Cartilage oligomeric matrix protein

From Wikipedia, the free encyclopedia

PDB rendering based on 1fbm.

Available structures: 1fbm, 1mz9, 1vdf

Identifiers

Symbol(s)

COMP; MED; EDM1; EPD1; MGC131819; MGC149768; PSACH; THBS5

External IDs

OMIM: 600310 MGI: 88469 HomoloGene: 74

Gene ontology
Molecular Function:	• extracellular matrix structural constituent • calcium ion binding • protein binding
Cellular Component:	• extracellular region • proteinaceous extracellular matrix
Biological Process:	• skeletal development • cell adhesion • organ morphogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000095 (mRNA)
NP_000086 (protein)

NM_016685 (mRNA)
NP_057894 (protein)

Location

Chr 19: 18.75 - 18.76 Mb

Chr 8: 73.3 - 73.31 Mb

Pubmed search

[1]

[2]

Cartilage oligomeric matrix protein, also known as COMP, is a human gene.^[1]

The protein encoded by this gene is a noncollagenous extracellular matrix (ECM) protein.^[2] 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).^[1]

[edit] References

^ ^a ^b Entrez Gene: COMP cartilage oligomeric matrix protein.
^ Paulsson M, Heinegård D (1981). "Purification and structural characterization of a cartilage matrix protein". Biochem. J. 197 (2): 367–75. PMID 7325960.

[edit] Further reading

Unger S, Hecht JT (2002). "Pseudoachondroplasia and multiple epiphyseal dysplasia: New etiologic developments.". Am. J. Med. Genet. 106 (4): 244–50. PMID 11891674.
Liu C (2006). "Transcriptional mechanism of COMP gene expression and chondrogenesis.". Journal of musculoskeletal & neuronal interactions 5 (4): 340–1. PMID 16340129.
Morozzi G, Fabbroni M, Bellisai F, et al. (2007). "Cartilage oligomeric matrix protein level in rheumatic diseases: potential use as a marker for measuring articular cartilage damage and/or the therapeutic efficacy of treatments.". Ann. N. Y. Acad. Sci. 1108: 398–407. PMID 17894003.
Månsson B, Carey D, Alini M, et al. (1995). "Cartilage and bone metabolism in rheumatoid arthritis. Differences between rapid and slow progression of disease identified by serum markers of cartilage metabolism.". J. Clin. Invest. 95 (3): 1071–7. PMID 7533784.
Hecht JT, Nelson LD, Crowder E, et al. (1995). "Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia.". Nat. Genet. 10 (3): 325–9. doi:10.1038/ng0795-325. PMID 7670471.
Briggs MD, Hoffman SM, King LM, et al. (1995). "Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene.". Nat. Genet. 10 (3): 330–6. doi:10.1038/ng0795-330. PMID 7670472.
Newton G, Weremowicz S, Morton CC, et al. (1995). "Characterization of human and mouse cartilage oligomeric matrix protein.". Genomics 24 (3): 435–9. doi:10.1006/geno.1994.1649. PMID 7713493.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Oehlmann R, Summerville GP, Yeh G, et al. (1994). "Genetic linkage mapping of multiple epiphyseal dysplasia to the pericentromeric region of chromosome 19.". Am. J. Hum. Genet. 54 (1): 3–10. PMID 8279467.
Briggs MD, Rasmussen IM, Weber JL, et al. (1994). "Genetic linkage of mild pseudoachondroplasia (PSACH) to markers in the pericentromeric region of chromosome 19.". Genomics 18 (3): 656–60. PMID 8307576.
Ballo R, Briggs MD, Cohn DH, et al. (1997). "Multiple epiphyseal dysplasia, ribbing type: a novel point mutation in the COMP gene in a South African family.". Am. J. Med. Genet. 68 (4): 396–400. PMID 9021009.
Susic S, McGrory J, Ahier J, Cole WG (1997). "Multiple epiphyseal dysplasia and pseudoachondroplasia due to novel mutations in the calmodulin-like repeats of cartilage oligomeric matrix protein.". Clin. Genet. 51 (4): 219–24. PMID 9184241.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Briggs MD, Mortier GR, Cole WG, et al. (1998). "Diverse mutations in the gene for cartilage oligomeric matrix protein in the pseudoachondroplasia-multiple epiphyseal dysplasia disease spectrum.". Am. J. Hum. Genet. 62 (2): 311–9. PMID 9463320.
Rosenberg K, Olsson H, Mörgelin M, Heinegård D (1998). "Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen.". J. Biol. Chem. 273 (32): 20397–403. PMID 9685393.
Hecht JT, Deere M, Putnam E, et al. (1998). "Characterization of cartilage oligomeric matrix protein (COMP) in human normal and pseudoachondroplasia musculoskeletal tissues.". Matrix Biol. 17 (4): 269–78. PMID 9749943.
Délot E, King LM, Briggs MD, et al. (1999). "Trinucleotide expansion mutations in the cartilage oligomeric matrix protein (COMP) gene.". Hum. Mol. Genet. 8 (1): 123–8. PMID 9887340.
Ikegawa S, Ohashi H, Nishimura G, et al. (1999). "Novel and recurrent COMP (cartilage oligomeric matrix protein) mutations in pseudoachondroplasia and multiple epiphyseal dysplasia.". Hum. Genet. 103 (6): 633–8. PMID 9921895.
Deere M, Sanford T, Francomano CA, et al. (1999). "Identification of nine novel mutations in cartilage oligomeric matrix protein in patients with pseudoachondroplasia and multiple epiphyseal dysplasia.". Am. J. Med. Genet. 85 (5): 486–90. PMID 10405447.
Thur J, Rosenberg K, Nitsche DP, et al. (2001). "Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX.". J. Biol. Chem. 276 (9): 6083–92. doi:10.1074/jbc.M009512200. PMID 11084047.