The oxidation of apocynin catalyzed by myeloperoxidase: proposal for NADPH oxidase inhibition.

Abstract:

:Apocynin has been used as an efficient inhibitor of the NADPH oxidase complex and its mechanism of inhibition is linked to prior activation through the action of peroxidases. Here we studied the oxidation of apocynin catalyzed by myeloperoxidase (MPO) and activated neutrophils. We found that apocynin is easily oxidized by MPO/H2O2 or activated neutrophils and has as products dimer and trimer derivatives. Since apocynin impedes the migration of the cytosolic component p47phox to the membrane and this effect could be related to its conjugation with essential thiol groups, we studied the reactivity of apocynin and its MPO-catalyzed oxidation products with glutathione (GSH). We found that apocynin and its oxidation products do not react with GSH. However, this thiol compound was efficiently oxidized by the apocynin radical during the MPO-catalyzed oxidation. We suggest that the reactivity of apocynin radical with thiol compounds could be involved in the inhibitory effect of this methoxy-catechol on NADPH oxidase complex.

journal_name

Arch Biochem Biophys

authors

Ximenes VF,Kanegae MP,Rissato SR,Galhiane MS

doi

10.1016/j.abb.2006.11.010

subject

Has Abstract

pub_date

2007-01-15 00:00:00

pages

134-41

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(06)00449-8

journal_volume

457

pub_type

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