PKB negatively modulates TGF-β responsiveness in prostate carcinoma PC-3 cells through its interacti

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Most prostate cancers are insensitive to growth-inhibitory effect of TGF-β, while PI3K-PKB signaling is highly activated in prostate cancers. We investigated whether the PI3K-PKB signaling con- tributes to TGF-β insensitivity in PTEN-null prostate cancer PC-3 cells. Cell growth analysis showed that inhibition of PI3K-PKB pathway by LY294002 en- hanced growth inhibition and cell cycle arrest induced by TGF-β. Furthermore, activation of PI3K-PKB pathway by insulin or overexpression of PKB de- creased the transcriptional activity of TGF-β, as measured by the TGF-β/Smad3-responsive CAGA- luciferase reporter, while inhibition of PI3K-PKB pathway by introducing PTEN, inactive PKB mutant or using LY294002 promoted TGF-β-induced expres- sion of CAGA-luciferase. Co-immunoprecipitation studies further demonstrated that Smad3 interacted with PKB through its linker region and MH2 domain. This interaction was facilitated by insulin and disrupted by TGF-β signaling activation. Our results suggest that the PI3K-PKB pathway may play an important role in rendering cell resistance to the antiproliferative effect of TGF-β and regulating cell response to TGF-β. Most prostate cancers are insensitive to growth-inhibitory effect of TGF-β, while PI3K-PKB signaling is highly activated in prostate cancers. We investigated whether the PI3K-PKB signaling con- tributes to TGF-β insensitivity in PTEN-null prostate cancer PC -3 cells. Cell growth analysis showed that inhibition of PI3K-PKB pathway by LY294002 en-hanced growth inhibition and cell cycle arrest induced by TGF-β. Further, activation of PI3K-PKB pathway by insulin or overexpression of PKB de- creased the transcriptional activity of TGF-β, as measured by the TGF-β / Smad3-responsive CAGA-luciferase reporter, while inhibition of PI3K-PKB pathway by introducing PTEN, inactive PKB mutant or using LY294002 promoted TGF-β-induced expresion of CAGA-luciferase. Co-immunoprecipitation studies further demonstrated that Smad3 interacted with PKB through its linker region and MH2 domain. This interaction was facilitated by insulin and disrupted by TGF-beta signaling activation. Our results sug gest that the PI3K-PKB pathway may play an important role in rendering cell resistance to the antiproliferative effect of TGF-β and regulating cell response to TGF-β.
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