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Norepinephrine-Induced Phosphorylation of a 25 kd Phosphoprotein in Rat Aorta Is Altered in Intraperitoneal Sepsis.

机译:去甲肾上腺素诱导大鼠主动脉中25kd磷酸化的磷酸化在腹膜内脓毒症中改变。

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An attenuation of the contractile response to norepinephrine (NE) has been previously demonstrated in rat aorta during intraperitoneal sepsis and endotoxemia. In this study, we determined whether NE-induced protein phosphorylation is altered in septic rat aorta as compared to control rat aorta. We found that the NE-induced phosphorylation of a 25 kd phosphoprotein was decreased. NE increased phosphorylation of the 25 kd band by 54% in the control aorta by only 12% in the septic aorta. Pyrophosphate gel purification of phosphorylated myosin showed that this 25 kd band was not related to the myosin-phosphorylated (P) light chain. These results further document that intrinsic alterations occur in the NE-mediated signal transduction system in rat aorta during sepsis and that such alterations could contribute to depressed aortic contractility. Keywords: Protein phosphorylation; Protein kinase; Phosphoinositide metabolism; Receptor. Reprints. (kt)

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