Document Detail


Modulation of autophagy and ubiquitin-proteasome pathways during ultra-endurance running.
MedLine Citation:
PMID:  22345427     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In this study, the coordinated activation of ubiquitin-proteasome pathway (UPP), autophagy-lysosomal pathway (ALP), and mitochondrial remodeling including mitophagy was assessed by measuring protein markers during ultra-endurance running exercise in human skeletal muscle. Eleven male, experienced ultra-endurance athletes ran for 24 h on a treadmill. Muscle biopsy samples were taken from the vastus lateralis muscle 2 h before starting and immediately after finishing exercise. Athletes ran 149.8 ± 16.3 km with an effective running time of 18 h 42 min ( ± 41 min). The phosphorylation state of Akt (-74 ± 5%; P < 0.001), FOXO3a (-49 ± 9%; P < 0.001), mTOR Ser2448 (-32 ± 14%; P = 0.028), and 4E-BP1 (-34 ± 7%; P < 0.001) was decreased, whereas AMPK phosphorylation state increased by 247 ± 170% (P = 0.042). Proteasome β2 subunit activity increased by 95 ± 44% (P = 0.028), whereas the activities associated with the β1 and β5 subunits remained unchanged. MuRF1 protein level increased by 55 ± 26% (P = 0.034), whereas MAFbx protein and ubiquitin-conjugated protein levels did not change. LC3bII increased by 554 ± 256% (P = 0.005), and the form of ATG12 conjugated to ATG5 increased by 36 ± 17% (P = 0.042). The mitochondrial fission marker phospho-DRP1 increased by 110 ± 47% (P = 0.003), whereas the fusion marker Mfn1 and the mitophagy markers Parkin and PINK1 remained unchanged. These results fit well with a coordinated regulation of ALP and UPP triggered by FOXO3 and AMPK during ultra-endurance exercise.
Authors:
Cécile Jamart; Marc Francaux; Guillaume Y Millet; Louise Deldicque; Delphine Frère; Léonard Féasson
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-02-16
Journal Detail:
Title:  Journal of applied physiology (Bethesda, Md. : 1985)     Volume:  112     ISSN:  1522-1601     ISO Abbreviation:  J. Appl. Physiol.     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-05-02     Completed Date:  2012-08-27     Revised Date:  2013-09-26    
Medline Journal Info:
Nlm Unique ID:  8502536     Medline TA:  J Appl Physiol (1985)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1529-37     Citation Subset:  IM    
Affiliation:
Institute of Neuroscience, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
Data Bank Information
Bank Name/Acc. No.:
ClinicalTrials.gov/NCT00428779
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MeSH Terms
Descriptor/Qualifier:
AMP-Activated Protein Kinases / metabolism
Adaptor Proteins, Signal Transducing / metabolism
Adult
Autophagy*
Biopsy
Blood Glucose / metabolism
Energy Intake
Energy Metabolism
Forkhead Transcription Factors / metabolism
GTP Phosphohydrolases / metabolism
Humans
Insulin / blood
Male
Microtubule-Associated Proteins / metabolism
Middle Aged
Mitochondria, Muscle / enzymology,  pathology
Mitochondrial Membrane Transport Proteins / metabolism
Mitochondrial Proteins / metabolism
Muscle Proteins / metabolism
Phosphoproteins / metabolism
Phosphorylation
Physical Endurance*
Proteasome Endopeptidase Complex / metabolism*
Protein Kinases / metabolism
Proto-Oncogene Proteins c-akt / metabolism
Quadriceps Muscle / enzymology*,  pathology*
Running
SKP Cullin F-Box Protein Ligases / metabolism
Serine
Signal Transduction
Small Ubiquitin-Related Modifier Proteins / metabolism
TOR Serine-Threonine Kinases / metabolism
Time Factors
Ubiquitin / metabolism*
Ubiquitin-Protein Ligases / metabolism
Chemical
Reg. No./Substance:
0/ATG12 protein, human; 0/ATG5 protein, human; 0/Adaptor Proteins, Signal Transducing; 0/Blood Glucose; 0/EIF4EBP1 protein, human; 0/FOXO3 protein, human; 0/Forkhead Transcription Factors; 0/Insulin; 0/MAP1LC3B protein, human; 0/Microtubule-Associated Proteins; 0/Mitochondrial Membrane Transport Proteins; 0/Mitochondrial Proteins; 0/Muscle Proteins; 0/Phosphoproteins; 0/Small Ubiquitin-Related Modifier Proteins; 0/Ubiquitin; 56-45-1/Serine; EC 2.7.-/Protein Kinases; EC 2.7.1.1/MTOR protein, human; EC 2.7.1.1/TOR Serine-Threonine Kinases; EC 2.7.11.1/AMP-Activated Protein Kinases; EC 2.7.11.1/PTEN-induced putative kinase; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 3.4.25.1/PSMB2 protein, human; EC 3.4.25.1/PSMB5 protein, human; EC 3.4.25.1/Proteasome Endopeptidase Complex; EC 3.4.99.-/ATP dependent 26S protease; EC 3.6.1.-/GTP Phosphohydrolases; EC 3.6.5.-/Mfn1 protein, human; EC 3.6.5.5/DNM1L protein, human; EC 6.3.2.19/FBXO32 protein, human; EC 6.3.2.19/SKP Cullin F-Box Protein Ligases; EC 6.3.2.19/TRIM63 protein, human; EC 6.3.2.19/Ubiquitin-Protein Ligases; EC 6.3.2.19/parkin protein

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