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Submitted on December 24, 2002
Accepted on May 28, 2003
1 Departments of Cellular & Molecular Physiology, and Surgery, Pennsylvania State College of Medicine, Hershey, PA 17033
* To whom correspondence should be addressed. E-mail: clang{at}psu.edu.
This study examined whether the acute elevation of insulin-like growth factor binding protein (IGFBP)-1 decreases the plasma free IGF-I concentration and alters in vivo rates of muscle protein synthesis and glucose uptake. The plasma concentration of human IGFBP-1 was increased to 
95 ng/ml in conscious catheterized rats infused intravenously with human IGFBP-1 for 4 h. Infusion of IGFBP-1 also increased the concentration of endogenous (e.g. rat) IGFBP-1 in the blood and this response was associated with a 2- to 3-fold elevation in IGFBP-1 mRNA in liver and kidney. IGFBP-1 did not significantly alter the plasma concentration of total IGF-I but decreased circulating free IGF-I levels by 50%. IGFBP-1 decreased protein synthesis in the predominantly fast-twitch gastrocnemius muscle (20%) and this change resulted from a decreased translational efficiency that was associated with a decreased phosphorylation of S6K1, but not 4E-BP1. Complementary studies demonstrated IGFBP-1 also decreased the rates of protein synthesis under basal conditions and in response to stimulation by IGF-I when added in vitro to the fast-twitch epitrochlearis muscle. In contrast, IGFBP-1 did not alter in vivo-determined rates of protein synthesis in the slow-twitch soleus muscle, heart, liver or kidney. The infusion of IGFBP-1 did not significantly alter the plasma glucose or lactate concentration or whole body rates of glucose production or disposal. The abovementioned changes were not mediated indirectly by changes in the plasma insulin or corticosterone concentrations, decreased high-energy phosphate content in muscle, or hepatoxicity produced by the infused IGFBP-1. These results demonstrate that acute in vivo elevation in IGFBP-1, of the magnitude observed in various catabolic conditions, is capable of selectively decreasing protein synthesis in fast-twitch skeletal muscle and up-regulating the hepatic and renal synthesis of IGFBP-1 per se. Hence, elevations in circulating and tissue levels of IGFBP-1 may be an important mediator for the muscle catabolism observed in various stress conditions.
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