Báo cáo y học: "Regulatory role of E-NTPase/E-NTPDase in Ca2+/Mg2+ transport via gated channel"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Regulatory role of E-NTPase/E-NTPDase in Ca2+/Mg2+ transport via gated channel | Theoretical Biology and Medical Modelling BioMed Central Research Open Access Regulatory role of E-NTPase E-NTPDase in Ca2 Mg2 transport via gated channel Hans M Schreiber1 and Subburaj Kannan 1 2 Address 1Division of Gastroenterology School of Medicine University of Pennsylvania Philadelphia PA 19104 USA and 2Departments of Microbiology and Immunology School of Medicine PO Box 25056 University of Texas Medical Branch 300 University Boulevard Galveston Texas 77550 USA Email Hans M Schreiber - skannan22@ SubburajKannan - skannan22@ Corresponding author Published 12 August 2004 Received 31 May 2004 Theoretical Biology and Medical Modelling 2004 1 3 doi 1742-4682-1-3 Accepted 12 August 2004 This article is available from http content 1 1 3 2004 Schreiber and Kannan licensee BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background E-NTPase E-NTPDase is activated by millimolar concentrations of Ca2 or Mg2 with a pH optimum of 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 Ca2 and Mg2 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. Background The mechanism by .

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