Journal of Applied Physiology AJP: Endocrinology and Metabolism
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J Appl Physiol 91: 2079-2087, 2001;
8750-7587/01 $5.00
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Vol. 91, Issue 5, 2079-2087, November 2001

Time course of the MAPK and PI3-kinase response within 24 h of skeletal muscle overload

Christian J. Carlson1,2, Zhiqiang Fan2, Scott E. Gordon2, and Frank W. Booth2

1 University of Texas Health Science Center at Houston, Graduate School of Biomedical Sciences, Houston, Texas 77030; and 2 University of Missouri College of Veterinary Medicine Department of Veterinary Biomedical Sciences, Department of Physiology and Dalton Cardiovascular Institute, Columbia, Missouri 65211

Knowledge of the molecular mechanisms by which skeletal muscle hypertrophies in response to increased mechanical loading may lead to the discovery of novel treatment strategies for muscle wasting and frailty. To gain insight into potential early signaling mechanisms associated with skeletal muscle hypertrophy, the temporal pattern of mitogen-activated protein kinase (MAPK) phosphorylation and phosphatidylinositol 3-kinase (PI3-kinase) activity during the first 24 h of muscle overload was determined in the rat slow-twitch soleus and fast-twitch plantaris muscles after ablation of the gastrocnemius muscle. p38alpha MAPK phosphorylation was elevated for the entire 24-h overload period in both muscles. In contrast, Erk 2 and p54 JNK phosphorylation were transiently increased by overload, returning to the levels of sham-operated controls by 24 h. PI3-kinase activity was increased by muscle overload only at 12 h of overload and only in the plantaris muscle. In summary, sustained elevation of p38alpha MAPK phosphorylation occurred early in response to muscle overload, identifying this pathway as a potential candidate for mediating early hypertrophic signals in response to skeletal muscle overload.

hypertrophy; growth; signaling; mitogen-activated protein kinase; phosphatidylinositol 3-kinase


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