ADAM8

ADAM metallopeptidase domain 8
Identifiers
Symbols	ADAM8; CD156; MS2
External IDs	OMIM: 602267 MGI: 107825 HomoloGene: 74384 GeneCards: ADAM8 Gene
EC number	3.4.24.-
Gene Ontology Molecular function • metalloendopeptidase activity • calcium ion binding • protein binding • peptidase activity • metallopeptidase activity • zinc ion binding • protein self-association • cell adhesion molecule binding Cellular component • podosome • cytoplasm • plasma membrane • integral to plasma membrane • cell surface • phagolysosome • dense core granule membrane • specific granule • tertiary granule • alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex • alpha9-beta1 integrin-ADAM8 complex Biological process • cell morphogenesis • angiogenesis • leukocyte migration involved in inflammatory response • positive regulation of acute inflammatory response • positive regulation of leukocyte migration • positive regulation of cellular extravasation • proteolysis • inflammatory response • positive regulation of protein processing • regulation of cell-cell adhesion • positive regulation of cell migration • positive regulation of T cell differentiation in thymus • activation of MAPK activity involved in innate immune response • negative regulation of neuron apoptosis • positive regulation of bone resorption • positive regulation of cell adhesion • lymphocyte chemotaxis • positive regulation of protein secretion • positive regulation of membrane protein ectodomain proteolysis • positive regulation of NF-kappaB transcription factor activity • positive regulation of protein kinase B signaling cascade • positive regulation of thymocyte apoptosis • cellular response to hypoxia • positive regulation of tumor necrosis factor (ligand) superfamily member 11 production Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	101	11501
Ensembl	ENSG00000151651	ENSMUSG00000025473
UniProt	P78325	Q05910
RefSeq (mRNA)	NM_001109.4	NM_007403.2
RefSeq (protein)	NP_001100.3	NP_031429.1
Location (UCSC)	Chr 10: 134.93 – 134.94 Mb	Chr 7: 147.16 – 147.18 Mb
PubMed search	[1]	[2]

A Disintegrin and metalloproteinase domain-containing protein 8 is an enzyme that in humans is encoded by the ADAM8 gene.

This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene may be involved in cell adhesion during neurodegeneration.

See also

• Cluster of differentiation

Further reading

• Yamamoto S, Higuchi Y, Yoshiyama K et al (1999). "ADAM family proteins in the immune system". Immunol. Today 20 (6): 278–84. doi:10.1016/S0167-5699(99)01464-4. PMID 10354553. 
• Schlomann U, Rathke-Hartlieb S, Yamamoto S et al (2001). "Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): implications for neuron-glia interactions during neurodegeneration". J. Neurosci. 20 (21): 7964–71. PMID 11050116. 
• Amour A, Knight CG, English WR et al (2002). "The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs". FEBS Lett. 524 (1–3): 154–8. doi:10.1016/S0014-5793(02)03047-8. PMID 12135759. 
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Ishikawa N, Daigo Y, Yasui W et al (2005). "ADAM8 as a novel serological and histochemical marker for lung cancer". Clin. Cancer Res. 10 (24): 8363–70. doi:10.1158/1078-0432.CCR-04-1436. PMID 15623614. 
• Kimura K, Wakamatsu A, Suzuki Y et al (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• Foley SC, Mogas AK, Olivenstein R et al (2007). "Increased expression of ADAM33 and ADAM8 with disease progression in asthma". J. Allergy Clin. Immunol. 119 (4): 863–71. doi:10.1016/j.jaci.2006.12.665. PMID 17339047. 
• Gómez-Gaviro M, Domínguez-Luis M, Canchado J et al (2007). "Expression and regulation of the metalloproteinase ADAM-8 during human neutrophil pathophysiological activation and its catalytic activity on L-selectin shedding". J. Immunol. 178 (12): 8053–63. PMID 17548643. 
• Valkovskaya N, Kayed H, Felix K et al (2008). "ADAM8 expression is associated with increased invasiveness and reduced patient survival in pancreatic cancer". J. Cell. Mol. Med. 11 (5): 1162–74. doi:10.1111/j.1582-4934.2007.00082.x. PMID 17979891. 

External links

• The MEROPS online database for peptidases and their inhibitors: M12.208

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