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Exercise-Induced Phosphorylation of the Novel Akt Substrates AS160 and Filamin A in Human Skeletal Muscle

¹ Department of Molecular Medicine and Surgery, Karolinska Institutet, Stockholm, Sweden
² School of Medical Sciences, RMIT University, Victoria, Australia

Address correspondence and reprint requests to Prof. Juleen R. Zierath, Karolinska Institutet, Department of Molecular MedicineSurgery, Section of Integrative Physiology, von Eulers väg 4, 4th Floor, S-171 77 Stockholm, Sweden. E-mail: juleen.zierath{at}ki.se

Abbreviations: AMPK, AMP-activated protein kinase; GAP, GTPase-activating protein; PAS, phospho-Akt substrate antibody; PKC, protein kinase C; PPO, peak power output

Skeletal muscle contraction stimulates multiple signaling cascades that govern a variety of metabolic and transcriptional events. Akt/protein kinase B regulates metabolism and growth/muscle hypertrophy, but contraction effects on this target and its substrates are varied and may depend on the mode of the contractile stimulus. Accordingly, we determined the effects of endurance or resistance exercise on phosphorylation of Akt and downstream substrates in six trained cyclists who performed a single bout of endurance or resistance exercise separated by 7 days. Muscle biopsies were taken from the vastus lateralis at rest and immediately after exercise. Akt Ser⁴⁷³ phosphorylation was increased (1.8-fold; P = 0.011) after endurance but was unchanged after resistance exercise. Conversely, Akt Thr³⁰⁸ phosphorylation was unaltered after either bout of exercise. Several exercise-responsive phosphoproteins were detected by immunoblot analysis with a phospho-Akt substrate antibody. pp160 and pp300 were identified as AS160 and filamin A, respectively, with increased phosphorylation (2.0- and 4.9-fold, respectively; P < 0.05) after endurance but not resistance exercise. In conclusion, AS160 and filamin A may provide an important link to mediate endurance exercise–induced bioeffects in skeletal muscle.

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