ADAM8

A Disintegrin and metalloproteinase domain-containing protein 8 is an enzyme that in humans is encoded by the ADAM8 gene.[5][6]

ADAM8
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4DD8
Identifiers
Aliases	ADAM8, CD156, CD156a, MS2, ADAM metallopeptidase domain 8
External IDs	OMIM: 602267 MGI: 107825 HomoloGene: 74384 GeneCards: ADAM8
Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10q26.3 Start 133,262,420 bp[1] End 133,276,868 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 F4 Start 139,978,932 bp[2] End 139,992,562 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • metal ion binding • protein self-association • peptidase activity • GO:0001948 protein binding • metalloendopeptidase activity • hydrolase activity • cell adhesion molecule binding • calcium ion binding • serine-type endopeptidase activity • metallopeptidase activity • zinc ion binding Cellular component • cytoplasm • integral component of membrane • alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex • membrane • tertiary granule • integral component of plasma membrane • cell surface • specific granule • dense core granule membrane • podosomes • phagolysosome • alpha9-beta1 integrin-ADAM8 complex • cell membrane • specific granule membrane • tertiary granule membrane • ficolin-1-rich granule membrane Biological process • positive regulation of inflammatory response • extracellular matrix disassembly • proteolysis • positive regulation of cellular extravasation • positive regulation of neutrophil extravasation • positive regulation of protein processing • regulation of cell-cell adhesion • positive regulation of protein secretion • inflammatory response • cellular response to hypoxia • positive regulation of T cell migration • positive regulation of tumor necrosis factor (ligand) superfamily member 11 production • positive regulation of acute inflammatory response • cell morphogenesis • positive regulation of thymocyte apoptotic process • positive regulation of bone resorption • negative regulation of neuron apoptotic process • positive regulation of fibronectin-dependent thymocyte migration • positive regulation of eosinophil migration • positive regulation of NF-kappaB transcription factor activity • leukocyte migration involved in inflammatory response • positive regulation of membrane protein ectodomain proteolysis • positive regulation of protein kinase B signaling • positive regulation of T cell differentiation in thymus • lymphocyte chemotaxis • positive regulation of cell adhesion • angiogenesis • neutrophil degranulation • cell-cell adhesion • positive regulation of MAP kinase activity • positive regulation of innate immune response Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	101	11501
Ensembl	ENSG00000151651	ENSMUSG00000025473
UniProt	P78325	Q05910
RefSeq (mRNA)	NM_001109 NM_001164489 NM_001164490	NM_001291066 NM_007403
RefSeq (protein)	NP_001100 NP_001157961 NP_001157962	NP_001277995 NP_031429
Location (UCSC)	Chr 10: 133.26 – 133.28 Mb	Chr 7: 139.98 – 139.99 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the ADAM (a disintegrin and metalloproteinase 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.[6]

See also

• Cluster of differentiation

References

1. GRCh38: Ensembl release 89: ENSG00000151651 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025473 - 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. Yoshiyama K, Higuchi Y, Kataoka M, Matsuura K, Yamamoto S (April 1997). "CD156 (human ADAM8): expression, primary amino acid sequence, and gene location". Genomics. 41 (1): 56–62. doi:10.1006/geno.1997.4607. PMID 9126482.
6. "Entrez Gene: ADAM8 ADAM metallopeptidase domain 8".

Further reading

• Yamamoto S, Higuchi Y, Yoshiyama K, Shimizu E, Kataoka M, Hijiya N, Matsuura K (June 1999). "ADAM family proteins in the immune system". Immunology Today. 20 (6): 278–84. doi:10.1016/S0167-5699(99)01464-4. PMID 10354553.
• Schlomann U, Rathke-Hartlieb S, Yamamoto S, Jockusch H, Bartsch JW (November 2000). "Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): implications for neuron-glia interactions during neurodegeneration". The Journal of Neuroscience. 20 (21): 7964–71. doi:10.1523/JNEUROSCI.20-21-07964.2000. PMC 6772711. PMID 11050116.
• Amour A, Knight CG, English WR, Webster A, Slocombe PM, Knäuper V, Docherty AJ, Becherer JD, Blobel CP, Murphy G (July 2002). "The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs". FEBS Letters. 524 (1–3): 154–8. doi:10.1016/S0014-5793(02)03047-8. PMID 12135759. S2CID 37423323.
• Ishikawa N, Daigo Y, Yasui W, Inai K, Nishimura H, Tsuchiya E, Kohno N, Nakamura Y (December 2004). "ADAM8 as a novel serological and histochemical marker for lung cancer". Clinical Cancer Research. 10 (24): 8363–70. doi:10.1158/1078-0432.CCR-04-1436. PMID 15623614.
• Foley SC, Mogas AK, Olivenstein R, Fiset PO, Chakir J, Bourbeau J, Ernst P, Lemière C, Martin JG, Hamid Q (April 2007). "Increased expression of ADAM33 and ADAM8 with disease progression in asthma". The Journal of Allergy and Clinical Immunology. 119 (4): 863–71. doi:10.1016/j.jaci.2006.12.665. PMID 17339047.
• Gómez-Gaviro M, Domínguez-Luis M, Canchado J, Calafat J, Janssen H, Lara-Pezzi E, Fourie A, Tugores A, Valenzuela-Fernández A, Mollinedo F, Sánchez-Madrid F, Díaz-González F (June 2007). "Expression and regulation of the metalloproteinase ADAM-8 during human neutrophil pathophysiological activation and its catalytic activity on L-selectin shedding". Journal of Immunology. 178 (12): 8053–63. doi:10.4049/jimmunol.178.12.8053. PMID 17548643.
• Valkovskaya N, Kayed H, Felix K, Hartmann D, Giese NA, Osinsky SP, Friess H, Kleeff J (2008). "ADAM8 expression is associated with increased invasiveness and reduced patient survival in pancreatic cancer". Journal of Cellular and Molecular Medicine. 11 (5): 1162–74. doi:10.1111/j.1582-4934.2007.00082.x. PMC 4401277. PMID 17979891.

External links

• The MEROPS online database for peptidases and their inhibitors: M12.208
• ADAM8 human gene location in the UCSC Genome Browser.
• ADAM8 human gene details in the UCSC Genome Browser.
• PDBe-KB provides an overview of all the structure information available in the PDB for Human Disintegrin and metalloproteinase domain-containing protein 8 (ADAM8)

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