trans Arachidonic acid isomers inhibit NADPH-oxidase activity by direct interaction with enzyme components

Biochimica Et Biophysica Acta
H SouabniMariano A Ostuni

Abstract

NADPH-oxidase is an enzyme that represents, when activated, the major source of non-mitochondrial reactive oxygen species. In phagocytes, this production is an indispensable event for the destruction of engulfed pathogens. The functional NADPH-oxidase complex consists of a catalytic membrane flavocytochrome b (Cytb(558)) and four cytosolic proteins p47(phox), p67(phox), Rac and p40(phox). The NADPH-oxidase activity is finely regulated spatially and temporally by cellular signaling events that trigger the translocation of the cytosolic subunits to its membrane partner involving post-translational modifications and activation by second messengers such as arachidonic acid (AA). Arachidonic acid in its natural cis-poly unsaturated form (C20:4) has been described to be an efficient activator of the enzyme in vivo and in vitro. In this work, we examined in a cell-free system whether a change of the natural cis geometry to the trans configuration, which could occur either by diet or be produced by the action of free radicals, may have consequences on the functioning of NADPH-oxidase. We showed the inability of mono-trans AA isomers to activate the NADPH-oxidase complex and demonstrated the inhibitory effect on the cis-AA-induced NADPH...Continue Reading

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Citations

Jan 5, 2014·Antioxidants & Redox Signaling·Joanna WieczfinskaRafal Pawliczak
Jun 4, 2014·The Biochemical Journal·Aymen EzzineLaura Baciou
Dec 3, 2014·Redox Biology·Rawand MasoudChantal Houée-Levin
Aug 27, 2014·Free Radical Biology & Medicine·Ralf P BrandesKatrin Schröder
Jul 6, 2016·Biochimica Et Biophysica Acta. General Subjects·Hager SouabniLaura Baciou
Sep 21, 2013·Chemical Reviews·Chryssostomos ChatgilialogluArmida Torreggiani

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