Research paperValidation of the (ω-l)-hydroxylation of lauric acid as an in vitro substrate probe for human liver CYP2E1
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Refined CYP2E1<sup>∗</sup> Template<sup>∗∗</sup> system to decipher the ligand-interactions
2021, Drug Metabolism and PharmacokineticsCitation Excerpt :Of course, further studies are necessary to clarify the interactions of these reactions rigidly. n-Hexane and lauric acid (dodecanoic acid) undergo CYP2E1-mediated ω 1 oxidations [47,48]. A placement was available at Rings D-B for the 2-oxidation of n-hexane (Supplement Fig. 2A).
CYP4A11 is repressed by retinoic acid in human liver cells
2006, FEBS LettersUnsaturated fatty acid regulation of peroxisome proliferator-activated receptor α activity in rat primary hepatoctes
2003, Journal of Biological ChemistryCitation Excerpt :NADPH-dependent microsomal fatty acid oxidation represents a likely route for the generation of these oxidized lipids. To determine whether this pathway contributes to the 20:5n-3 control of gene expression, hepatocytes were treated with the inhibitor of microsomal oxidation, diethyldithiocarbamate (DDC) (27). Studies with isolated rat hepatic microsomal preparations indicated that DDC is a robust inhibitor of NADPH-dependent oxidation of both 20:4n-6 and 20:5n-3.2 Arachidonic acid typically has a marginal effect on mRNACYP4A in primary hepatocytes (15, 16) and PPARα activity (Fig. 1).
Cloning and expression of a pig liver taurochenodeoxycholic acid 6α-hydroxylase (CYP4A21): A novel member of the CYP4A subfamily
2001, Journal of Biological ChemistryCitation Excerpt :The 6α-hydroxylase activity in microsomes from transfected COS cells and pig liver microsomes is comparable, but the ω- and (ω-1)-hydroxylase activities, present in pig liver microsomes, were not detectable with microsomes from the transfected COS cells. It has been shown in rat and human liver that formation of a ω-hydroxy metabolite of lauric acid is a marker of CYP4A enzyme activity, whereas other cytochrome P450 isoenzymes, like members of the CYP2 family, hydroxylate primarily the (ω-1)-position of lauric acid (26-29). The present results strongly indicate that 6α-hydroxylation of taurochenodeoxycholic acid and ω-hydroxylation of lauric acid in pig liver microsomes are performed by two distinct isozymes.