Regular ArticleThe Human Cytochrome P450 1A1 mRNA Is Rapidly Degraded In HepG2 Cells
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Environmental pollutants parathion, paraquat and bisphenol A show distinct effects towards nuclear receptors-mediated induction of xenobiotics-metabolizing cytochromes P450 in human hepatocytes
2015, Toxicology LettersCitation Excerpt :Our findings also pose the question, why PTH was able to induce expression of CYP3A4/2A6 mRNAs and proteins with comparable potency to RIF, but induction of CYP1A1/2 proteins were almost negligible in human hepatocytes next to mRNA level (Fig. 4). A likely explanation may involve lower stability of CYP1A1 mRNA in the absence of ligand (Lekas et al., 2000) and consequently limited translation to protein. Parathion intoxication is usually a result of suicidal attempts and proceeds via oral ingestion.
Induction of cytochromes P450 1A1 and 1A2 by tanshinones in human HepG2 hepatoma cell line
2011, Toxicology and Applied PharmacologyCitation Excerpt :Compared with the control (t1/2 = 5.33 ± 0.23 h), CTS (t1/2 = 5.61 ± 0.44 h), DHTI (t1/2 = 5.41 ± 0.54 h), TIIA (t1/2 = 5.72 ± 0.35 h), or TI (t1/2 = 5.63 ± 0.17 h) did not significantly alter the half-life of CYP1A1 mRNA, indicating that the increase in CYP1A1 mRNA transcripts in response to tanshinone was not due to decrease its degradation. Consistent with previous report (Lekas et al., 2000), CYP1A2 mRNA was long-lived in HepG2 cells in our study, with half-life > 24 h. Moreover, tanshinones had little effect on the CYP1A2 mRNA half-life. In addition, we used resveratrol, an antagonist of AhR, to test whether the induction effects of tanshinones are AhR-dependent.
Cytochrome P450 1A1 gene regulation by UVB involves crosstalk between the aryl hydrocarbon receptor and nuclear factor κB
2010, Chemico-Biological InteractionsCitation Excerpt :Endogenous CYP1A1 gene expression patterns and luciferase reporter activity behaved very similar upon both UVB irradiation (Fig. 1A and E) and FICZ treatment (Fig. 1B). The similarities in time-dependent induction of reporter activity and gene expression are explained by nearly identical half-lives of the luciferase and CYP1A1 mRNA (Luc t1/2 ∼ 2 hours; [25]; CYP1A1 t1/2 = 2.4 hours [26]) and protein (Luc and CYP1A1 t1/2 ∼ 3 hours; [27,28]) making both systems useful for studying rapid changes in AhR stimulation. The activation of AhR signaling and subsequent upregulation of CYP1A1 gene expression is accompanied by the degradation of activated receptor via the ubiquitin 26S-proteasomal pathway [29,30].
1,10-Phenanthroline stabilizes mRNA of the carcinogen-metabolizing enzyme, cytochrome P450 1a1
2010, Toxicology Letters
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