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(The FASEB Journal. 1998;12:871-880.)
© 1998 FASEB

RESEARCH COMMUNICATION

Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-{kappa}B activation in response to tumor necrosis factor {alpha}

Yi-ping Lia, Robert J. Schwartzb, Ian D. Waddellc, Brian R. Hollowayc, and Michael B. Reida,1

a Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
b Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030, USA
c Zeneca Pharmaceuticals, Alderley Park, Cheshire, England, SK10 4TG

Skeletal muscle atrophy and weakness are thought to be stimulated by tumor necrosis factor {alpha} (TNF-{alpha}) in a variety of chronic diseases. However, little is known about the direct effects of TNF-{alpha} on differentiated skeletal muscle cells or the signaling mechanisms involved. We have tested the effects of TNF-{alpha} on the mouse-derived C2C12 muscle cell line and on primary cultures from rat skeletal muscle. TNF-{alpha} treatment of differentiated myotubes stimulated time- and concentration-dependent reductions in total protein content and loss of adult myosin heavy chain (MHCf) content; these changes were evident at low TNF-{alpha} concentrations (1–3 ng/ml) that did not alter muscle DNA content and were not associated with a decrease in MHCf synthesis. TNF-{alpha} activated binding of nuclear factor {kappa}B (NF-{kappa}B) to its targeted DNA sequence and stimulated degradation of I-{kappa}B{alpha}, an NF-{kappa}B inhibitory protein. TNF-{alpha} stimulated total ubiquitin conjugation whereas a 26S proteasome inhibitor (MG132 10–40 µM) blocked TNF-{alpha} activation of NF-{kappa}B. Catalase 1 kU/ml inhibited NF-{kappa}B activation by TNF-{alpha}; exogenous hydrogen peroxide 200 µM activated NF-{kappa}B and stimulated I-{kappa}B{alpha} degradation. These data demonstrate that TNF-{alpha} directly induces skeletal muscle protein loss, that NF-{kappa}B is rapidly activated by TNF-{alpha} in differentiated skeletal muscle cells, and that TNF-{alpha}/NF-{kappa}B signaling in skeletal muscle is regulated by endogenous reactive oxygen species.—Li, Y.-P., Schwartz, R. J., Waddell, I. D., Holloway, B. R., Reid, M. B. Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-{kappa}B activation in response to tumor necrosis factor {alpha}. FASEB J. 12, 871–880 (1998)


Key Words: cachexia • myosin • cytokines • inflammatory disease • tumor necrosis factor • ubiquitin • free radicals




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