PMID: 15350185Sep 8, 2004Paper

Increased in vivo phosphorylation of insulin receptor at serine 994 in the liver of obese insulin-resistant Zucker rats

The Journal of Endocrinology
Marcelo P CobaDaniel Turyn

Abstract

Serine phosphorylation of the insulin receptor (IR) has been proposed to exert an inhibitory influence on its tyrosine kinase activity. Previous works using site-directed mutagenesis suggested that serine 994 of the IR (IR Ser 994) might be part of an inhibitory domain of the receptor. In this study we examined whether this residue is subjected to phosphorylation in vivo. We used a site-phosphospecific antibody to determine the extent of phosphorylation of IR Ser 994 in insulin target tissues from two animal models of insulin resistance with different IR kinase (IRK) activity: obese (fa/fa) Zucker rats and transgenic mice overexpressing bovine growth hormone (PEPCK-bGH mice). Phosphorylation at IR Ser 994 was markedly increased in liver of obese rats. This alteration appeared to be tissue-selective since no phosphorylation on Ser 994 was detected in IRs isolated from skeletal muscle of these animals. On the other hand, the phosphorylation level of IR Ser 994 was very low in liver of PEPCK-bGH mice and did not differ from that of the control group. We have also demonstrated that protein kinase (PK) C isoforms alpha, betaI and zeta are able to promote the in vitro phosphorylation of the IR on Ser 994. Differential findings in the...Continue Reading

Citations

Jan 24, 2014·Clinical Science·Fernando P DominiciJorge F Giani
Nov 28, 2016·Journal of Neurochemistry·Matthias Gralle
Apr 5, 2014·American Journal of Physiology. Gastrointestinal and Liver Physiology·Shaoning JiangJoseph L Messina
Sep 6, 2014·Biologie aujourd'hui·Anaïs GondoinAnne-Françoise Burnol
Aug 2, 2018·Physiological Reviews·Max C Petersen, Gerald I Shulman
Dec 19, 2017·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Der Jiun OoiMaznah Ismail

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