Identificação de isoformas miosínicas estruturais de músculo gastrocnêmio de ratos treinados e sedentários em gel bidimensional

Abstract

Molecular biology and human physiology providing tools by which physical activity can be assessed in terms of action and interaction in the body, inducing structural and functional changes. Thus, muscle proteins can be used as potential molecular markers. This study characterized the expression of myosin isoforms, by a two-dimensional electrophoretic map, in skeletal muscle of rats, as a result of induced exercise in treadmill. Wistar male rats were divided randomly into two groups: sedentary and exercise, held in ideal conditions. The exercise group was subjected to sessions of training on alternate days, 30 minutes per day for 12 weeks, using speed of 7 m / min to 20 m / min. The electrophoretic twodimensional standard on acid pI range, presented various protein groups such as myosin, tropomyosin, troponin and actin, identified in silico. Within these groups, there was the presence of some light isoforms of myosin and a slow isoform of troponin T. The proteomic gels become important in analysis of the skeletal muscle composition. The protein isoforms, especially myosin, may be useful in characterizing the exercise training in terms of expression of proteins and could help in evaluation of the exercise.