Length-dependent potentiation and myosin light chain phosphorylation in rat gastrocnemius muscle

D. E. Rassier, L. A. Tubman and B. R. MacIntosh Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, Alberta, Canada. Changes in muscle length affect the degree of staircase potentiation in skeletal muscle, but the mechanism by which this occurs is unknown. In this study, we...

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Veröffentlicht in:American Journal of Physiology: Cell Physiology 1997-07, Vol.273 (1), p.C198-C204
Hauptverfasser: Rassier, D. E, Tubman, L. A, MacIntosh, B. R
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Sprache:eng
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Zusammenfassung:D. E. Rassier, L. A. Tubman and B. R. MacIntosh Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, Alberta, Canada. Changes in muscle length affect the degree of staircase potentiation in skeletal muscle, but the mechanism by which this occurs is unknown. In this study, we tested the hypothesis that length-dependent change in staircase is modulated by phosphorylation of the myosin regulatory light chains (RLC), since this is believed to be the main mechanism of potentiation. In situ isometric contractile responses of rat gastrocnemius muscle during 10 s of repetitive stimulation at 10 Hz were analyzed at optimal length (Lo), Lo - 10%, and Lo + 10%. The degree of enhancement of developed tension during 10 s of repetitive stimulation was observed to be length dependent, with increases of 118.5 +/- 7.8, 63.1 +/- 3.9, and 45.6 +/- 4.1% (means +/- SE) at Lo - 10%, Lo, and Lo + 10%, respectively. Staircase was accompanied by increases in the average rate of force development of 105.6 +/- 7.7, 55.6 +/- 4.1, and 37.2 +/- 4.4% for Lo - 10%, Lo, and Lo + 10%, respectively. RLC phosphorylation after 10 s of 10-Hz stimulation was higher than under resting conditions but not different among Lo - 10% (40 +/- 3.5%), Lo (35 +/- 3.5%), and Lo + 10% (41 +/- 3.5%). This study shows that there is a length dependence of staircase potentiation in mammalian skeletal muscle that may not be directly modulated by RLC phosphorylation. Interaction of RLC phosphorylation with length-dependent changes in Ca2+ release and intermyofilament spacing may explain these observations.
ISSN:0363-6143
0002-9513
1522-1563
DOI:10.1152/ajpcell.1997.273.1.C198