Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/66822
Type: Artigo de periódico
Title: Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle
Author: Pardo-Andreu, GL
Cavalheiro, RA
Dorta, DJ
Naal, Z
Delgado, R
Vercesi, AE
Curti, C
Abstract: Mangiferin acts as a strong antioxidant on mitochondria. However, when in the presence of Ca2+, mangiferin elicits mitochondrial permeability transition (MPT), as evidenced by cyclosporin A-sensitive mitochondrial swelling. We now provide evidence, by means of electrochemical and UV-visible spectro-scopical analysis, that Fe(III) coordinates with mangiferin. The resulting mangiferin-Fe(III) complex does not elicit MPT and prevents MPT by scavenging reactive oxygen species. Indeed, the complex protects mitochondrial membrane protein thiols and glutathione from oxidation. Fe(III) also significantly increases the ability of mangiferin to scavenge the 2,2-diphenyl-1-picrylhydrazyl radical, as well as to display antioxidant activity toward antimycin A-induced H2O2 production and t-butyl hydroperoxide-promoted membrane lipid peroxidation in mitochondria. We postulate that coordination with Fe(III) constitutes a potential protective mechanism toward the prooxidant action of mangiferin and other catechol-containing antioxidants regarding MPT induction. Potential therapeutic relevance of this finding for conditions of pathological iron overload is discussed.
Country: EUA
Editor: Amer Soc Pharmacology Experimental Therapeutics
Citation: Journal Of Pharmacology And Experimental Therapeutics. Amer Soc Pharmacology Experimental Therapeutics, v. 320, n. 2, n. 646, n. 653, 2007.
Rights: fechado
Identifier DOI: 10.1124/jpet.106.112003
Date Issue: 2007
Appears in Collections:Unicamp - Artigos e Outros Documentos

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