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

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 sho...

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Bibliographic Details
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:
Aspirin
c-jun N terminal kinase
growth hormone
Insulin
insulin receptor
insulin receptor substrate
IRS
JNK
phosphatidylinositol 3-kinase
PI 3-kinase
Tyrosine phosphorylation
WAT
white adipose tissue
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2005.04.075