軟骨オリゴマー基質タンパク質 COMP
WordNet
- (geology) amass of fine-grained rock in which fossils, crystals, or gems are embedded
- mold used in the production of phonograph records, type, or other relief surface
- the body substance in which tissue cells are embedded (同)intercellular substance, ground_substance
- (mathematics) a rectangular array of quantities or expressions set out by rows and columns; treated as a single element and manipulated according to rules
- an enclosure within which something originates or develops (from the Latin for womb)
- the formative tissue at the base of a nail
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
- tough elastic tissue; mostly converted to bone in adults (同)gristle
PrepTutorEJDIC
- (複数形 matrices, ~・es)(発生・成長の)母体 / 鋳型・模型;(レコードの)原盤;(活字の)母型,字母 / (金属・化石・宝石などの含んだ)母岩・《古》子宮・基盤; (細胞)細胞間質; (地学)基質; (印)字母; 紙型; 鋳型; (鉱)母岩; (数)行列; (コンピュータ)マトリックス (入力導線と出力導線の回路網); (言)母型文 (matrix sentence)
- 蛋白(たんばく)質
- 軟骨[組織]
- マトリクシング(4チャンネルに再生転換できる2チャンネルの録音方式)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/02/19 15:17:19」(JST)
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Cartilage oligomeric matrix protein |
PDB rendering based on 1fbm.
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Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
3FBY
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Identifiers |
Symbols |
COMP ; EDM1; EPD1; MED; PSACH; THBS5 |
External IDs |
OMIM: 600310 MGI: 88469 HomoloGene: 74 GeneCards: COMP Gene |
Gene ontology |
Molecular function |
• protease binding
• extracellular matrix structural constituent
• calcium ion binding
• protein binding
• collagen binding
• heparin binding
• heparan sulfate proteoglycan binding
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Cellular component |
• extracellular region
• proteinaceous extracellular matrix
• extracellular space
• extracellular matrix
• extracellular exosome
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Biological process |
• skeletal system development
• growth plate cartilage development
• apoptotic process
• cell adhesion
• organ morphogenesis
• extracellular matrix organization
• negative regulation of apoptotic process
• limb development
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
1311 |
12845 |
Ensembl |
ENSG00000105664 |
ENSMUSG00000031849 |
UniProt |
P49747 |
Q9R0G6 |
RefSeq (mRNA) |
NM_000095 |
NM_016685 |
RefSeq (protein) |
NP_000086 |
NP_057894 |
Location (UCSC) |
Chr 19:
18.78 – 18.79 Mb |
Chr 8:
70.37 – 70.38 Mb |
PubMed search |
[1] |
[2] |
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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.[1][2][3]
Contents
- 1 Function
- 2 References
- 3 Further reading
- 4 External links
Function
The protein encoded by this gene is a noncollagenous extracellular matrix (ECM) protein.[4] 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).[3]
COMP is a marker of cartilage turnover.[5] It is present in high quantities in fibrotic scars and systemic sclerosis, and it appears to have a role in vascular wall remodeling.[6]
References
- ^ 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.
- ^ 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.
- ^ a b "Entrez Gene: COMP cartilage oligomeric matrix protein".
- ^ Paulsson M, Heinegård D (Aug 1981). "Purification and structural characterization of a cartilage matrix protein". The Biochemical Journal 197 (2): 367–75. PMC 1163135. PMID 7325960.
- ^ 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 / OARS, Osteoarthritis Research Society 18 (1): 34–40. doi:10.1016/j.joca.2009.07.004. PMID 19679221.
- ^ 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
- Unger S, Hecht JT (2002). "Pseudoachondroplasia and multiple epiphyseal dysplasia: New etiologic developments". American Journal of Medical Genetics 106 (4): 244–50. doi:10.1002/ajmg.10234. 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, Pucci G, Galeazzi M (Jun 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". Annals of the New York Academy of Sciences 1108 (1): 398–407. doi:10.1196/annals.1422.041. PMID 17894003.
- Månsson B, Carey D, Alini M, Ionescu M, Rosenberg LC, Poole AR, Heinegård D, Saxne T (Mar 1995). "Cartilage and bone metabolism in rheumatoid arthritis. Differences between rapid and slow progression of disease identified by serum markers of cartilage metabolism". The Journal of Clinical Investigation 95 (3): 1071–7. doi:10.1172/JCI117753. PMC 441442. PMID 7533784.
- Hecht JT, Nelson LD, Crowder E, Wang Y, Elder FF, Harrison WR, Francomano CA, Prange CK, Lennon GG, Deere M (Jul 1995). "Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia". Nature Genetics 10 (3): 325–9. doi:10.1038/ng0795-325. PMID 7670471.
