ArticleThe Biochemical journal2017
Nitric oxide stimulates cellular degradation of human CYP51A1, the highly conserved lanosterol 14α-demethylase.
Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- CYP51A1 in health and disease: from sterol metabolism to regulated cell death.Cell death discovery · 2025Review
- Topology surveillance of the lanosterol demethylase CYP51A1 by signal peptide peptidase.Journal of cell science · 2024Article
- Identification of key genes in diabetic nephropathy based on lipid metabolism.Experimental and therapeutic medicine · 2024Article
- High-Throughput Production of Diverse Xenobiotic Metabolites with Cytochrome P450-Transduced Huh7 Hepatoma Cell Lines.Drug metabolism and disposition: the biological fate of chemicals · 2022Article
- Post-translational control of the long and winding road to cholesterol.The Journal of biological chemistry · 2020Review
- Regulation of cytochrome P450 enzyme activity and expression by nitric oxide in the context of inflammatory disease.Drug metabolism reviews · 2020Review
- Tyrosine Nitration Contributes to Nitric Oxide-Stimulated Degradation of CYP2B6.Molecular pharmacology · 2020Article
- Nitric Oxide Mediated Degradation of CYP2A6 via the Ubiquitin-Proteasome Pathway in Human Hepatoma Cells.Drug metabolism and disposition: the biological fate of chemicals · 2020Article
- The cholesterol synthesis enzyme lanosterol 14α-demethylase is post-translationally regulated by the E3 ubiquitin ligase MARCH6.The Biochemical journal · 2020Article
- Posttranslational regulation of CYP2J2 by nitric oxide.Free radical biology & medicine · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Nitric oxide (NO) is known to down-regulate drug-metabolizing cytochrome P450 enzymes in an enzyme-selective manner. Ubiquitin-proteasome-dependent and -independent pathways have been reported. Here, we studied the regulation of expression of human CYP51A1, the lanosterol 14α-demethylase required for synthesis of cholesterol and other sterols in mammals, which is found in every kingdom of life. In Huh7 human hepatoma cells, treatment with NO donors caused rapid post-translational down-regulation of CYP51A1 protein. Human NO synthase (NOS)-dependent down-regulation was also observed in cultured human hepatocytes treated with a cytokine mixture and in Huh7 cells expressing human NOS2 under control of a doxycycline-regulated promoter. This down-regulation was partially attenuated by proteasome inhibitors, but only trace levels of ubiquitination could be found. Further studies with inhibitors of other proteolytic pathways suggest a possible role for calpains, especially when the proteasome is inhibited. NO donors also down-regulated CYP51A1 mRNA in Huh7 cells, but to a lesser degree, than the down-regulation of the protein.
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