CYP2B6 (Cytochrome P450 Family 2 Subfamily B Member 6)

AB129 elevated CYP1A1 and CYP1A2 gene expression but increased only EROD activity. RBBR upregulated CYP1A2 and CYP2B6 gene expression, but did not affect the activity of any measured cytochrome assays.

This study demonstrates that common CYP2B6 variants alter testosterone metabolism in a human breast cancer model, potentially disrupting steroid hormone balance and contributing to a tumour-promoting environment. These findings highlight the potential relevance of pharmacogenetic profiling in breast cancer risk assessment.

Among the cytochrome P450 enzyme superfamily, CYP2B6 metabolizes drugs such as cyclophosphamide, efavirenz, methadone, and ecstasy. SIGNIFICANCE STATEMENT: The study found that the transcription factor activating transcription factor 5 regulates CYP2B6 expression in glioblastoma cell lines. Introducing a transactivator of transcription-fused cell-penetrating dominant-negative activating transcription factor 5 peptide downregulates CYP2B6 protein expression, suggesting its potential for personalized dosing strategies by targeting CYP2B6.

Notably, CYP2B6 emerged as a promising predictor of PARP inhibitor (PARPi) sensitivity, offering potential therapeutic implications. In conclusion, our study, harnessing machine learning and experimental validation, has uncovered novel biomarkers of HRD and PARPi sensitivity, shedding light on potential avenues for tailored clinical treatment strategies in COAD, thereby advancing personalized medicine.

No variants in our analysis were statistically associated with HC. The data suggest that CYP2B6 variants may increase the risk for HC in FA patients who received a CY based preparative therapy but these risk variants must be further evaluated in a larger population.

Finally, BDE-99 weakly induced PIG-A gene mutations in C3A, while negative in HepG2 cells. In conclusion, our study suggest that BDE-99 may be activated by human CYP2B6 for chromosome-breaking effects.

These data demonstrate that key-actors of the human hepatic detoxification system are impacted by triazole pesticides, which may have to be considered for the risk assessment of these agrochemicals. They additionally highlight that the use of human HepaSH cells as surrogates to primary human hepatocytes represents an attractive and promising way for studying hepatic effects of environmental chemicals.

Thus, we show that E2-mediated CYP2B6 regulation in BC cells depends on steroid hormone exposure in a cell line-specific manner. Our data indicates the importance of being careful with conclusions drawn from CYP2B6 induction findings in vitro, as we demonstrate potential influences of hormonal changes on CYP2B6 expression, which could impact steroid hormone homeostasis and, consequently, BC risk.

Additionally, T-AⅢ inhibited EGFR phosphorylation in nude mice. Our results demonstrated that T-AⅢ is a novel CAR activator through inhibition of the EGFR pathway.

In conclusion, our findings showed that the CYP2B6*9 (G516T) polymorphism is associated with B-CLL susceptibility among Egyptian patients. This variant greatly affected the clinical outcome and can serve as a good therapeutic marker in predicting response to cyclophosphamide treatment.

The findings from this study supported that polymorphism of CYP2B6*5gene may be involved in the development of GI cancer. However, other SNPs of CYP1A, CYP1B, and CYP2C genes did not signify the risk for GI cancer in the studied population of rural Maharashtra.

In PIG-A assays in HepG2 cells NNN and NAB were weakly positive and simply negative, respectively; however, in C3A cells both compounds significantly induced gene mutations, NNN being slight more potent. Conclusively, both NNN and NAB are mutagenic and clastogenic, depending on metabolic activation by partially different CYP enzymes.