Depressed Na+-K+-ATPase activity in skeletal muscle at fatigue is correlated with increased Na+-K+-ATPase mRNA expression following intense exercise

Petersen, A. C., Murphy, K. T., Snow, Rod, Leppik, J. A., Aughey, R. J., Garnham, Andrew, Cameron-Smith, David and McKenna, M. J. 2005, Depressed Na+-K+-ATPase activity in skeletal muscle at fatigue is correlated with increased Na+-K+-ATPase mRNA expression following intense exercise, American journal of physiology: regulatory, intergrative and comparative physiology, vol. 289, pp. 266-274.

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Title Depressed Na+-K+-ATPase activity in skeletal muscle at fatigue is correlated with increased Na+-K+-ATPase mRNA expression following intense exercise
Formatted title Depressed Na+-K+-ATPase activity in skeletal muscle at fatigue is correlated with increased Na+-K+-ATPase mRNA expression following intense exercise
Author(s) Petersen, A. C.
Murphy, K. T.
Snow, Rod
Leppik, J. A.
Aughey, R. J.
Garnham, Andrew
Cameron-Smith, David
McKenna, M. J.
Journal name American journal of physiology: regulatory, intergrative and comparative physiology
Volume number 289
Start page 266
End page 274
Publisher American Physiological Society
Place of publication Bethesda, Md.
Publication date 2005
ISSN 0363-6119
1522-1490
Keyword(s) Na+-K+ pump
signaling
muscle fatigue
ouabain binding
Summary We investigated whether depressed muscle Na+-K+-ATPase activity with exercise reflected a loss of Na+-K+-ATPase units, the time course of its recovery postexercise, and whether this depressed activity was related to increased Na+-K+-ATPase isoform gene expression. Fifteen subjects performed fatiguing, knee extensor exercise at ~40% maximal work output per contraction. A vastus lateralis muscle biopsy was taken at rest, fatigue, 3 h, and 24 h postexercise and analyzed for maximal Na+-K+-ATPase activity via 3-O-methylfluorescein phosphatase (3-O-MFPase) activity, Na+-K+-ATPase content via [3H]ouabain binding sites, and Na+-K+-ATPase α1-, α2-, α3-, ß1-, ß2- and ß3-isoform mRNA expression by real-time RT-PCR. Exercise [352 (SD 267) s] did not affect [3H]ouabain binding sites but decreased 3-O-MFPase activity by 10.7 (SD 8)% (P < 0.05), which had recovered by 3 h postexercise, without further change at 24 h. Exercise elevated α1-isoform mRNA by 1.5-fold at fatigue (P < 0.05). This increase was inversely correlated with the percent change in 3-O-MFPase activity from rest to fatigue (%Δ3-O-MFPaserest-fatigue) (r = –0.60, P < 0.05). The average postexercise (fatigue, 3 h, 24 h) {alpha}1-isoform mRNA was increased 1.4-fold (P < 0.05) and approached a significant inverse correlation with %Δ3-O-MFPaserest-fatigue (r = –0.56, P = 0.08). Exercise elevated α2-isoform mRNA at fatigue 2.5-fold (P < 0.05), which was inversely correlated with %Δ3-O-MFPaserest-fatigue (r = –0.60, P = 0.05). The average postexercise α2-isoform mRNA was increased 2.2-fold (P < 0.05) and was inversely correlated with the %Δ3-O-MFPaserest-fatigue (r = –0.68, P < 0.05). Nonsignificant correlations were found between %Δ3-O-MFPaserest-fatigue and other isoforms. Thus acute exercise transiently decreased Na+-K+-ATPase activity, which was correlated with increased Na+-K+-ATPase gene expression. This suggests a possible signal-transduction role for depressed muscle Na+-K+-ATPase activity with exercise.
Language eng
Field of Research 060107 Enzymes
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2005, American Physiological Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30008818

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