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Articles in PresS, published online ahead of print October 29, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00190.2002
Submitted on May 6, 2002
Accepted on October 24, 2002
1 Department of Kinesiology, University of Waterloo, Waterloo, ON, Canada
* To whom correspondence should be addressed. E-mail: green{at}healthy.uwaterloo.ca.
Prolonged exercise followed by a brief period of reduced activity has been shown to result in an overshoot in maximal SR Ca2+-ATPase activity (Vmax) in rat locomoter muscles Ferrington et al. (1996). To investigate the functional significance and underlying mechanisms for the increase in Vmax, we analyzed Ca2+-ATPase activity and Ca2+-uptake in SR vesicles from the fast rat gastrocnemius muscles following prolonged running (RUN) and following prolonged running plus 45 min of low-intensity activity (RUN+) or no activity (REC45) and compared them to controls (CON). Although no differences were observed between RUN and CON, both Vmax and Ca2+-uptake were higher (P<0.05) by 43% and 63% respectively, in RUN+ and by 35% and 34% respectively, in REC45. The increase in Vmax was accompanied by increases (P<0.05) in the phosphorylated enzyme intermediate measured by [
32-P] ATP. No differences between groups for each condition were found for the fluorescent probes, fluorescein isothiocyanate (FITC) and (N-cyclohexyl-N1 -dimethylamino-
-narpthyl) carbodiimide (NCD-4), competitive inhibitors of the nucleotide binding and calcium binding sites on the enzyme, respectively. Similarly, no differences for the Ca2+-ATPase were observed between groups in nitro-tyrosine and phospho-serine residues, a measure of nitrosylation and phosphosylation states, respectively. Western blots indicated no changes in relative isoform content of SERCA 1 and SERCA 2a. It is concluded that the increase in Vmax of the Ca2+-ATPase observed in recovery is not due to changes in enzyme nitroslyation or phosphorylation, to changes in ATP and Ca2+-binding affinity or to changes in protein content of the Ca2+-ATPase.
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