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Matrix Biol. 2007 Oct;26(8):587-96. Epub 2007 Jul 7.

Control of matrix metalloproteinase catalytic activity.

Author information

1
Center for Lung Biology, University of Washington, Seattle, WA 98109, USA.

Abstract

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 tumor progression, fibrosis, chronic 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.

PMID:
17669641
PMCID:
PMC2246078
DOI:
10.1016/j.matbio.2007.07.001
[Indexed for MEDLINE]
Free PMC Article

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