Presence of NADPH-cytochrome P450 reductase in central catecholaminergic neurones

Lena Haglund, Christer Köhler, Tapio Haaparanta, Menek Goldstein, Jan Åke Gustafsson

Research output: Contribution to journalArticlepeer-review

53 Scopus citations


The cytochrome P450-containing mixed function oxidases metabolize a variety of endogenous and exogenous compounds including drags, carcinogens, fatty acids and steroids1. Mixed function oxidases have been detected in several tissues2, including brain3. The enzyme system consists of a lipid fraction (phosphatidylcholine), cytochrome P450 and NADPH-cytochrome P450 reductase4. NADPH-cytochrome P450 reductase has been purified to apparent homogeneity and demonstrated to supply reducing equivalents from NADPH to cytochrome P450 (refs 5-7). Detection of NADPH-cytochrome P450 reductase thus represents an indirect means of demonstrating the presence of cytochrome P450. Although the role of cytochrome P450 in the central nervous system (CNS) is not known, it may include such different functions as metabolism of xenobiotics8, aromatization of androgens to oestrogene9 and the formation of catecholoestrogens10. Despite the potentially very important role(s) of cytochrome P450 in brain function, its exact regional distribution remains essentially unknown. Using a specific antibody against rat liver NADPH-cytochrome P450 reductase in combination with immunohistochemical techniques, we have now localized this enzyme to defined catecholamine (CA)-containing structures of the rat and monkey brain.

Original languageEnglish (US)
Pages (from-to)259-262
Number of pages4
Issue number5948
StatePublished - 1984

ASJC Scopus subject areas

  • General


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