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ADAM (protein)

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. 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. Nonetheless, not all human ADAMs have a functional protease domain, which indicates that their biological function mainly depends on protein–protein interactions. Those ADAMs which are active proteases 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, thereby activating it. ADAM genes are found in animals, choanoflagellates, fungi and some groups of green algae. Most green algae and all land plants probably had ADAM proteins but lost them.

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

ADAM family members

ProteinDescription
ADAM1ADAM1 (fertilin α) is a subunit of an integral sperm membrane heterodimeric glycoprotein called fertilin, which plays an important role in sperm-egg interactions.
ADAM2title = Entrez Gene: ADAM2 ADAM metallopeptidase domain 2 (fertilin beta)url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=2515}}
ADAM7title = Entrez Gene: ADAM metallopeptidase domain 7url = https://www.ncbi.nlm.nih.gov/gene/8756 }}
ADAM8title = Entrez Gene: ADAM8 ADAM metallopeptidase domain 8url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=101}}
ADAM9title = Entrez Gene: ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma)url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8754}}
ADAM10title = Entry of ADAM10 endopeptidase (EC-Number 3.4.24.81 )url = http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.81}}
ADAM11title = Entrez Gene: ADAM11 ADAM metallopeptidase domain 11url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=4185}}
ADAM12ADAM12, a metalloprotease that binds insulin growth factor binding protein-3 (IGFBP-3), appears to be an effective early Down syndrome marker.
ADAM15Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein–tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling.
ADAM17ADAM17 is understood to be involved in the processing of tumor necrosis factor alpha (TNF-α) at the surface of the cell, and from within the intracellular membranes of the trans-Golgi network. ADAM17 also has a role in the shedding of L-selectin, a cellular adhesion molecule.
ADAM18title = Entrez Gene: ADAM18 ADAM metallopeptidase domain 18url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8749}} Synonymous with ADAM27.
ADAM19title = Entrez Gene: ADAM19 ADAM metallopeptidase domain 19 (meltrin beta)url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8728}}
ADAM20Exclusively expressed in the testes.
ADAM21Note: Synonymous with ADAM31.
ADAM22title = Entrez Gene: ADAM22 ADAM metallopeptidase domain 22url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=53616}}
ADAM23title = Entrez Gene: ADAM23 ADAM metallopeptidase domain 23url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8745}}
ADAM28title = Entrez Gene: ADAM28 ADAM metallopeptidase domain 28url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=10863}}
ADAM29
ADAM30
ADAM33title = Entrez Gene: ADAM33 ADAM metallopeptidase domain 33url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=80332}}

Medicine

Therapeutic ADAM inhibitors might potentiate anti-cancer therapy.

References

References

  1. Brocker, C. (October 2009). "Evolutionary divergence and functions of the ADAM and ADAMTS gene families.". Human Genomics.
  2. (1995). "ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain". Dev. Biol..
  3. "ADAM, cysteine-rich (IPR006586)".
  4. (October 2008). "The ADAM metalloproteinases". Mol. Aspects Med..
  5. Liu, P.C.. (2006). "Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells.". Cancer Biology and Therapy.
  6. (2020). "The evolution of ADAM gene family in eukaryotes". Genomics.
  7. (22 August 1997). "Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF alpha and Notch.". Cell.
  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. (October 2006). "ADAM17 deficiency by mature neutrophils has differential effects on L-selectin shedding". Blood.
  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. (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.
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protein-families single-pass-transmembrane-proteins proteases ec-3.4.24
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