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impairs heart and skeletal muscle protein synthesis
by altering translation initiation
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)-
. Rats
had vascular catheters implanted, and TNF- was infused continuously for 24 h. TNF- decreased in vivo-determined rates of global
protein synthesis in gastrocnemius (39%) and heart (25%). The
TNF--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- 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-2B
or
the content and phosphorylation state of eIF-2. Skeletal muscle and heart from TNF--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 
-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
eIF-4E availability.
eukaryotic initiation factors-2B and -4E; 4E-binding protein-1; elongation factors-1 and -2; rats; tumor necrosis factor-
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