5'-AMP Activated Protein Kinase is Involved in the Regulation of Myocardial β-Oxidative Capacity in Mice

Nis Ottesen Stride; Steen Larsen; Jonas Thue Treebak; Christina Neigaard Hansen; Martin Hey-Mogensen; Tobias Speerschneider; Thomas Jensen; Jacob Jeppesen; Jørgen Wojtaszewski; Erik Richter; Lars Køber; Flemming Dela

doi:10.3389/fphys.2012.00033

5'-AMP Activated Protein Kinase is Involved in the Regulation of Myocardial β-Oxidative Capacity in Mice

Nis Ottesen Stride, Steen Larsen, Jonas Thue Treebak, Christina Neigaard Hansen, Martin Hey-Mogensen, Tobias Speerschneider, Thomas Jensen, Jacob Jeppesen, Jørgen Wojtaszewski, Erik Richter, Lars Køber, Flemming Dela

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Abstract

5'-adenosine monophosphate-activated protein kinase (AMPK) is considered central in regulation of energy status and substrate utilization within cells. In heart failure the energetic state is compromised and substrate metabolism is altered. We hypothesized that this could be linked to changes in AMPK activity and we therefore investigated mitochondrial oxidative phosphorylation capacity from the oxidation of long- and medium-chain fatty acids (LCFA and MCFA) in cardiomyocytes from young and old mice expressing a dominant negative AMPKα2 (AMPKα2-KD) construct and their wildtype (WT) littermates. We found a 35-45% (P

Originalsprog	Engelsk
Tidsskrift	Frontiers in Physiology
Vol/bind	3
Sider (fra-til)	33
ISSN	1664-042X
DOI	https://doi.org/10.3389/fphys.2012.00033
Status	Udgivet - 2012

Adgang til dokumentet

10.3389/fphys.2012.00033

Citationsformater

5'-AMP Activated Protein Kinase is Involved in the Regulation of Myocardial β-Oxidative Capacity in Mice. / Stride, Nis Ottesen; Larsen, Steen; Treebak, Jonas Thue; Hansen, Christina Neigaard; Hey-Mogensen, Martin; Speerschneider, Tobias; Jensen, Thomas; Jeppesen, Jacob; Wojtaszewski, Jørgen; Richter, Erik; Køber, Lars; Dela, Flemming.

I: Frontiers in Physiology, Bind 3, 2012, s. 33.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Stride, Nis Ottesen ; Larsen, Steen ; Treebak, Jonas Thue ; Hansen, Christina Neigaard ; Hey-Mogensen, Martin ; Speerschneider, Tobias ; Jensen, Thomas ; Jeppesen, Jacob ; Wojtaszewski, Jørgen ; Richter, Erik ; Køber, Lars ; Dela, Flemming. / 5'-AMP Activated Protein Kinase is Involved in the Regulation of Myocardial β-Oxidative Capacity in Mice. I: Frontiers in Physiology. 2012 ; Bind 3. s. 33.

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abstract = "5'-adenosine monophosphate-activated protein kinase (AMPK) is considered central in regulation of energy status and substrate utilization within cells. In heart failure the energetic state is compromised and substrate metabolism is altered. We hypothesized that this could be linked to changes in AMPK activity and we therefore investigated mitochondrial oxidative phosphorylation capacity from the oxidation of long- and medium-chain fatty acids (LCFA and MCFA) in cardiomyocytes from young and old mice expressing a dominant negative AMPKα2 (AMPKα2-KD) construct and their wildtype (WT) littermates. We found a 35-45% (P ",

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T1 - 5'-AMP Activated Protein Kinase is Involved in the Regulation of Myocardial β-Oxidative Capacity in Mice

AU - Stride, Nis Ottesen

AU - Larsen, Steen

AU - Treebak, Jonas Thue

AU - Hansen, Christina Neigaard

AU - Hey-Mogensen, Martin

AU - Speerschneider, Tobias

AU - Jensen, Thomas

AU - Jeppesen, Jacob

AU - Wojtaszewski, Jørgen

AU - Richter, Erik

AU - Køber, Lars

AU - Dela, Flemming

PY - 2012

Y1 - 2012

N2 - 5'-adenosine monophosphate-activated protein kinase (AMPK) is considered central in regulation of energy status and substrate utilization within cells. In heart failure the energetic state is compromised and substrate metabolism is altered. We hypothesized that this could be linked to changes in AMPK activity and we therefore investigated mitochondrial oxidative phosphorylation capacity from the oxidation of long- and medium-chain fatty acids (LCFA and MCFA) in cardiomyocytes from young and old mice expressing a dominant negative AMPKα2 (AMPKα2-KD) construct and their wildtype (WT) littermates. We found a 35-45% (P

AB - 5'-adenosine monophosphate-activated protein kinase (AMPK) is considered central in regulation of energy status and substrate utilization within cells. In heart failure the energetic state is compromised and substrate metabolism is altered. We hypothesized that this could be linked to changes in AMPK activity and we therefore investigated mitochondrial oxidative phosphorylation capacity from the oxidation of long- and medium-chain fatty acids (LCFA and MCFA) in cardiomyocytes from young and old mice expressing a dominant negative AMPKα2 (AMPKα2-KD) construct and their wildtype (WT) littermates. We found a 35-45% (P

U2 - 10.3389/fphys.2012.00033

DO - 10.3389/fphys.2012.00033

M3 - Journal article

C2 - 22371704

VL - 3

SP - 33

JO - Frontiers in Physiology

JF - Frontiers in Physiology

SN - 1664-042X

ER -