The effect of low frequency stimulation on myosin light chain phosphorylation in skeletal muscle.
Phosphorylation of the P-light chain of myosin from skeletal muscle by myosin light chain kinase is dependent upon calmodulin and Ca2+. Investigations were performed to determine if the rapid Ca2+ transients that occur during low frequency repetitive stimulation are sufficient to activate myosin light chain kinase with significant P-light chain phosphorylation. In addition, P-light chain phosphorylation was correlated with potentiation of isomeric twitch tension (staircase phenomenon). Stimulation of rat gastrocnemius muscle at 5 Hz in situ results in a time-dependent phosphorylation of the P-light chain of myosin. Initially, there was a rapid rate of phosphorylation within the first 10 muscle twitches (0.19 to 0.40 mol of phosphate/mol of P-light chain) followed by a slower rate of phosphorylation. These data indicate that myosin light chain kinase can be activated during repetitive stimulation at a low frequency in the range that occurs in vivo, despite the fact that the muscle is in the relaxed state during most of the period between each stimulation. Potentiation of isometric twitch tension was found to be temporally correlated to light chain phosphorylation at 5 Hz. It is postulated that the transient changes in intracellular Ca2+ concentration associated with low frequency stimulation are sufficient to activate myosin light chain kinase, and, furthermore, the magnitude of the potentiation of isometric twitch tension may be related to the extent of phosphorylation of myosin during a stimulus train.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002147:Calmodulin / Q000494:pharmacology; D005260:Female; D007700:Kinetics; D009119:Muscle Contraction; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D011919:Rats, Inbred Strains
D002147:Calmodulin; D009218:Myosins; D002118:Calcium