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dc.contributor.authorBrocca, Lorenza
dc.contributor.authorMcPhee, Jamie
dc.contributor.authorLonga, Emanuela
dc.contributor.authorCanepari, Monica
dc.contributor.authorSeynnes, Olivier R.
dc.contributor.authorde Vito, Giuseppe
dc.contributor.authorPellegrino, Maria A.
dc.contributor.authorNarici, Marco
dc.contributor.authorBottinelli, Roberto
dc.date.accessioned2018-09-05T07:29:03Z
dc.date.available2018-09-05T07:29:03Z
dc.date.created2017-11-15T08:50:27Z
dc.date.issued2017
dc.identifier.citationJournal of Physiology. 2017, 595, 4823-4844.nb_NO
dc.identifier.issn0022-3751
dc.identifier.urihttp://hdl.handle.net/11250/2560818
dc.descriptionI Brage finner du siste tekst-versjon av artikkelen, og den kan inneholde ubetydelige forskjeller fra forlagets pdf-versjon. Forlagets pdf-versjon finner du på wiley.com / In Brage you'll find the final text version of the article, and it may contain insignificant differences from the journal's pdf version. The definitive version is available at wiley.comnb_NO
dc.description.abstractContradictory results have been reported on the impact of ageing on structure and functions of skeletal muscle fibres, likely to be due to a complex interplay between ageing and other phenomena such as disuse and diseases. Here we recruited healthy, physically and socially active young (YO) and elderly (EL) men in order to study ageing per se without the confounding effects of impaired physical function. In vivo analyses of quadriceps and in vitro analyses of vastus lateralis muscle biopsies were performed. In EL subjects, our results show that (i) quadriceps volume, maximum voluntary contraction isometric torque and patellar tendon force were significantly lower; (ii) muscle fibres went through significant atrophy and impairment of specific force (isometric force/cross-sectional area) and unloaded shortening velocity; (iii) myosin/actin ratio and myosin content in individual muscle fibres were not altered; (iv) the muscle proteome went through quantitative adaptations, namely an up-regulation of the content of several groups of proteins among which were myofibrillar proteins and antioxidant defence systems; (v) the muscle proteome went through qualitative adaptations, namely phosphorylation of several proteins, including myosin light chain-2 slow and troponin T and carbonylation of myosin heavy chains. The present results indicate that impairment of individual muscle fibre structure and function is a major feature of ageing per se and that qualitative adaptations of muscle proteome are likely to be more involved than quantitative adaptations in determining such a phenomenon.nb_NO
dc.description.abstractStructure and function of human muscle fibres and muscle proteome in physically active older mennb_NO
dc.language.isoengnb_NO
dc.subjectadultnb_NO
dc.subjectagednb_NO
dc.subjectaging/metabolismnb_NO
dc.subjectexercisenb_NO
dc.subjecthumannb_NO
dc.subjectmalenb_NO
dc.subjectmuscle proteins/metabolismnb_NO
dc.subjectmuscle, skeletal/metabolismnb_NO
dc.subjectmuscle, skeletal/pathologynb_NO
dc.subjectmuscular atrophy/metabolismnb_NO
dc.subjectoxidation-reductionnb_NO
dc.subjectphosphorylationnb_NO
dc.subjectprotein processing, post-translationalnb_NO
dc.subjectproteomenb_NO
dc.subjectyoung adultnb_NO
dc.titleStructure and function of human muscle fibres and muscle proteome in physically active older mennb_NO
dc.title.alternativeStructure and function of human muscle fibres and muscle proteome in physically active older mennb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.description.versionacceptedVersionnb_NO
dc.source.pagenumber4823-4844nb_NO
dc.source.volume595nb_NO
dc.source.journalJournal of Physiologynb_NO
dc.source.issue14nb_NO
dc.identifier.doi10.1113/JP274148
dc.identifier.cristin1514226
dc.description.localcodeSeksjon for fysisk prestasjonsevne / Department of Physical Performancenb_NO
cristin.unitcode150,31,0,0
cristin.unitnameSeksjon for fysisk prestasjonsevne
cristin.ispublishedtrue
cristin.fulltextpostprint
cristin.qualitycode2


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