RESUMO
The mechanisms of exercise-induced fatigue have not been investigated using proteomic techniques, an approach that could improve our understanding and generate novel information regarding the effects of exercise. In this study, the proteom alterations of rat skeletal muscle were investigated during exercise-induced fatigue. The proteins were extracted from the skeletal muscle of SD rat thigh, and then analyzed by two-dimensional electrophoresis and PDQuest software. Compared to control samples, 10 significantly altered proteins were found in exercise samples, two of them were upregulated and eight of them were downregulated. These proteins were identified by MALDI TOF-MS. The two upregulated proteins were identified as MLC1 and myosin L2 (DTNB) regulatory light-chain precursors. The eight decreased proteins are Glyceraldehyde-3-phosphate Dehydrogenas (GAPDH); Beta enolase; Creatine kinase M chain (M-CK); ATP-AMP Transphosphorylase (AK1); myosin heavy chain (MHC); actin; Troponin I, fast-skeletal muscle (Troponin I fast-twitch isoform), fsTnI; Troponin T, fast-skeletal muscle isoforms (TnTF). In these proteins, four of the eight decreased proteins are related directly or indirectly to exercise induced fatigue. The other proteins represent diverse sets of proteins including enzymyes related to energy metabolism, skeletal muscle fabric protein and protein with unknown functions. They did not exhibit evident relationship with exercise-induced fatigue. Whereas the two identified increased proteins exhibit evident relationship with fatigue. These findings will help in understanding the mechanisms involved in exercise-induced fatigue.
Assuntos
Animais , Masculino , Ratos , Fadiga Muscular/fisiologia , Proteínas Musculares/metabolismo , Músculo Esquelético/metabolismo , Esforço Físico/fisiologia , Peso Corporal/fisiologia , Eletroforese em Gel Bidimensional , Metabolismo Energético/fisiologia , Espectrometria de Massas , Modelos Animais , Proteínas Musculares/química , Proteômica , Distribuição Aleatória , Ratos Sprague-Dawley , Natação/fisiologia , Troponina I/química , Troponina I/metabolismo , Troponina T/química , Troponina T/metabolismoRESUMO
Alzheimer’s disease (AD) is a common and devastating disease and there is no readily available biomarker to aid diagnosis or monitor progression of it. To further understand the pathogenic mechanism of AD, proteomic approach was used to study the cerebral synaptosomes proteins of rats injected with A1-40. Compared with the untreated samples, 14 proteins were found apparently altered through 2-dimensional gel electrophoresis. 12 of them were down-regulated and 2 were up-regulated. Three proteins including alpha-2-globin chain, peptidyl-prolycis-trans isomerase A (PPIaseA) and cofilin-1 protein were identified by matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS) and SWISS-PROT database query. Alpha-2-globin chain has not been shown to be associated with AD. PPIaseA and cofilin-1 protein are correlated with cell apoptosis and signaling. The altered proteins identified may help to understand the pathogenesis of AD.