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| Item Type: | Article |
|---|---|
| Title: | Eicosapentaenoic acid metabolism by cytochrome P450 enzymes of the CYP2C subfamily |
| Creators Name: | Barbosa-Sicard, E., Markovic, M., Honeck, H., Christ, B., Muller, D.N. and Schunck, W.H. |
| Abstract: | CYP2C enzymes epoxidize arachidonic acid (AA) to metabolites involved in the regulation of vascular and renal function. We tested the hypothesis that eicosapentaenoic acid (EPA), a n-3 polyunsaturated fatty acid, may serve as an alternative substrate. Human CYP2C8 and CYP2C9, as well as rat CYP2C11 and CYP2C23, were co-expressed with NADPH-CYP reductase in a baculovirus/insect cell system. The recombinant enzymes showed high EPA and AA epoxygenase activities and the catalytic efficiencies were almost equal comparing the two substrates. The 17,18-double bond was the preferred site of EPA epoxidation by CYPs 2C8, 2C11, and 2C23. 17(R),18(S)-Epoxyeicosatetraenoic acid was produced with an optical purity of about 70% by CYPs 2C9, 2C11, and 2C23 whereas CYP2C8 showed the opposite enantioselectivity. These results demonstrate that EPA is an efficient substrate of CYP2C enzymes and suggest that n-3 PUFA-rich diets may shift the CYP2C-dependent generation of physiologically active eicosanoids from AA- to EPA-derived metabolites. |
| Keywords: | CYP2C11, CYP2C23, CYP2C8, CYP2C9, Cytochrome P450, Eicosanoid, Eicosapentaenoic Acid, Epoxidation, N-3 Polyunsaturated Fatty Acid, Animals, Rats |
| Source: | Biochemical and Biophysical Research Communications |
| ISSN: | 0006-291X |
| Publisher: | Academic Press |
| Volume: | 329 |
| Number: | 4 |
| Page Range: | 1275-1281 |
| Date: | 22 April 2005 |
| Official Publication: | https://doi.org/10.1016/j.bbrc.2005.02.103 |
| PubMed: | View item in PubMed |
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