期刊论文详细信息
FEBS Letters | |
Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases | |
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
【 预 览 】
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