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Details on Person Syndecans are type I transmembrane proteins, with an N-termi...
| Class:Id | Summation:3000184 |
|---|---|
| _displayName | Syndecans are type I transmembrane proteins, with an N-termi... |
| _timestamp | 2013-07-04 14:29:34 |
| created | [InstanceEdit:3000161] Jupe, S, 2013-01-24 |
| literatureReference | [LiteratureReference:2682306] Transmembrane domain-induced oligomerization is crucial for the functions of syndecan-2 and syndecan-4 [LiteratureReference:2681684] Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region [LiteratureReference:2682218] Function of the syndecan-4 cytoplasmic domain in oligomerization and association with ?-actinin in turkey muscle satellite cells [LiteratureReference:2682229] Syndecans in wound healing, inflammation and vascular biology [LiteratureReference:3787977] Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids [LiteratureReference:3787939] Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor activation [LiteratureReference:3788048] Induction of syndecan-1 expression in stromal fibroblasts promotes proliferation of human breast cancer cells |
| modified | [InstanceEdit:3000194] Jupe, S, 2013-01-24 [InstanceEdit:3597657] Jupe, S, 2013-05-22 [InstanceEdit:3787960] Jupe, S, 2013-07-04 |
| text | Syndecans are type I transmembrane proteins, with an N-terminal ectodomain that contains several consensus sequences for glycosaminoglycan (GAG) attachment and a short C-terminal cytoplasmic domain. Syndecan-1 and -3 GAG attachment sites occur in two distinct clusters, one near the N-terminus and the other near the membrane-attachment site, separated by a proline and threonine-rich 'spacer'. Syndecan ectodomain sequences are poorly conserved in the family and between species, but the transmembrane and cytoplasmic domains are highly conserved. Syndecan-1 and -3 form a subfamily. Syndecan core proteins form dimers (Choi et al. 2007) and at least syndecan-3 and -4 form oligomers (Asundi & Carey 1995, Shin et al. 2012). Syndecan-1 is the major syndecan of epithelial cells including vascular endothelium. Syndecan-2 is present mostly in mesenchymal, neuronal and smooth muscle cells. Syndecan-3 is the major syndecan of the nervous system, while syndecan-4 is ubiquitously expressed but at lower levels than the other syndecans (refs in Alexopoulou et al. 2007). The core syndecan protein has three to five heparan sulfate or chondroitin sulfate chains, which interact with a variety of ligands including fibroblast growth factors, vascular endothelial growth factor, transforming growth factor-beta, fibronectin, collagen, vitronectin and several integrins. Syndecans may act as integrin coreceptors. Interactions between fibronectin and syndecans are modulated by tenascin-C. Syndecans bind a wide variety of soluble and insoluble ligands, inckluding extracellular matrix components, cell adhesion molecules, growth factors, cytokines, and proteinases. As the cleaved ectodomains of syndecans retain the ability to bind ligands, ectodomain shedding is a mechanism for releasing soluble effectors that may compete for ligands with their cell-bound counterparts (Kainulainen et al. 1998). Shed ectodomains are found in inflammatory fluids (Subramanian et al. 1997) and may induce the proliferation of cancer cells (Maeda et al. 2004). |
| (summation) | [Pathway:3000170] Syndecan interactions [Homo sapiens] |
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