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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...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2004
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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 |
Sumario: | 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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