A comparative proteomics study of skeletal muscle mitochondria from myostatin null mice

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dc.contributor.authorPuddick, Jonathan
dc.contributor.authorMartinus, Ryan Dennis
dc.date.accessioned2011-10-11T03:14:23Z
dc.date.available2011-10-11T03:14:23Z
dc.date.issued2011
dc.description.abstractMyostatin is a secreted protein which is known to be a negative regulator of skeletal muscle growth. Numerous studies have demonstrated that down-regulating the expression of myostatin results in an increase in muscle mass. This increase in skeletal muscle is accompanied by a marked change in the muscle fibre composition from one reliant on mitochondrial oxidative metabolism to one more focused on glycolytic metabolism. A comparative proteomics study was undertaken to investigate the effect of this altered metabolism has on the mitochondria from the gastrocnemius muscle of myostatin null mice, compared with those from wild type mice. The majority of the proteins identified showed no significant modulation between the two phenotypes, but gives an interesting insight into observations made in previous studies. Several proteins were shown to be modulated; however, only one of these was able to be identified. This protein which had sequence similarity to aldehyde reductase, was up-regulated in myostatin null mitochondria. The significance of this observation remains to be established. Interestingly, this protein has been implicated in detoxification of harmful products of lipid peroxidation.en_NZ
dc.identifier.citationPuddick, J. & Martinus, R.D. (2011). A comparative proteomics study of skeletal muscle mitochondria from myostatin null mice. Cell Biology International Reports, published online 26 September 2011.en_NZ
dc.identifier.doi10.1042/CBR20110006en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/5823
dc.language.isoen
dc.publisherPortland Press Ltden_NZ
dc.relation.isPartOfCell Biology International Reportsen_NZ
dc.relation.urihttp://www.cellbiolintrep.org/cbr/imps/abs/CBR20110006.htmen_NZ
dc.subjectgastrocnemius muscleen_NZ
dc.subjectmitochondriaen_NZ
dc.subjectmyostatinen_NZ
dc.subjectpeptide mass fingerprintingen_NZ
dc.subjectproteomicsen_NZ
dc.subject2-dimensional electrophoresisen_NZ
dc.titleA comparative proteomics study of skeletal muscle mitochondria from myostatin null miceen_NZ
dc.typeJournal Articleen_NZ
pubs.begin-page1en_NZ
pubs.elements-id36523
pubs.end-page21en_NZ
pubs.volumeonlineen_NZ
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