Cross-linking of the β2 integrin, CD11b/CD18, on human eosinophils induces protein tyrosine phosphorylation and cellular degranulation

Masahiko Kato, Hirohito Kita, Kenichi Tokuyama, Akihiro Morikwa

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Adhesion molecules, including integrins, play an important role in the selective recruitment of eosinophils. It has recently been shown that integrins also modulate the functions of eosinophils. Here, we tested the hypothesis that cross-linking of the β2 integrin, α(M)β2 (Mac-1, CD11b/CD18), leads to intracellular signaling events such as activation of protein tyrosine kinases leading to eosinophil degranulation. Cross-linking of cell surface CD11b/CD18 with anti-CD11b antibody and goat anti-mouse IgG immobilized onto the plate triggered tyrosine phosphorylation of several intracellular proteins, including the one with a 115-kD molecular mass (pp115). The same stimulus also provoked degranulation of eosinophils. These findings suggest that engagement of β2 integrin on eosinophils triggers the activation of intracellular signaling cascade which leads to cellular degranulation.

Original languageEnglish (US)
Pages (from-to)68-71
Number of pages4
JournalInternational archives of allergy and immunology
Volume117
Issue numberSUPPL. 1
DOIs
StatePublished - Sep 1998

Keywords

  • Degranulation
  • Eosinophil
  • Integrin
  • Signal transduction
  • Tyrosine kinase

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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