期刊
MATRIX BIOLOGY
卷 44-46, 期 -, 页码 255-263出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.matbio.2015.02.007
关键词
Metalloproteinase; Metzincin; TIMP; Extracellular matrix; Endocytosis
资金
- Arthritis Research UK [20563]
- Arthritis Research UK Career Development Fellow [19466]
- Arthritis Research UK Centre for Osteoarthritis Pathogenesis [20205]
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS) [AR40994]
- Versus Arthritis [19466, 20563] Funding Source: researchfish
Matrix metalloproteinases (MMPs) and adamalysin-like metalloproteinase with thrombospondin motifs (ADAMTSs) belong to the metzincin superfamily of metalloproteinases and they play key roles in extracellular matrix catabolism, activation and inactivation of cytokines, chemokines, growth factors, and other proteinases at the cell surface and within the extracellular matrix. Their activities are tightly regulated in a number of ways, such as transcriptional regulation, proteolytic activation and interaction with tissue inhibitors of metalloproteinases (TIMPs). Here, we highlight recent studies that have illustrated novel mechanisms regulating the extracellular activity of these enzymes. These include allosteric activation of metalloproteinases by molecules that bind outside the active site, modulation of location and activity by interaction with cell surface and extracellular matrix molecules, and endocytic clearance from the extracellular milieu by low-density lipoprotein receptor-related protein 1 (LRP1). (C) 2015 Published by Elsevier B.V.
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