The E-NTPDase family of ectonucleotidases: Structure function relationships and pathophysiological significance
Top Cited Papers
Open Access
- 30 May 2006
- journal article
- research article
- Published by Springer Nature in Purinergic Signalling
- Vol. 2 (2) , 409-430
- https://doi.org/10.1007/s11302-006-9003-5
Abstract
Ectonucleotidases are ectoenzymes that hydrolyze extracellular nucleotides to the respective nucleosides. Within the past decade, ectonucleotidases belonging to several enzyme families have been discovered, cloned and characterized. In this article, we specifically address the cell surface-located members of the ecto-nucleoside triphosphate diphosphohydrolase (E-NTPDase/CD39) family (NTPDase1,2,3, and 8). The molecular identification of individual NTPDase subtypes, genetic engineering, mutational analyses, and the generation of subtype-specific antibodies have resulted in considerable insights into enzyme structure and function. These advances also allow definition of physiological and patho-physiological implications of NTPDases in a considerable variety of tissues. Biological actions of NTPDases are a consequence (at least in part) of the regulated phosphohydrolytic activity on extracellular nucleotides and consequent effects on P2-receptor signaling. It further appears that the spatial and temporal expression of NTPDases by various cell types within the vasculature, the nervous tissues and other tissues impacts on several patho-physiological processes. Examples include acute effects on cellular metabolism, adhesion, activation and migration with other protracted impacts upon developmental responses, inclusive of cellular proliferation, differentiation and apoptosis, as seen with atherosclerosis, degenerative neurological diseases and immune rejection of transplanted organs and cells. Future clinical applications are expected to involve the development of new therapeutic strategies for transplantation and various inflammatory cardiovascular, gastrointestinal and neurological diseases.Keywords
This publication has 260 references indexed in Scilit:
- CD39, NTPDase 1, is attached to the plasma membrane by two transmembrane domains. Why?Purinergic Signalling, 2006
- The structure of the nucleoside triphosphate diphosphohydrolases (NTPDases) as revealed by mutagenic and computational modeling analysesPurinergic Signalling, 2006
- E-NTPDases in human airways: Regulation and relevance for chronic lung diseasesPurinergic Signalling, 2006
- Nucleoside triphosphate diphosphohydrolase‐2 is the ecto‐ATPase of type I cells in taste budsJournal of Comparative Neurology, 2006
- A capillary electrophoresis method for the characterization of ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) and the analysis of inhibitors by in-capillary enzymatic microreactionPurinergic Signalling, 2005
- Cloning and characterization of the ecto-nucleotidase NTPDase3 from rat brain: Predicted secondary structure and relation to other members of the E-NTPDase family and actinPurinergic Signalling, 2005
- Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8Purinergic Signalling, 2005
- Release and extracellular metabolism of ATP by ecto-nucleotidase eNTPDase 1–2 in hypothalamic and pituitary cellsPurinergic Signalling, 2005
- Glial modulation of synaptic transmission in cultureGlia, 2004
- CD39 as a Caveolar-Associated EctonucleotidaseBiochemical and Biophysical Research Communications, 1999