Myosin light chain phosphorylation and contractile performance of human skeletal muscle.
Twitch tension and maximal unloaded velocity of human knee extensor muscles were studied under conditions of low phosphate content of the phosphorylatable light chains (P-light chains) of myosin and elevated phosphate content, following a 10-s maximal voluntary isometric contraction (MVC). After the MVC, twitch tension was significantly potentiated, with greater potentiation observed at a shorter muscle length (p less than 0.05). The MVC was associated with at least a twofold increase in phosphate content of the fast (LC2F) and two slow (LC2S and LC2S') P-light chains, but this increase was unrelated to muscle length. No significant differences in knee extension velocity were observed between conditions where P-light chains had low or elevated phosphate content. Positive but nonsignificant correlations were noted between the extent of twitch potentiation and phosphate content of individual P-light chains as well as the percentage of type II muscle fibres in vastus lateralis muscle. No significant relationships were determined for myosin light chain kinase activity and either P-light chain phosphorylation or type II fibre percentage. These data suggest that, unlike other mammalian fast muscles, P-light chain phosphorylation of mixed human muscles is not strongly associated with altered contractile performance.
Stuart
D S
DS
Department of Kinesiology, University of Waterloo, Ont., Canada.
Lingley
M D
MD
Grange
R W
RW
Houston
M E
ME
D000293:Adolescent; D000328:Adult; D004558:Electric Stimulation; D005260:Female; D006801:Humans; D007537:Isometric Contraction; D008297:Male; D009119:Muscle Contraction; D009132:Muscles / Q000378:metabolism*; D009219:Myosin-Light-Chain Kinase / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D010766:Phosphorylation
D009219:Myosin-Light-Chain Kinase; D009218:Myosins