Effectors of the mammalian plasma membrane NADH-oxidoreductase system. Short-chain ubiquinone analogues as potent stimulators
Autor: | François Vaillant, Ernst J. Wolvetang, Alfons Lawen, Gabrielle L. McMullen, Jari A Larm |
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Rok vydání: | 1996 |
Předmět: |
Male
Ubiquinone Physiology Respiratory chain NADH-oxidase Reductase Cofactor Multienzyme Complexes Superoxides Oxidoreductase Animals NADH NADPH Oxidoreductases Rats Wistar Plasma membrane NADH-oxidoreductase chemistry.chemical_classification Oxidase test biology Cell Membrane Active site ρ0 cells Cell Biology Rats Enzyme chemistry Biochemistry Coenzyme Q – cytochrome c reductase biology.protein ubiquinone analogues NADH∶ferricyanide reductase |
Zdroj: | Monash University Scopus-Elsevier |
ISSN: | 1573-6881 0145-479X |
DOI: | 10.1007/bf02110443 |
Popis: | In the presence of effectors variations in the two recognized activities of the plasma membrane NADH-oxidoreductase system were studied in separate, specific in vitro assays. We report here that ubiquinone analogues that contain a short, less hydrophobic side chain than coenzyme Q-10 dramatically stimulate the NADH-oxidase activity of isolated rat liver plasma membranes whereas they show no effect on the reductase activity of isolated membranes. If measured in assays of the NADH:ferricyanide reductase of living cultured cells these compounds have only a limited effect; the oxidase activity of whole cells is not measurable in our hands. We have furthermore identified selective inhibitors of both enzyme activities. In particular, the NADH-oxidase activity can be significantly inhibited by structural analogues of ubiquinone, such as capsaicin and resiniferatoxin. The NADH:ferricyanide reductase, on the other hand, is particularly sensitive to pCMBS, indicating the presence of a sulfhydryl group of groups at its active site. The identification of these specific effectors of the different enzyme activities of the PMOR yields further insights into the function of this system. |
Databáze: | OpenAIRE |
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