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Endogenous protein phosphorylation by resting and activated human
neutrophils
PC Andrews and BM Babior
NADPH oxidase is an enzyme in the plasma membrane of the neutrophil that
catalyzes the production of O2-, a species central to the oxygen- dependent
killing mechanisms of this cell. The oxidase is dormant in resting cells
and is activated upon the addition of a stimulus. Neutrophils of patients
with chronic granulomatous disease (CGD) manifest no oxidase activity when
stimulated. The possible role of protein phosphorylation in the activation
of NADPH oxidase was examined in normal and CGD neutrophils by measuring
the incorporation of 32Pi into proteins as determined by gel
electrophoresis followed by autoradiography. Resting neutrophils from
normal subjects exhibit at least 40 distinct phosphoprotein bands. The
level of phosphorylation of these bands was examined after the addition of
phorbol myristate acetate (PMA), opsonized zymosan, digitonin,
N-formyl-methionyl- phenylalanine (FMLP), or NaF. PMA and opsonized zymosan
increased the phosphorylation of a set of 6 protein bands. Digitonin and
FMLP consistently caused the phosphorylation of 4 of these protein bands,
while NaF failed to induce increased phosphorylation of any protein band.
All activators tested caused the dephosphorylation of one specific protein
band. The time course of phosphorylation (dephosphorylation) was examined
using PMA as the activating agent. Increased phosphorylation of one protein
band was evident by 12 sec after the addition of PMA. The most slowly
phosphorylated protein band did not slow evidence of change until 5 min
after the addition of PMA. Three of the phosphoproteins examined were
phosphorylated either earlier than or concomitant with the activation of
NADPH oxidase. CGD neutrophils were compared with normal cells for their
ability to phosphorylate proteins in response to PMA. The phosphoprotein
banding patterns of CGD neutrophils were identical with those of normal
neutrophils in both the resting and activated states. The evidence
presented shows that the phosphorylation of proteins is a prominent feature
of neutrophil metabolism. The striking similarity of phosphorylation
changes induced by the various activators tested suggests that protein
phosphorylation may play a role in some aspects of neutrophil activation.
Evidence was not obtained, however, regarding a link between protein
phosphorylation and activation of NADPH oxidase.
Volume 61,
Issue 2,
pp. 333-340,
02/01/1983
Copyright © 1983 by The American Society of Hematology
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