cartilage oligomeric matrix protein
Last updated 18 Aug 2020
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The COMP gene provides the instructions for making the COMP protein. This protein is found in the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. Specifically, the COMP protein is located in the extracellular matrix surrounding the cells that make up ligaments and tendons, and near cartilage-forming cells (chondrocytes). Chondrocytes play an important role in bone formation (osteogenesis). In the bones of the spine, hips, and limbs, the process of osteogenesis starts with the formation of cartilage, which is then converted into bone.
Normal function
The COMP gene provides the instructions for making the COMP protein. This protein is found in the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. Specifically, the COMP protein is located in the extracellular matrix surrounding the cells that make up ligaments and tendons, and near cartilage-forming cells (chondrocytes). Chondrocytes play an important role in bone formation (osteogenesis). In the bones of the spine, hips, and limbs, the process of osteogenesis starts with the formation of cartilage, which is then converted into bone.
The normal function of the COMP protein is not fully known. It is believed to play a role in cell growth and division (proliferation) and the self-destruction of cells (apoptosis), as well as in the regulation of cell movement and attachment. Research has also shown that the COMP protein binds strongly to calcium.
Conditions referring to this gene or chromosome
Other names
cartilage oligomeric matrix protein (pseudoachondroplasia, epiphyseal dysplasia 1, multiple)
COMP_HUMAN
EDM1
EPD1
MED
PSACH
pseudoachondroplasia (epiphyseal dysplasia 1, multiple)
THBS5
thrombospondin-5
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Further reading and references
- cartilage oligomeric matrix protein; MedlinePlus, National Library of Medicine.
- Briggs MD, Chapman KL. Pseudoachondroplasia and multiple epiphyseal dysplasia: mutation review, molecular interactions, and genotype to phenotype correlations. Hum Mutat. 2002 May;19(5):465-78. doi: 10.1002/humu.10066.
- Chen TL, Posey KL, Hecht JT, Vertel BM. COMP mutations: domain-dependent relationship between abnormal chondrocyte trafficking and clinical PSACH and MED phenotypes. J Cell Biochem. 2008 Feb 15;103(3):778-87. doi: 10.1002/jcb.21445.
- Developmental Biology (sixth edition, 2000): Osteogenesis: The Development of Bones
- Gagarina V, Carlberg AL, Pereira-Mouries L, Hall DJ. Cartilage oligomeric matrix protein protects cells against death by elevating members of the IAP family of survival proteins. J Biol Chem. 2008 Jan 4;283(1):648-659. doi: 10.1074/jbc.M704035200. Epub 2007 Nov 8.
- Hecht JT, Makitie O, Hayes E, Haynes R, Susic M, Montufar-Solis D, Duke PJ, Cole WG. Chondrocyte cell death and intracellular distribution of COMP and type IX collagen in the pseudoachondroplasia growth plate. J Orthop Res. 2004 Jul;22(4):759-67. doi: 10.1016/j.orthres.2003.11.010.
- Jakkula E, Makitie O, Czarny-Ratajczak M, Jackson GC, Damignani R, Susic M, Briggs MD, Cole WG, Ala-Kokko L. Mutations in the known genes are not the major cause of MED; distinctive phenotypic entities among patients with no identified mutations. Eur J Hum Genet. 2005 Mar;13(3):292-301. doi: 10.1038/sj.ejhg.5201314.
- Posey KL, Yang Y, Veerisetty AC, Sharan SK, Hecht JT. Model systems for studying skeletal dysplasias caused by TSP-5/COMP mutations. Cell Mol Life Sci. 2008 Mar;65(5):687-99. doi: 10.1007/s00018-007-7485-0.
- Zankl A, Jackson GC, Crettol LM, Taylor J, Elles R, Mortier GR, Spranger J, Zabel B, Unger S, Merrer ML, Cormier-Daire V, Hall CM, Wright MJ, Bonafe L, Superti-Furga A, Briggs MD. Preselection of cases through expert clinical and radiological review significantly increases mutation detection rate in multiple epiphyseal dysplasia. Eur J Hum Genet. 2007 Feb;15(2):150-4. doi: 10.1038/sj.ejhg.5201744. Epub 2006 Nov 29.
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