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Effect of exercise and training on phospholemman phosphorylation in human skeletal muscle

Benziane, Boubacar, Widegren, Ulrika, Pirkmajer, Sergej, Henriksson, Jan, Stepto, Nigel and Chibalin, Alexander V (2011) Effect of exercise and training on phospholemman phosphorylation in human skeletal muscle. The American Journal of Physiology - Endocrinology and Metabolism, 301 (3). E456-E466. ISSN 0193-1849 (online) 1522-1555 (print)

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Phospholemman (PLM, FXYD1) is a partner protein and regulator of the Na+-K+-ATPase (Na+-K+ pump). We explored the impact of acute and short-term training exercise on PLM physiology in human skeletal muscle. A group of moderately trained males (n = 8) performed a 1-h acute bout of exercise by utilizing a one-legged cycling protocol. Muscle biopsies were taken from vastus lateralis at 0 and 63 min (non-exercised leg) and 30 and 60 min (exercised leg). In a group of sedentary males (n = 9), we determined the effect of a 10-day intense aerobic cycle training on Na+-K+-ATPase subunit expression, PLM phosphorylation, and total PLM expression as well as PLM phosphorylation in response to acute exercise (1 h at ∼72% V̇o2peak). Biopsies were taken at rest, immediately following, and 3 h after an acute exercise bout before and at the conclusion of the 10-day training study. PLM phosphorylation was increased both at Ser63 and Ser68 immediately after acute exercise (75%, P < 0.05, and 30%, P < 0.05, respectively). Short-term training had no adaptive effect on PLM phosphorylation at Ser63 and Ser68, nor was the total amount of PLM altered posttraining. The protein expressions of α1-, α2-,and β1-subunits of Na+-K+-ATPase were increased after training (113%, P < 0.05, 49%, P < 0.05, and 27%, P < 0.05, respectively). Whereas an acute bout of exercise increased the phosphorylation of PKCα/βII on Thr638/641 pre- and posttraining, phosphorylation of PKCζ/λ on Thr403/410 was increased in response to acute exercise only after the 10-day training. In conclusion, we show that only acute exercise, and not short-term training, increases phosphorylation of PLM on Ser63 and Ser68, and data from one-legged cycling indicate that this effect of exercise on PLM phosphorylation is not due to systemic factors. Our results provide evidence that phosphorylation of PLM may play a role in the acute regulation of the Na+-K+-ATPase response to exercise.

Item Type: Article
Uncontrolled Keywords: ResPubID23445, cycle exercise, protein kinase C, Na+-K+-ATPase, protein interaction
Subjects: Historical > Faculty/School/Research Centre/Department > Institute of Sport, Exercise and Active Living (ISEAL)
Current > FOR Classification > 1106 Human Movement and Sports Science
Historical > SEO Classification > 970111 Expanding Knowledge in the Medical and Health Sciences
Depositing User: VUIR
Date Deposited: 09 Aug 2012 06:49
Last Modified: 28 Jul 2020 07:49
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Citations in Scopus: 26 - View on Scopus

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