|Modulation of autophagy and ubiquitin-proteasome pathways during ultra-endurance running.|
|PMID: 22345427 Owner: NLM Status: MEDLINE|
|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.|
|Cécile Jamart; Marc Francaux; Guillaume Y Millet; Louise Deldicque; Delphine Frère; Léonard Féasson|
Related Documents :
|11734447 - Roles of mechanical forces and collagen failure in the development of elastase-induced ...
22487987 - Effects of heat acclimation on endurance capacity and prolactin response to exercise in...
21502887 - Effect of inspiratory muscle training on exercise tolerance in asthmatic individuals.
16231607 - Characterization of knitted polymeric scaffolds for potential use in ligament tissue en...
19411087 - Adding exercise training to rosuvastatin treatment: influence on serum lipids and bioma...
16298747 - Vulnerability of the mid aged rat myocardium to the age-induced oxidative stress: influ...
|Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-02-16|
|Title: Journal of applied physiology (Bethesda, Md. : 1985) Volume: 112 ISSN: 1522-1601 ISO Abbreviation: J. Appl. Physiol. Publication Date: 2012 May|
|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|
|Languages: eng Pagination: 1529-37 Citation Subset: IM|
|Institute of Neuroscience, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.|
|Data Bank Information|
Bank Name/Acc. No.:
|APA/MLA Format Download EndNote Download BibTex|
AMP-Activated Protein Kinases
Adaptor Proteins, Signal Transducing / metabolism
Blood Glucose / metabolism
Forkhead Transcription Factors / metabolism
GTP Phosphohydrolases / metabolism
Insulin / blood
Microtubule-Associated Proteins / metabolism
Mitochondria, Muscle / enzymology, pathology
Mitochondrial Membrane Transport Proteins / metabolism
Mitochondrial Proteins / metabolism
Muscle Proteins / metabolism
Phosphoproteins / metabolism
Proteasome Endopeptidase Complex / metabolism*
Protein Kinases / metabolism
Proto-Oncogene Proteins c-akt / metabolism
Quadriceps Muscle / enzymology*, pathology*
SKP Cullin F-Box Protein Ligases / metabolism
Small Ubiquitin-Related Modifier Proteins / metabolism
TOR Serine-Threonine Kinases / metabolism
Ubiquitin / metabolism*
Ubiquitin-Protein Ligases / metabolism
|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 18.104.22.168/MTOR protein, human; EC 22.214.171.124/TOR Serine-Threonine Kinases; EC 126.96.36.199/AMP-Activated Protein Kinases; EC 188.8.131.52/PTEN-induced putative kinase; EC 184.108.40.206/Proto-Oncogene Proteins c-akt; EC 220.127.116.11/PSMB2 protein, human; EC 18.104.22.168/PSMB5 protein, human; EC 22.214.171.124/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 126.96.36.199/DNM1L protein, human; EC 188.8.131.52/FBXO32 protein, human; EC 184.108.40.206/SKP Cullin F-Box Protein Ligases; EC 220.127.116.11/TRIM63 protein, human; EC 18.104.22.168/Ubiquitin-Protein Ligases; EC 22.214.171.124/parkin protein|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: The Role of Free Radicals in Traumatic Brain Injury.
Next Document: EMG activity in hyoid muscles during pig suckling.