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Title 

Quantitative proteome analysis of age-related changes in mouse gastrocnemius muscle using mTRAQ

Authors 

Chae Young HwangK KimJeong Yi ChoiYoung Jae BahnSeung Min LeeY K KimC LeeKi Sun Kwon

Publisher 

Wiley-Blackwell

Issue Date 

2014

Citation 

Proteomics, vol. 14, no. 1, pp. 121-132

Keywords 

AgingAnimal proteomicsBiomarkerMTRAQSkeletal muscle

Abstract 

Aging is associated with a progressive loss of skeletal muscular function that often leads to progressive disability and loss of independence. Although muscle aging is well documented, the molecular mechanisms of this condition still remain unclear. To gain greater insight into the changes associated with aging of skeletal muscle, we performed quantitative proteomic analyses on young (6 months) and aged (27 months) mouse gastrocnemius muscles using mTRAQ stable isotope mass tags. We identified and quantified a total of 4585 peptides corresponding to 236 proteins (protein probability >0.9). Among them, 33 proteins were more than 1.5-fold upregulated and 20 proteins were more than 1.5-fold downregulated in aged muscle compared with young muscle. An ontological analysis revealed that differentially expressed proteins belonged to distinct functional groups, including ion homeostasis, energy metabolism, protein turnover, and Ca2+ signaling. Identified proteins included aralar1, β-enolase, fatty acid-binding protein 3, 3-hydroxyacyl-CoA dehydrogenase (Hadh), F-box protein 22, F-box, and leucine-rich repeat protein 18, voltage-dependent L-type calcium channel subunit beta-1, ryanodine receptor (RyR), and calsequestrin. Ectopic expression of calsequestrin in C2C12 myoblast resulted in decreased activity of nuclear factor of activated T-cells and increased levels of atrogin-1 and MuRF1 E3 ligase, suggesting that these differentially expressed proteins are involved in muscle aging.

ISSN 

1615-9853

Link 

http://dx.doi.org/10.1002/pmic.201200497

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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