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- W4256156914 abstract "Background: Human hepatoma cells extract glutamine at rates severalfold greater than normal hepatocytes through a high-affinity transporter encoded by the ATB0 gene, which contains two putative phosphorylation sites for protein kinase C (PKC). The studies presented here were undertaken to determine whether System B0-mediated glutamine uptake regulates hepatoma growth and whether PKC regulates the activity of this transporter. Methods: SK-Hep cells were treated with the PKC activator phorbol 12-myristate 13-acetate (PMA) and the initial-rate transport of glutamine and other nutrients measured at specific times thereafter. Growth rates were monitored during culture ± PMA or an excess of system B0 substrates relative to glutamine. Results: PMA treatment exerted a rapid (half-life ~ 15 minutes) concentration-dependent inhibition of glutamine uptake rates to 50% of control values via a posttranslational mechanism that decreased transporter maximum velocity. This effect persisted after 24 hours and was abrogated by the PKC inhibitor staurosporine. PMA also significantly decreased amino acid transport System y+ and System L activities but not System A. Chronic treatment with PMA (PKC depletion) inhibited SK-Hep growth, as did attenuation of System B0-mediated glutamine uptake with other B0 substrates. Conclusions: System B0-mediated glutamine uptake regulates hepatoma cell growth, whereas PKC influences both processes. (Surgery 1998;124:260-8)" @default.
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- W4256156914 date "1998-08-01" @default.
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- W4256156914 title "Protein kinase C regulates nutrient uptake and growth in hepatoma cells" @default.
- W4256156914 doi "https://doi.org/10.1067/msy.1998.90568" @default.
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