- Briggs MD, Hoffman SM, King LM, Olsen AS, Mohrenweiser H, Leroy JG, Mortier GR, Rimoin DL, Lachman RS, Gaines ES (Jul 1995). "Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene". Nature Genetics 10 (3): 330–6. doi:10.1038/ng0795-330. PMID 7670472.
- Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Oehlmann R, Summerville GP, Yeh G, Weaver EJ, Jimenez SA, Knowlton RG (Jan 1994). "Genetic linkage mapping of multiple epiphyseal dysplasia to the pericentromeric region of chromosome 19". American Journal of Human Genetics 54 (1): 3–10. PMC 1918067. PMID 8279467.
- 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.
- Ballo R, Briggs MD, Cohn DH, Knowlton RG, Beighton PH, Ramesar RS (Feb 1997). "Multiple epiphyseal dysplasia, ribbing type: a novel point mutation in the COMP gene in a South African family". American Journal of Medical Genetics 68 (4): 396–400. doi:10.1002/(SICI)1096-8628(19970211)68:4<396::AID-AJMG4>3.0.CO;2-K. PMID 9021009.
- Susic S, McGrory J, Ahier J, Cole WG (Apr 1997). "Multiple epiphyseal dysplasia and pseudoachondroplasia due to novel mutations in the calmodulin-like repeats of cartilage oligomeric matrix protein". Clinical Genetics 51 (4): 219–24. doi:10.1111/j.1399-0004.1997.tb02458.x. PMID 9184241.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Briggs MD, Mortier GR, Cole WG, King LM, Golik SS, Bonaventure J, Nuytinck L, De Paepe A, Leroy JG, Biesecker L, Lipson M, Wilcox WR, Lachman RS, Rimoin DL, Knowlton RG, Cohn DH (Feb 1998). "Diverse mutations in the gene for cartilage oligomeric matrix protein in the pseudoachondroplasia-multiple epiphyseal dysplasia disease spectrum". American Journal of Human Genetics 62 (2): 311–9. doi:10.1086/301713. PMC 1376889. PMID 9463320.
- Rosenberg K, Olsson H, Mörgelin M, Heinegård D (Aug 1998). "Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen". The Journal of Biological Chemistry 273 (32): 20397–403. doi:10.1074/jbc.273.32.20397. PMID 9685393.
- Hecht JT, Deere M, Putnam E, Cole W, Vertel B, Chen H, Lawler J (Aug 1998). "Characterization of cartilage oligomeric matrix protein (COMP) in human normal and pseudoachondroplasia musculoskeletal tissues". Matrix Biology 17 (4): 269–78. doi:10.1016/S0945-053X(98)90080-4. PMID 9749943.
- Délot E, King LM, Briggs MD, Wilcox WR, Cohn DH (Jan 1999). "Trinucleotide expansion mutations in the cartilage oligomeric matrix protein (COMP) gene". Human Molecular Genetics 8 (1): 123–8. doi:10.1093/hmg/8.1.123. PMID 9887340.
- Ikegawa S, Ohashi H, Nishimura G, Kim KC, Sannohe A, Kimizuka M, Fukushima Y, Nagai T, Nakamura Y (Dec 1998). "Novel and recurrent COMP (cartilage oligomeric matrix protein) mutations in pseudoachondroplasia and multiple epiphyseal dysplasia". Human Genetics 103 (6): 633–8. doi:10.1007/s004390050883. PMID 9921895.
- Deere M, Sanford T, Francomano CA, Daniels K, Hecht JT (Aug 1999). "Identification of nine novel mutations in cartilage oligomeric matrix protein in patients with pseudoachondroplasia and multiple epiphyseal dysplasia". American Journal of Medical Genetics 85 (5): 486–90. doi:10.1002/(SICI)1096-8628(19990827)85:5<486::AID-AJMG10>3.0.CO;2-O. PMID 10405447.
- Thur J, Rosenberg K, Nitsche DP, Pihlajamaa T, Ala-Kokko L, Heinegård D, Paulsson M, Maurer P (Mar 2001). "Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX". The Journal of Biological Chemistry 276 (9): 6083–92. doi:10.1074/jbc.M009512200. PMID 11084047.
