Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases

Kazushi Imai; Moriaki Kusakabe; Teruyo Sakakura; Isao Nakanishi; Yasunori Okada

doi:10.1016/0014-5793(94)00960-0

Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases

Kazushi Imai, Moriaki Kusakabe, Teruyo Sakakura, Isao Nakanishi, Yasunori Okada

Department of Pathology

Research output: Contribution to journal › Article › peer-review

66 Citations (Scopus)

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.

Original language	English
Pages (from-to)	216-218
Number of pages	3
Journal	FEBS Letters
Volume	352
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(94)00960-0
Publication status	Published - 1994 Sep 26

Keywords

Matrix metalloproteinase
Serine proteinase
Tenascin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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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.",

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AU - Imai, Kazushi

AU - Kusakabe, Moriaki

AU - Sakakura, Teruyo

AU - Nakanishi, Isao

AU - Okada, Yasunori

PY - 1994/9/26

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AB - 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.

KW - Matrix metalloproteinase

KW - Serine proteinase

KW - Tenascin

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