Two types of
IgE receptors,
Fc epsilon receptor I (
Fc epsilon RI) and
Fc epsilon receptor II (
Fc epsilon RII), are known to be involved in
IgE-mediated
allergy.
Fc epsilon RI is expressed on mast cells and basophils, and cross-linkage of
Fc epsilon RI leads to the release of chemical mediators from these cells.
Fc epsilon RI consists of alpha, beta and gamma chains, and cDNAs encoding these chains were recently cloned.
Fc epsilon RII is expressed on various cells such as mature mu+delta+ B cells and activated monocytes and eosinophils. The
cDNA encoding B cell
Fc epsilon RII was cloned by several groups including ours, and
Fc epsilon RII was found to be a single chain receptor expressed with its N-terminal inside the cells, homologous to C-type
animal lectins. Subsequently, we identified two species of
Fc epsilon RII, Fc epsilon RIIb, whose structures differ only at the N-terminal cytoplasmic region but share the same C-terminal extracellular region. These two receptors are generated utilizing different transcriptional initiation sites and 5' exons. Fc epsilon RIIa is constitutively expressed only on B cells. While Fc epsilon RIIb is inducible by
IL-4 on B cells, monocytes and eosinophils. By employing transformants expressing Fc epsilon RIIa or Fc epsilon RIIb, it was demonstrated that Fc epsilon RIIa is involved in
IgE-mediated endocytosis, whereas Fc epsilon RIIb functions in
IgE-dependent phagocytosis.(ABSTRACT TRUNCATED AT 250 WORDS)