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δ‐Aminolevulinate Dehydratase Inhibition by Phenyl Selenoacetylene: Effect of Reaction with Hydrogen Peroxide

Bolzan, Rodrigo Cordeiro ; Folmer, Vanderlei ; Farina, Marcelo ; Zeni, Gilson ; Nogueira, Cristina Wayne ; Rocha, João Batista Teixeira ; Emanuelli, Tatiana

Pharmacology & toxicology, 2002-04, Vol.90 (4), p.214-219

Oxford, UK: Munksgaard International Publishers

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Título:
δ‐Aminolevulinate Dehydratase Inhibition by Phenyl Selenoacetylene: Effect of Reaction with Hydrogen Peroxide
Autor: Bolzan, Rodrigo Cordeiro ; Folmer, Vanderlei ; Farina, Marcelo ; Zeni, Gilson ; Nogueira, Cristina Wayne ; Rocha, João Batista Teixeira ; Emanuelli, Tatiana
Assuntos: Acetylene - analogs & derivatives ; Acetylene - pharmacology ; Animals ; Biological and medical sciences ; Chemical and industrial products toxicology. Toxic occupational diseases ; Cucumis sativus - chemistry ; Dithiothreitol - pharmacology ; Dose-Response Relationship, Drug ; Enzyme Inhibitors - pharmacology ; Hydrogen Peroxide - metabolism ; Liver - enzymology ; Male ; Medical sciences ; Metals and various inorganic compounds ; Organoselenium Compounds - pharmacology ; Plant Extracts ; Plant Leaves - enzymology ; Porphobilinogen Synthase - antagonists & inhibitors ; Rats ; Rats, Wistar ; Toxicology
É parte de: Pharmacology & toxicology, 2002-04, Vol.90 (4), p.214-219
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
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Descrição: : The effect of phenyl selenoacetylene and its selenoxide on δ‐aminolevulinate dehydratase from liver of adult rats (mammalian source) and from cucumber leaves (plant source) was investigated. In vivo, selenides can be oxidized to selenoxides by flavin‐containing monooxygenases and selenoxides can regenerate selenides by thiol oxidation. The compound phenyl selenoacetylene was converted to selenoxides by reaction with hydrogen peroxide. Phenyl selenoacetylene inhibited mammalian and plant δ‐aminolevulinate dehydratase with an IC50 about 250 μM and >400 μM, respectively. Its selenoxide inhibited the enzyme more strongly, with IC50 values of 45 μM and 100 μM for the mammalian and plant source, respectively. The selenoxide inhibitory action was antagonized by dithiothreitol suggesting the involvement of –SH groups. Moreover, δ‐aminolevulinate dehydratase from a plant source was inhibited by the selenoxide, suggesting a possible involvement of –SH groups located at a site distinct from the region implicated in Zn2+ binding in mammalian δ‐aminolevulinate dehydratase. The results of the present study suggest that (i) δ‐aminolevulinate dehydratase is a potential molecular target for phenyl selenoacetylene, due to the oxidation of enzyme sulfhydryl groups, and that (ii) the monooxygenation of this selenocompound, which in vivo could be possibly mediated by flavin‐containing monooxigenases, increases its inhibitory effect.
Editor: Oxford, UK: Munksgaard International Publishers
Idioma: Inglês

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δ‐Aminolevulinate Dehydratase Inhibition by Phenyl Selenoacetylene: Effect of Reaction with Hydrogen Peroxide

Bolzan, Rodrigo Cordeiro ; Folmer, Vanderlei ; Farina, Marcelo ; Zeni, Gilson ; Nogueira, Cristina Wayne ; Rocha, João Batista Teixeira ; Emanuelli, Tatiana

Oxford, UK: Munksgaard International Publishers

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