Journal of Applied Physiology
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J Appl Physiol 90: 29-34, 2001;
8750-7587/01 $5.00
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Vol. 90, Issue 1, 29-34, January 2001

Exercise-associated differences in an array of proteins involved in signal transduction and glucose transport

Mei Yu1,2, Eva Blomstrand2,3, Alexander V. Chibalin1,2, Harriet Wallberg-Henriksson1,2, Juleen R. Zierath1,2, and Anna Krook1,2

1 Department of Clinical Physiology, Karolinska Hospital, SE-171 76 Stockholm; 2 Department of Physiology and Pharmacology, Karolinska Institute, SE-171 77 Stockholm; and 3 Department of Sport and Health Sciences, Stockholm University College of Physical Education and Sports, SE-114 86 Stockholm, Sweden

Vastus lateralis muscle biopsies were obtained from endurance-trained (running ~50 km/wk) and untrained (no regular physical exercise) men, and the expression of an array of insulin-signaling intermediates was determined. Expression of insulin receptor and insulin receptor substrate-1 and -2 was decreased 44% (P < 0.05), 57% (P < 0.001), and 77% (P < 0.001), respectively, in trained vs. untrained muscle. The downstream signaling target, Akt kinase, was not altered in trained subjects. Components of the mitogenic signaling cascade were also assessed. Extracellular signal-regulated kinase 1/2 mitogen-activated protein kinase expression was 190% greater (P < 0.05), whereas p38 mitogen-activated protein kinase expression was 32% lower (P < 0.05), in trained vs. untrained muscle. GLUT-4 protein expression was twofold higher (P < 0.05), and the GLUT-4 vesicle-associated protein, the insulin-regulated aminopeptidase, was increased 4.7-fold (P < 0.05) in trained muscle. In conclusion, the expression of proteins involved in signal transduction is altered in skeletal muscle from well-trained athletes. Downregulation of early components of the insulin-signaling cascade may occur in response to increased insulin sensitivity associated with endurance training.

insulin receptor; insulin receptor substrate; GLUT-4; mitogen-activated protein kinase; citrate synthase


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