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• W2162297602 abstract "We investigated the inhibitory effects of intracellular cyclic adenosine monophosphate (cAMP) levels in regulating class 3 aldehyde dehydrogenase (<i>aldh3</i>) gene expression using cultures of primary rat hepatocytes and transient transfection experiments with HepG2 cells. In addition to regulation by an <i>Ah</i> receptor-dependent mechanism, expression of many members of the <i>Ah</i> gene battery have been shown to be negatively regulated. As was seen for the cytochrome P450 (<i>cyp1A1</i>) gene, <i>aldh3</i> is transcriptionally inducible by polycyclic aromatic hydrocarbons (PAH), and this induction involving function of the arylhydrocarbon (<i>Ah</i>) receptor is inhibited by the protein kinase C (PKC) inhibitors, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine di-HCl (H7) and staurosporine. However, PAH induction of ALDH-3 activity, protein, and mRNA was potentiated 2-4-fold by addition of the protein kinase A (PKA) inhibitors, <i>N</i>-(2-(methylamino)ethyl)-5-isoquinolinesulfonamide di-HCl (H8) and <i>N</i>-(2-guanidinoethyl)-5-isoquinolinesulfonamide HCl (HA1004). These PKA inhibitors had no effect on the PAH induction of the <i>cyp1A1</i> Protein kinase A activity of cultured hepatocytes was specifically inhibited by H8 and HA1004 in a concentration-dependent manner, but not by H7, and there was an inverse correlation observed between potentiation of PAH-induced <i>aldh3</i> gene expression and inhibition of specific PKA activity by the PKA inhibitors. The cAMP analog dibutyryl cAMP, the adenylate cyclase activator forskolin, and the protein phosphatase 1 and 2A inhibitor okadaic acid all dramatically inhibited both PAH induction and H8 potentiation of PAH induction of <i>aldh3</i> expression but had no effect on induction of <i>cyp1A1</i> expression in cultured hepatocytes. Both basal and PAH-dependent expression of a chloramphenicol acetyltransferase expression plasmid containing approximately 3.5 kilobase pairs of the 5′-flanking region of <i>aldh3</i> (pALDH3.5CAT) were enhanced 3-4-fold by the PKA inhibitor H8 but not by the PKC inhibitor H7 (>20 μM). cAMP analogs, activators of PKA activity, or protein phosphatase inhibitors diminished expression of the reporter gene in a manner identical to the native gene in cultured rat hepatocytes. Using deletion analysis of the pALDH3.5CAT construct, we demonstrated the existence of a negative regulatory region in the 5′-flanking region between −1057 and −991 base pairs which appears to be responsible for the cAMP-dependent regulation of this gene under both basal and PAH-induced conditions. At least two apparently independent mechanisms which involve protein phosphorylation regulate <i>aldh3</i> expression. One involves function of the <i>Ah</i> receptor which requires PKC protein phosphorylation to positively regulate both <i>aldh3</i> and <i>cyp1A1</i> gene expression and the other a cAMP-responsive process which allows PKA activity to negatively regulate expression of <i>aldh3</i> under either basal or inducible conditions." @default.
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• W2162297602 date "1997-02-01" @default.
• W2162297602 modified "2023-10-15" @default.
• W2162297602 title "cAMP-dependent Negative Regulation of Rat Aldehyde Dehydrogenase Class 3 Gene Expression" @default.
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• W2162297602 doi "https://doi.org/10.1074/jbc.272.6.3238" @default.
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