SLRP interaction can protect collagen fibrils from cleavage by collagenases |
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Authors: | Yeqing Geng David McQuillan Peter J. Roughley |
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Affiliation: | Genetics Unit, Shriners Hospital for Children, 1529 Cedar Avenue, Montreal, Quebec, Canada H3G 1A6. |
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Abstract: | 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. |
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Keywords: | Decorin Fibromodulin Lumican Type I collagen Type II collagen Collagenase-1 Collagenase-3 |
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