Encyclopedia of Signaling Molecules

2012 Edition
| Editors: Sangdun Choi

E-NTPDase Family

  • Jean Sévigny
Reference work entry
DOI: https://doi.org/10.1007/978-1-4419-0461-4_197

Synonyms

Historical Background

Nucleoside triphosphate diphosphohydrolases (NTPDases), originally ATP diphosphohydrolases (ATPDases) with the common name apyrase, are by definition enzymes which split the γ- and β-phosphate residues of triphospho- and diphosphonucleosides such as ATP and ADP, respectively. Before the cloning of the gene, the common name apyrase was generally used for enzymes that exhibit this activity in plants and invertebrates while the terms ecto-ATPase and ATP diphosphohydrolase (ATPDase) were rather used in vertebrates. Shortly after cloning the first gene encoding such an enzyme, the nomenclature was unified in mammals to NTPDase, which better reflects the ability of these enzymes to convert not only ATP and ADP, but also other triphospho- and diphosphonucleosides.

A first apyrase was discovered in potato...

This is a preview of subscription content, log in to check access.

References

  1. Beaudoin AR, Sévigny J, Picher M. ATP-diphosphohydrolases, apyrases, and nucleotide phosphohydrolases: biochemical properties and functions. In: Lee AG, editor. ATPases. Greenwich: JAI Press; 1996. p. 369–401.CrossRefGoogle Scholar
  2. Bigonnesse F, Lévesque SA, Kukulski F, Lecka J, Robson SC, Fernandes MJG, et al. Cloning and characterization of mouse nucleoside triphosphate diphosphohydrolase-8. Biochemistry. 2004;43(18):5511–9.PubMedCrossRefGoogle Scholar
  3. Deaglio S, Robson SC. Ectonucleotidases as regulators of purinergic signaling in thrombosis, inflammation, and immunity. Adv Pharmacol. 2011;61:301–32.PubMedCrossRefGoogle Scholar
  4. Enjyoji K, Sévigny J, Lin Y, Frenette PS, Christie PD, Schulte Am Esch IIJ, et al. Targeted disruption of CD39/ATP diphosphohydrolase results in disordered hemostasis and thromboregulation. Nat Med. 1999;5(9):1010–7.PubMedCrossRefGoogle Scholar
  5. Friedman DJ, Kunzli BM, Yi AR, Sévigny J, Berberat PO, Enjyoji K, et al. From the Cover: CD39 deletion exacerbates experimental murine colitis and human polymorphisms increase susceptibility to inflammatory bowel disease. Proc Nat Acad Sci USA. 2009;106(39):16788–93.PubMedCrossRefGoogle Scholar
  6. Grinthal A, Guidotti G. CD39, NTPDase 1, is attached to the plasma membrane by two transmembrane domains. Why? Purinergic Signal. 2006;2(2):391–8.PubMedCrossRefGoogle Scholar
  7. Ivanenkov VV, Meller J, Kirley TL. Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling. Biochemistry. 2005;44(25):8998–9012.PubMedCrossRefGoogle Scholar
  8. Kaczmarek E, Koziak K, Sévigny J, Siegel JB, Anrather J, Beaudoin AR, et al. Identification and characterization of CD39 vascular ATP diphosphohydrolase. J Biol Chem. 1996;271(51):33116–22.PubMedCrossRefGoogle Scholar
  9. Kegel B, Braun N, Heine P, Maliszewski CR, Zimmermann H. An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain. Neuropharmacology. 1997;36(9):1189–200.PubMedCrossRefGoogle Scholar
  10. Kirley TL. Complementery DNA cloning and sequencing of the chicken muscle ecto-ATPase – homology with the lymphoid cell activation antigen CD39. J Biol Chem. 1997;272(2):1076–81.PubMedGoogle Scholar
  11. Knowles AF. The GDA1_CD39 superfamily: NTPDases with diverse functions. Purinergic Signal. 2011;7(1):21–45.PubMedCrossRefGoogle Scholar
  12. Kukulski F, Lévesque SA, Lavoie EG, Lecka J, Bigonnesse F, Knowles AF, et al. Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8. Purinergic Signal. 2005;1(2):193–204.PubMedCrossRefGoogle Scholar
  13. Kukulski F, Lévesque SA, Sévigny J. Impact of ectoenzymes on P2 and P1 receptor signaling. Adv Pharmacol. 2011;61:263–99.PubMedCrossRefGoogle Scholar
  14. Massé K, Bhamra S, Eason R, Dale N, Jones EA. Purine-mediated signalling triggers eye development. Nature. 2007;449(7165):1058–62.PubMedCrossRefGoogle Scholar
  15. Mizumoto N, Kumamoto T, Robson SC, Sévigny J, Matsue H, Enjyoji K, et al. CD39 is the dominant langerhans cell-associated ecto-NTPDase: modulatory roles in inflammation and immune responsiveness. Nat Med. 2002;8(4):358–65.PubMedCrossRefGoogle Scholar
  16. Plesner L. Ecto-ATPases: identities and functions. Int Rev Cytol. 1995;158:141–214.PubMedCrossRefGoogle Scholar
  17. Robson SC, Sévigny J, Zimmermann H. The E-NTPDase family of ectonucleotidases: structure function relationships and pathophysiological significance. Purinergic Signal. 2006;2(2):409–30.PubMedCrossRefGoogle Scholar
  18. Sévigny J, Sundberg C, Braun N, Guckelberger O, Csizmadia E, Qawi I, et al. Differential catalytic properties and vascular topography of murine nucleoside triphosphate diphosphohydrolase 1 (NTPDase1) and NTPDase2 have implications for thromboregulation. Blood. 2002;99(8):2801–9.PubMedCrossRefGoogle Scholar
  19. Smith TM, Kirley TL. Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases. Biochim Biophys Acta Protein Struct Mol Enzymol. 1998;1386(1):65–78.CrossRefGoogle Scholar
  20. Wang T-F, Guidotti G. CD39 is an ecto-(Ca2+, Mg2+)-apyrase. J Biol Chem. 1996;271:9898–901.PubMedCrossRefGoogle Scholar
  21. Yegutkin GG. Nucleotide- and nucleoside-converting ectoenzymes: important modulators of purinergic signalling cascade. Biochim Biophys Acta. 2008;1783(5):673–94.PubMedCrossRefGoogle Scholar
  22. Zebisch M, Strater N. Structural insight into signal conversion and inactivation by NTPDase2 in purinergic signaling. Proc Natl Acad Sci USA. 2008;105(19):6882–7.PubMedCrossRefGoogle Scholar
  23. Zimmermann H, Beaudoin AR, Bollen M, W. GJ, Guidotti G, Kirley TL, et al., editors. Proposed nomenclature for two novel nucleotide hydrolyzing enzyme families expressed on the cell surface. Proceedings of the Second International Workshop on Ecto-ATPases and Related Ectonucleotidases; 1999/2000; Diepenbeek, Belgium\Maastricht: Shaker; 2000Google Scholar

Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  1. 1.Department of Microbiology-Infectiology and ImmunologyCentre de Recherche en Rhumatologie et Immunologie, CHUQ Research Centre, Université LavalQuebecCanada