SLRPs bind TGF Beta

Stable Identifier
Homo sapiens
Small Leucine-rich Repeat Proteogycans bind TGF beta
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Small leucine rich repeat proteoglycans (SLRPs) are a family of extracellular glycoproteins that includes decorin (DCN), biglycan (BGN), fibromodulin, lumican and asporin (Hedbom & Heinegard 1993, Ezura et al. 2000, Schaefer & Iozzo 2008, Iozzo & Schaefer 2010). DCN inhibits cellular proliferation in a TGF-Beta-dependent manner in Chinese hamster ovary (CHO) cells (Yamaguchi et al. 1990), arterial smooth muscle cells (Fischer et al. 2001), human hepatic stellate cells (Shi et al. 2006) and fibroblasts (Zhang et al. 2007). DCN, BGN and fibromodulin can all bind to TGF-Beta (Hildebrand 1994). Binding is mediated by the leucine rich repeat suggesting that all members of the SLRP family have TGF-beta binding capability (Schönherr et al. 1998). DCN has independent binding sites for collagen and TGF-Beta (Schönherr et al. 1998, Cabello-Verrugio et al. 2012). DCN binding is thought to sequester TGF-Beta extracellularly, thereby diminishing its biological activity (Markmann et al. 2000). DCN treatment has beneficial effects in fibrotic disorders involving TGF-Beta overproduction (Border et al. 1992; Kolb et al. 2001, Baghy et al. 2012). BGN attenuates the proliferative actions of TGF-beta1 on fibroblasts (Kobayashi et al. 2003). DCN and BGN appear to mediate crosstalk between Toll-like receptors (TLRs), NOD-like receptors (NLRs) and transforming growth factor Beta (TGFBeta) receptors (reviewed in Moreth et al. 2012).

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