Effects of alpha-AMPK knockout on exercise-induced gene activation in mouse skeletal muscle

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Standard

Effects of alpha-AMPK knockout on exercise-induced gene activation in mouse skeletal muscle. / Jørgensen, Sebastian Beck; Wojtaszewski, Jørgen; Viollet, Benoit; Andreelli, Fabrizio; Birk, Jesper Bratz; Hellsten, Ylva; Schjerling, Peter; Vaulont, Sophie; Neufer, P. Darrell; Richter, Erik A.; Pilegaard, Henriette.

I: The FASEB Journal, Bind 19, Nr. 9, 2005, s. 1146-1148.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Jørgensen, SB, Wojtaszewski, J, Viollet, B, Andreelli, F, Birk, JB, Hellsten, Y, Schjerling, P, Vaulont, S, Neufer, PD, Richter, EA & Pilegaard, H 2005, 'Effects of alpha-AMPK knockout on exercise-induced gene activation in mouse skeletal muscle', The FASEB Journal, bind 19, nr. 9, s. 1146-1148. https://doi.org/10.1096/fj.04-3144fje

APA

Jørgensen, S. B., Wojtaszewski, J., Viollet, B., Andreelli, F., Birk, J. B., Hellsten, Y., ... Pilegaard, H. (2005). Effects of alpha-AMPK knockout on exercise-induced gene activation in mouse skeletal muscle. The FASEB Journal, 19(9), 1146-1148. https://doi.org/10.1096/fj.04-3144fje

Vancouver

Jørgensen SB, Wojtaszewski J, Viollet B, Andreelli F, Birk JB, Hellsten Y o.a. Effects of alpha-AMPK knockout on exercise-induced gene activation in mouse skeletal muscle. The FASEB Journal. 2005;19(9):1146-1148. https://doi.org/10.1096/fj.04-3144fje

Author

Jørgensen, Sebastian Beck ; Wojtaszewski, Jørgen ; Viollet, Benoit ; Andreelli, Fabrizio ; Birk, Jesper Bratz ; Hellsten, Ylva ; Schjerling, Peter ; Vaulont, Sophie ; Neufer, P. Darrell ; Richter, Erik A. ; Pilegaard, Henriette. / Effects of alpha-AMPK knockout on exercise-induced gene activation in mouse skeletal muscle. I: The FASEB Journal. 2005 ; Bind 19, Nr. 9. s. 1146-1148.

