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dc.contributor.authorGarcia de la Serrana Castillo, Daniel
dc.contributor.authorJohnston, Ian Alistair
dc.date.accessioned2013-10-17T14:01:02Z
dc.date.available2013-10-17T14:01:02Z
dc.date.issued2013-09-06
dc.identifier.citationGarcia de la Serrana Castillo , D & Johnston , I A 2013 , ' Expression of heat shock protein (Hsp90) paralogues is regulated by amino acids in skeletal muscle of Atlantic salmon ' , PLoS One , vol. 8 , no. 9 , e74295 . https://doi.org/10.1371/journal.pone.0074295en
dc.identifier.issn1932-6203
dc.identifier.otherPURE: 74798142
dc.identifier.otherPURE UUID: d3fe58f6-3b73-4a52-8f4d-98d4d87031d6
dc.identifier.otherScopus: 84883646552
dc.identifier.otherORCID: /0000-0002-7796-5754/work/47136025
dc.identifier.urihttp://hdl.handle.net/10023/4102
dc.description.abstractHeat shock proteins 90 (Hsp90) have an essential role in sarcomere formation and differentiation in skeletal muscle and also act as molecular chaperones during protein folding impacting a wide range of physiological processes. We characterised and provided a phylogenetically consistent nomenclature for the complete repertoire of six Hsp90 paralogues present in duplicated salmonid fish genomes (Hsp90α1a, Hsp90α1b, Hsp90α2a, Hsp90α2b, Hsp90ß1a and Hsp90ß1b). The expression of paralogues in fast skeletal muscle was investigated using in vivo fasting-feeding experiments and primary myogenic cultures. Fasted juvenile Atlantic salmon (Salmo salar) showed a transient 2 to 8-fold increase in the expression of all 4 Hsp90α paralogues within 24h of satiation feeding. Hsp90α1a and hsp90α1b also showed a pronounced secondary increase in expression after 10 days, concomitant with muscle differentiation and the expression of myogenin and sarcomeric proteins (mlc2, myhc). Hsp90ß1b was constitutively expressed whereas Hsp90ß1a expression was downregulated 10-fold between fasted and fed individuals. Hsp90α1a and Hsp90α1b were upregulated 10 to 15-fold concomitant with myotube formation and muscle differentiation in vitro whereas other Hsp90 paralogues showed no change in expression. In cells starved of amino acid (AA) and serum for 72h the addition of AA, but not insulin-like growth factor 1, increased phosphorylation of mTor and expression of all 4 hsp90α paralogues and associated co-chaperones including hsp30, tbcb, pdia4, pdia6, stga and fk504bp1, indicating a general activation of the protein folding response. In contrast, Hsp90ß1a expression in vitro was unresponsive to AA treatment indicating that some other as yet uncharacterised signal(s) regulate its expression in response to altered nutritional state.
dc.language.isoeng
dc.relation.ispartofPLoS Oneen
dc.rights© 2013 Garcia de la serrana, Johnston. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.subjectQH426 Geneticsen
dc.subject.lccQH426en
dc.titleExpression of heat shock protein (Hsp90) paralogues is regulated by amino acids in skeletal muscle of Atlantic salmonen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Marine Alliance for Science & Technology Scotlanden
dc.contributor.institutionUniversity of St Andrews.Scottish Oceans Instituteen
dc.contributor.institutionUniversity of St Andrews.Centre for Research into Ecological & Environmental Modellingen
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0074295
dc.description.statusPeer revieweden


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