Aspirin inhibits serine phosphorylation of insulin receptor substrate 1 in growth hormone treated animals

FEBS Lett. 2005 Jun 6;579(14):3152-8. doi: 10.1016/j.febslet.2005.04.075.

Abstract

In this study, we demonstrate that pretreatment with aspirin inhibits GH-induced insulin resistance. GH was observed to lead to serine phosphorylation of IRS-1, a phenomenon which was reversed by aspirin in liver, muscle and WAT in parallel with a reduction in JNK activity. In addition, our data show an impairment of insulin activation in the IR/IRS/PI(3)kinase pathway and a reduction in IRS-1 protein levels in rats treated with GH, which was also reversed in the animals pretreated with aspirin. Overall, these results provide new insights into the mechanism of GH-induced insulin resistance.

Publication types

  • Research Support, Non-U.S. Gov't
  • Retracted Publication

MeSH terms

  • Adipose Tissue / drug effects
  • Adipose Tissue / metabolism
  • Animals
  • Aspirin / pharmacology*
  • Growth Hormone / pharmacology*
  • Insulin / pharmacology
  • Insulin Receptor Substrate Proteins
  • JNK Mitogen-Activated Protein Kinases / metabolism
  • Liver / drug effects
  • Liver / metabolism
  • Male
  • Muscles / drug effects
  • Muscles / metabolism
  • Phosphoproteins / metabolism*
  • Phosphorylation / drug effects
  • Phosphoserine / metabolism*
  • Proto-Oncogene Proteins c-jun / metabolism
  • Rats
  • Rats, Wistar
  • Receptor, Insulin / metabolism

Substances

  • Insulin
  • Insulin Receptor Substrate Proteins
  • Irs1 protein, rat
  • Phosphoproteins
  • Proto-Oncogene Proteins c-jun
  • Phosphoserine
  • Growth Hormone
  • Receptor, Insulin
  • JNK Mitogen-Activated Protein Kinases
  • Aspirin