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Search: WFRF:(Rahn T) > (2000-2004)

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  • Rondinone, C M, et al. (author)
  • Phosphorylation of PDE3B by phosphatidylinositol 3-kinase associated with the insulin receptor
  • 2000
  • In: Journal of Biological Chemistry. - 1083-351X. ; 275:14, s. 10093-10098
  • Journal article (peer-reviewed)abstract
    • Phosphatidylinositol 3-kinase mediates several actions of insulin including its antilipolytic effect. This effect is elicited by the insulin-stimulated serine phosphorylation and activation of cGMP-inhibited phosphodiesterase (PDE3B). In human adipocytes, we found that insulin differentially stimulated phosphatidylinositol 3-kinase activity; the lipid kinase activity was associated with IRS-1, whereas the serine kinase activity was associated with the insulin receptor and phosphorylated a number of proteins including p85, p110, and a 135-kDa protein identified as PDE3B. PDE3B phosphorylation was associated with enzyme activation, thus initiating the antilipolytic effect of insulin. These results show a novel pathway for intracellular signaling through the insulin receptor leading to the serine phosphorylation of key proteins involved in insulin action.
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