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1 Instituto de Química y Fisicoquímica Biológicas, University of Buenos Aires-Consejo Nacional de Investigaciones Científicas of Argentina, Facultad de Farmacia y Bioquímica, 1113 Buenos Aires, Argentina; and 2 Department of Physiology, School of Medicine, Southern Illinois University, Carbondale, Illinois 62901-6512
Growth hormone (GH) excess is associated with insulin resistance, but the molecular mechanisms of this association are poorly understood. In the current work, we have examined the consequences of exposure to high GH levels on the early steps of the insulin-signaling system in the muscle of bovine (b) GH-transgenic mice. The protein content and the tyrosine phosphorylation state of the insulin receptor (IR), the IR substrate-1 (IRS-1), the association between IRS-1 and the p85 subunit of phosphatidylinositol (PI) 3-kinase, and the phosphotyrosine-derived PI 3-kinase activity in this tissue were studied. We found that in skeletal muscle of bGH-transgenic mice, exposure to high circulating GH levels results in 1) reduced IR abundance, 2) reduced IR tyrosine phosphorylation, 3) reduced efficiency of IRS-1 tyrosine phosphorylation, and 4) defective activation of PI 3-kinase by insulin. These alterations may be related to the insulin resistance exhibited by these animals.
insulin receptor; insulin receptor substrate-1; phosphatidylinositol 3-kinase; growth hormone; insulin resistance
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