Bibtex

@article{d361ff60a56011dbbee902004c4f4f50,
title = "Effects of alpha-AMPK knockout on exercise-induced gene activation in mouse skeletal muscle",
abstract = "We tested the hypothesis that 5'AMP-activated protein kinase (AMPK) plays an important role in regulating the acute, exercise-induced activation of metabolic genes in skeletal muscle, which were dissected from whole-body a2- and a1-AMPK knockout (KO) and wild-type (WT) mice at rest, after treadmill running (90 min), and in recovery. Running increased a1-AMPK kinase activity, phosphorylation (P) of AMPK, and acetyl-CoA carboxylase (ACC){\ss} in a2-WT and a2-KO muscles and increased a2-AMPK kinase activity in a2-WT. In a2-KO muscles, AMPK-P and ACC{\ss}-P were markedly lower compared with a2-WT. However, in a1-WT and a1-KO muscles, AMPK-P and ACC{\ss}-P levels were identical at rest and increased similarly during exercise in the two genotypes. The a2-KO decreased peroxisome-proliferator-activated receptor ¿ coactivator (PGC)-1a, uncoupling protein-3 (UCP3), and hexokinase II (HKII) transcription at rest but did not affect exercise-induced transcription. Exercise increased the mRNA content of PGC-1a, Forkhead box class O (FOXO)1, HKII, and pyruvate dehydrogenase kinase 4 (PDK4) similarly in a2-WT and a2-KO mice, whereas glucose transporter GLUT 4, carnitine palmitoyltransferase 1 (CPTI), lipoprotein lipase, and UCP3 mRNA were unchanged by exercise in both genotypes. CPTI mRNA was lower in a2-KO muscles than in a2-WT muscles at all time-points. In a1-WT and a1-KO muscles, running increased the mRNA content of PGC-1a and FOXO1 similarly. The a2-KO was associated with lower muscle adenosine 5'-triphosphate content, and the inosine monophosphate content increased substantially at the end of exercise only in a2-KO muscles. In addition, subcutaneous injection of 5-aminoimidazole-4-carboxamide-1-{\ss}-4-ribofuranoside (AICAR) increased the mRNA content of PGC-1a, HKII, FOXO1, PDK4, and UCP3, and a2-KO abolished the AICAR-induced increases in PGC-1a and HKII mRNA. In conclusion, KO of the a2- but not the a1-AMPK isoform markedly diminished AMPK activation during running. Nevertheless, exercise-induced activation of the investigated genes in mouse skeletal muscle was not impaired in a1- or a2-AMPK KO muscles. Although it cannot be ruled out that activation of the remaining a-isoform is sufficient to increase gene activation during exercise, the present data do not support an essential role of AMPK in regulating exercise-induced gene activation in skeletal muscle.",
author = "J{\o}rgensen, {Sebastian Beck} and J{\o}rgen Wojtaszewski and Benoit Viollet and Fabrizio Andreelli and Birk, {Jesper Bratz} and Ylva Hellsten and Peter Schjerling and Sophie Vaulont and Neufer, {P. Darrell} and Richter, {Erik A.} and Henriette Pilegaard",
note = "PUF 2005 5200 033",
year = "2005",
doi = "10.1096/fj.04-3144fje",
language = "English",
volume = "19",
pages = "1146--1148",
journal = "F A S E B Journal",
issn = "0892-6638",
publisher = "Federation of American Societies for Experimental Biology",
number = "9",

}

RIS

TY - JOUR

T1 - Effects of alpha-AMPK knockout on exercise-induced gene activation in mouse skeletal muscle

AU - Jørgensen, Sebastian Beck

AU - Wojtaszewski, Jørgen

AU - Viollet, Benoit

AU - Andreelli, Fabrizio

AU - Birk, Jesper Bratz

AU - Hellsten, Ylva

AU - Schjerling, Peter

AU - Vaulont, Sophie

AU - Neufer, P. Darrell

AU - Richter, Erik A.

AU - Pilegaard, Henriette

N1 - PUF 2005 5200 033

PY - 2005

Y1 - 2005

N2 - We tested the hypothesis that 5'AMP-activated protein kinase (AMPK) plays an important role in regulating the acute, exercise-induced activation of metabolic genes in skeletal muscle, which were dissected from whole-body a2- and a1-AMPK knockout (KO) and wild-type (WT) mice at rest, after treadmill running (90 min), and in recovery. Running increased a1-AMPK kinase activity, phosphorylation (P) of AMPK, and acetyl-CoA carboxylase (ACC)ß in a2-WT and a2-KO muscles and increased a2-AMPK kinase activity in a2-WT. In a2-KO muscles, AMPK-P and ACCß-P were markedly lower compared with a2-WT. However, in a1-WT and a1-KO muscles, AMPK-P and ACCß-P levels were identical at rest and increased similarly during exercise in the two genotypes. The a2-KO decreased peroxisome-proliferator-activated receptor ¿ coactivator (PGC)-1a, uncoupling protein-3 (UCP3), and hexokinase II (HKII) transcription at rest but did not affect exercise-induced transcription. Exercise increased the mRNA content of PGC-1a, Forkhead box class O (FOXO)1, HKII, and pyruvate dehydrogenase kinase 4 (PDK4) similarly in a2-WT and a2-KO mice, whereas glucose transporter GLUT 4, carnitine palmitoyltransferase 1 (CPTI), lipoprotein lipase, and UCP3 mRNA were unchanged by exercise in both genotypes. CPTI mRNA was lower in a2-KO muscles than in a2-WT muscles at all time-points. In a1-WT and a1-KO muscles, running increased the mRNA content of PGC-1a and FOXO1 similarly. The a2-KO was associated with lower muscle adenosine 5'-triphosphate content, and the inosine monophosphate content increased substantially at the end of exercise only in a2-KO muscles. In addition, subcutaneous injection of 5-aminoimidazole-4-carboxamide-1-ß-4-ribofuranoside (AICAR) increased the mRNA content of PGC-1a, HKII, FOXO1, PDK4, and UCP3, and a2-KO abolished the AICAR-induced increases in PGC-1a and HKII mRNA. In conclusion, KO of the a2- but not the a1-AMPK isoform markedly diminished AMPK activation during running. Nevertheless, exercise-induced activation of the investigated genes in mouse skeletal muscle was not impaired in a1- or a2-AMPK KO muscles. Although it cannot be ruled out that activation of the remaining a-isoform is sufficient to increase gene activation during exercise, the present data do not support an essential role of AMPK in regulating exercise-induced gene activation in skeletal muscle.

