Search results for BGN

Showing 14 results out of 36

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Species

Types

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Reaction types

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Protein (7 results from a total of 29)

BGN

Identifier: R-HSA-2466264
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: BGN: P21810

BGN

Identifier: R-HSA-2065224
Species: Homo sapiens
Compartment: lysosomal lumen
Primary external reference: UniProt: P21810

BGN

Identifier: R-HSA-2064245
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: P21810
Identifier: R-HSA-2064015
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: BGN: P21810
Identifier: R-HSA-5607516
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: P21810
Identifier: R-HSA-2065139
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: P21810
Identifier: R-HSA-2065124
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: P21810

Set (1 results from a total of 1)

BGN

Identifier: R-HSA-2466248
Species: Homo sapiens
Compartment: extracellular region

Reaction (4 results from a total of 4)

Identifier: R-HSA-2466238
Species: Homo sapiens
Compartment: extracellular region
Biglycan (BGN) is a member of the small leucine-rich repeat proteoglycan family (SLRPs) which also includes decorin, fibromodulin (Hedlund et al. 1994 - binding to collagen II), lumican and asporin (Hedbom & Heinegard 1993, Ezura et al. 2000). All appear to be involved in collagen fibril formation and matrix assembly (Ameye & Young 2002).

BGN-deficient mice exhibit larger and irregular fibrils leading to thin dermis and reduced bone mass (Corsi et al. 2002, Xu et al. 1998). BGN binds collagen types I (Schönherr et al. 1995), II (Bovine, using pig BGN - Vynios et al. 2001, Bovine, using bovine BGN - Douglas et al. 2008), III (Bovine, using bovine BGN - Douglas et al. 2008), VI (Wiberg et al. 2001) and IX (Chen et al. 2006 - species source of collagen/BGN unknown).
Identifier: R-HSA-2466106
Species: Homo sapiens
Compartment: extracellular region
Biglycan is a member of the small leucine-rich repeat proteoglycan family (SLRPs) which also includes decorin, fibromodulin (Hedlund et al. 1994 - binding to collagen II), lumican and asporin (Hedbom & Heinegard 1993, Ezura et al. 2000). All appear to be involved in collagen fibril formation and matrix assembly (Ameye & Young 2002).

Biglycan binds collagen types I (Schönherr et al. 1995), II (Bovine, using pig byglycan - Vynios et al. 2001, Bovine, using bovine biglycan - Douglas et al. 2008), III (Bovine, using bovine biglycan - Douglas et al. 2008), VI (Wiberg et al. 2001, 2002, human) and IX (Chen et al. 2006 - species source of collagen/biglycan unknown).
Identifier: R-HSA-2327886
Species: Homo sapiens
Compartment: extracellular region
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).
Identifier: R-NUL-2466133
Species: Homo sapiens, Cercopithecus aethiops
Compartment: extracellular region
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).

Complex (2 results from a total of 2)

Identifier: R-HSA-2796107
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2466258
Species: Homo sapiens
Compartment: extracellular region
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