SLRP interaction can protect collagen fibrils from cleavage by collagenases
- 作者：Yeqing Geng ; David McQuillan ; Peter J. Roughley
- 关键词：Decorin ; Fibromodulin ; Lumican ; Type I collagen ; Type II collagen ; Collagenase-1 ; Collagenase-3
- 刊名：Matrix Biology
- 出版年：2006
- 期刊代码：64_0945053x
- 类别：imm
- 出版时间：October 2006
- 卷：25
- 期：8
- 页码：484-491
- 文件大小：1441 K
摘要
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.