesion Molecules, Neuronal; D016326:Extracellular Matrix Proteins; D009363:Neoplasm Proteins; D019063:Tenascin; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase; D019272:Leukocyte Elastase; D008666:Metalloendopeptidases