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Role of the mitogen-activated protein kinases and tyrosine kinases during leukotriene B4-induced eosinophil activation.

Authors
  • Lindsay, M A
  • Haddad, E B
  • Rousell, J
  • Teixeira, M M
  • Hellewell, P G
  • Barnes, P J
  • Giembycz, M A
Type
Published Article
Journal
Journal of Leukocyte Biology
Publisher
Wiley
Publication Date
Oct 01, 1998
Volume
64
Issue
4
Pages
555–562
Identifiers
PMID: 9766637
Source
Medline
License
Unknown

Abstract

Exposure of guinea-pig eosinophils to leukotriene B4 (LTB4; 1 microM) resulted in a rapid generation of H2O2 (index of NADPH oxidase activation), stimulated [3H]arachidonic acid (AA) release (index of phospholipase A2 activity), and promoted CD18-dependent homotypic aggregation. Under similar conditions, LTB4 (1 microM) induced a rapid activation of extracellular-regulated kinases-1 and 2 (ERK-1/2) but not c-jun N-terminal kinases 46 and 54 (JNK-46/54) or p38 mitogen-activated protein kinase (p38 MAP kinase). To examine the role of ERK-1/2 in the mechanism of eosinophil activation, a selective inhibitor of MAP kinase kinase-1/2 (MEK-1/2), PD098059, was employed. However, PD 098059 at concentrations that attenuated ERK-1/2 activation had no significant affect on eosinophil activation. In contrast, a role for tyrosine kinases in LTB4-induced eosinophil activation was suggested by studies with the tyrosine kinase inhibitors, herbimycin A and lavendustin A. However, the results of those experiments implied divergent pathways for the control of eosinophil responses because the inhibitors were more effective at attenuating H2O2 generation than [3H]AA release, and had little effect on homotypic aggregation.

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