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J. Biol. Chem., Vol. 275, Issue 21, 15876-15884, May 26, 2000
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From the The adhesion molecules known as selectins mediate
the capture of neutrophils from the bloodstream. We have previously
reported that ligation and cross-linking of L-selectin on the
neutrophil surface enhances the adhesive function of
L-Selectin Signaling of Neutrophil Adhesion and Degranulation
Involves p38 Mitogen-activated Protein Kinase*
§,,
,,,, and Department of Pediatrics, Leukocyte Biology
Section, Baylor College of Medicine, Houston, Texas 77030-2600, the
¶ Department of Clinical Studies, Central Laboratory, The Royal
Veterinary and Agricultural University, DK-1870 Frederiksberg C,
Copenhagen, Denmark, the Department of Immunology and
Rheumatology, Merck Research Laboratories, Rahway, New Jersey 07065, and ** Biomedical Engineering, University of California,
Davis, California 95616-5294
2-integrins in a synergistic manner with
chemotactic agonists. In this work, we examined degranulation and
adhesion of neutrophils in response to cross-linking of L-selectin and
addition of interleukin-8. Cross-linking of L-selectin induced priming
of degranulation that was similar to that observed with the alkaloid
cytochalasin B. Activation mediated by L-selectin of neutrophil shape
change and adhesion through CD11b/CD18 were strongly blocked by Merck
C, an imidazole-based inhibitor of p38 mitogen-activated protein kinase
(MAPK), but not by a structurally similar non-binding regioisomer.
Priming by L-selectin of the release of secondary, tertiary, and
secretory, but not primary, granules was blocked by inhibition of p38
MAPK. Peak phosphorylation of p38 MAPK was observed within 1 min of
cross-linking L-selectin, whereas phosphorylation of ERK1/2 was highest
at 10 min. Phosphorylation of p38 MAPK, but not ERK1/2, was inhibited
by Merck C. These data suggest that signal transduction as a
result of clustering L-selectin utilizes p38 MAPK to effect neutrophil
shape change, integrin activation, and the release of secondary,
tertiary, and secretory granules.
*
This work was supported by National Institutes of Health
Grants R01 DK 32471 (to J. E. S.), R01 HL42550 (C. Wayne
Smith, Director, Leukocyte Biology Section), and R01 AI 31652 (to
S. I. S.), the Whitaker Foundation (to S. I. S.),
and American Heart Association Established Investigator Award 9640162N
(to S. I. S.).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.
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