Cartilage oligomeric matrix protein

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COMP
Protein COMP PDB 1fbm.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCOMP, EDM1, EPD1, MED, PSACH, THBS5, cartilage oligomeric matrix protein, TSP5
External IDsOMIM: 600310 MGI: 88469 HomoloGene: 74 GeneCards: COMP
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for COMP
Genomic location for COMP
Band19p13.11Start18,782,773 bp[1]
End18,791,305 bp[1]
RNA expression pattern
PBB GE COMP 205713 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000095

NM_016685

RefSeq (protein)

NP_000086

NP_057894

Location (UCSC)Chr 19: 18.78 – 18.79 MbChr 8: 70.37 – 70.38 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cartilage oligomeric matrix protein (COMP), also known as thrombospondin-5, is an extracellular matrix (ECM) protein primarily present in cartilage. In humans it is encoded by the COMP gene.[5][6][7]

Function[edit]

The protein encoded by this gene is a noncollagenous extracellular matrix (ECM) protein.[8] It consists of five identical glycoprotein subunits, each with EGF-like and calcium-binding (thrombospondin-like) domains. Oligomerization results from formation of a five-stranded coiled coil and disulfide bonds. Binding to other ECM proteins such as collagen appears to depend on divalent cations. Mutations can cause the osteochondrodysplasias pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (MED).[7]

COMP is a marker of cartilage turnover.[9] It is present in high quantities in fibrotic scars and systemic sclerosis, and it appears to have a role in vascular wall remodeling.[10]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105664 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031849 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Newton G, Weremowicz S, Morton CC, Copeland NG, Gilbert DJ, Jenkins NA, Lawler J (Dec 1994). "Characterization of human and mouse cartilage oligomeric matrix protein". Genomics. 24 (3): 435–9. doi:10.1006/geno.1994.1649. PMID 7713493.
  6. ^ Briggs MD, Rasmussen IM, Weber JL, Yuen J, Reinker K, Garber AP, Rimoin DL, Cohn DH (Dec 1993). "Genetic linkage of mild pseudoachondroplasia (PSACH) to markers in the pericentromeric region of chromosome 19". Genomics. 18 (3): 656–60. doi:10.1016/S0888-7543(05)80369-6. PMID 8307576.
  7. ^ a b "Entrez Gene: COMP cartilage oligomeric matrix protein".
  8. ^ Paulsson M, Heinegård D (Aug 1981). "Purification and structural characterization of a cartilage matrix protein". The Biochemical Journal. 197 (2): 367–75. doi:10.1042/bj1970367. PMC 1163135. PMID 7325960.
  9. ^ Petersen SG, Saxne T, Heinegard D, Hansen M, Holm L, Koskinen S, Stordal C, Christensen H, Aagaard P, Kjaer M (Jan 2010). "Glucosamine but not ibuprofen alters cartilage turnover in osteoarthritis patients in response to physical training". Osteoarthritis and Cartilage. 18 (1): 34–40. doi:10.1016/j.joca.2009.07.004. PMID 19679221.
  10. ^ Halper J, Kjaer M (2014). "Basic components of connective tissues and extracellular matrix: elastin, fibrillin, fibulins, fibrinogen, fibronectin, laminin, tenascins and thrombospondins". Advances in Experimental Medicine and Biology. 802: 31–47. doi:10.1007/978-94-007-7893-1_3. PMID 24443019.

Further reading[edit]

External links[edit]