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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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Detalles Bibliográficos
Autores principales: Schreiber, Hans M, Kannan, Subburaj
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2004
Materias:
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.
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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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