External links
- GeneReviews/NCBI/NIH/UW entry on Pseudoachondroplasia
- GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant
- cartilage matrix protein at the US National Library of Medicine Medical Subject Headings (MeSH)
PDB gallery
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1fbm: ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN IN COMPLEX WITH ALL-TRANS RETINOL
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1mz9: Storage function of COMP:the crystal structure of the coiled-coil domain in complex with vitamin D3
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1vdf: ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN
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Protein: scleroproteins
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Extracellular matrix |
Collagen |
Fibril forming |
- type I
- type II (COL2A1)
- type III
- type V
- COL24A1
- COL26A1
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Other |
- FACIT: type IX
- type XII (COL12A1)
- COL14A1
- COL16A1
- COL19A1
- COL20A1
- COL21A1
- COL22A1
- basement membrane: type IV
- COL4A1
- COL4A2
- COL4A3
- COL4A4
- COL4A5
- COL4A6
- multiplexin: COL15A1
- type XVIII
- transmembrane: COL13A1
- COL17A1
- COL23A1
- COL25A1
- other: type VI
- COL6A1
- COL6A2
- COL6A3
- COL6A5
- type VII (COL7A1)
- type VIII
- type X (COL10A1)
- type XI
- COL27A1
- COL28A1
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Enzymes |
- Prolyl hydroxylase/Lysyl hydroxylase
- Cartilage associated protein/Leprecan
- ADAMTS2
- Procollagen peptidase
- Lysyl oxidase
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Laminin |
- alpha
- LAMA1
- LAMA2
- LAMA3
- LAMA4
- LAMA5
- beta
- gamma
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Other |
- ALCAM
- Elastin
- Vitronectin
- FRAS1
- FREM2
- Decorin
- FAM20C
- ECM1
- Matrix gla protein
- Tectorin
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Other |
- Keratin/Cytokeratin
- Gelatin
- Reticulin
- Cartilage oligomeric matrix protein
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UpToDate Contents
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English Journal
- Cartilage oligomeric matrix protein (COMP) in murine brachiocephalic and carotid atherosclerotic lesions.
- Bond AR1, Hultgårdh-Nilsson A2, Knutsson A3, Jackson CL4, Rauch U5.
- Atherosclerosis.Atherosclerosis.2014 Oct;236(2):366-72. doi: 10.1016/j.atherosclerosis.2014.07.029. Epub 2014 Aug 5.
- OBJECTIVE: To investigate the hypothesis that COMP can influence the morphology, stability and size of murine atherosclerotic lesions.METHODS: ApoE- and ApoE/COMP-knockout mice were fed a high-fat diet to develop atherosclerotic plaques at lesion sites of three different types; inflammatory and fibr
- PMID 25133350
- Biochemical markers of joint tissue damage increase shortly after a joint bleed; an explorative human and canine in vivo study.
- van Vulpen LF1, van Meegeren ME2, Roosendaal G3, Jansen NW4, van Laar JM5, Schutgens RE6, Mastbergen SC7, Lafeber FP8.
- Osteoarthritis and cartilage / OARS, Osteoarthritis Research Society.Osteoarthritis Cartilage.2014 Sep 16. pii: S1063-4584(14)01254-0. doi: 10.1016/j.joca.2014.09.008. [Epub ahead of print]
- OBJECTIVE: Evaluation whether biomarkers of joint damage are sensitive to change shortly after a joint bleed in hemophilia patients and in a canine model of blood-induced joint damage.METHODS: Blood and urine samples were collected from 10 hemophilia patients after they reported a joint bleed: withi
- PMID 25219667
- Extracellular Matrix and Developing Growth Plate.
- Myllyharju J.
- Current osteoporosis reports.Curr Osteoporos Rep.2014 Sep 12. [Epub ahead of print]
- Growth plate is a specialized cartilaginous structure that mediates the longitudinal growth of skeletal bones. It consists of ordered zones of chondrocytes that secrete an extracellular matrix (ECM) composed of specific types of collagens and proteoglycans. Several heritable human skeletal dysplasia
- PMID 25212565
Japanese Journal
- Three Dimensional Spheroid Culture of Canine Amniotic Fluid Derived Mesenchymal Stem Cells Enhances Differentiation Efficacycy
- Journal of the Faculty of Agriculture, Kyushu University 60(2), 377-384, 2015-09-18
- NAID 120005661372
- Culture temperature affects redifferentiation and cartilaginous extracellular matrix formation in dedifferentiated human chondrocytes.
- The combined effects of iguratimod with anti-TNFα antibody on experimental arthritis models in mice
Related Links
- The official name of this gene is “cartilage oligomeric matrix protein.” COMP is the gene's official symbol. The COMP gene is also known by other names, listed below. Read more about gene names and symbols on the About ...
- UCSD Nature Molecule Pages Published online: 4 Nov 2010 | doi:10.1038/mp.a002469.01 Cartilage oligomeric matrix protein Basis Sequence: Mouse Karen Posey 1, Françoise Coustry 1, Jacqueline T Hecht 1, Jack Lawler 2 1 ...
Related Pictures
★リンクテーブル★
[★]
- 英
- cartilage oligomeric matrix protein、COMP
[★]
[★]
[★]
- 関
- oligomer
[★]
- 関
- oligomeric