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

Mark A. Lindsay, El Bdaoui Haddad, Jonathan Rousell, Mauro M. Teixeira, Paul G. Hellewell, Peter J. Barnes, Mark A. Giembycz

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36 Citations (SciVal)

Abstract

Exposure of guinea-pig eosinophils to leukotriene B4 (LTB4; 1 μM) 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 μM) induced a rapid activation of extracellular- regulated kinases-1 and 2 (ERK- 1/4 ) 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- 1/4 in the mechanism of eosinophil activation, a selective inhibitor of MAP kinase kinase- 1/4 (MEK- 1/4 ), PD098059, was employed. However, PD 098059 at concentrations that attenuated ERK- 1/4 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.

Original languageEnglish
Pages (from-to)555-562
Number of pages8
JournalJournal of Leukocyte Biology
Volume64
Issue number4
DOIs
Publication statusPublished - 1 Oct 1998

Keywords

  • Homotypic aggregation
  • NADPH oxidase
  • Phospholipase A

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Cell Biology

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