Phosphorylation of the respiratory burst oxidase subunit p67 phox during human neutrophil activation: regulation by protein kinase C-dependent and independent …
J El Benna, PMC Dang, M Gaudry, M Fay… - Journal of Biological …, 1997 - ASBMB
The respiratory burst oxidase of phagocytes and B lymphocytes catalyzes the reduction of
oxygen to superoxide anion (O· ̄ 2) at the expense of NADPH. This multicomponent
enzyme is dormant in resting cells but is activated on exposure to an appropriate stimulus.
The phosphorylation-dependent mechanisms regulating the activation of the respiratory
burst oxidase are unclear, particularly the phosphorylation status of the cytosolic component
p67 phox. In this study, we found that activation of human neutrophils with formyl-methionyl …
oxygen to superoxide anion (O· ̄ 2) at the expense of NADPH. This multicomponent
enzyme is dormant in resting cells but is activated on exposure to an appropriate stimulus.
The phosphorylation-dependent mechanisms regulating the activation of the respiratory
burst oxidase are unclear, particularly the phosphorylation status of the cytosolic component
p67 phox. In this study, we found that activation of human neutrophils with formyl-methionyl …