Phosphorylation of rabbit skeletal muscle myosin in situ

R. L. Moore, M. E. Houston, G. A. Iwamoto, J. T. Stull

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Myosin light chain (P light chain) is phosphorylated by Ca2+ calmodulin-dependent myosin light chain kinase. Based on studies with rat skeletal muscles, it has been shown that P light chain phosphorylation correlated to the extent of potentiation of isometric twitch tension. It is not clear whether this correlation exists in rabbit skeletal muscle, which has been the primary source of contractile proteins for biochemical studies. Therefore, phosphorylation of myosin P light chain in rabbit slow-twitch soleus and fast-twitch plantaris muscles in situ was examined. Electrical stimulation (5 Hz, 20 seconds) of plantaris muscle produced an increase in the phosphate content of P light chain from 0.17 to 0.45 mol phosphate/mol P light chain. This increase in phosphate content was accompanied by a 58% increase in maximal isometric twitch tension. Tetanic stinulation (100 Hz, 15 seconds) of rabbit soleus muscle resulted in only a small increase in P light chain phosphate content from 0.02 to 0.10 mol phosphate/mol P light chain, and posttetanic twitch tension did not increase significantly. The correlation between potentiated isometric twitch tension and P light chain phosphorylation in rabbit fast-twitch muscle is similar to that observed in rat skeletal muscle. These results were consistent with the hypothesis that phosphorylation of rabbit skeletal muscle myosin, which results in an increase in actin-activated ATPase activity, may be related to isometric twitch potentiation.

Original languageEnglish (US)
Pages (from-to)301-305
Number of pages5
JournalJournal of Cellular Physiology
Volume125
Issue number2
StatePublished - 1985

Fingerprint

Skeletal Muscle Myosins
Phosphorylation
Muscle
Skeletal Muscle
Rabbits
Light
Phosphates
Myosin Light Chains
Myosins
Rats
Myosin-Light-Chain Kinase
Contractile Proteins
Calmodulin
Electric Stimulation
Muscles

ASJC Scopus subject areas

  • Cell Biology
  • Clinical Biochemistry
  • Physiology

Cite this

Phosphorylation of rabbit skeletal muscle myosin in situ. / Moore, R. L.; Houston, M. E.; Iwamoto, G. A.; Stull, J. T.

In: Journal of Cellular Physiology, Vol. 125, No. 2, 1985, p. 301-305.

Research output: Contribution to journalArticle

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