Degradation of cartilage aggrecan by collagenase‐3 (MMP‐13)

FEBS Letters

Last, Karena¹  Fosang, Amanda J.¹  Murphy, Gillian²  Neame, Peter J.³  Knäuper, Vera² 

[1] Orthopaedic Molecular Biology Research Unit, Melbourne University Department of Paediatrics, Royal Children's Hospital, Parkville 3052, Australia;Strangeways Research Laboratory, Cambridge CB1 4RN, UK;Shriners Hospital for Crippled Children, Tampa Unit, FL 33612, USA

关键词: Aggrecan;    Matrix metalloproteinase;    Collagenase;    Arthritis;    Cartilage degradation;    IGD;    interglobular domain of aggrecan;    MMPs;    matrix metalloproteinases;    HRP;    horseradish peroxidase;    APMA;    4-aminophenylmercuric acetate;    AEBSF;    [4-(2-aminoethyl)benzene]sulfonylfluoride;    PBS;    phosphate-buffered saline;    ECL;    enhanced chemiluminescence;   

DOI  :  10.1016/0014-5793(95)01539-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Degradation of the large cartilage proteoglycan aggrecan in arthritis involves an unidentified enzyme aggrecanase, and at least one of the matrix metalloproteinases. Proteinase-sensitive cleavage sites in the aggrecan interglobular domain (IGD) have been identified for many of the human MMPs, as well as for aggrecanase and other proteinases. The major MMP expressed by chondrocytes stimulated with retinoic acid to degrade their matrix is collagenase-3 or MMP-13. Because of its potential role in aggrecan degradation we examined the specificity of MMP-13 for an aggrecan substrate. The results show that MMP-13 cleaves aggrecan in the IGD at the same site (..PEN_341-FFG..) identified for other members of the MMP family, and also at a novel site ..VKP₃₈₄-VFE.. not previously observed for other proteinases.

【 授权许可】

Unknown