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Retracted: Aspirin inhibits serine phosphorylation of insulin receptor substrate 1 in growth hormone treated animals
Author(s) -
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.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.04.075
Subject(s) - insulin resistance , aspirin , serine , medicine , endocrinology , phosphorylation , insulin receptor , insulin receptor substrate , insulin , irs1 , chemistry , kinase , growth hormone , hormone , biochemistry
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.