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dc.contributor.authorSmith, Neil T.
dc.contributor.authorSoriano-Arroquia, Ana
dc.contributor.authorGoljanek-Whysall, Katarzyna
dc.contributor.authorJackson, Malcolm J.
dc.contributor.authorMcDonagh, Brian
dc.date.accessioned2018-09-20T16:24:59Z
dc.date.available2018-09-20T16:24:59Z
dc.date.issued2018-02-01
dc.identifier.citationSmith, Neil T. Soriano-Arroquia, Ana; Goljanek-Whysall, Katarzyna; Jackson, Malcolm J.; McDonagh, Brian (2018). Redox responses are preserved across muscle fibres with differential susceptibility to aging. Journal of Proteomics 177 , 112-123
dc.identifier.issn1874-3919
dc.identifier.urihttp://hdl.handle.net/10379/13948
dc.description.abstractAge-related loss of muscle mass and function is associated with increased frailty and loss of independence. The mechanisms underlying the susceptibility of different muscle types to age-related atrophy are not fully understood. Reactive oxygen species (ROS) are recognised as important signalling molecules in healthy muscle and redox sensitive proteins can respond to intracellular changes in ROS concentrations modifying reactive thiol groups on Cysteine (Cys) residues. Conserved Cys residues tend to occur in functionally important locations and can have a direct impact on protein function through modifications at the active site or determining protein conformation. The aim of this work was to determine age-related changes in the redox proteome of two metabolically distinct murine skeletal muscles, the quadriceps a predominantly glycolytic muscle and the soleus which contains a higher proportion of mitochondria. To examine the effects of aging on the global proteome and the oxidation state of individual redox sensitive Cys residues, we employed a label free proteomics approach including a differential labelling of reduced and reversibly oxidised Cys residues. Our results indicate the proteomic response to aging is dependent on muscle type but redox changes that occur primarily in metabolic and cytoskeletal proteins are generally preserved between metabolically distinct tissues. Biological significance: Skeletal muscle containing fast twitch glycolytic fibres are more susceptible to age related atrophy compared to muscles with higher proportions of oxidative slow twitch fibres. Contracting skeletal muscle generates reactive oxygen species that are required for correct signalling and adaptation to exercise and it is also known that the intracellular redox environment changes with age. To identify potential mechanisms for the distinct response to age, this article combines a global proteomic approach and a differential labelling of reduced and reversibly oxidised Cysteine residues in two metabolically distinct skeletal muscles, quadriceps and soleus, from adult and old mice. Our results indicate that the global proteomic changes with age in skeletal muscles are dependent on fibre type. However, redox specific changes are preserved across muscle types and accompanied with a reduction in the number of redox sensitive Cysteine residues.
dc.publisherElsevier BV
dc.relation.ispartofJournal of Proteomics
dc.subjectskeletal muscle
dc.subjectaging
dc.subjectredox proteomics
dc.subjectcysteine oxidation
dc.subjectsarcopenia
dc.subjectsknac
dc.subjectrat skeletal-muscle
dc.subjectcontractile activity
dc.subjectproteomics reveals
dc.subjectmetabolic pathways
dc.subjectprotein-synthesis
dc.subjectca2+ sensitivity
dc.subjectoxidative stress
dc.subjects-nitrosylation
dc.subjectfree-radicals
dc.subjectage
dc.titleRedox responses are preserved across muscle fibres with differential susceptibility to aging
dc.typeArticle
dc.identifier.doi10.1016/j.jprot.2018.02.015
dc.local.publishedsourcehttp://europepmc.org/articles/pmc5884322?pdf=render
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