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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

Författare

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.

Avdelning/ar

Publiceringsår

1994

Språk

Engelska

Sidor

314-318

Publikation/Tidskrift/Serie

FEBS Letters

Volym

350

Issue

2-3

Dokumenttyp

Artikel i tidskrift

Förlag

Wiley-Blackwell

Ämne

  • Biological Sciences

Nyckelord

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

Status

Published

Forskningsgrupp

  • Diabetes - Clinical Obesity
  • Insulin Signal Transduction

ISBN/ISSN/Övrigt

  • ISSN: 1873-3468