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J. Biol. Chem., Vol. 275, Issue 47, 36713-36719, November 24, 2000
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From the The respiratory burst of human neutrophils is
primed by a number of pro-inflammatory stimuli, including tumor
necrosis factor-
Priming of the Neutrophil Respiratory Burst Involves p38
Mitogen-activated Protein Kinase-dependent Exocytosis of
Flavocytochrome b558-containing Granules*
§,
**
Molecular Signaling Group, Department of
Medicine and the Department of Biochemistry and Molecular
Biology, University of Louisville, Louisville, Kentucky 40202-1718, the ¶ Department of Host-defense Biochemistry, Institute of
Tropical Medicine, Nagasaki University, 1-12-4 Sakamoto,
Nagasaki 852-8523, Japan, and the ** Veterans Affairs Medical Center,
Louisville, Kentucky 40204
(TNF) and lipopolysaccharide (LPS); however, the
mechanism of priming remains unknown. LPS has been shown previously to
increase membrane expression of flavocytochrome
b558, a component of the NADPH oxidase. This
study shows that TNF also increases membrane expression of
flavocytochrome b558. Mitogen-activated protein kinase (MAPK) modules have been implicated in the action of priming agents. Pharmacologic inhibitors of MAPKs, SB203580 and PD098059, revealed that priming of the respiratory burst and up-regulation of
flavocytochrome b558 are dependent on p38 MAPK
but not on extracellular-signal regulated kinase (ERK). TNF and LPS
primed respiratory burst activity and increased membrane expression of
CD35 and CD66b, specific markers of secretory vesicles and specific
granules that contain flavocytochrome b558,
with similar time courses and concentration dependences. These
processes also required p38 MAPK but were independent of ERK. TNF
failed to prime respiratory burst activity or to increase membrane CD35
expression in enucleated neutrophil cytoplasts. These data suggest that
one mechanism by which TNF and LPS prime neutrophil respiratory
burst activity is by increasing membrane expression of flavocytochrome
b558 through exocytosis of intracellular granules in a process regulated by p38 MAPK.
*
This work was supported in part by grants from the
Department of Veterans Affairs (to K. R. M.), the American Heart
Association, Ohio Valley Affiliate (to K. R. M. and R. A. W.), and
the Jewish Hospital Foundation (to K. R. M. and R. A. W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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