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Hypothesis on Skeletal Muscle Aging: Mitochondrial Adenine Nucleotide Translocator Decreases Reactive Oxygen Species Production While Preserving Coupling Efficiency

hal.structure.identifierCentre de recherche Cardio-Thoracique de Bordeaux [Bordeaux] [CRCTB]
dc.contributor.authorDIOLEZ, Philippe
hal.structure.identifierCentre de Gériatrie
hal.structure.identifierCentre de résonance magnétique des systèmes biologiques [CRMSB]
dc.contributor.authorBOURDEL-MARCHASSON, Isabelle
hal.structure.identifierUniversity of California [Los Angeles] [UCLA]
dc.contributor.authorCALMETTES, Guillaume
hal.structure.identifierCentre de recherche Cardio-Thoracique de Bordeaux [Bordeaux] [CRCTB]
dc.contributor.authorPASDOIS, Philippe
hal.structure.identifierCentre de recherche Cardio-Thoracique de Bordeaux [Bordeaux] [CRCTB]
dc.contributor.authorDETAILLE, Dominique
hal.structure.identifierCentre de résonance magnétique des systèmes biologiques [CRMSB]
dc.contributor.authorROULAND, Richard
hal.structure.identifierUniversité du Québec à Montréal = University of Québec in Montréal [UQAM]
dc.contributor.authorGOUSPILLOU, Gilles
dc.date.accessioned2021-10-07T16:28:42Z
dc.date.available2021-10-07T16:28:42Z
dc.date.issued2015
dc.identifier.issn1664-042X
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/112609
dc.description.abstractEnMitochondrial membrane potential is the major regulator of mitochondrial functions, including coupling efficiency and production of reactive oxygen species (ROS). Both functions are crucial for cell bioenergetics. We previously presented evidences for a specific modulation of adenine nucleotide translocase (ANT) appearing during aging that results in a decrease in membrane potential-and therefore ROS production-but surprisingly increases coupling efficiency under conditions of low ATP turnover. Careful study of the bioenergetic parameters (oxidation and phosphorylation rates, membrane potential) of isolated mitochondria from skeletal muscles (gastrocnemius) of aged and young rats revealed a remodeling at the level of the phosphorylation system, in the absence of alteration of the inner mitochondrial membrane (uncoupling) or respiratory chain complexes regulation. We further observed a decrease in mitochondrial affinity for ADP in aged isolated mitochondria, and higher sensitivity of ANT to its specific inhibitor atractyloside. This age-induced modification of ANT results in an increase in the ADP concentration required to sustain the same ATP turnover as compared to young muscle, and therefore in a lower membrane potential under phosphorylating-in vivo-conditions. Thus, for equivalent ATP turnover (cellular ATP demand), coupling efficiency is even higher in aged muscle mitochondria, due to the down-regulation of inner membrane proton leak caused by the decrease in membrane potential. In the framework of the radical theory of aging, these modifications in ANT function may be the result of oxidative damage caused by intra mitochondrial ROS and may appear like a virtuous circle where ROS induce a mechanism that reduces their production, without causing uncoupling, and even leading in improved efficiency. Because of the importance of ROS as therapeutic targets, this new mechanism deserves further studies.
dc.language.isoen
dc.publisherFrontiers
dc.subject.enmitochondrial membrane potential
dc.subject.enmuscle energetics
dc.subject.enoxygen free radicals
dc.subject.enmitochondria
dc.subject.enskeletal muscle aging
dc.subject.enadenosine nucleotide translocator
dc.title.enHypothesis on Skeletal Muscle Aging: Mitochondrial Adenine Nucleotide Translocator Decreases Reactive Oxygen Species Production While Preserving Coupling Efficiency
dc.typeArticle de revue
dc.identifier.doi10.3389/fphys.2015.00369
dc.subject.halSciences du Vivant [q-bio]/Médecine humaine et pathologie/Physiologie [q-bio.TO]
bordeaux.journalFrontiers in Physiology
bordeaux.page369
bordeaux.volume6
bordeaux.hal.laboratoriesCentre de Résonance Magnétique des Systèmes Biologiques (CRMSB) - UMR 5536*
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionCNRS
bordeaux.peerReviewedoui
hal.identifierhal-02483504
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02483504v1
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