期刊
MATRIX BIOLOGY
卷 26, 期 8, 页码 587-596出版社
ELSEVIER
DOI: 10.1016/j.matbio.2007.07.001
关键词
matrix metalloproteinase; zymogen; proteolysis; adaptor molecules
资金
- NHLBI NIH HHS [R01 HL077555-05, P01 HL029594, R01 HL077555, HL29594, HL077555] Funding Source: Medline
As their name implies, MMPs were first described as proteases that degrade extracellular matrix proteins, such as collagens, elastin, proteoglycans, and laminins. However, studies of MMP function in vivo have revealed that these proteinases act on a variety of extracellular protein substrates, often to activate latent forms of effector proteins, such as antimicrobial peptides and cytokines, or to alter protein function, such as shedding of cell-surface proteins. Because their substrates are diverse, MMPs are involved in variety of homeostatic functions, such as bone remodeling, wound healing, and several aspects of immunity. However, MMPs are also involved in a number of pathological processes, such as turner progression, fibrosis, chronic in inflammation, tissue destruction, and more. A key step in regulating MMP proteolysis is the conversion of the zymogen into an active proteinase. Several proMMPs are activated in the secretion pathway by furin proprotein convertases, but for most the activation mechanisms are largely not known. In this review, we discuss both authentic and potential mechanisms of proMMP activation. (c) 2007 Elsevier B.V/International Society of Matrix Biology. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据