Abstract
Aging is characterized by several bimolecular changes that result in structural as well as physiological deleterious effects to the tendinous tissue. In this context, strength training (ST) is of great clinical importance for elderly people since it is able to minimize, slow down or even stop molecular, structural and mechanical changes. Objective: To investigate the proteomic profile in order to identify and characterize the general distribution of proteins of the Achilles tendon (AT) in young and senile rats either sedentary or submitted to strength training protocols (ST). Materials and methods: 24 Wistar novergicus albino rats were used, aged 4 and 24 months, divided into four experimental groups: young rats (6), young trained rats (6), senile rats (6) and senile trained rats (6). A 12-week strength training was conducted once every two days. Afterwards, the CT were removed and subjected to LC-MS/MS proteomics analysis. Results: a total of 29 proteins were identified in the four groups analyzed. Seven of those proteins (COMP, COL1A1, COL1A2, CAIII, FAPB3, GSN, S100A6 and Tf) showed decreased intensity levels as a result of aging; eight of them (COMP, COL1A1, DNAAF1,
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