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Details on Person Small leucine rich repeat proteoglycans (SLRPs) are a family...

Class:IdSummation:2466265
_displayNameSmall leucine rich repeat proteoglycans (SLRPs) are a family...
_timestamp2013-05-22 16:17:34
created[InstanceEdit:2466194] Jupe, S, 2012-09-06
literatureReference[LiteratureReference:2299698] Binding of fibromodulin and decorin to separate sites on fibrillar collagens
[LiteratureReference:2299690] Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons
[LiteratureReference:3597743] Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction
[LiteratureReference:3597735] Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans
[LiteratureReference:2466192] Negative regulation of transforming growth factor-beta by the proteoglycan decorin
[LiteratureReference:2466104] Retroviral overexpression of decorin differentially affects the response of arterial smooth muscle cells to growth factors
[LiteratureReference:2466144] Effects of rhDecorin on TGF-beta1 induced human hepatic stellate cells LX-2 activation
[LiteratureReference:2327890] Influence of decorin expression on transforming growth factor-beta-mediated collagen gel retraction and biglycan induction
[LiteratureReference:2466159] Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta
[LiteratureReference:2466230] Decorin core protein fragment Leu155-Val260 interacts with TGF-beta but does not compete for decorin binding to type I collagen
[LiteratureReference:3597759] The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-?-dependent signaling, and inhibits TGF-?-dependent fibrotic response in skeletal muscles
[LiteratureReference:2466105] Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease
[LiteratureReference:2466142] Proteoglycans decorin and biglycan differentially modulate TGF-beta-mediated fibrotic responses in the lung
[LiteratureReference:2466198] Recombinant human decorin inhibits cell proliferation and downregulates TGF-beta1 production in hypertrophic scar fibroblasts
[LiteratureReference:3597748] Decorin-TGF? axis in hepatic fibrosis and cirrhosis
[LiteratureReference:2466161] Hepatocyte growth factor regulates proteoglycan synthesis in interstitial fibroblasts
[LiteratureReference:3597740] Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation
modified[InstanceEdit:2867920] Jupe, S, 2012-12-19
[InstanceEdit:3597718] Jupe, S, 2013-05-22
textSmall 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).
(summation)[Reaction:2327886] SLRPs bind TGF Beta [Homo sapiens]
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