Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases

FEBS Letters

Nakanishi, Isao²  Imai, Kazushi²  Okada, Yasunori²  Kusakabe, Moriaki³  Sakakura, Teruyo¹ 

[1] Department of Pathology, School of Medicine, Mie University, 2-174 Edobashi, Tsu, Mie 514, Japan;Department of Pathology, School of Medicine, Kanazawa University, 13-1 Takara-machi, Kanazawa, Ishikawa 920, Japan;Laboratory of Cell Biology, Riken, Tsukuba Life Science Center, The Institution of Physical and Chemical Research, 3-1-1 Koyadai, Tsukuba, Ibaraki 305, Japan

关键词: Tenascin;    Matrix metalloproteinase;    Serine proteinase;    MMP;    matrix metalloproteinase;    DIFP;    diisopropyl flurophosphate;    EDTA;    ethylenediaminetetraacetic acid;    APMA;    4-aminophenylmercuric acetate;    SDS-PAGE;    sodium dodecyl sulfatepolyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(94)00960-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown