Activation of AMPKα2 Is Not Required for Mitochondrial FAT/CD36 Accumulation during Exercise.

Exercise has been shown to induce the translocation of fatty acid translocase (FAT/CD36), a fatty acid transport protein, to both plasma and mitochondrial membranes. While previous studies have examined signals involved in the induction of FAT/CD36 translocation to sarcolemmal membranes, to date the...

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Main Authors: Cynthia Monaco, Jamie Whitfield, Swati S Jain, Lawrence L Spriet, Arend Bonen, Graham P Holloway
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4429092?pdf=render
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author Cynthia Monaco
Jamie Whitfield
Swati S Jain
Lawrence L Spriet
Arend Bonen
Graham P Holloway
author_facet Cynthia Monaco
Jamie Whitfield
Swati S Jain
Lawrence L Spriet
Arend Bonen
Graham P Holloway
author_sort Cynthia Monaco
collection DOAJ
description Exercise has been shown to induce the translocation of fatty acid translocase (FAT/CD36), a fatty acid transport protein, to both plasma and mitochondrial membranes. While previous studies have examined signals involved in the induction of FAT/CD36 translocation to sarcolemmal membranes, to date the signaling events responsible for FAT/CD36 accumulation on mitochondrial membranes have not been investigated. In the current study muscle contraction rapidly increased FAT/CD36 on plasma membranes (7.5 minutes), while in contrast, FAT/CD36 only increased on mitochondrial membranes after 22.5 minutes of muscle contraction, a response that was exercise-intensity dependent. Considering that previous research has shown that AMP activated protein kinase (AMPK) α2 is not required for FAT/CD36 translocation to the plasma membrane, we investigated whether AMPK α2 signaling is necessary for mitochondrial FAT/CD36 accumulation. Administration of 5-Aminoimidazole-4-carboxamide ribonucleotide (AICAR) induced AMPK phosphorylation, and resulted in FAT/CD36 accumulation on SS mitochondria, suggesting AMPK signaling may mediate this response. However, SS mitochondrial FAT/CD36 increased following acute treadmill running in both wild-type (WT) and AMPKα 2 kinase dead (KD) mice. These data suggest that AMPK signaling is not required for SS mitochondrial FAT/CD36 accumulation. The current data also implicates alternative signaling pathways that are exercise-intensity dependent, as IMF mitochondrial FAT/CD36 content only occurred at a higher power output. Taken altogether the current data suggests that activation of AMPK signaling is sufficient but not required for exercise-induced accumulation in mitochondrial FAT/CD36.
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spelling doaj.art-317b42c79e8c48d1ac84a3bed701af6a2022-12-22T02:02:20ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01105e012612210.1371/journal.pone.0126122Activation of AMPKα2 Is Not Required for Mitochondrial FAT/CD36 Accumulation during Exercise.Cynthia MonacoJamie WhitfieldSwati S JainLawrence L SprietArend BonenGraham P HollowayExercise has been shown to induce the translocation of fatty acid translocase (FAT/CD36), a fatty acid transport protein, to both plasma and mitochondrial membranes. While previous studies have examined signals involved in the induction of FAT/CD36 translocation to sarcolemmal membranes, to date the signaling events responsible for FAT/CD36 accumulation on mitochondrial membranes have not been investigated. In the current study muscle contraction rapidly increased FAT/CD36 on plasma membranes (7.5 minutes), while in contrast, FAT/CD36 only increased on mitochondrial membranes after 22.5 minutes of muscle contraction, a response that was exercise-intensity dependent. Considering that previous research has shown that AMP activated protein kinase (AMPK) α2 is not required for FAT/CD36 translocation to the plasma membrane, we investigated whether AMPK α2 signaling is necessary for mitochondrial FAT/CD36 accumulation. Administration of 5-Aminoimidazole-4-carboxamide ribonucleotide (AICAR) induced AMPK phosphorylation, and resulted in FAT/CD36 accumulation on SS mitochondria, suggesting AMPK signaling may mediate this response. However, SS mitochondrial FAT/CD36 increased following acute treadmill running in both wild-type (WT) and AMPKα 2 kinase dead (KD) mice. These data suggest that AMPK signaling is not required for SS mitochondrial FAT/CD36 accumulation. The current data also implicates alternative signaling pathways that are exercise-intensity dependent, as IMF mitochondrial FAT/CD36 content only occurred at a higher power output. Taken altogether the current data suggests that activation of AMPK signaling is sufficient but not required for exercise-induced accumulation in mitochondrial FAT/CD36.http://europepmc.org/articles/PMC4429092?pdf=render
spellingShingle Cynthia Monaco
Jamie Whitfield
Swati S Jain
Lawrence L Spriet
Arend Bonen
Graham P Holloway
Activation of AMPKα2 Is Not Required for Mitochondrial FAT/CD36 Accumulation during Exercise.
PLoS ONE
title Activation of AMPKα2 Is Not Required for Mitochondrial FAT/CD36 Accumulation during Exercise.
title_full Activation of AMPKα2 Is Not Required for Mitochondrial FAT/CD36 Accumulation during Exercise.
title_fullStr Activation of AMPKα2 Is Not Required for Mitochondrial FAT/CD36 Accumulation during Exercise.
title_full_unstemmed Activation of AMPKα2 Is Not Required for Mitochondrial FAT/CD36 Accumulation during Exercise.
title_short Activation of AMPKα2 Is Not Required for Mitochondrial FAT/CD36 Accumulation during Exercise.
title_sort activation of ampkα2 is not required for mitochondrial fat cd36 accumulation during exercise
url http://europepmc.org/articles/PMC4429092?pdf=render
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AT lawrencelspriet activationofampka2isnotrequiredformitochondrialfatcd36accumulationduringexercise
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