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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

  • Tova Rahn
  • Martin Ridderstråle
  • Hans Törnqvist
  • Vincent Manganiello
  • Gudrun Fredrikson
  • Per Belfrage
  • Eva Degerman
Publishing year: 1994
Language: English
Pages: 314-318
Publication/Series: FEBS Letters
Volume: 350
Issue: 2-3
Document type: Journal article
Publisher: Wiley-Blackwell

Abstract 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.


  • Biological Sciences
  • Insulin
  • Phosphatidylinositol 3-kinase
  • Inhibitor
  • Adipocyte
  • Lipolysis
  • cGMP-inhibited cAMP phosphodiesterase


  • Clinical Obesity
  • Insulin Signal Transduction
  • ISSN: 1873-3468
Eva Degerman
E-mail: eva [dot] degerman [at] med [dot] lu [dot] se


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