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Inhibits Serum and Insulin-Like Growth Factor-I Stimulated Protein Synthesis1
Departments of Medicine (R.A.F, M.C.G) and Surgery (C.H.L.), State University of New York at Stony Brook, Stony Brook, New York 11794
Address all correspondence and requests for reprints to: Marie C. Gelato, Division of Endocrinology, Health Science Center T-15, Room 060, State University of New York at Stony Brook, Stony Brook, New York 11794-8154. E-mail: mgelato{at}epo.som.sunysb.edu
Tumor necrosis factor-
(TNF-) induces cachexia and is postulated
to be responsible for muscle wasting in several pathophysiological
conditions. The purpose of the present study was to investigate whether
exposure of human myoblasts to TNF- could directly inhibit the
ability of serum or insulin-like growth factor I (IGF-I) to stimulate
protein synthesis as assessed by the incorporation of
[3H]phenylalanine into protein. Serum and IGF-I
stimulated protein synthesis dose dependently. Half-maximal stimulation
of protein synthesis occurred at 05% serum and 8 ng/ml of IGF-I,
respectively. TNF- inhibited IGF-I-stimulated protein synthesis in a
dose-dependent manner. Additionally, as little as 2 ng/ml of TNF-
impaired the ability of IGF-I to stimulate protein synthesis by 33%
and, at a dose of 100 ng/ml, TNF- completely prevented the increase
in protein synthesis induced by either serum or a maximally stimulating
dose of IGF-I. Inhibition of protein synthesis was independent of
whether TNF- and growth factors were added to cells simultaneously
or if the cells were pretreated with growth factors. Exposure of
myoblasts to TNF- for 10 min completely inhibited serum-induced
stimulation of protein synthesis. TNF- inhibited protein synthesis
up to 48 h after addition of the cytokine. TNF- also inhibited
serum-stimulated protein synthesis in human myoblasts that were
differentiated into myotubes. In contrast, exposure of myoblasts to
TNF- had no effect on IGF-I binding and failed to alter the ability
of either IGF-I or serum to stimulate [3H]thymidine
uptake. These data indicate that transient exposure of myoblasts or
myotubes to TNF- inhibits protein synthesis. Thus, the anabolic
actions of IGF-I on muscle protein synthesis may be impaired during
catabolic conditions in which TNF- is over expressed.
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