ADAM8

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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A Disintegrin and metalloproteinase domain-containing protein 8 is an enzyme that in humans is encoded by the ADAM8 gene.[1][2]

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.[2]

See also

References

  1. 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.
  2. 2.0 2.1 "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. 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.
  • 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. PMID 17979891.

External links

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


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