ADAMTS‐1 cleaves a cartilage proteoglycan, aggrecan

FEBS Letters

Nakamura, Hiroyuki²  Okada, Yasunori²  Kawashima, Hiroto⁴  Miyasaka, Masayuki⁴  Kuno, Kouji¹  Matsushima, Kouji³  Ohno, Hiroshi¹ 

[1]Department of Molecular Membrane Biology, Cancer Research Institute, Kanazawa University, 13-1, Takara-machi, Kanazawa, Ishikawa 920-0934, Japan

[2]Department of Pathology, Keio University School of Medicine, 35, Shinanomachi, Shinjuku-ku, Tokyo 160-0016, Japan

[3]Department of Molecular Preventive Medicine, School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan

[4]Department of Bioregulation, Biomedical Research Center, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita 565-0871, Japan

关键词: Aggrecan;    Disintegrin and metalloproteinase thrombospondin;    Extracellular matrix;    Cartilage degradation;    ADAM;    disintegrin and metalloproteinase;    CS;    chondroitin sulfate;    DMEM;    Dulbecco's modified Eagle's medium;    ECM;    extracellular matrix;    IGD;    interglobular domain;    KS;    keratan sulfate;    MMP;    matrix metalloproteinase;    PAGE;    polyacrylamide gel electrophoresis;    SDS;    sodium dodecyl sulfate;    TSP;    thrombospondin;   

DOI  :  10.1016/S0014-5793(00)01854-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A disintegrin-like and metalloproteinase with thrombospondin type I motifs-1 (ADAMTS-1) is an extracellular matrix-anchored metalloproteinase. In this study we have demonstrated that ADAMTS-1 is able to cleave a major cartilage proteoglycan, aggrecan. N-terminal sequencing analysis of the cleavage product revealed that ADAMTS-1 cleaves the Glu¹⁸⁷¹–Leu¹⁸⁷² bond within the chondroitin sulfate attachment domain of aggrecan. In addition, deletional analysis demonstrated that the C-terminal spacer region of ADAMTS-1 is necessary to degrade aggrecan. These results suggest that ADAMTS-1 may be involved in the turnover of aggrecan in vivo.

【 授权许可】

Unknown