Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

ADAM17

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_72-2

Synonyms

Definition

ADAM17 is a zinc-dependent metalloprotease belonging to the ADAM (A disintegrin and metalloproteinase) family of type I transmembrane proteins. ADAM17 is involved in the ectodomain shedding of a wide variety of membrane-bound ligands and cytokines that are implicated in diverse biological processes including growth and inflammation.

Characteristics

Structure

The 50 kb ADAM17 gene, which is located at chromosome 2p25, consists of 19 exons, and encodes an 824 amino acid protein. ADAM17 is synthesized as an inactive precursor protein consisting of five domains: the pro-, metalloprotease, cysteine-rich, transmembrane, and cytoplasmic domains. Prior to ADAM17 maturation, a conserved cysteine residue within the pro-domain interacts with the active site zinc atom maintaining the enzyme biologically inert. The active site of the metalloprotease domain contains a histidine consensus sequence (HExxHxxGxxH)...

Keywords

Epidermal Growth Factor Receptor Small Cell Lung Cancer Cell Epidermal Growth Factor Receptor Ligand ADAM17 Activity Hair Follicle Development 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Blobel CP (2005) ADAMS: key components in EGFR signalling and development. Nat Rev Mol Cell Biol 6:32–43CrossRefPubMedGoogle Scholar
  2. Franovic A, Robert I, Smith K et al (2006) Multiple acquired renal carcinoma tumor capabilities abolished upon silencing of ADAM17. Cancer Res 66:8083–8090CrossRefPubMedGoogle Scholar
  3. Lee DC, Sunnarborg SW, Hinkle CL et al (2003) TACE/ADAM17 processing of EGFR ligands indicates a role as a physiological convertase. Ann N Y Acad Sci 995:22–38CrossRefPubMedGoogle Scholar
  4. Seals DF, Courtneidge SA (2003) The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 17:7–30CrossRefPubMedGoogle Scholar
  5. Zhou BS, Peyton M, He B et al (2006) Targeting ADAM-mediated ligand cleavage to inhibit HER3 and EGFR pathways in non-small cell lung cancer. Cancer Cell 10:39–50CrossRefPubMedPubMedCentralGoogle Scholar

See Also

  1. (2012) EGFR In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1211. doi:10.1007/978-3-642-16483-5_1828Google Scholar
  2. (2012) ERK. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, pp 1307–1308. doi:10.1007/978-3-642-16483-5_1987Google Scholar
  3. (2012) Extracellular Signal-Regulated Kinase. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1365. doi:10.1007/978-3-642-16483-5_2070Google Scholar
  4. (2012) HER3. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1680. doi:10.1007/978-3-642-16483-5_2678Google Scholar
  5. (2012) Heregulin. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1684. doi:10.1007/978-3-642-16483-5_2685Google Scholar
  6. (2012) Integrin. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1884. doi:10.1007/978-3-642-16483-5_3084Google Scholar
  7. (2012) Metalloproteases. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 2259. doi:10.1007/978-3-642-16483-5_3666Google Scholar
  8. (2012) Notch Signaling. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 2559. doi:10.1007/978-3-642-16483-5_4131Google Scholar
  9. (2012) Phorbol 12-Myristate 13-Acetate. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 2865. doi:10.1007/978-3-642-16483-5_4523Google Scholar
  10. (2012) PMA. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, pp 2930–2931. doi:10.1007/978-3-642-16483-5_4641Google Scholar
  11. (2012) Renal Cancer. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, pp 3225–3226. doi:10.1007/978-3-642-16483-5_6575Google Scholar
  12. (2012) Small-Molecule Inhibitors. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3455. doi:10.1007/978-3-642-16483-5_5375Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Department of Cellular and Molecular Medicine, Faculty of MedicineUniversity of OttawaOttawaCanada