Protein phosphorylation and the respiratory burst.

The exposure of 32P-loaded neutrophils to any of a variety of activating agents induces changes in the levels of phosphorylation of a large number of phosphoproteins. The uptake of phosphate by one set of phosphoproteins in particular, a family whose members migrate at Mr 48K with near neutral pI values, appears to be closely related to the activation of the respiratory burst oxidase, the O2--producing enzyme of phagocytes that is responsible for the generation of microbicidal oxidants by these cells. Evidence for the relationship between the phosphorylation of these proteins and the activation of the respiratory burst oxidase has been furnished by kinetic studies as well as by studies on protein phosphorylation in neutrophils from patients with chronic granulomatous disease, a group of inherited disorders affecting this oxidase. The details of this relationship are obscure, although the evidence suggests that these phosphoproteins act in substoichiometric amounts with respect to the oxidase.