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pubmed-article:1632795pubmed:abstractTextMicrosomal NADPH-driven electron transport is known to initiate lipid peroxidation by activating oxygen in the presence of iron. This pro-oxidant effect can mask an antioxidant function of NADPH-driven electron transport in microsomes via vitamin E recycling from its phenoxyl radicals formed in the course of peroxidation. To test this hypothesis we studied the effects of NADPH on the endogenous vitamin E content and lipid peroxidation induced in liver microsomes by an oxidation system independent of iron: an azo-initiator of peroxyl radicals, 2,2'-azobis (2,4-dimethylvaleronitrile), (AMVN), in the presence of an iron chelator deferoxamine. We found that under conditions NADPH: (i) inhibited lipid peroxidation; (ii) this inhibitory effect was less pronounced in microsomes from vitamin E-deficient rats than in microsomes from normal rats; (iii) protected vitamin E from oxidative destruction; (iv) reduced chromanoxyl radicals of vitamin E homologue with a 6-carbon side-chain, chromanol-alpha-C-6. Thus NADPH-driven electron transport may function both to initiate and/or inhibit lipid peroxidation in microsomes depending on the availability of transition metal catalysts.lld:pubmed
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pubmed-article:1632795pubmed:articleTitleNADPH-dependent inhibition of lipid peroxidation in rat liver microsomes.lld:pubmed
pubmed-article:1632795pubmed:affiliationDepartment of Molecular and Cell Biology, University of California, Berkeley 94720.lld:pubmed
pubmed-article:1632795pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1632795pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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