High impact information on ENTPD1

• A comparison of the kinetic properties of this ATPDase with those of pig pancreas (Type I) and bovine aorta (Type II) lead us to believe that this enzyme is an hitherto undescribed type of ATPDase [1].
• Resistance of ATP analogues to hydrolysis and their potency as NTPDase inhibitors were evaluated [2].
• To elucidate the physiological role played by nucleoside triphosphate diphosphohydrolase (NTPDase; EC 3.6.1.5), adenine nucleotide analogues, modified on the purine ring, have been synthesized and tested as potential inhibitors [2].
• Because in previous studies on isolated turkey erythrocytes and rat astrocytes 8-BuS-ATP was not able to trigger any P2Y(1)-receptor-mediated effect, it therefore appears that this NTPDase inhibitor does not interfere with purinergic receptors [2].
• The nucleoside triphosphate diphosphohydrolases (NTPDase; EC 3.6.1. 5) are a family of ectonucleotidases associated with vascular endothelial and smooth muscle cells [3].

Biological context of ENTPD1

• All the non-hydrolysable analogues tested, except alpha,beta-metADP, competed with ATP and ADP for the ATPDase catalytic site, reducing their hydrolysis by 35-50% [4].
• Vascular ATP-diphosphohydrolase (ATPDase) has been demonstrated on both aortic EC and smooth muscle cells and may play a key regulatory role in hemostasis and platelet reactivity by converting extracellular ATP and ADP to AMP [5].
• We conclude that endothelial ATPDase activity may be regulated by exogenous fatty acids and that underlying mechanisms include alterations in the nature of the phospholipid composition of EC membranes that influence responses to oxidative stress reactions [5].
• Such a wide distribution suggests that the ATPDase may affect a variety of physiological effects mediated by extracellular nucleotides, such as airway smooth muscle tone, surfactant secretion, platelet aggregation, and inflammation [6].

Anatomical context of ENTPD1

• Assays were conducted with a purified ATPDase from smooth muscle cells of bovine aorta [4].
• Demonstration of an ectoATP-diphosphohydrolase (E.C.3.6.1.5.) in non-vascular smooth muscles of the bovine trachea [7].
• Enzyme markers indicate that the ATPDase is associated with the plasma membrane [7].

Associations of ENTPD1 with chemical compounds

• Ca(2+)-channel blockers and nucleoside triphosphate diphosphohydrolase (NTPDase) influence of diltiazem, nifedipine, and verapamil [3].
• Considering the external localization of the NTPDase catalytic site and its Ca(2+) requirement for enzyme activity, a possible interference of calcium antagonists (nifedipine, verapamil-HCl, and diltiazem-HCl and some of its metabolites) could be anticipated [3].
• EC cultures supplemented with saturated or a monounsaturated (oleic acid) fatty acid(s) had markedly increased ATPDase activity, whereas those exposed to polyunsaturated fatty acids showed substantive decreases [5].
• In the present study, we purified the lung ATPDase by column chromatographies followed by polyacrylamide gel electrophoresis under nondenaturing conditions [6].
• A polyclonal antibody raised against the pancreas ATPDase, which specifically recognized the 78-kDa glycoprotein on Western blot, was used to carry out an immunological survey of the enzyme distribution in bovine lungs [6].

Analytical, diagnostic and therapeutic context of ENTPD1

• Western blots with Ringo, an antibody that recognizes the different isoforms of mammalian NTPDases, show a small but reproducible difference in estimated molecular masses (75 kDa for liver vs 78 kDa for spleen NTPDase) [8].

References