A disintegrin and metalloproteinase

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Diagram of an ectodomain shedding ADAM metalloprotease.

ADAM (A Disintegrin And Metalloproteinase)[1][2] is a family of peptidase proteins.[3] It is also known as the adamalysin family or MDC family(metalloproteinase-like, Disintegrin-like, cysteine rich). ADAMs are classified as sheddases because they cut off or shed extracellular portions of transmembrane proteins. For example, ADAM10 can cut off part of the HER2 receptor, activating it.[4] Therapeutic ADAM inhibitors can potentiate anti-cancer therapy.[citation needed]

It is categorized under EC 3.4.24.46.

ADAM[edit]

Family members are:

See also[edit]

References[edit]

  1. ^ 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. PMID 18762209. 
  2. ^ Brocker, C; Vasiliou, V; Nebert, DW (Oct 2009). "Evolutionary divergence and functions of the ADAM and ADAMTS gene families.". Human Genomics 4 (1): 43–55. PMC 3500187. PMID 19951893. 
  3. ^ 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. 
  4. ^ 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. 

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