Exercise regulates Akt and glycogen synthase kinase-3 activities in human skeletal muscle

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Exercise regulates Akt and glycogen synthase kinase-3 activities in human skeletal muscle. / Sakamoto, Kei; Arnolds, David E.W.; Ekberg, Ingvar; Thorell, Anders; Goodyear, Laurie J.

In: Biochemical and Biophysical Research Communications, Vol. 319, No. 2, 25.06.2004, p. 419-425.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Sakamoto, K, Arnolds, DEW, Ekberg, I, Thorell, A & Goodyear, LJ 2004, 'Exercise regulates Akt and glycogen synthase kinase-3 activities in human skeletal muscle', Biochemical and Biophysical Research Communications, vol. 319, no. 2, pp. 419-425. https://doi.org/10.1016/j.bbrc.2004.05.020

APA

Sakamoto, K., Arnolds, D. E. W., Ekberg, I., Thorell, A., & Goodyear, L. J. (2004). Exercise regulates Akt and glycogen synthase kinase-3 activities in human skeletal muscle. Biochemical and Biophysical Research Communications, 319(2), 419-425. https://doi.org/10.1016/j.bbrc.2004.05.020

Vancouver

Sakamoto K, Arnolds DEW, Ekberg I, Thorell A, Goodyear LJ. Exercise regulates Akt and glycogen synthase kinase-3 activities in human skeletal muscle. Biochemical and Biophysical Research Communications. 2004 Jun 25;319(2):419-425. https://doi.org/10.1016/j.bbrc.2004.05.020

Author

Sakamoto, Kei ; Arnolds, David E.W. ; Ekberg, Ingvar ; Thorell, Anders ; Goodyear, Laurie J. / Exercise regulates Akt and glycogen synthase kinase-3 activities in human skeletal muscle. In: Biochemical and Biophysical Research Communications. 2004 ; Vol. 319, No. 2. pp. 419-425.

Bibtex

@article{f1830a95479340d9be9ad1e83173e9e0,
title = "Exercise regulates Akt and glycogen synthase kinase-3 activities in human skeletal muscle",
abstract = "Activation of Akt and deactivation of GSK3 are critical signals regulating a number of cellular processes in multiple systems. Whether physical exercise alters Akt and GSK3 activity in human skeletal muscle is controversial. β-Catenin, a GSK3 substrate and important Wnt signaling protein that alters gene transcription, has not been investigated in human skeletal muscle. In the present study, eight healthy human subjects performed 30min of cycling exercise at 75% of maximum workload (submaximal) followed by 6 bouts of 60s at 125% maximum workload (maximal). Biopsies of vastus lateralis muscle were taken at rest (basal), and within 15s following cessation of the submaximal and maximal exercise bouts. Exercise at both submaximal and maximal intensities significantly increased Akt activity (40% and 110%, respectively). Increases in Akt activity were accompanied by increases in Akt Thr308 and Ser 473 phosphorylation, decreased GSK3α activity (∼30% at both intensities), and increased phosphorylation of GSK3α Ser21. Exercise at both intensities also decreased β-catenin Ser 33/37Thr41 phosphorylation (50-60% at both intensities). These results demonstrate that Akt, GSK3, and β-catenin signaling are regulated by exercise in human skeletal muscle, and as such identify them as possible molecular mediators of exercise's effect on metabolic and transcriptional processes in skeletal muscle.",
keywords = "Adaptation, Akt, Contraction, Exercise, Glycogen synthase, Glycogen synthase kinase-3, Human, Protein kinase, Signaling, Skeletal muscle",
author = "Kei Sakamoto and Arnolds, {David E.W.} and Ingvar Ekberg and Anders Thorell and Goodyear, {Laurie J.}",
year = "2004",
month = jun,
day = "25",
doi = "10.1016/j.bbrc.2004.05.020",
language = "English",
volume = "319",
pages = "419--425",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Exercise regulates Akt and glycogen synthase kinase-3 activities in human skeletal muscle

AU - Sakamoto, Kei

AU - Arnolds, David E.W.

AU - Ekberg, Ingvar

AU - Thorell, Anders

AU - Goodyear, Laurie J.

PY - 2004/6/25

Y1 - 2004/6/25

N2 - Activation of Akt and deactivation of GSK3 are critical signals regulating a number of cellular processes in multiple systems. Whether physical exercise alters Akt and GSK3 activity in human skeletal muscle is controversial. β-Catenin, a GSK3 substrate and important Wnt signaling protein that alters gene transcription, has not been investigated in human skeletal muscle. In the present study, eight healthy human subjects performed 30min of cycling exercise at 75% of maximum workload (submaximal) followed by 6 bouts of 60s at 125% maximum workload (maximal). Biopsies of vastus lateralis muscle were taken at rest (basal), and within 15s following cessation of the submaximal and maximal exercise bouts. Exercise at both submaximal and maximal intensities significantly increased Akt activity (40% and 110%, respectively). Increases in Akt activity were accompanied by increases in Akt Thr308 and Ser 473 phosphorylation, decreased GSK3α activity (∼30% at both intensities), and increased phosphorylation of GSK3α Ser21. Exercise at both intensities also decreased β-catenin Ser 33/37Thr41 phosphorylation (50-60% at both intensities). These results demonstrate that Akt, GSK3, and β-catenin signaling are regulated by exercise in human skeletal muscle, and as such identify them as possible molecular mediators of exercise's effect on metabolic and transcriptional processes in skeletal muscle.

AB - Activation of Akt and deactivation of GSK3 are critical signals regulating a number of cellular processes in multiple systems. Whether physical exercise alters Akt and GSK3 activity in human skeletal muscle is controversial. β-Catenin, a GSK3 substrate and important Wnt signaling protein that alters gene transcription, has not been investigated in human skeletal muscle. In the present study, eight healthy human subjects performed 30min of cycling exercise at 75% of maximum workload (submaximal) followed by 6 bouts of 60s at 125% maximum workload (maximal). Biopsies of vastus lateralis muscle were taken at rest (basal), and within 15s following cessation of the submaximal and maximal exercise bouts. Exercise at both submaximal and maximal intensities significantly increased Akt activity (40% and 110%, respectively). Increases in Akt activity were accompanied by increases in Akt Thr308 and Ser 473 phosphorylation, decreased GSK3α activity (∼30% at both intensities), and increased phosphorylation of GSK3α Ser21. Exercise at both intensities also decreased β-catenin Ser 33/37Thr41 phosphorylation (50-60% at both intensities). These results demonstrate that Akt, GSK3, and β-catenin signaling are regulated by exercise in human skeletal muscle, and as such identify them as possible molecular mediators of exercise's effect on metabolic and transcriptional processes in skeletal muscle.

KW - Adaptation

KW - Akt

KW - Contraction

KW - Exercise

KW - Glycogen synthase

KW - Glycogen synthase kinase-3

KW - Human

KW - Protein kinase

KW - Signaling

KW - Skeletal muscle

UR - http://www.scopus.com/inward/record.url?scp=2642541582&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2004.05.020

DO - 10.1016/j.bbrc.2004.05.020

M3 - Journal article

C2 - 15178423

AN - SCOPUS:2642541582

VL - 319

SP - 419

EP - 425

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -

ID: 239777521