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Am J Physiol Endocrinol Metab 282: E336-E347, 2002. First published October 2, 2001; doi:10.1152/ajpendo.00366.2001
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Vol. 282, Issue 2, E336-E347, February 2002

TNF-alpha impairs heart and skeletal muscle protein synthesis by altering translation initiation

Charles H. Lang1, Robert A. Frost1, Angus C. Nairn2, David A. MacLean1, and Thomas C. Vary1

1 Departments of Cellular and Molecular Physiology and Surgery, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033; and 2 Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, New York 10021

This study examined potential mechanisms contributing to the inhibition of protein synthesis in skeletal muscle and heart after administration of tumor necrosis factor (TNF)-alpha . Rats had vascular catheters implanted, and TNF-alpha was infused continuously for 24 h. TNF-alpha decreased in vivo-determined rates of global protein synthesis in gastrocnemius (39%) and heart (25%). The TNF-alpha -induced decrease in protein synthesis in the gastrocnemius involved a reduction in the synthesis of both myofibrillar and sarcoplasmic proteins. To identify potential mechanisms responsible for regulating mRNA translation, we examined several eukaryotic initiation factors (eIFs) and elongation factors (eEFs). TNF-alpha decreased the activity of eIF-2B in muscle (39%) but not in heart. This diminished activity was not caused by a reduction in the content of eIF-2Bepsilon or the content and phosphorylation state of eIF-2alpha . Skeletal muscle and heart from TNF-alpha -treated rats demonstrated 1) an increased binding of the translation repressor 4E-binding protein-1 (4E-BP1) with eIF-4E, 2) a decreased amount of eIF-4E associated with eIF-4G, and 3) a decreased content of the hyperphosphorylated gamma -form of 4E-BP1. In contrast, the infusion of TNF-alpha did not alter the content of eEF-1alpha or eEF-2, or the phosphorylation state of eEF-2. In summary, these data suggest that TNF-alpha impairs skeletal muscle and heart protein synthesis, at least in part, by decreasing mRNA translational efficiency resulting from an impairment in translation initiation associated with alterations in eIF-4E availability.

eukaryotic initiation factors-2B and -4E; 4E-binding protein-1; elongation factors-1 and -2; rats; tumor necrosis factor-alpha


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