Human cytochrome P450 1B1 (CYP1B1)) Yeast Reductase for Sale

Human cytochrome P450 1B1 (CYP1B1) is found mainly in extrahepatic tissues and is overexpressed in a smorgasbord of human tumors. In contrast, V79 cells stably expressing human P450 1B1 generated exclusively DB[a,l]PDE-DNA adducts. Differences in the total level of DNA binding were also observed.

Metabolic activation of 17β-estradiol (E2) to 4-hydroxy E2 by CYP1B1 has been postulated to be an important factor in mammary carcinogenesis. The forbiddance of recombinant human CYP1B1 by 2,2′,4,6′-tetramethoxystilbene (TMS) was investigated using either the Escherichia coli membranes of recombinant human CYP1B1 Cytochrome P450 1B1 (human) Yeast Reductase coexpressed with human NADPH-P450 reductase or using purified enzyme. 2,2′,4,6′-TMS showed potent and selective inhibition of ethoxyresorufin O-deethylation (EROD) activity of CYP1B1 with IC50 evaluates of 2 nM. 2,2′,foursome,6′-TMS exhibited 175-fold selectivity for CYP1B1 over CYP (IC50, 350 nM) and 85-fold selectivity for CYP1B1 over CYP (IC50, 170 nM). However, inhibition of human NADPH-P450 reductase activity by 2,2′,4,6′-TMS was negligible.

This compound has been found to be an environmental pollutant, and in rodent bioassays it is the most carcinogenic PAH yet discovered. Activation of DB[a,l]P in various metabolizing systems occurs via fjord region DB[a,l]P-11, 12-dihydrodiol 13,14-epoxides (DB[a,l]PDE): we found that DB[a,cubic decimetre]P is stereoselectively metabolized in human mammary carcinoma MCF-7 cells to the (-)-anti- and (+)-syn-DB[a,l]PDE which both bind extensively to cellular DNA. To follow up this study and to relate specific DNA adducts to activation by individual P450 isoforms, the newly established V79 cells stably expressing human P450 1B1 personified compared with those expressing human P450. The modes of inhibition by 2,2′,4,6′-TMS were noncompetitive for CYP and CYP1B1. DNA adduct formation in both V79 cell lines differed distinctively after incubation with DB[a,l]P or its enantiomeric 11,12-dihydrodiols. Human P450 catalyzed the formation of DB[atomic number 13]PDE-DNA adducts as well as several highly polar DNA adducts as yet unidentified. The proportion of these highly polar adducts to DB[atomic number 13]PDE adducts was dependent upon both the concentration of DB[a,l]P and the time of vulnerability.

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