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induces protein synthesis through PI3-kinase-Akt/PKB
pathway in cardiac myocytes
1 First Department of Internal Medicine and 2 Second Department of Internal Medicine, Kobe University School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe, 650-0017, Japan
The activation of phosphatidylinositol (PI)
3-kinase and Akt/protein kinase B (PKB) by tumor necrosis
factor (TNF)-
and their roles on stimulation of protein
synthesis were investigated in cultured neonatal rat cardiac myocytes.
Treatment of cells with TNF- resulted in enlargement of cell surface
area and stimulation of protein synthesis without affecting myocyte
viability. TNF- induced marked activation of PI3-kinase and Akt/PKB,
and the activation of PI3-kinase and Akt/PKB was rapid (maximal at 10 and 15 min, respectively) and concentration dependent. Akt/PKB
activation by TNF- was inhibited by a PI3-kinase-specific inhibitor
LY-294002 and adenovirus-mediated expression of a dominant negative
mutant of PI3-kinase, indicating that TNF- activates Akt/PKB through PI3-kinase activation. Furthermore, TNF--induced protein
synthesis was inhibited by pretreatment with LY-294002 and expression
of a dominant negative mutant of PI3-kinase or Akt/PKB. These results indicate that activation of the PI3-kinase-Akt/PKB pathway plays an
essential role in protein synthesis induced by TNF- in cardiac myocytes.
cardiac hypertrophy; signal transduction; tumor necrosis
factor-; phosphatidylinositol 3-kinase; protein kinase B
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