Am J Physiol Cell Physiol AJP: Regulatory, Integrative and Comparative Physiology
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Am J Physiol Cell Physiol (May 11, 2005). doi:10.1152/ajpcell.00632.2004
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Submitted on December 22, 2004
Accepted on May 7, 2005

Regulation of I{kappa}B kinase and NF-{kappa}B in contracting adult rat skeletal muscle

Richard C Ho1, Michael F Hirshman1, Yangfeng Li1, Dongsheng Cai1, Jocelyn R Farmer1, William G Aschenbach1, Carol A Witczak1, Steven E Shoelson1, and Laurie J Goodyear1*

1 Research Division, Joslin Diabetes Center, Boston, MA, USA; Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA

* To whom correspondence should be addressed. E-mail: laurie.goodyear{at}joslin.harvard.edu.

Nuclear factor-{kappa}B (NF-{kappa}B) is a transcription factor with important roles in regulating innate immune and inflammatory responses. NF-{kappa}B is activated through the phosphorylation of its inhibitor, I{kappa}B, by the I{kappa}B kinase (IKK) complex. Physical exercise elicits changes in skeletal muscle gene expression, yet signaling cascades and transcription factors involved remain largely unknown. To determine whether NF-{kappa}B signaling is regulated by exercise in vivo, rats were run on a motorized treadmill for 5-60 min. Exercise resulted in up to 2-fold increases in IKK{alpha}/{beta} phosphorylation in the soleus and red gastrocnemius muscles throughout the time course studied. In red gastrocnemius muscles, NF-{kappa}B activity increased 50% 1-3 h following 60 min of treadmill exercise, and returned to basal by 5 h. Contraction of isolated extensor digitorum longus (EDL) muscles in vitro increased IKK{alpha}/{beta} phosphorylation 10-fold and this was accompanied by a parallel increase in I{kappa}B{alpha} phosphorylation. Additional kinases that are activated by exercise include p38, extracellular-signal regulated protein kinase (ERK), and AMP-activated protein kinase (AMPK). Inhibitors of p38 (SB203580) and ERK (U0126) impaired contraction-mediated IKK phosphorylation by 39 ± 4% (p=0.06) and 35 ± 10% (p=0.09), respectively, and in combination by 76 ± 5% (p<0.05), suggesting that these kinases might influence the activation of IKK and NF-{kappa}B during exercise. In contrast, AICAR, an activator of AMPK, had no effect on either IKK or NF-{kappa}B activity. In conclusion, acute submaximal exercise transiently stimulates NF-{kappa}B signaling in skeletal muscle. This activation is intrinsic to the muscle, since it can occur in the absence of exercise-derived systemic factors.




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