5´AMP activated protein kinase α2 controls substrate metabolism during post-exercise recovery via regulation of pyruvate dehydrogenase kinase 4

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Standard

5´AMP activated protein kinase α2 controls substrate metabolism during post-exercise recovery via regulation of pyruvate dehydrogenase kinase 4. / Fritzen, Andreas Mæchel; Lundsgaard, Annemarie; Jeppesen, Jacob; Christiansen, Mette Landau Brabæk; Biensø, Rasmus Sjørup; Dyck, Jason R B; Pilegaard, Henriette; Kiens, Bente.

I: Journal of Physiology, Bind 593, Nr. 21, 2015, s. 4765-4780.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Fritzen, AM, Lundsgaard, A, Jeppesen, J, Christiansen, MLB, Biensø, RS, Dyck, JRB, Pilegaard, H & Kiens, B 2015, '5´AMP activated protein kinase α2 controls substrate metabolism during post-exercise recovery via regulation of pyruvate dehydrogenase kinase 4' Journal of Physiology, bind 593, nr. 21, s. 4765-4780. https://doi.org/10.1113/JP270821

APA

Fritzen, A. M., Lundsgaard, A., Jeppesen, J., Christiansen, M. L. B., Biensø, R. S., Dyck, J. R. B., ... Kiens, B. (2015). 5´AMP activated protein kinase α2 controls substrate metabolism during post-exercise recovery via regulation of pyruvate dehydrogenase kinase 4. Journal of Physiology, 593(21), 4765-4780. https://doi.org/10.1113/JP270821

Vancouver

Fritzen AM, Lundsgaard A, Jeppesen J, Christiansen MLB, Biensø RS, Dyck JRB o.a. 5´AMP activated protein kinase α2 controls substrate metabolism during post-exercise recovery via regulation of pyruvate dehydrogenase kinase 4. Journal of Physiology. 2015;593(21):4765-4780. https://doi.org/10.1113/JP270821

Author

Fritzen, Andreas Mæchel ; Lundsgaard, Annemarie ; Jeppesen, Jacob ; Christiansen, Mette Landau Brabæk ; Biensø, Rasmus Sjørup ; Dyck, Jason R B ; Pilegaard, Henriette ; Kiens, Bente. / 5´AMP activated protein kinase α2 controls substrate metabolism during post-exercise recovery via regulation of pyruvate dehydrogenase kinase 4. I: Journal of Physiology. 2015 ; Bind 593, Nr. 21. s. 4765-4780.

Bibtex

@article{f87b61cc7977494993c6ca7914b0cc07,
title = "5´AMP activated protein kinase α2 controls substrate metabolism during post-exercise recovery via regulation of pyruvate dehydrogenase kinase 4",
abstract = "It is well known that exercise has a major impact on substrate metabolism for many hours after exercise. However, the regulatory mechanisms increasing lipid oxidation and facilitating glycogen resynthesis in the post-exercise period are unknown. To address this, substrate oxidation was measured after prolonged exercise and during the following six hours post exercise in 5´AMP activated protein kinase (AMPK)α2 and α1 knock-out (KO) and wild type (WT) mice with free access to food. Substrate oxidation was similar during exercise at the same relative intensity between genotypes. During post-exercise recovery, a lower lipid oxidation (P < 0.05) and higher glucose oxidation were observed in AMPKα2 KO (respiratory exchange ratio (RER) = 0.84 ± 0.02) than in WT and AMPKα1 KO (average RER = 0.80 ± 0.01) without genotype differences in muscle malonyl CoA or free-carnitine concentrations. A similar increase in muscle pyruvate dehydrogenase kinase 4 (PDK4) mRNA expression in WT and AMPKα2 KO was observed following exercise, which is consistent with AMPKα2 -deficiency not affecting the exercise-induced activation of the PDK4 transcriptional regulators, HDAC4 and SIRT1. Interestingly, PDK4 protein content increased (63 {\%}, P < 0.001) in WT but remained unchanged in AMPKα2 KO. In accordance with the lack of increase in PDK4 protein content, lower (P < 0.01) inhibitory pyruvate dehydrogenase (PDH)-E1α Ser(293) phosphorylation was observed in AMPKα2 KO muscle compared to WT. These findings indicate that AMPKα2 regulates muscle metabolism post-exercise through inhibition of the PDH complex and hence glucose oxidation, subsequently creating conditions for increased fatty acid oxidation. This article is protected by copyright. All rights reserved.",
author = "Fritzen, {Andreas M{\ae}chel} and Annemarie Lundsgaard and Jacob Jeppesen and Christiansen, {Mette Landau Brab{\ae}k} and Biens{\o}, {Rasmus Sj{\o}rup} and Dyck, {Jason R B} and Henriette Pilegaard and Bente Kiens",
note = "CURIS 2015 NEXS 365",
year = "2015",
doi = "10.1113/JP270821",
language = "English",
volume = "593",
pages = "4765--4780",
journal = "The Journal of Physiology",
issn = "0022-3751",
publisher = "Wiley-Blackwell",
number = "21",

