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Regulatory role of E-NTPase/E-NTPDase in Ca(2+)/Mg(2+ )transport via gated channel
BACKGROUND: E-NTPase/E-NTPDase is activated by millimolar concentrations of Ca(2+ )or Mg(2+ )with a pH optimum of 7.5 for the hydrolysis of extracellular NTP and NDP. It has been generally accepted that E-NTPase/E-NTPDase plays regulatory role in purinergic signalling, but other functions may yet be...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2004
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC516237/ https://www.ncbi.nlm.nih.gov/pubmed/15307889 http://dx.doi.org/10.1186/1742-4682-1-3 |
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author | Schreiber, Hans M Kannan, Subburaj |
author_facet | Schreiber, Hans M Kannan, Subburaj |
author_sort | Schreiber, Hans M |
collection | PubMed |
description | BACKGROUND: E-NTPase/E-NTPDase is activated by millimolar concentrations of Ca(2+ )or Mg(2+ )with a pH optimum of 7.5 for the hydrolysis of extracellular NTP and NDP. It has been generally accepted that E-NTPase/E-NTPDase plays regulatory role in purinergic signalling, but other functions may yet be discovered. RESULTS: In this article it is proposed on the basis of published data that E-NTPase/E-NTPDase could play a role in the influx and efflux of Ca(2+)and Mg(2+ )in vivo. CONCLUSIONS: Attenuation of extracellular Ca2+ influx by rat cardiac sarcoplasmic anti-E-NTPase antibodies and oligomerization studies on mammalian CD39 conclusively point towards the existence of a new channel in the membrane. Further studies on these properties of the E-NTPase/E-NTPDase may provide detailed mechanisms and identify the potential patho-physiological significance. |
format | Text |
id | pubmed-516237 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-5162372004-09-09 Regulatory role of E-NTPase/E-NTPDase in Ca(2+)/Mg(2+ )transport via gated channel Schreiber, Hans M Kannan, Subburaj Theor Biol Med Model Research BACKGROUND: E-NTPase/E-NTPDase is activated by millimolar concentrations of Ca(2+ )or Mg(2+ )with a pH optimum of 7.5 for the hydrolysis of extracellular NTP and NDP. It has been generally accepted that E-NTPase/E-NTPDase plays regulatory role in purinergic signalling, but other functions may yet be discovered. RESULTS: In this article it is proposed on the basis of published data that E-NTPase/E-NTPDase could play a role in the influx and efflux of Ca(2+)and Mg(2+ )in vivo. CONCLUSIONS: Attenuation of extracellular Ca2+ influx by rat cardiac sarcoplasmic anti-E-NTPase antibodies and oligomerization studies on mammalian CD39 conclusively point towards the existence of a new channel in the membrane. Further studies on these properties of the E-NTPase/E-NTPDase may provide detailed mechanisms and identify the potential patho-physiological significance. BioMed Central 2004-08-12 /pmc/articles/PMC516237/ /pubmed/15307889 http://dx.doi.org/10.1186/1742-4682-1-3 Text en Copyright © 2004 Schreiber and Kannan; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open-access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Schreiber, Hans M Kannan, Subburaj Regulatory role of E-NTPase/E-NTPDase in Ca(2+)/Mg(2+ )transport via gated channel |
title | Regulatory role of E-NTPase/E-NTPDase in Ca(2+)/Mg(2+ )transport via gated channel |
title_full | Regulatory role of E-NTPase/E-NTPDase in Ca(2+)/Mg(2+ )transport via gated channel |
title_fullStr | Regulatory role of E-NTPase/E-NTPDase in Ca(2+)/Mg(2+ )transport via gated channel |
title_full_unstemmed | Regulatory role of E-NTPase/E-NTPDase in Ca(2+)/Mg(2+ )transport via gated channel |
title_short | Regulatory role of E-NTPase/E-NTPDase in Ca(2+)/Mg(2+ )transport via gated channel |
title_sort | regulatory role of e-ntpase/e-ntpdase in ca(2+)/mg(2+ )transport via gated channel |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC516237/ https://www.ncbi.nlm.nih.gov/pubmed/15307889 http://dx.doi.org/10.1186/1742-4682-1-3 |
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