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

• Published in: FEBS letters 2005-06, Vol.579 (14), p.3152-3158
• Main Authors: Prattali, Raphael R., Barreiro, Guilherme C., Caliseo, Caio T., Fugiwara, Felipe Y., Ueno, Mirian, Prada, Patrícia O., Velloso, Licio A., Saad, Mario J.A., Carvalheira, José B.C.
• Format: Article
• Language: English
• Subjects: Adipose Tissue - drug effects; Adipose Tissue - metabolism; Animals; Aspirin; Aspirin - pharmacology; Growth hormone; Growth Hormone - pharmacology; Insulin; 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; Tyrosine phosphorylation
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2005.04.075

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.