Myosin light chain phosphorylation and phosphorylase a activity in rat extensor digitorum longus muscle

David R. Manning; James T. Stull

doi:10.1016/0006-291X(79)91604-8

Myosin light chain phosphorylation and phosphorylase a activity in rat extensor digitorum longus muscle

David R. Manning, James T. Stull

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Abstract

Phosphorylation of the 18,500 dalton light chain of myosin and conversion of phosphorylase b to a were examined in relation to isometric tension development. Following a l sec tetanic contraction, light chain phosphate content increased from a pre-tetanic value of 0.10 to 0.75 mol phosphate/mol at 7 sec; phosphorylase a activity (ratio of activity -5′AMP +5′AMP) increased from 0.03 to 0.42 at 4 sec and decreased to control values within 20 sec. Light chain phosphate content, however, declined much more slowly and correlated to post-tetanic potentiation of peak twitch tension. Our results suggest light chain phosphorylation is not obligatory for contraction but may play a role in post-tetanic potentiation.

Original language	English (US)
Pages (from-to)	164-170
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	90
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(79)91604-8
State	Published - Sep 12 1979

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Myosin light chain phosphorylation and phosphorylase a activity in rat extensor digitorum longus muscle",

abstract = "Phosphorylation of the 18,500 dalton light chain of myosin and conversion of phosphorylase b to a were examined in relation to isometric tension development. Following a l sec tetanic contraction, light chain phosphate content increased from a pre-tetanic value of 0.10 to 0.75 mol phosphate/mol at 7 sec; phosphorylase a activity (ratio of activity -5′AMP +5′AMP) increased from 0.03 to 0.42 at 4 sec and decreased to control values within 20 sec. Light chain phosphate content, however, declined much more slowly and correlated to post-tetanic potentiation of peak twitch tension. Our results suggest light chain phosphorylation is not obligatory for contraction but may play a role in post-tetanic potentiation.",

author = "Manning, {David R.} and Stull, {James T.}",

note = "Funding Information: Acknowledgments: This work was done during the tenure of an Established Investigatorship of the American Heart Association for J.T.S. and as a Predoctoral Trainee in the Division of Pharmacology at the University of California, San Diego, for D.R.M. (GM 02267). Support was provided by grants from the Muscular Dystrophy Association and NIH (HL 23990). We appreciate the valuable technical assistance of Ms. Diana Skripka and discussions and preprint of similar work by Drs. M. and K. Bat-any",

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doi = "10.1016/0006-291X(79)91604-8",

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T1 - Myosin light chain phosphorylation and phosphorylase a activity in rat extensor digitorum longus muscle

AU - Manning, David R.

AU - Stull, James T.

N1 - Funding Information: Acknowledgments: This work was done during the tenure of an Established Investigatorship of the American Heart Association for J.T.S. and as a Predoctoral Trainee in the Division of Pharmacology at the University of California, San Diego, for D.R.M. (GM 02267). Support was provided by grants from the Muscular Dystrophy Association and NIH (HL 23990). We appreciate the valuable technical assistance of Ms. Diana Skripka and discussions and preprint of similar work by Drs. M. and K. Bat-any

PY - 1979/9/12

Y1 - 1979/9/12

N2 - Phosphorylation of the 18,500 dalton light chain of myosin and conversion of phosphorylase b to a were examined in relation to isometric tension development. Following a l sec tetanic contraction, light chain phosphate content increased from a pre-tetanic value of 0.10 to 0.75 mol phosphate/mol at 7 sec; phosphorylase a activity (ratio of activity -5′AMP +5′AMP) increased from 0.03 to 0.42 at 4 sec and decreased to control values within 20 sec. Light chain phosphate content, however, declined much more slowly and correlated to post-tetanic potentiation of peak twitch tension. Our results suggest light chain phosphorylation is not obligatory for contraction but may play a role in post-tetanic potentiation.

AB - Phosphorylation of the 18,500 dalton light chain of myosin and conversion of phosphorylase b to a were examined in relation to isometric tension development. Following a l sec tetanic contraction, light chain phosphate content increased from a pre-tetanic value of 0.10 to 0.75 mol phosphate/mol at 7 sec; phosphorylase a activity (ratio of activity -5′AMP +5′AMP) increased from 0.03 to 0.42 at 4 sec and decreased to control values within 20 sec. Light chain phosphate content, however, declined much more slowly and correlated to post-tetanic potentiation of peak twitch tension. Our results suggest light chain phosphorylation is not obligatory for contraction but may play a role in post-tetanic potentiation.

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Myosin light chain phosphorylation and phosphorylase a activity in rat extensor digitorum longus muscle

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