ADAM_Protein

ADAM (protein)

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]

Diagram of an ectodomain shedding ADAM metalloprotease.
Quick Facts Disintegrin and metalloproteinase domain-containing proteins, Identifiers ...

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

More information Protein, Description ...

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. "ADAM, cysteine-rich (IPR006586)". InterPro. Retrieved 18 February 2016.
  3. 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.
  4. 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.
  5. Danforth's Obstetrics and Gynecology, 10th Edition; Copyright 2008 Lippincott Williams & Wilkins; Chapter 7: Prenatal Diagnosis, Page 113
  6. 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.

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