Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1788, Issue 7, Pages 1517-1522Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2009.04.007
Keywords
Heat production; Ca2+-ATPase; Thermogenesis; Heavy sarcoplasmic reticulum; Light sarcoplasmic reticulum
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Funding
- PRONEX - Financiadora de Estudos e Projetos (FINEP)
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Fundacao de Amparo a Pesquisa do Estado do Rio de Janeiro (FAPERJ)
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In this work, we compared the effect of K+ on vesicles derived from the longitudinal (LSR) and terminal cisternae (HSR) of rabbit white muscle. In HSR, K+ was found to inhibit both the Ca2+ accumulation and the heat released during ATP hydrolysis by the Ca2+-ATPase (SERCA1). This was not observed in LSR. Valinomycin abolished the HSR Ca2+-uptake inhibition promoted by physiological K+ concentrations, but it did not modify the thermogenic activity of the Ca2+ pump. The results with HSR are difficult to interpret, assuming that a single K+ is binding to either the ryanodine channel or to the Ca2+-ATPase. It is suggested that an increase of K+ in the assay medium alters the interactions among the various proteins found in HSR thus modifying the properties of both the ryanodine channel and SERCA1. (C) 2009 Elsevier B.V. All rights reserved.
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