A Phenylarsine Oxide-Binding Protein of Neutrophil Cytosol, Which Belongs to the S100 Family, Potentiates NADPH Oxidase Activation

Autor: Doussie`re, Jacques, Bouzidi, Farid, Vignais, Pierre V.
Zdroj: Biochemical and Biophysical Research Communications; August 3, 2001, Vol. 285 Issue: 5 p1317-1320, 4p
Abstrakt: By photoaffinity labeling with a tritiated azido derivative of phenylarsine oxide (PAO), 4[N-(4-azido-2-nitrophenyl)amino-[3H]acetamido]phenylarsine oxide ([3H]azidoPAO), we demonstrate that PAO binds selectively to the S100 A8/A9 complex of bovine neutrophil cytosol (previously known as p7/p23, homologous to the MRP-8/MRP-14 complex of human phagocytes). Using a semirecombinant cell free assay of oxidase activation and the determination of oxidase activity by the production of the superoxide anion O−2, we found that the PAO binding protein (p7/p23) was able to potentiate the activation of NADH oxidase and that this effect was synergized by PAO. The p7/p23 protein complex of bovine neutrophils can therefore be considered as a positive regulator of NADPH oxidase activation in neutrophils.
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