Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases

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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.