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Comparative proteomic analysis of the aging soleus and extensor digitorum longus rat muscles using TMT labeling and mass spectrometry.
Chaves, Daniela F S; Carvalho, Paulo C; Lima, Diogo B; Nicastro, Humberto; Lorenzeti, Fábio M; Siqueira-Filho, Mário; Hirabara, Sandro M; Alves, Paulo H M; Moresco, James J; Yates, John R; Lancha, Antonio H.
Affiliation
  • Chaves DF; Laboratory of Applied Nutrition and Metabolism, School of Physical Education and Sports, University of São Paulo , Av. Prof. Mello Moraes, 65, 05508-900 São Paulo, SP, Brazil.
J Proteome Res ; 12(10): 4532-46, 2013 Oct 04.
Article in En | MEDLINE | ID: mdl-24001182
ABSTRACT
Sarcopenia describes an age-related decline in skeletal muscle mass, strength, and function that ultimately impairs metabolism and leads to poor balance, frequent falling, limited mobility, and a reduction in quality of life. Here we investigate the pathogenesis of sarcopenia through a proteomic shotgun approach. In brief, we employed tandem mass tags to quantitate and compare the protein profiles obtained from young versus old rat slow-twitch type of muscle (soleus) and a fast-twitch type of muscle (extensor digitorum longus, EDL). Our results disclose 3452 and 1848 proteins identified from soleus and EDL muscles samples, of which 78 and 174 were found to be differentially expressed, respectively. In general, most of the proteins were structural related and involved in energy metabolism, oxidative stress, detoxification, or transport. Aging affected soleus and EDL muscles differently, and several proteins were regulated in opposite ways. For example, pyruvate kinase had its expression and activity different in both soleus and EDL muscles. We were able to verify with existing literature many of our differentially expressed proteins as candidate aging biomarkers and, most importantly, disclose several new candidate biomarkers such as the glioblastoma amplified sequence, zero ß-globin, and prolargin.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Aging / Muscle, Skeletal / Proteome / Muscle Proteins Limits: Animals Language: En Journal: J Proteome Res Journal subject: BIOQUIMICA Year: 2013 Type: Article Affiliation country: Brazil

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Aging / Muscle, Skeletal / Proteome / Muscle Proteins Limits: Animals Language: En Journal: J Proteome Res Journal subject: BIOQUIMICA Year: 2013 Type: Article Affiliation country: Brazil