Induction of Akt Phosphorylation in Rat Primary Astrocytes by H2O2 Occurs Upstream of Phosphatidylinositol 3-Kinase: No Evidence for Oxidative Inhibition of PTEN

We show that treatment of rat primary astrocytes with H2O2 resulted in increased Akt phosphorylation that was blocked by wortmannin

Scott Salsman; Nicole Felts; Quentin N. Pye; Robert A. Floyd; Kenneth Hensley

2002

Scholarcy highlights

  • Phosphorylation of the serine/threonine kinase Akt has previously been shown to be increased by treatment of cells with H2O2; the target of H2O2 has not been clearly identified
  • We show that treatment of rat primary astrocytes with H2O2 resulted in increased Akt phosphorylation that was blocked by wortmannin
  • Addition of phosphatidylinositol 3,4-bisphosphate to cells resulted in an increase in Akt phosphorylation. This increase was additive to that induced by H2O2 and was blocked by wortmannin. These results suggest that activation of Akt by H2O2 occurs upstream of phosphatidylinositol 3-kinase activity in astrocytes
  • The proportions of phosphorylated to non-phosphorylated constituents of phosphoinositide 3-kinase/Akt/mTOR/S6K were determined to address their activation upon metformin treatment
  • Rotenone treatment of THP-1 cells led to upregulation of cyclooxygenase-2 and secretion of prostaglandin E2. These results suggest that rotenone-induced activation of reactive oxygen species/PI3K/Akt pathway in THP-1 cells leads to the release of factors that are toxic to SH-SY5Y cells and have implications for the onset of Parkinson's disease
  • Using adenovirus-mediated gene transfer in LDL receptor deficient mice, we show that the cholesterol lowering potential of apoE4mut1 is dependent on the expression of a functional classical LDLr
  • Our results suggest that the differential expression of CXCR4 in intratumoral stroma and SDF1 in adjacent normal mammary cells may predict clinical outcome in breast cancer patients

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