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- W2019299719 abstract "MDR3 is a phospholipid translocator homologous to MDR1 P-glycoprotein. MDR3 localizes to the canalicular membrane and contributes to the secretion of bile. To elucidate the role of protein kinase C in the regulation of MDR3 gene expression, we investigated the effect of phorbol 12-myristate 13-acetate (PMA) on the level of MDR3 mRNA in human Chang liver cells by a reverse transcription-polymerase chain reaction method. The steady-state expression of MDR3 mRNA was decreased by PMA after treatment for 8-20 hr and at concentrations of 1-100 nM. PMA also decreased the doxorubicin-induced expression of MDR3 mRNA. 4alpha-Phorbol 12,13-didecanoate, a negative control compound, did not decrease the expression at these concentrations. The down-regulatory effect of PMA was partially suppressed by the protein kinase C inhibitors 2-[1-(3-dimethylaminopropyl)-1H-indol-3-yl]-3-(1H-indol-3-yl)maleimide (GF109203X) and calphostin C. Furthermore, cycloheximide, a protein synthesis inhibitor, antagonized the effect of PMA. From these results, it was suggested that the level of MDR3 mRNA was negatively regulated by a protein kinase C- and protein synthesis-dependent system and that the system regulated both the stable and inducible expression of MDR3 mRNA." @default.
- W2019299719 created "2016-06-24" @default.
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- W2019299719 date "2001-06-01" @default.
- W2019299719 modified "2023-10-16" @default.
- W2019299719 title "Protein kinase C-mediated down-regulation of MDR3 mRNA expression in Chang liver cells11Abbreviations: MDR, multidrug resistance; P-gp, P-glycoprotein; PCR, polymerase chain reaction; PMA, phorbol 12-myristate 13-acetate; 4α-PDD, 4α-phorbol 12,13-didecanoate; and PKC, protein kinase C." @default.
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- W2019299719 doi "https://doi.org/10.1016/s0006-2952(01)00601-3" @default.
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