}

RIS

TY - JOUR

T1 - 5´AMP activated protein kinase α2 controls substrate metabolism during post-exercise recovery via regulation of pyruvate dehydrogenase kinase 4

AU - Fritzen, Andreas Mæchel

AU - Lundsgaard, Annemarie

AU - Jeppesen, Jacob

AU - Christiansen, Mette Landau Brabæk

AU - Biensø, Rasmus Sjørup

AU - Dyck, Jason R B

AU - Pilegaard, Henriette

AU - Kiens, Bente

N1 - CURIS 2015 NEXS 365

PY - 2015

Y1 - 2015

N2 - It is well known that exercise has a major impact on substrate metabolism for many hours after exercise. However, the regulatory mechanisms increasing lipid oxidation and facilitating glycogen resynthesis in the post-exercise period are unknown. To address this, substrate oxidation was measured after prolonged exercise and during the following six hours post exercise in 5´AMP activated protein kinase (AMPK)α2 and α1 knock-out (KO) and wild type (WT) mice with free access to food. Substrate oxidation was similar during exercise at the same relative intensity between genotypes. During post-exercise recovery, a lower lipid oxidation (P < 0.05) and higher glucose oxidation were observed in AMPKα2 KO (respiratory exchange ratio (RER) = 0.84 ± 0.02) than in WT and AMPKα1 KO (average RER = 0.80 ± 0.01) without genotype differences in muscle malonyl CoA or free-carnitine concentrations. A similar increase in muscle pyruvate dehydrogenase kinase 4 (PDK4) mRNA expression in WT and AMPKα2 KO was observed following exercise, which is consistent with AMPKα2 -deficiency not affecting the exercise-induced activation of the PDK4 transcriptional regulators, HDAC4 and SIRT1. Interestingly, PDK4 protein content increased (63 %, P < 0.001) in WT but remained unchanged in AMPKα2 KO. In accordance with the lack of increase in PDK4 protein content, lower (P < 0.01) inhibitory pyruvate dehydrogenase (PDH)-E1α Ser(293) phosphorylation was observed in AMPKα2 KO muscle compared to WT. These findings indicate that AMPKα2 regulates muscle metabolism post-exercise through inhibition of the PDH complex and hence glucose oxidation, subsequently creating conditions for increased fatty acid oxidation. This article is protected by copyright. All rights reserved.

AB - It is well known that exercise has a major impact on substrate metabolism for many hours after exercise. However, the regulatory mechanisms increasing lipid oxidation and facilitating glycogen resynthesis in the post-exercise period are unknown. To address this, substrate oxidation was measured after prolonged exercise and during the following six hours post exercise in 5´AMP activated protein kinase (AMPK)α2 and α1 knock-out (KO) and wild type (WT) mice with free access to food. Substrate oxidation was similar during exercise at the same relative intensity between genotypes. During post-exercise recovery, a lower lipid oxidation (P < 0.05) and higher glucose oxidation were observed in AMPKα2 KO (respiratory exchange ratio (RER) = 0.84 ± 0.02) than in WT and AMPKα1 KO (average RER = 0.80 ± 0.01) without genotype differences in muscle malonyl CoA or free-carnitine concentrations. A similar increase in muscle pyruvate dehydrogenase kinase 4 (PDK4) mRNA expression in WT and AMPKα2 KO was observed following exercise, which is consistent with AMPKα2 -deficiency not affecting the exercise-induced activation of the PDK4 transcriptional regulators, HDAC4 and SIRT1. Interestingly, PDK4 protein content increased (63 %, P < 0.001) in WT but remained unchanged in AMPKα2 KO. In accordance with the lack of increase in PDK4 protein content, lower (P < 0.01) inhibitory pyruvate dehydrogenase (PDH)-E1α Ser(293) phosphorylation was observed in AMPKα2 KO muscle compared to WT. These findings indicate that AMPKα2 regulates muscle metabolism post-exercise through inhibition of the PDH complex and hence glucose oxidation, subsequently creating conditions for increased fatty acid oxidation. This article is protected by copyright. All rights reserved.

U2 - 10.1113/JP270821

DO - 10.1113/JP270821

M3 - Journal article

VL - 593

SP - 4765

EP - 4780

JO - The Journal of Physiology

JF - The Journal of Physiology

SN - 0022-3751

IS - 21

ER -

ID: 144416089