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Details on Person Cartilage oligomeric matrix protein (COMP, thrombospondin-5)...

Class:Id	Summation:2424247
_displayName	Cartilage oligomeric matrix protein (COMP, thrombospondin-5)...
_timestamp	2012-12-19 17:24:48
created	[InstanceEdit:2424251] Jupe, S, 2012-07-20
literatureReference	[LiteratureReference:2426258] Distribution of cartilage molecules in the developing mouse joint [LiteratureReference:2426329] Cartilage matrix proteins. An acidic oligomeric protein (COMP) detected only in cartilage [LiteratureReference:2426316] Electron microscopy of native cartilage oligomeric matrix protein purified from the Swarm rat chondrosarcoma reveals a five-armed structure [LiteratureReference:2299622] Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen [LiteratureReference:2426246] Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX [LiteratureReference:2426330] Matrix-matrix interaction of cartilage oligomeric matrix protein and fibronectin [LiteratureReference:2426306] Interactions between the cartilage oligomeric matrix protein and matrilins. Implications for matrix assembly and the pathogenesis of chondrodysplasias [LiteratureReference:2299634] Interaction of cartilage matrix protein with aggrecan. Increased covalent cross-linking with tissue maturation [LiteratureReference:2426295] Interaction of cartilage oligomeric matrix protein/thrombospondin 5 with aggrecan [LiteratureReference:2426335] Pseudoachondroplasia and multiple epiphyseal dysplasia: a 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution [LiteratureReference:2426308] Cartilage oligomeric matrix protein is a calcium-binding protein, and a mutation in its type 3 repeats causes conformational changes
modified	[InstanceEdit:2426268] Jupe, S, 2012-07-31 [InstanceEdit:2867920] Jupe, S, 2012-12-19
text	Cartilage oligomeric matrix protein (COMP, thrombospondin-5) is a 524-kDa pentameric glycoprotein expressed primarily in cartilage, tendon, ligament and synovium. In adult cartilage, COMP is located primarily in the inter-territorial matrix between chondrocytes (Murphy et al. 1999). The mature protein is pentameric with each monomer linked to its neighbour by a disulphide bond, located at the amino terminus of the protein (Hedbom et al. 1992, Morgelin et al. 1992). COMP binds directly to collagen types I, II and IX (Rosenberg et al. 1998, Thur et al. 2001) at the fibril periphery. In addition it binds fibronectin (FN1) (Di Cesare et al. 2002), matrilins 1, 3 and 4 (Mann et al. 2004), and through the glycosaminoglycans heparan sulphate and chondroitin sulphate to aggrecan (Hauser et al. 1996, Chen et al. 2007). Mutations in COMP lead to pseudoachondroplasia and multiple epiphyseal dysplasia (Jackson et al. 2012). COMP binding to FN1 and probably to other partners requires the presence of the divalent cations Ca2+, Mg2+ or Mn2+. Each COMP subunit binds approximately 10 calcium ions (Chen et al. 2000).
(summation)	[Reaction:2424252] COMP binds collagen, fibronectin, aggrecan and matrilins [Homo sapiens]
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