Circulation Research. 2003;92:827-839
doi: 10.1161/01.RES.0000070112.80711.3D
doi: 10.1161/01.RES.0000070112.80711.3D
© 2003 American Heart Association, Inc.
Review |
Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases
Structure, Function, and Biochemistry
From the Kennedy Institute of Rheumatology Division, Faculty of Medicine, Imperial College London, London, UK.
Correspondence to Dr Hideaki Nagase, Kennedy Institute of Rheumatology Division, Faculty of Medicine, Imperial College London, 1 Aspenlea Rd, London W6 8LH, UK. E-mail h.nagase{at}imperial.ac.uk
Matrix metalloproteinases (MMPs), also designated matrixins, hydrolyze components of the extracellular matrix. These proteinases play a central role in many biological processes, such as embryogenesis, normal tissue remodeling, wound healing, and angiogenesis, and in diseases such as atheroma, arthritis, cancer, and tissue ulceration. Currently 23 MMP genes have been identified in humans, and most are multidomain proteins. This review describes the members of the matrixin family and discusses substrate specificity, domain structure and function, the activation of proMMPs, the regulation of matrixin activity by tissue inhibitors of metalloproteinases, and their pathophysiological implication.
Key Words: extracellular matrix • protease • protease inhibitors
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