Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9

Kazushi Imai; Hideo Shikata; Yasunori Okada

doi:10.1016/0014-5793(95)00752-U

Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9

Kazushi Imai, Hideo Shikata, Yasunori Okada

Department of Pathology

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

59 Citations (Scopus)

Abstract

The susceptibility of vitronectin (Vn) purified from human plasma to digestion by matrix metalloproteinases (MMPs) was examined. MMP-2, -3, -7 and -9 except for MMP-1 degraded Vn into multiple fragments. MMP-7 showed the highest activity to the substrate among these MMPs, digesting 8-, 30- and 44-fold more preferentially than MMP-2, -3 and -9, respectively. These data suggest that MMP-2, -3, -7 and -9 may be responsible for the pathological degradation and/or normal turnover of Vn.

Original language	English
Pages (from-to)	249-251
Number of pages	3
Journal	FEBS Letters
Volume	369
Issue number	2-3
DOIs	https://doi.org/10.1016/0014-5793(95)00752-U
Publication status	Published - 1995 Aug 7

Keywords

Degradation
Kinetics
Matrix metalloproteinase
Vitronectin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(95)00752-U

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abstract = "The susceptibility of vitronectin (Vn) purified from human plasma to digestion by matrix metalloproteinases (MMPs) was examined. MMP-2, -3, -7 and -9 except for MMP-1 degraded Vn into multiple fragments. MMP-7 showed the highest activity to the substrate among these MMPs, digesting 8-, 30- and 44-fold more preferentially than MMP-2, -3 and -9, respectively. These data suggest that MMP-2, -3, -7 and -9 may be responsible for the pathological degradation and/or normal turnover of Vn.",

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T1 - Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9

AU - Imai, Kazushi

AU - Shikata, Hideo

AU - Okada, Yasunori

PY - 1995/8/7

Y1 - 1995/8/7

N2 - The susceptibility of vitronectin (Vn) purified from human plasma to digestion by matrix metalloproteinases (MMPs) was examined. MMP-2, -3, -7 and -9 except for MMP-1 degraded Vn into multiple fragments. MMP-7 showed the highest activity to the substrate among these MMPs, digesting 8-, 30- and 44-fold more preferentially than MMP-2, -3 and -9, respectively. These data suggest that MMP-2, -3, -7 and -9 may be responsible for the pathological degradation and/or normal turnover of Vn.

AB - The susceptibility of vitronectin (Vn) purified from human plasma to digestion by matrix metalloproteinases (MMPs) was examined. MMP-2, -3, -7 and -9 except for MMP-1 degraded Vn into multiple fragments. MMP-7 showed the highest activity to the substrate among these MMPs, digesting 8-, 30- and 44-fold more preferentially than MMP-2, -3 and -9, respectively. These data suggest that MMP-2, -3, -7 and -9 may be responsible for the pathological degradation and/or normal turnover of Vn.

KW - Degradation

KW - Kinetics

KW - Matrix metalloproteinase

KW - Vitronectin

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Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9

Abstract

Keywords

ASJC Scopus subject areas

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