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Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases
Author(s) -
Imai Kazushi,
Kusakabe Moriaki,
Sakakura Teruyo,
Nakanishi Isao,
Okada Yasunori
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00960-0
Subject(s) - matrix metalloproteinase , tenascin , cathepsin g , elastase , extracellular matrix , tenascin c , serine , serine protease , chemistry , biochemistry , cathepsin , neutrophil elastase , microbiology and biotechnology , enzyme , biology , immunology , inflammation , protease , fibronectin
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.