Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle. / Birk, Jesper Bratz; Wojtaszewski, Jørgen.

I: Journal of Physiology, Bind 577, Nr. 3, 2006, s. 1021-1032.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Birk, JB & Wojtaszewski, J 2006, 'Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle', Journal of Physiology, bind 577, nr. 3, s. 1021-1032. https://doi.org/10.1113/jphysiol.2006.120972

APA

Birk, J. B., & Wojtaszewski, J. (2006). Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle. Journal of Physiology, 577(3), 1021-1032. https://doi.org/10.1113/jphysiol.2006.120972

Vancouver

Birk JB, Wojtaszewski J. Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle. Journal of Physiology. 2006;577(3):1021-1032. https://doi.org/10.1113/jphysiol.2006.120972

Author

Birk, Jesper Bratz ; Wojtaszewski, Jørgen. / Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle. I: Journal of Physiology. 2006 ; Bind 577, Nr. 3. s. 1021-1032.

Bibtex

@article{f8616e70ad2d11dbbee902004c4f4f50,
title = "Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle",
abstract = "5'AMP-activated protein kinase (AMPK) is a key regulator of cellular metabolism and is regulated in muscle during exercise. We have previously established that only three of 12 possible AMPK a/{\ss}/¿-heterotrimers are present in human skeletal muscle. Previous studies describe discrepancies between total AMPK activity and regulation of its target acetyl-CoA-carboxylase (ACC){\ss}. Also, exercise training decreases expression of the regulatory ¿3 AMPK subunit and attenuates a2 AMPK activity during exercise. We hypothesize that these observations reflect a differential regulation of the AMPK heterotrimers. We provide evidence here that only the a2/{\ss}2/¿3 subunit is phosphorylated and activated during high-intensity exercise in vivo. The activity associated with the remaining two AMPK heterotrimers, a1/{\ss}2/¿1 and a2/{\ss}2/¿1, is either unchanged (20 min, 80{\%} maximal oxygen uptake (VO2,peak)) or decreased (30 or 120 s sprint-exercise). The differential activity of the heterotrimers leads to a total a-AMPK activity, that is decreased (30 s trial), unchanged (120 s trial) and increased (20 min trial). AMPK activity associated with the a2/{\ss}2/¿3 heterotrimer was strongly correlated to ¿3-associated a-Thr-172 AMPK phosphorylation (r2 = 0.84, P < 0.001) and to ACC{\ss} Ser-221 phosphorylation (r2 = 0.65, P < 0.001). These data single out the a2/{\ss}2/¿3 heterotrimer as an important actor in exercise-regulated AMPK signalling in human skeletal muscle, probably mediating phosphorylation of ACC{\ss}.",
author = "Birk, {Jesper Bratz} and J{\o}rgen Wojtaszewski",
note = "PUF 2006 5200 156",
year = "2006",
doi = "10.1113/jphysiol.2006.120972",
language = "English",
volume = "577",
pages = "1021--1032",
journal = "The Journal of Physiology",
issn = "0022-3751",
publisher = "Wiley-Blackwell",
number = "3",

}

RIS

TY - JOUR

T1 - Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle

AU - Birk, Jesper Bratz

AU - Wojtaszewski, Jørgen

N1 - PUF 2006 5200 156

PY - 2006

Y1 - 2006

N2 - 5'AMP-activated protein kinase (AMPK) is a key regulator of cellular metabolism and is regulated in muscle during exercise. We have previously established that only three of 12 possible AMPK a/ß/¿-heterotrimers are present in human skeletal muscle. Previous studies describe discrepancies between total AMPK activity and regulation of its target acetyl-CoA-carboxylase (ACC)ß. Also, exercise training decreases expression of the regulatory ¿3 AMPK subunit and attenuates a2 AMPK activity during exercise. We hypothesize that these observations reflect a differential regulation of the AMPK heterotrimers. We provide evidence here that only the a2/ß2/¿3 subunit is phosphorylated and activated during high-intensity exercise in vivo. The activity associated with the remaining two AMPK heterotrimers, a1/ß2/¿1 and a2/ß2/¿1, is either unchanged (20 min, 80% maximal oxygen uptake (VO2,peak)) or decreased (30 or 120 s sprint-exercise). The differential activity of the heterotrimers leads to a total a-AMPK activity, that is decreased (30 s trial), unchanged (120 s trial) and increased (20 min trial). AMPK activity associated with the a2/ß2/¿3 heterotrimer was strongly correlated to ¿3-associated a-Thr-172 AMPK phosphorylation (r2 = 0.84, P < 0.001) and to ACCß Ser-221 phosphorylation (r2 = 0.65, P < 0.001). These data single out the a2/ß2/¿3 heterotrimer as an important actor in exercise-regulated AMPK signalling in human skeletal muscle, probably mediating phosphorylation of ACCß.

AB - 5'AMP-activated protein kinase (AMPK) is a key regulator of cellular metabolism and is regulated in muscle during exercise. We have previously established that only three of 12 possible AMPK a/ß/¿-heterotrimers are present in human skeletal muscle. Previous studies describe discrepancies between total AMPK activity and regulation of its target acetyl-CoA-carboxylase (ACC)ß. Also, exercise training decreases expression of the regulatory ¿3 AMPK subunit and attenuates a2 AMPK activity during exercise. We hypothesize that these observations reflect a differential regulation of the AMPK heterotrimers. We provide evidence here that only the a2/ß2/¿3 subunit is phosphorylated and activated during high-intensity exercise in vivo. The activity associated with the remaining two AMPK heterotrimers, a1/ß2/¿1 and a2/ß2/¿1, is either unchanged (20 min, 80% maximal oxygen uptake (VO2,peak)) or decreased (30 or 120 s sprint-exercise). The differential activity of the heterotrimers leads to a total a-AMPK activity, that is decreased (30 s trial), unchanged (120 s trial) and increased (20 min trial). AMPK activity associated with the a2/ß2/¿3 heterotrimer was strongly correlated to ¿3-associated a-Thr-172 AMPK phosphorylation (r2 = 0.84, P < 0.001) and to ACCß Ser-221 phosphorylation (r2 = 0.65, P < 0.001). These data single out the a2/ß2/¿3 heterotrimer as an important actor in exercise-regulated AMPK signalling in human skeletal muscle, probably mediating phosphorylation of ACCß.

U2 - 10.1113/jphysiol.2006.120972

DO - 10.1113/jphysiol.2006.120972

M3 - Journal article

VL - 577

SP - 1021

EP - 1032

JO - The Journal of Physiology

JF - The Journal of Physiology

SN - 0022-3751

IS - 3

ER -

ID: 377872