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J. Biol. Chem., Vol. 261, Issue 20, 9109-9115, 07, 1986
T Hayakawa, K Suzuki, S Suzuki, PC Andrews and BM Babior
Two-dimensional gel electrophoresis was used to study protein
phosphorylation in granules, membranes, and soluble fractions from human
neutrophils that had been loaded with 32Pi. In resting cells, label was
incorporated primarily into proteins of the membranes and the soluble
supernatant; little appeared in the granules. Activation of 32P- loaded
neutrophils resulted in an increase in the 32P content of a small number of
membrane and soluble proteins without a change in the labeling of the
granule fraction. The identity of the proteins affected by activation
depended on the activating agent used; all of the activating agents,
however, caused an increase in the labeling of a group of approximately
48-kDa proteins that appeared to be distributed between the membranes and
the soluble supernatant. To investigate the role of phosphorylation in the
activation of the respiratory burst oxidase, the incorporation of 32P into
phosphoproteins was studied in neutrophils from patients with chronic
granulomatous disease. When these cells were exposed to phorbol myristate
acetate, one of the agents used for the activation of normal neutrophils,
the 48-kDa proteins in the membranes and supernatants failed to take up
additional 32P. Phosphorylation patterns in normal neutrophils activated
under nitrogen were similar to the patterns seen with cells activated in
air, suggesting that the differences in phosphorylation between normal and
chronic granulomatous disease neutrophils did not represent secondary
effects of the oxidants produced by the normal cells, but reflected primary
biochemical differences between the normal and the defective phagocytes. We
postulate from these results that the uptake of phosphate by the 48-kDa
protein group may be involved in the activation of the respiratory burst
oxidase.
A possible role for protein phosphorylation in the activation of the respiratory burst in human neutrophils. Evidence from studies with cells from patients with chronic granulomatous disease
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