Structure and function of matrix metalloproteinases and TIMPs.
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.
Nagase
Hideaki
H
Department of Matrix Biology, Kennedy Institute of Rheumatology Division, Faculty of Medicine, Imperial College London, 1 Aspenlea Road, London W6 8LH, UK. h.nagase@imperial.ac.uk
Visse
Robert
R
Murphy
Gillian
G
D000818:Animals; D002318:Cardiovascular Diseases / Q000201:enzymology; D002319:Cardiovascular System / Q000201:enzymology*; D005109:Extracellular Matrix / Q000201:enzymology*; D006801:Humans; D061965:Matrix Metalloproteinase Inhibitors; D020782:Matrix Metalloproteinases / Q000737:chemistry*; D013329:Structure-Activity Relationship; D019714:Tissue Inhibitor of Metalloproteinases / Q000737:chemistry* / Q000378:metabolism
D061965:Matrix Metalloproteinase Inhibitors; D019714:Tissue Inhibitor of Metalloproteinases; D020782:Matrix Metalloproteinases