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dc.contributor.authorParker, Nen
dc.contributor.authorAffourtit, Cen
dc.contributor.authorVidal-Puig, Aen
dc.contributor.authorBrand, MDen
dc.date.accessioned2015-07-09T08:18:14Z
dc.date.available2015-07-09T08:18:14Z
dc.date.issued2008-05-15en
dc.identifier.urihttp://hdl.handle.net/10026.1/3420
dc.description.abstract

Leak of protons into the mitochondrial matrix during substrate oxidation partially uncouples electron transport from phosphorylation of ADP, but the functions and source of basal and inducible proton leak in vivo remain controversial. In the present study we describe an endogenous activation of proton conductance in mitochondria isolated from rat and mouse skeletal muscle following addition of respiratory substrate. This endogenous activation increased with time, required a high membrane potential and was diminished by high concentrations of serum albumin. Inhibition of this endogenous activation by GDP [classically considered specific for UCPs (uncoupling proteins)], carboxyatractylate and bongkrekate (considered specific for the adenine nucleotide translocase) was examined in skeletal muscle mitochondria from wild-type and Ucp3-knockout mice. Proton conductance through endogenously activated UCP3 was calculated as the difference in leak between mitochondria from wild-type and Ucp3-knockout mice, and was found to be inhibited by carboxyatractylate and bongkrekate, but not GDP. Proton conductance in mitochondria from Ucp3-knockout mice was strongly inhibited by carboxyatractylate, bongkrekate and partially by GDP. We conclude the following: (i) at high protonmotive force, an endogenously generated activator stimulates proton conductance catalysed partly by UCP3 and partly by the adenine nucleotide translocase; (ii) GDP is not a specific inhibitor of UCP3, but also inhibits proton translocation by the adenine nucleotide translocase; and (iii) the inhibition of UCP3 by carboxyatractylate and bongkrekate is likely to be indirect, acting through the adenine nucleotide translocase.

en
dc.format.extent131 - 139en
dc.languageengen
dc.language.isoengen
dc.subjectAnimalsen
dc.subjectAtractylosideen
dc.subjectBongkrekic Aciden
dc.subjectEnergy Metabolismen
dc.subjectFemaleen
dc.subjectIon Channelsen
dc.subjectMaleen
dc.subjectMalonatesen
dc.subjectMembrane Potential, Mitochondrialen
dc.subjectMiceen
dc.subjectMice, Knockouten
dc.subjectMitochondria, Muscleen
dc.subjectMitochondrial ADP, ATP Translocasesen
dc.subjectMitochondrial Proteinsen
dc.subjectMuscle, Skeletalen
dc.subjectNitrogen Oxidesen
dc.subjectPalmitatesen
dc.subjectProton Pumpsen
dc.subjectRatsen
dc.subjectRats, Wistaren
dc.subjectSerum Albumin, Bovineen
dc.subjectTime Factorsen
dc.subjectUncoupling Agentsen
dc.subjectUncoupling Protein 3en
dc.titleEnergization-dependent endogenous activation of proton conductance in skeletal muscle mitochondria.en
dc.typeJournal Article
plymouth.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/18251717en
plymouth.issue1en
plymouth.volume412en
plymouth.publication-statusPublisheden
plymouth.journalBiochem Jen
dc.identifier.doi10.1042/BJ20080006en
plymouth.organisational-group/Plymouth
plymouth.organisational-group/Plymouth/00 Groups by role
plymouth.organisational-group/Plymouth/00 Groups by role/Academics
plymouth.organisational-group/Plymouth/Faculty of Medicine and Dentistry
plymouth.organisational-group/Plymouth/Faculty of Medicine and Dentistry/Biomedical Research Group
plymouth.organisational-group/Plymouth/Faculty of Medicine and Dentistry/Biomedical Research Group/RC Reporting Group BRG
plymouth.organisational-group/Plymouth/Faculty of Medicine and Dentistry/School of Biomedical Sciences
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA/UoA01 Clinical Medicine
plymouth.organisational-group/Plymouth/Research Groups
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)/CBR
dc.publisher.placeEnglanden
dc.identifier.eissn1470-8728en
dc.rights.embargoperiodNo embargoen
rioxxterms.versionofrecord10.1042/BJ20080006en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.typeJournal Article/Reviewen


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