Myosin light chain phosphorylation-dephosphorylation in mammalian skeletal muscle

D. R. Manning, J. T. Stull

Research output: Contribution to journalArticle

112 Scopus citations

Abstract

Phosphorylation of the myosin light chain 2 (LC2) subunit was examined in rat fast-twitch and slow-twitch skeletal muscles in response to repetitive stimulation at 23 and 35°C and on incubation of fast-twitch skeletal muscle with isoproterenol. After a 1-s tetany at 35°C, LC2 phosphate content in extensor digitorum longus muscle increased rapidly and transiently from 0.21 to 0.51 mol phosphate/mol LC2. This pattern of phosphorylation was similar to that observed at 23°C. Increases in LC2 phosphate content were dependent on the frequency and duration of stimulation. In soleus muscle LC2 phosphate content was minimal following a 1-s tetany but increased markedly following more prolonged tetanies. On incubation of extensor digitorum longus muscle with isoproterenol (20 μM), LC2 phosphate content did not change, whereas phosphorylase α levels increased. A positive correlation existed between LC2 phosphate content and potentiation of peak twitch tension in both types of muscles, suggesting a physiological function for LC2 phosphorylation.

Original languageEnglish (US)
Pages (from-to)C234-C241
JournalAmerican Journal of Physiology - Cell Physiology
Volume11
Issue number2
StatePublished - Jan 1 1982

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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