The structure, regulation, and function of human matrix metalloproteinase-13.
Matrix metalloproteinase-13 (MMP-13) is a proteolytic enzyme that belongs to a large family of extracellular matrix-degrading endopeptidases that are characterized by a zinc-binding motif at their catalytic sites. MMP-13 has a key role in the MMP activation cascade and appears to be critical in bone metabolism and homeostasis. It also has an important role in tumor invasion and metastasis. This commentary provides a detailed overview of the regulatory mechanisms, structure, and function of human MMP-13 and highlights the key factors involved in the biology of this important molecule.
Department of Pathology, University of Aberdeen, Foresterhill, UK.
Matthew F
MF
Leeman
Stephanie
S
Curran
Graeme I
GI
Murray
D017364:Collagenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016207:Cytokines / Q000502:physiology; D004789:Enzyme Activation; D015971:Gene Expression Regulation, Enzymologic; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D053509:Matrix Metalloproteinase 13; D009369:Neoplasms / Q000201:enzymology / Q000235:genetics; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
D016207:Cytokines; D017364:Collagenases; C507079:MMP13 protein, human; D053509:Matrix Metalloproteinase 13