Essential role of phosphatidylinositol 3-kinase in insulin-induced activation and phosphorylation of the cGMP-inhibited cAMP phosphodiesterase in rat adipocytes. Studies using the selective inhibitor wortmannin

Summary, in English

Incubation of rat adipocytes with wortmannin, a potent and selective phosphatidylinositol 3-kinase (PI 3-kinase) inhibitor, completely blocked the antilipolytic action of insulin (IC50 = 100 nM), the insulin-induced activation and phosphorylation of cGMP-inhibited cAMP phosphodiesterase (cGI-PDE) as well as the activation of the insulin-stimulated cGI-PDE kinase (IC50 = 10-30 nM). No direct effects of the inhibitor on the insulin-stimulated cGI-PDE kinase, the cGI-PDE and the hormone-sensitive lipase were observed. These data suggest that activation of PI 3-kinase upstream of the insulin-stimulated cGI-PDE kinase in the antilipolytic insulin signalchain has an essential role for insulin-induced cGI-PDE activation/phosphorylation and anti-lipolysis.

• Author: Tova Rahn; Martin Ridderstråle; Hans Törnqvist; Vincent Manganiello; Gudrun Fredrikson; Per Belfrage; Eva Degerman
• Department/s: Diabetes - Clinical Obesity; Insulin Signal Transduction
• Publishing year: 1994
• Language: English
• Pages: 314-318
• Publication/Series: FEBS Letters
• Volume: 350
• Issue: 2-3
• Links: http://dx.doi.org/10.1016/0014-5793(94)00797-7
• Document type: Journal article
• Publisher: Wiley-Blackwell
• Topic: Biological Sciences
• Keywords: Insulin; Phosphatidylinositol 3-kinase; Inhibitor; Adipocyte; Lipolysis; cGMP-inhibited cAMP phosphodiesterase
• Status: Published
• Research group: Diabetes - Clinical Obesity; Insulin Signal Transduction
• ISBN/ISSN/Other: ISSN: 1873-3468