Mechanisms of action of malondialdehyde and 4-hydroxynonenal on xanthine oxidoreductase

Archives of Biochemistry and Biophysics
G CighettiP Allevi

Abstract

Studies have been made on the possible involvement of malondialdehyde (MDA) and (E)-4-hydroxynon-2-enal (HNE), two terminal compounds of lipid peroxidation, in modifying xanthine oxidoreductase activity through interaction with the oxidase (XO) and/or dehydrogenase (XDH) forms. The effect of the two aldehydes on XO (reversible, XO(rev), and irreversible, XO(irr)) and XDH was studied using xanthine oxidase from milk and xanthine oxidoreductase partially purified from rat liver. The incubation of milk xanthine oxidase with these aldehydes resulted in the inactivation of the enzyme following pseudo-first-order kinetics: enzyme activity was completely abolished by MDA (0.5-4 mM), while residual activity (5% of the starting value) associated with an XO(irr) form was always observed when the enzyme was incubated in the presence of HNE (0.5-4 mM). The addition of glutathione to the incubation mixtures prevented enzyme inactivation by HNE. The study on the xanthine oxidoreductase partially purified from rat liver showed that MDA decreases the total enzyme activity, acting only with the XO forms. On the contrary HNE leaves the same level of total activity but causes the conversion of XDH into an XO(irr) form.

References

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Citations

Jan 25, 2011·Journal of Bioenergetics and Biomembranes·Luciane C AlbericiHelena C F Oliveira
Aug 26, 2009·Free Radical Biology & Medicine·Luciane C AlbericiAnibal E Vercesi
Dec 22, 2005·Mass Spectrometry Reviews·Philippe A Guy, François Fenaille
Feb 22, 2014·Chemical Research in Toxicology·Yohan D'SouzaBrian M Bennett
Aug 20, 2021·Antioxidants & Redox Signaling·Luciane C Alberici, Helena C F Oliveira
Sep 10, 2021·Antioxidants & Redox Signaling·Elise MalardLaurent Chatre

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