Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases.
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.
Imai
K
K
Department of Pathology, School of Medicine, Kanazawa University, Ishikawa, Japan.
Kusakabe
M
M
Sakakura
T
T
Nakanishi
I
I
Okada
Y
Y
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
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