AMP-activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient?

Research output: Contribution to journalReviewpeer-review

Standard

AMP-activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient? / Jensen, Thomas Elbenhardt; Wojtaszewski, Jørgen; Richter, Erik A.

In: Acta Physiologica (Print Edition), Vol. 196, No. 1, 2009, p. 155-174.

Research output: Contribution to journalReviewpeer-review

Harvard

Jensen, TE, Wojtaszewski, J & Richter, EA 2009, 'AMP-activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient?', Acta Physiologica (Print Edition), vol. 196, no. 1, pp. 155-174. https://doi.org/10.1111/j.1748-1716.2009.01979.x

APA

Jensen, T. E., Wojtaszewski, J., & Richter, E. A. (2009). AMP-activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient? Acta Physiologica (Print Edition), 196(1), 155-174. https://doi.org/10.1111/j.1748-1716.2009.01979.x

Vancouver

Jensen TE, Wojtaszewski J, Richter EA. AMP-activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient? Acta Physiologica (Print Edition). 2009;196(1):155-174. https://doi.org/10.1111/j.1748-1716.2009.01979.x

Author

Jensen, Thomas Elbenhardt ; Wojtaszewski, Jørgen ; Richter, Erik A. / AMP-activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient?. In: Acta Physiologica (Print Edition). 2009 ; Vol. 196, No. 1. pp. 155-174.

Bibtex

@article{a7c4d7808e4011de8bc9000ea68e967b,
title = "AMP-activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient?",
abstract = "In skeletal muscle, the contraction-activated heterotrimeric 5'-AMP-activated protein kinase (AMPK) protein is proposed to regulate the balance between anabolic and catabolic processes by increasing substrate uptake and turnover in addition to regulating the transcription of proteins involved in mitochondrial biogenesis and other aspects of promoting an oxidative muscle phenotype. Here, the current knowledge on the expression of AMPK subunits in human quadriceps muscle and evidence from rodent studies suggesting distinct AMPK subunit expression pattern in different muscle types is reviewed. Then, the intensity and time dependence of AMPK activation in human quadriceps and rodent muscle are evaluated. Subsequently, a major part of this review critically examines the evidence supporting a necessary and/or sufficient role of AMPK in a broad spectrum of skeletal muscle contraction-relevant processes. These include glucose uptake, glycogen synthesis, post-exercise insulin sensitivity, fatty acid (FA) uptake, intramuscular triacylglyceride hydrolysis, FA oxidation, suppression of protein synthesis, proteolysis, autophagy and transcriptional regulation of genes relevant to promoting an oxidative phenotype.",
author = "Jensen, {Thomas Elbenhardt} and J{\o}rgen Wojtaszewski and Richter, {Erik A.}",
note = "CURIS 2009 5200 084",
year = "2009",
doi = "10.1111/j.1748-1716.2009.01979.x",
language = "English",
volume = "196",
pages = "155--174",
journal = "Acta Physiologica",
issn = "1748-1708",
publisher = "Wiley-Blackwell",
number = "1",

}

RIS

TY - JOUR

T1 - AMP-activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient?

AU - Jensen, Thomas Elbenhardt

AU - Wojtaszewski, Jørgen

AU - Richter, Erik A.

N1 - CURIS 2009 5200 084

PY - 2009

Y1 - 2009

N2 - In skeletal muscle, the contraction-activated heterotrimeric 5'-AMP-activated protein kinase (AMPK) protein is proposed to regulate the balance between anabolic and catabolic processes by increasing substrate uptake and turnover in addition to regulating the transcription of proteins involved in mitochondrial biogenesis and other aspects of promoting an oxidative muscle phenotype. Here, the current knowledge on the expression of AMPK subunits in human quadriceps muscle and evidence from rodent studies suggesting distinct AMPK subunit expression pattern in different muscle types is reviewed. Then, the intensity and time dependence of AMPK activation in human quadriceps and rodent muscle are evaluated. Subsequently, a major part of this review critically examines the evidence supporting a necessary and/or sufficient role of AMPK in a broad spectrum of skeletal muscle contraction-relevant processes. These include glucose uptake, glycogen synthesis, post-exercise insulin sensitivity, fatty acid (FA) uptake, intramuscular triacylglyceride hydrolysis, FA oxidation, suppression of protein synthesis, proteolysis, autophagy and transcriptional regulation of genes relevant to promoting an oxidative phenotype.

AB - In skeletal muscle, the contraction-activated heterotrimeric 5'-AMP-activated protein kinase (AMPK) protein is proposed to regulate the balance between anabolic and catabolic processes by increasing substrate uptake and turnover in addition to regulating the transcription of proteins involved in mitochondrial biogenesis and other aspects of promoting an oxidative muscle phenotype. Here, the current knowledge on the expression of AMPK subunits in human quadriceps muscle and evidence from rodent studies suggesting distinct AMPK subunit expression pattern in different muscle types is reviewed. Then, the intensity and time dependence of AMPK activation in human quadriceps and rodent muscle are evaluated. Subsequently, a major part of this review critically examines the evidence supporting a necessary and/or sufficient role of AMPK in a broad spectrum of skeletal muscle contraction-relevant processes. These include glucose uptake, glycogen synthesis, post-exercise insulin sensitivity, fatty acid (FA) uptake, intramuscular triacylglyceride hydrolysis, FA oxidation, suppression of protein synthesis, proteolysis, autophagy and transcriptional regulation of genes relevant to promoting an oxidative phenotype.

U2 - 10.1111/j.1748-1716.2009.01979.x

DO - 10.1111/j.1748-1716.2009.01979.x

M3 - Review

C2 - 19243572

VL - 196

SP - 155

EP - 174

JO - Acta Physiologica

JF - Acta Physiologica

SN - 1748-1708

IS - 1

ER -

ID: 13916512