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

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 associate...

Full description

Saved in:
Bibliographic Details
Published in:Proteomics (Weinheim) 2014-01, Vol.14 (1), p.121-132
Main Authors: Hwang, Chae Young, Kim, Kyutae, Choi, Jeong Yi, Bahn, Young Jae, Lee, Seung-Min, Kim, Yoon Ki, Lee, Cheolju, Kwon, Ki-Sun
Format: Article
Language:English
Subjects:
Age
Aging
Aging - physiology
Animal proteomics
Animals
Biomarker
Biomarkers - analysis
Biomarkers - chemistry
Calsequestrin
Immunoblotting
Isotope Labeling
Mass Spectrometry
Mice
mTRAQ
Muscle, Skeletal - chemistry
Muscle, Skeletal - metabolism
NFATC Transcription Factors
Proteins
Proteins - analysis
Proteins - chemistry
Proteome - analysis
Proteome - chemistry
Proteome - physiology
Proteomics - methods
Rodents
Skeletal muscle
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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
1615-9861
DOI:10.1002/pmic.201200497