Differential effects of flavonols on inactivation of α1-antitrypsin induced by hypohalous acids and the myeloperoxidase–hydrogen peroxide–halide system
| Autor: | Pavel Salavei, Hamama Bouriche, Juergen Arnhold, Jacqueline Lessig |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Flavonols
biology Hypochlorous acid Bromates Chemistry Elastase Biophysics Hydrogen Peroxide Biochemistry Hypochlorous Acid Enzyme Activation chemistry.chemical_compound Rutin Halogens alpha 1-Antitrypsin Myeloperoxidase Hypobromous acid biology.protein Myricetin Kaempferol Molecular Biology Peroxidase |
| Zdroj: | Archives of Biochemistry and Biophysics. 459:137-142 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/j.abb.2006.10.030 |
| Popis: | Alpha1-antitrypsin is well known for its ability to inhibit human neutrophil elastase. Pretreatment of alpha1-antitrypsin with hypohalous acids HOCl and HOBr as well as with the myeloperoxidase-hydrogen peroxide-chloride (or bromide) system inactivated this proteinase. The flavonols rutin, quercetin, myricetin, and kaempferol inhibited the inactivation of alpha1-antitrypsin by HOCl and HOBr with rutin having the most pronounced effect. In contrast, these flavonols did not remove the proteinase inactivation by the myeloperoxidase-hydrogen peroxide-halide system. Taurine did not protect against the inactivation of alpha1-antitrypsin by HOCl, HOBr, or the myeloperoxidase-hydrogen peroxide-halide system, while methionine was efficient in all systems. A close association between myeloperoxidase and alpha1-antitrypsin was revealed by native gel electrophoresis and in-gel peroxidase staining. In addition, alpha1-antitrypsin binds to the myeloperoxidase components transferred after SDS-PAGE on a blotting membrane. With this complex formation, myeloperoxidase overcomes the natural antioxidative protective system of plasma and prevents the inactivation of alpha1-antitrypsin. |
| Databáze: | OpenAIRE |
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