Lipopolysaccharide primes human basophils for enhanced mediator release: requirement for plasma co-factor and CD14

Biochem Biophys Res Commun. 1994 Sep 15;203(2):1295-301. doi: 10.1006/bbrc.1994.2323.

Abstract

Lipopolysaccharide (LPS) is known to enhance IgE-mediated basophil degranulation. Recently, the complex of LPS and plasma LPS-binding protein(LBP) has been shown to induce secretory response via CD14 in monocytes and neutrophils. In the current study, we observed that the sensitivity to LPS of basophils was increased to 100-fold by co-incubation with plasma. LPS promptly completed its effect and amplified degranulation by stimuli bypassing IgE-receptors. Treatment with anti-CD14 completely abolished the priming effect of LPS. These results indicate that the priming effect of LPS on basophil mediator release is mediated via CD14, and that plasma co-factor, possibly identical to LBP, potentiates this reaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acute-Phase Proteins*
  • Antigens, CD / physiology*
  • Antigens, Differentiation, Myelomonocytic / physiology*
  • Arachidonic Acid / metabolism
  • Basophils / physiology*
  • Calcimycin / pharmacology
  • Carrier Proteins / physiology
  • Histamine Release
  • Humans
  • Immunoglobulin E / physiology
  • Kinetics
  • Lipopolysaccharide Receptors
  • Lipopolysaccharides / pharmacology*
  • Membrane Glycoproteins*
  • N-Formylmethionine Leucyl-Phenylalanine / pharmacology
  • Tetradecanoylphorbol Acetate / pharmacology

Substances

  • Acute-Phase Proteins
  • Antigens, CD
  • Antigens, Differentiation, Myelomonocytic
  • Carrier Proteins
  • Lipopolysaccharide Receptors
  • Lipopolysaccharides
  • Membrane Glycoproteins
  • lipopolysaccharide-binding protein
  • Arachidonic Acid
  • Immunoglobulin E
  • Calcimycin
  • N-Formylmethionine Leucyl-Phenylalanine
  • Tetradecanoylphorbol Acetate