stringtranslate.com

ADAM (protein)

Diagram of an ectodomain shedding ADAM metalloprotease.

ADAMs (short for a disintegrin and metalloproteinase) are a family of single-pass transmembrane and secreted metalloendopeptidases.[1][2] All ADAMs are characterized by a particular domain organization featuring a pro-domain, a metalloprotease, a disintegrin, a cysteine-rich, an epidermal-growth factor like and a transmembrane domain, as well as a C-terminal cytoplasmic tail.[3] Nonetheless, not all human ADAMs have a functional protease domain, which indicates that their biological function mainly depends on protein–protein interactions.[4] Those ADAMs which are active proteases are classified as sheddases because they cut off or shed extracellular portions of transmembrane proteins.[4] For example, ADAM10 can cut off part of the HER2 receptor, thereby activating it.[5] ADAM genes are found in animals, choanoflagellates, fungi and some groups of green algae. Most green algae and all land plants likely lost ADAM proteins.[6]

ADAMs are categorized under the EC 3.4.24.46 enzyme group, and in the MEROPS peptidase family M12B.[3] The terms adamalysin and MDC family (metalloproteinase-like, disintegrin-like, cysteine rich) have been used to refer to this family historically.[7]

ADAM family members

Medicine

Therapeutic ADAM inhibitors might potentiate anti-cancer therapy.[23]

See also

References

  1. ^ Brocker, C; Vasiliou, V; Nebert, DW (October 2009). "Evolutionary divergence and functions of the ADAM and ADAMTS gene families". Human Genomics. 4 (1): 43–55. doi:10.1186/1479-7364-4-1-43. PMC 3500187. PMID 19951893.
  2. ^ Wolfsberg TG, Straight PD, Gerena RL, et al. (1995). "ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain". Dev. Biol. 169 (1): 378–383. doi:10.1006/dbio.1995.1152. PMID 7750654.
  3. ^ a b "ADAM, cysteine-rich (IPR006586)". InterPro. Retrieved 18 February 2016.
  4. ^ a b Edwards DR, Handsley MM, Pennington CJ (October 2008). "The ADAM metalloproteinases". Mol. Aspects Med. 29 (5): 258–89. doi:10.1016/j.mam.2008.08.001. PMC 7112278. PMID 18762209.
  5. ^ Liu, P.C.; et al. (2006). "Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells". Cancer Biology and Therapy. 5 (6): 657–664. doi:10.4161/cbt.5.6.2708. PMID 16627989.
  6. ^ Souza J, Lisboa A, Santos T, Andrade M, Neves V, Teles-Souza J, Jesus H, Bezerra T, Falcão V, Oliveira R, Del-Bem L (2020). "The evolution of ADAM gene family in eukaryotes". Genomics. 112 (5): 3108–3116. doi:10.1016/j.ygeno.2020.05.010. PMID 32437852. S2CID 218832838.
  7. ^ Blobel, CP (22 August 1997). "Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF alpha and Notch". Cell. 90 (4): 589–92. doi:10.1016/s0092-8674(00)80519-x. PMID 9288739. S2CID 17710705.
  8. ^ "Entrez Gene: ADAM2 ADAM metallopeptidase domain 2 (fertilin beta)".
  9. ^ "Entrez Gene: ADAM metallopeptidase domain 7".
  10. ^ "Entrez Gene: ADAM8 ADAM metallopeptidase domain 8".
  11. ^ "Entrez Gene: ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma)".
  12. ^ "Entry of ADAM10 endopeptidase (EC-Number 3.4.24.81 )".
  13. ^ "Entrez Gene: ADAM11 ADAM metallopeptidase domain 11".
  14. ^ Danforth's Obstetrics and Gynecology, 10th Edition; Copyright 2008 Lippincott Williams & Wilkins; Chapter 7: Prenatal Diagnosis, Page 113
  15. ^ "Entrez Gene: ADAM15 ADAM metallopeptidase domain 15 (metargidin)".
  16. ^ Li Y, Brazzell J, Herrera A, Walcheck B (October 2006). "ADAM17 deficiency by mature neutrophils has differential effects on L-selectin shedding". Blood. 108 (7): 2275–9. doi:10.1182/blood-2006-02-005827. PMC 1895557. PMID 16735599.
  17. ^ "Entrez Gene: ADAM18 ADAM metallopeptidase domain 18".
  18. ^ "Entrez Gene: ADAM19 ADAM metallopeptidase domain 19 (meltrin beta)".
  19. ^ "Entrez Gene: ADAM22 ADAM metallopeptidase domain 22".
  20. ^ "Entrez Gene: ADAM23 ADAM metallopeptidase domain 23".
  21. ^ "Entrez Gene: ADAM28 ADAM metallopeptidase domain 28".
  22. ^ "Entrez Gene: ADAM33 ADAM metallopeptidase domain 33".
  23. ^ Guo, Zhen; Jin, Xunbo; Jia, Haiyan (2013). "Inhibition of ADAM-17 more effectively down-regulates the Notch pathway than that of γ-secretase in renal carcinoma". Journal of Experimental & Clinical Cancer Research. 32 (1): 26. doi:10.1186/1756-9966-32-26. PMC 3662624. PMID 23659326.

External links