An antigen-activated DFP-inhibitable enzyme controls basophil densensitization

W. Kazimierczak, H. L. Meier, D. W. MacGlashan, L. M. Lichtenstein

Research output: Contribution to journalArticle

Abstract

Diisopropyl fluorophosphate (DFP), an inhibitor of serine esterases, enhances IgE-mediated histamine release from human basophils and blocks the desensitization process (i.e., the antigen-induced hyporesponsiveness) in these cells. Both activities occur at relatively low concentrations of DFP (0.1 to 0.5 mM) and are dependent on an antigen-activated intracellular event: if DFP is removed before antigen addition, it has neither effect. Neither hydrolyzed DFP nor the non-phosphorylating diisopropyl methyl phosphate enhanced histamine release or blocked desensitization. In addition to providing a demonstrable biochemical correlate of desensitization, our data suggest that the desensitization process controls the release of mediators of allergic reactions.

Original languageEnglish (US)
Pages (from-to)399-405
Number of pages7
JournalJournal of Immunology
Volume132
Issue number1
StatePublished - Jan 1 1984

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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  • Cite this

    Kazimierczak, W., Meier, H. L., MacGlashan, D. W., & Lichtenstein, L. M. (1984). An antigen-activated DFP-inhibitable enzyme controls basophil densensitization. Journal of Immunology, 132(1), 399-405.