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Articles in PresS, published online ahead of print October 2, 2001
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00366.2001
Submitted on August 16, 2001
Accepted on September 11, 2001
1 Cellular & Molecular Physiology, Penn State College of Medicine, Hershey, PA, USA
2 Molecular & Cellular Neuroscience, Rockefeller Univeristy, New York, NY, USA
* To whom correspondence should be addressed. E-mail: clang{at}psu.edu.
The present study examined potential mechanisms contributing to the inhibition of protein synthesis in fast-twitch skeletal muscle (gastrocnemius) and heart after administration of tumor necrosis factor (TNF) . Male rats had vascular catheters implanted and TNF continuously infused for the next 24 h. TNF decreased in vivo determined rates of global protein synthesis in gastrocnemius (39%), soleus (23%) and heart (25%), but not diaphragm. The TNF-induced decrease in protein synthesis in gastrocnemius involved a reduction in the synthesis of both myofibrillar and sacroplasmic proteins. Protein synthesis was also decreased in small intestine, unchanged in kidney, lung and brain, and increased in liver and spleen in response to TNF. TNF did not alter total RNA content in any tissue examined suggesting that the changes in protein synthesis were caused by changes in translational efficiency not ribosomal number. To identify potential mechanisms responsible for regulating mRNA translation we examined several eukaryotic initiation factors (eIFs) and elongation factors (eEFs). TNF decreased the activity of eIF2B in muscle (39%), but not in heart. This diminished activity could not be explained by a reduction in the content of eIF2B or the content and phosphorylation state of eIF2. Although TNF did not alter the content of eIF4E in either gastrocnemius or heart, it did alter the distribution of eIF4E in both tissues. Compared with control animals, skeletal muscle and heart from TNF-treated rats demonstrated 1) an increased binding of the translation repressor 4E-binding protein-1 (4E-BP1) with eIF4E, 2) a decreased amount of eIF4E associated with eIF4G, and 3) a decreased content of the hyperphosphorylated -form of 4E-BP1. In contrast, the infusion of TNF did not alter the content of eEF-1 or eEF-2, or the phosphorylation state of eEF-2. In summary, these data suggest that TNF 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 eIF4E availability.
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