ADAM8

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

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; OMA:ADAM8 - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10q26.3 Start 133,262,420 bp End 133,276,868 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 F4 Start 139,558,845 bp End 139,572,475 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte blood spleen monocyte bone marrow cells pancreatic ductal cell periodontal fiber appendix upper lobe of left lung right lung Top expressed in granulocyte stroma of bone marrow decidua trachea calvaria tibiofemoral joint lumbar spinal ganglion gastrula vein mesenteric lymph nodes More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding protein self-association peptidase activity 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 podosome phagolysosome alpha9-beta1 integrin-ADAM8 complex plasma 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: 139.56 – 139.57 Mb PubMed search
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.

See also

• Cluster of differentiation

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 10354553.278-84&rft.date=1999-06&rft_id=info:doi/10.1016/S0167-5699(99)01464-4&rft_id=info:pmid/10354553&rft.aulast=Yamamoto&rft.aufirst=S&rft.au=Higuchi, Y&rft.au=Yoshiyama, K&rft.au=Shimizu, E&rft.au=Kataoka, M&rft.au=Hijiya, N&rft.au=Matsuura, K&rfr_id=info:sid/en.wikipedia.org:ADAM8" class="Z3988">
• 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 11050116.7964-71&rft.date=2000-11&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6772711#id-name=PMC&rft_id=info:pmid/11050116&rft_id=info:doi/10.1523/JNEUROSCI.20-21-07964.2000&rft.aulast=Schlomann&rft.aufirst=U&rft.au=Rathke-Hartlieb, S&rft.au=Yamamoto, S&rft.au=Jockusch, H&rft.au=Bartsch, JW&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6772711&rfr_id=info:sid/en.wikipedia.org:ADAM8" class="Z3988">
• 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 37423323.1–3&rft.pages=154-8&rft.date=2002-07&rft_id=https://api.semanticscholar.org/CorpusID:37423323#id-name=S2CID&rft_id=info:pmid/12135759&rft_id=info:doi/10.1016/S0014-5793(02)03047-8&rft.aulast=Amour&rft.aufirst=A&rft.au=Knight, CG&rft.au=English, WR&rft.au=Webster, A&rft.au=Slocombe, PM&rft.au=Knäuper, V&rft.au=Docherty, AJ&rft.au=Becherer, JD&rft.au=Blobel, CP&rft.au=Murphy, G&rft_id=https://doi.org/10.1016%2FS0014-5793%2802%2903047-8&rfr_id=info:sid/en.wikipedia.org:ADAM8" class="Z3988">
• 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 15623614.8363-70&rft.date=2004-12&rft_id=info:doi/10.1158/1078-0432.CCR-04-1436&rft_id=info:pmid/15623614&rft.aulast=Ishikawa&rft.aufirst=N&rft.au=Daigo, Y&rft.au=Yasui, W&rft.au=Inai, K&rft.au=Nishimura, H&rft.au=Tsuchiya, E&rft.au=Kohno, N&rft.au=Nakamura, Y&rft_id=https://doi.org/10.1158%2F1078-0432.CCR-04-1436&rfr_id=info:sid/en.wikipedia.org:ADAM8" class="Z3988">
• 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 17339047.863-71&rft.date=2007-04&rft_id=info:doi/10.1016/j.jaci.2006.12.665&rft_id=info:pmid/17339047&rft.aulast=Foley&rft.aufirst=SC&rft.au=Mogas, AK&rft.au=Olivenstein, R&rft.au=Fiset, PO&rft.au=Chakir, J&rft.au=Bourbeau, J&rft.au=Ernst, P&rft.au=Lemière, C&rft.au=Martin, JG&rft.au=Hamid, Q&rft_id=https://doi.org/10.1016%2Fj.jaci.2006.12.665&rfr_id=info:sid/en.wikipedia.org:ADAM8" class="Z3988">
• 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 17548643.8053-63&rft.date=2007-06&rft_id=info:doi/10.4049/jimmunol.178.12.8053&rft_id=info:pmid/17548643&rft.aulast=Gómez-Gaviro&rft.aufirst=M&rft.au=Domínguez-Luis, M&rft.au=Canchado, J&rft.au=Calafat, J&rft.au=Janssen, H&rft.au=Lara-Pezzi, E&rft.au=Fourie, A&rft.au=Tugores, A&rft.au=Valenzuela-Fernández, A&rft.au=Mollinedo, F&rft.au=Sánchez-Madrid, F&rft.au=Díaz-González, F&rft_id=https://doi.org/10.4049%2Fjimmunol.178.12.8053&rfr_id=info:sid/en.wikipedia.org:ADAM8" class="Z3988">
• 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 17979891.1162-74&rft.date=2008&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4401277#id-name=PMC&rft_id=info:pmid/17979891&rft_id=info:doi/10.1111/j.1582-4934.2007.00082.x&rft.aulast=Valkovskaya&rft.aufirst=N&rft.au=Kayed, H&rft.au=Felix, K&rft.au=Hartmann, D&rft.au=Giese, NA&rft.au=Osinsky, SP&rft.au=Friess, H&rft.au=Kleeff, J&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4401277&rfr_id=info:sid/en.wikipedia.org:ADAM8" class="Z3988">

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.