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ADAMTS8
Identifiers
Aliases	ADAMTS8, ADAM-TS8, METH2, ADAM metallopeptidase with thrombospondin type 1 motif 8
External IDs	OMIM: 605175; MGI: 1353468; HomoloGene: 5108; GeneCards: ADAMTS8; OMA:ADAMTS8 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q24.3 Start 130,404,923 bp End 130,428,609 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9 A4|9 16.49 cM Start 30,853,858 bp End 30,875,134 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in middle temporal gyrus upper lobe of left lung endothelial cell lower lobe of lung right lung Brodmann area 23 entorhinal cortex tail of epididymis right coronary artery visceral pleura Top expressed in tunica media of zone of aorta lumbar spinal ganglion soleus muscle ankle atrium internal carotid artery endocardial cushion semi-lunar valve inner muscle layer tunica adventitia of aorta More reference expression data BioGPS n/a
Gene ontology Molecular function integrin binding zinc ion binding peptidase activity metalloendopeptidase activity heparin binding low-affinity phosphate transmembrane transporter activity metallopeptidase activity hydrolase activity metal ion binding Cellular component extracellular region extracellular matrix collagen-containing extracellular matrix Biological process proteolysis negative regulation of cell population proliferation phosphate ion transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11095 30806 Ensembl ENSG00000134917 ENSMUSG00000031994 UniProt Q9UP79 P57110 RefSeq (mRNA) NM_007037 NM_013906 NM_001326292 RefSeq (protein) NP_008968 NP_038934.2 Location (UCSC) Chr 11: 130.4 – 130.43 Mb Chr 9: 30.85 – 30.88 Mb PubMed search
Wikidata
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A disintegrin and metalloproteinase with thrombospondin motifs 8 is an enzyme that in humans is encoded by the ADAMTS8 gene.

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.

Clinical significance

A number of disorders have been mapped in the vicinity of this gene, most notably lung neoplasms.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000134917 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000031994 – 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. 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.
6. ^ "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.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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