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Department of Cellular and Molecular Physiology and Department of Surgery, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033
We examined the
effects of TNF-binding protein (TNFBP) on regulatory mechanisms of
muscle protein synthesis during sepsis in four groups of rats: Control;
Control+TNFBP; Septic; and Septic+TNFBP. Saline (1.0 ml) or TNFBP (1 mg/kg, 1.0 ml) was injected daily starting 4 h before the induction of
sepsis. The effect of TNFBP on gastrocnemius weight, protein content,
and the rate of protein synthesis was examined 5 days later. Sepsis
reduced the rate of protein synthesis by 35% relative to controls by
depressing translational efficiency. Decreases in protein synthesis
were accompanied by similar reductions in protein content and muscle
weight. Treatment of septic animals with TNFBP for 5 days prevented the
sepsis-induced inhibition of protein synthesis and restored
translational efficiency to control values. TNFBP treatment of Control
rats for 5 days was without effect on muscle protein content or protein
synthesis. We also assessed potential mechanisms regulating
translational efficiency. The phosphorylation state of
p70S6 kinase was not altered by
sepsis. Sepsis reduced the gastrocnemius content of eukaryotic
initiation factor 2B
(eIF2B), but not eIF2
. The decrease in
eIF2B content was prevented by treatment of septic rats with TNFBP.
TNFBP ameliorates the sepsis-induced changes in protein metabolism in
gastrocnemius, indicating a role for TNF in the septic process. The
data suggest that TNF may impair muscle protein synthesis by reducing
expression of specific initiation factors during sepsis.
tumor necrosis factor; gastrocnemius; eukaryotic initiation factors; p70S6 kinase
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