Copyright © 2005, European Society of Cardiology
Structure and function of matrix metalloproteinases and TIMPs
aDepartment of Matrix Biology, Kennedy Institute of Rheumatology Division, Faculty of Medicine, Imperial College London, 1 Aspenlea Road, London W6 8LH, UK
bDepartment of Oncology, University of Cambridge, Cambridge Institute for Medical, Research, Hills Road, Cambridge, CB2 2XY, UK
* Corresponding author. Tel.: +44 20 8383 4488; fax: +44 20 8383 4994. Email address: h.nagase{at}imperial.ac.uk
Matrix metalloproteinases (MMPs), also called matrixins, function in the extracellular environment of cells and degrade both matrix and non-matrix proteins. They play central roles in morphogenesis, wound healing, tissue repair and remodelling in response to injury, e.g. after myocardial infarction, and in progression of diseases such as atheroma, arthritis, cancer and chronic tissue ulcers. They are multi-domain proteins and their activities are regulated by tissue inhibitors of metalloproteinases (TIMPs). This review introduces the members of the MMP family and discusses their domain structure and function, proenyme activation, the mechanism of inhibition by TIMPs and their significance in physiology and pathology.
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