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Originally published In Press as doi:10.1074/jbc.M103318200 on May 7, 2001
J. Biol. Chem., Vol. 276, Issue 27, 25078-25087, July 6, 2001
Uncoupled ATPase Activity and Heat Production by the
Sarcoplasmic Reticulum Ca2+-ATPase
REGULATION BY ADP*
Leopoldo
de Meis
From the Instituto de Ciências Biomédicas, Departamento
de Bioquímica Médica, Universidade Federal do Rio de
Janeiro, Cidade Universitária, RJ 21941-590, Brazil
Sarcoplasmic reticulum vesicles of rabbit
skeletal muscle accumulate Ca2+ at the expense of ATP
hydrolysis. The heat released during the hydrolysis of each ATP
molecule varies depending on whether or not a Ca2+ gradient
is formed across the vesicle membrane. After Ca2+
accumulation, a part of the Ca2+-ATPase activity is not
coupled with Ca2+ transport (Yu, X., and Inesi, G. (1995)
J. Biol. Chem. 270, 4361-4367). I now show that both
the heat produced during substrate hydrolysis and the uncoupled ATPase
activity vary depending on the ADP/ATP ratio in the medium. With a low
ratio, the Ca2+ transport is exothermic, and the formation
of the gradient increases the amount of heat produced during the
hydrolysis of each ATP molecule cleaved. With a high ADP/ATP ratio, the
Ca2+ transport is endothermic, and formation of a gradient
increased the amount of heat absorbed from the medium. Heat is absorbed from the medium when the Ca2+ efflux is coupled with the
synthesis of ATP (5.7 kcal/mol of ATP). When there is no ATP synthesis,
the Ca2+ efflux is exothermic (14-16 kcal/Ca2+
mol). It is concluded that in the presence of a low ADP concentration the uncoupled ATPase activity is the dominant route of heat production. With a high ADP/ATP ratio, the uncoupled ATPase activity is abolished, and the Ca2+ transport is endothermic. The possible
correlation of these findings with thermogenesis and anoxia is discussed.
*
This work was supported by grants from PRONEX - Financiadora
de Estudos e Projetos (FINEP), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) and by
Fundação de Amparo à Pesquisa do Estado do Rio de
Janeiro (FAPERJ).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence may be addressed. Tel.: 55-21-270-1635;
Fax: 55-21-270-8647; E-mail: demeis@bioqmed.ufjr.br.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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