AB - We tested the hypothesis that 5'AMP-activated protein kinase (AMPK) plays an important role in regulating the acute, exercise-induced activation of metabolic genes in skeletal muscle, which were dissected from whole-body a2- and a1-AMPK knockout (KO) and wild-type (WT) mice at rest, after treadmill running (90 min), and in recovery. Running increased a1-AMPK kinase activity, phosphorylation (P) of AMPK, and acetyl-CoA carboxylase (ACC)ß in a2-WT and a2-KO muscles and increased a2-AMPK kinase activity in a2-WT. In a2-KO muscles, AMPK-P and ACCß-P were markedly lower compared with a2-WT. However, in a1-WT and a1-KO muscles, AMPK-P and ACCß-P levels were identical at rest and increased similarly during exercise in the two genotypes. The a2-KO decreased peroxisome-proliferator-activated receptor ¿ coactivator (PGC)-1a, uncoupling protein-3 (UCP3), and hexokinase II (HKII) transcription at rest but did not affect exercise-induced transcription. Exercise increased the mRNA content of PGC-1a, Forkhead box class O (FOXO)1, HKII, and pyruvate dehydrogenase kinase 4 (PDK4) similarly in a2-WT and a2-KO mice, whereas glucose transporter GLUT 4, carnitine palmitoyltransferase 1 (CPTI), lipoprotein lipase, and UCP3 mRNA were unchanged by exercise in both genotypes. CPTI mRNA was lower in a2-KO muscles than in a2-WT muscles at all time-points. In a1-WT and a1-KO muscles, running increased the mRNA content of PGC-1a and FOXO1 similarly. The a2-KO was associated with lower muscle adenosine 5'-triphosphate content, and the inosine monophosphate content increased substantially at the end of exercise only in a2-KO muscles. In addition, subcutaneous injection of 5-aminoimidazole-4-carboxamide-1-ß-4-ribofuranoside (AICAR) increased the mRNA content of PGC-1a, HKII, FOXO1, PDK4, and UCP3, and a2-KO abolished the AICAR-induced increases in PGC-1a and HKII mRNA. In conclusion, KO of the a2- but not the a1-AMPK isoform markedly diminished AMPK activation during running. Nevertheless, exercise-induced activation of the investigated genes in mouse skeletal muscle was not impaired in a1- or a2-AMPK KO muscles. Although it cannot be ruled out that activation of the remaining a-isoform is sufficient to increase gene activation during exercise, the present data do not support an essential role of AMPK in regulating exercise-induced gene activation in skeletal muscle.

U2 - 10.1096/fj.04-3144fje

DO - 10.1096/fj.04-3144fje

M3 - Journal article

C2 - 15878932

VL - 19

SP - 1146

EP - 1148

JO - F A S E B Journal

JF - F A S E B Journal

SN - 0892-6638

IS - 9

ER -

ID: 89161