| ADAMTS8 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | ADAMTS8, ADAM-TS8, METH2, ADAM metallopeptidase with thrombospondin type 1 motif 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 605175 MGI: 1353468 HomoloGene: 5108 GeneCards: ADAMTS8 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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A disintegrin and metalloproteinase with thrombospondin motifs 8 is an enzyme that in humans is encoded by the ADAMTS8 gene.[5][6]
Function
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains two C-terminal TS motifs, and disrupts angiogenesis in vivo.[6]
Clinical significance
A number of disorders have been mapped in the vicinity of this gene, most notably lung neoplasms.[6]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000134917 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031994 - Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Vazquez F, Hastings G, Ortega MA, Lane TF, Oikemus S, Lombardo M, Iruela-Arispe ML (Sep 1999). "METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity". J Biol Chem. 274 (33): 23349–57. doi:10.1074/jbc.274.33.23349. PMID 10438512.
- 1 2 3 "Entrez Gene: ADAMTS8 ADAM metallopeptidase with thrombospondin type 1 motif, 8".
Further reading
- Wågsäter D, Björk H, Zhu C, et al. (2008). "ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques". Atherosclerosis. 196 (2): 514–22. doi:10.1016/j.atherosclerosis.2007.05.018. PMID 17606262.
- Dunn JR, Reed JE, du Plessis DG, et al. (2006). "Expression of ADAMTS-8, a secreted protease with antiangiogenic properties, is downregulated in brain tumours". Br. J. Cancer. 94 (8): 1186–93. doi:10.1038/sj.bjc.6603006. PMC 2361255. PMID 16570050.
- Porter S, Span PN, Sweep FC, et al. (2006). "ADAMTS8 and ADAMTS15 expression predicts survival in human breast carcinoma". Int. J. Cancer. 118 (5): 1241–7. doi:10.1002/ijc.21476. PMID 16152618. S2CID 20711295.
- Dunn JR, Panutsopulos D, Shaw MW, et al. (2004). "METH-2 silencing and promoter hypermethylation in NSCLC". Br. J. Cancer. 91 (6): 1149–54. doi:10.1038/sj.bjc.6602107. PMC 2747718. PMID 15328519.
- Collins-Racie LA, Flannery CR, Zeng W, et al. (2005). "ADAMTS-8 exhibits aggrecanase activity and is expressed in human articular cartilage". Matrix Biol. 23 (4): 219–30. doi:10.1016/j.matbio.2004.05.004. PMID 15296936.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Georgiadis KE, Hirohata S, Seldin MF, Apte SS (2000). "ADAM-TS8, a novel metalloprotease of the ADAM-TS family located on mouse chromosome 9 and human chromosome 11". Genomics. 62 (2): 312–5. doi:10.1006/geno.1999.6014. PMID 10610729.
External links
- The MEROPS online database for peptidases and their inhibitors: M12.226
- Human ADAMTS8 genome location and ADAMTS8 gene details page in the UCSC Genome Browser.
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