4.6 Article

SLRP interaction can protect collagen fibrils from cleavage by collagenases

Journal

MATRIX BIOLOGY
Volume 25, Issue 8, Pages 484-491

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.matbio.2006.08.259

Keywords

decorin; fibromodulin; lumican; type I collagen; type II collagen; collagenase-1; collagenase-3

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Decorin, fibromodulin and lumican are small leucine-rich repeat proteoglycans (SLRPs) which interact with the surface of collagen fibrils. Together with other molecules they form a coat on the fibril surface which could impede the access to collagenolytic proteinases. To address this hypothesis, fibrils of type I or type II collagen were formed in vitro and treated with either collagenase-1 (MMP1) or collagenase-3 (MMP13). The fibrils were either treated directly or following incubation in the presence of the recombinant SLRPs. The susceptibility of the uncoated and SLRP-coated fibrils to collagenase cleavage was assessed by SDS/PAGE. Interaction with either recombinant decorin, fibromodulin or lumican results in decreased collagenase cleavage of both fibril types. Thus SLRP interaction can help protect collagen fibrils from cleavage by collagenases. (c) 2006 Elsevier B.V./International Society of Matrix Biology. All rights reserved.

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