Cytokine-induced protein tyrosine phosphorylation is essential for cytokine priming of human eosinophils

J Allergy Clin Immunol. 1998 Jan;101(1 Pt 1):103-9. doi: 10.1016/S0091-6749(98)70200-3.

Abstract

Background: Human eosinophils are strongly modulated by the eosinophilotrophic cytokines IL-5, IL-3, and granulocyte-macrophage colony-stimulating factor (GM-CSF). A clear intracellular effect of these cytokines is the induction of tyrosine phosphorylation of multiple cellular substrates. However, the relevance of tyrosine phosphorylation for eosinophil functioning has not been established.

Objective: In this study we have investigated dose-response and time curves of IL-5-, IL-3-, and GM-CSF-induced tyrosine phosphorylation in eosinophils. Moreover, we have evaluated the importance of IL-5-induced tyrosine phosphorylation for priming of human eosinophils.

Methods: Cytokine-induced tyrosine phosphorylation was monitored on western blot with an antiphosphotyrosine antibody (4G10). To probe the relevance of tyrosine phosphorylation for priming, eosinophils were primed with IL-5 in the presence of the tyrosine kinase inhibitor herbimycin A. Platelet activating factor (PAF) was used as a control priming agent. Subsequently, the eosinophils were incubated with serum-treated zymosan (STZ) to activate the respiratory burst. Binding of STZ was determined by FACS analysis.

Results: IL-5-, IL-3-, and GM-CSF-induced tyrosine phosphorylation was found at concentrations that primed eosinophil effector mechanism (median effective dose values: approximately 5.10(-11) mol/L, approximately 5.10(-10) mol/L, and approximately 5.10(-12) mol/L for IL-5, IL-3, and GM-CSF, respectively). Cytokine-induced tyrosine phosphorylation was transient with an optimum value at 15 minutes. IL-5 priming of STZ-induced activation of the respiratory burst was blocked by herbimycin A, whereas PAF still primed this response. In fact, herbimycin A inhibited IL-5 priming of STZ binding to human eosinophils. On the other hand, PAF priming of STZ binding was not affected by herbimycin A. Both IL-5-induced and PAF-induced tyrosine phosphorylation were inhibited by herbimycin A.

Conclusion: These data demonstrate for the first time that IL-5 priming of opsonized particle-induced responses is mediated by tyrosine kinase activity in human eosinophils.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Benzoquinones
  • Cytokines / pharmacology*
  • Enzyme Inhibitors / pharmacology
  • Eosinophils / drug effects*
  • Eosinophils / immunology
  • Eosinophils / metabolism*
  • Granulocyte-Macrophage Colony-Stimulating Factor / pharmacology
  • Humans
  • In Vitro Techniques
  • Interleukin-3 / pharmacology
  • Interleukin-5 / pharmacology
  • Lactams, Macrocyclic
  • Phosphorylation
  • Platelet Activating Factor / pharmacology
  • Protein-Tyrosine Kinases / antagonists & inhibitors
  • Protein-Tyrosine Kinases / metabolism
  • Proteins / metabolism
  • Quinones / pharmacology
  • Respiratory Burst / drug effects
  • Rifabutin / analogs & derivatives
  • Tyrosine / metabolism*
  • Zymosan / metabolism

Substances

  • Benzoquinones
  • Cytokines
  • Enzyme Inhibitors
  • Interleukin-3
  • Interleukin-5
  • Lactams, Macrocyclic
  • Platelet Activating Factor
  • Proteins
  • Quinones
  • Rifabutin
  • Tyrosine
  • herbimycin
  • Granulocyte-Macrophage Colony-Stimulating Factor
  • Zymosan
  • Protein-Tyrosine Kinases