Search: id:"swepub:oai:DiVA.org:uu-87940" >
Myonuclear domain s...
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Liu, Jing-XiaUmeå universitet,Uppsala universitet,Klinisk neurofysiologi,Anatomi,Department of Neurosciences, Uppsala University, Uppsala, Sweden
(author)
Myonuclear domain size and myosin isoform expression in muscle fibres from mammals representing a 100 000-fold difference in body size
- Article/chapterEnglish2009
Publisher, publication year, extent ...
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2008-12-22
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Wiley,2009
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printrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:uu-87940
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https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-87940URI
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https://doi.org/10.1113/expphysiol.2008.043877DOI
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-20597URI
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https://res.slu.se/id/publ/27336URI
Supplementary language notes
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Language:English
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Summary in:English &language:-1_t
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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This comparative study of myonuclear domain (MND) size in mammalian species representing a 100 000-fold difference in body mass, ranging from 25 g to 2500 kg, was undertaken to improve our understanding of myonuclear organization in skeletal muscle fibres. Myonuclear domain size was calculated from three-dimensional reconstructions in a total of 235 single muscle fibre segments at a fixed sarcomere length. Irrespective of species, the largest MND size was observed in muscle fibres expressing fast myosin heavy chain (MyHC) isoforms, but in the two smallest mammalian species studied (mouse and rat), MND size was not larger in the fast-twitch fibres expressing the IIA MyHC isofom than in the slow-twitch type I fibres. In the larger mammals, the type I fibres always had the smallest average MND size, but contrary to mouse and rat muscles, type IIA fibres had lower mitochondrial enzyme activities than type I fibres. Myonuclear domain size was highly dependent on body mass in the two muscle fibre types expressed in all species, i.e. types I and IIA. Myonuclear domain size increased in muscle fibres expressing both the β/slow (type I; r= 0.84, P < 0.001) and the fast IIA MyHC isoform (r= 0.90; P < 0.001). Thus, MND size scales with body size and is highly dependent on muscle fibre type, independent of species. However, myosin isoform expression is not the sole protein determining MND size, and other protein systems, such as mitochondrial proteins, may be equally or more important determinants of MND size.
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Höglund, Anna-StinaUppsala universitet,Klinisk neurofysiologi,Department of Neurosciences, Uppsala University, Uppsala, Sweden
(author)
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Karlsson, PatrickUppsala universitet,Centrum för bildanalys,Datoriserad bildanalys,Centre for Image Analyses, Uppsala University, Uppsala, Sweden(Swepub:uu)pakar031
(author)
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Lindblad, JoakimSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Uppsala universitet,Centrum för bildanalys,Datoriserad bildanalys,Centre for Image Analyses, University of Agricultural Sciences, Uppsala, Sweden,,Centre for Image Analysis(Swepub:slu)51900
(author)
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Qaisar, RizwanUppsala universitet,Klinisk neurofysiologi,Professor Lars Larsson group,Department of Neurosciences, Uppsala University, Uppsala, Sweden(Swepub:uu)rizqa267
(author)
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Aare, SudhakarUppsala universitet,Klinisk neurofysiologi,Department of Neurosciences, Uppsala University, Uppsala, Sweden(Swepub:uu)sudaa881
(author)
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Bengtsson, EwertUppsala universitet,Centrum för bildanalys,Datoriserad bildanalys,Centre for Image Analyses, Uppsala University, Uppsala, Sweden(Swepub:uu)ewertbs
(author)
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Larsson, LarsUppsala universitet,Klinisk neurofysiologi,Department of Neurosciences, Uppsala University, Uppsala, Sweden,Center for Development and Health Genetics, The Pennsylvania State University, University Park, PA, USA(Swepub:uu)lalar021
(author)
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Uppsala universitetKlinisk neurofysiologi
(creator_code:org_t)
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Sveriges lantbruksuniversitet
Related titles
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In:Experimental Physiology: Wiley94:1, s. 117-1290958-06701469-445X
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