Mast cells and basophils are known to be triggered by allergens via cr
oss-linking with their high-affinity IgE-binding receptors, Fc epsilon
RI. The anaphylatoxic activity of the complement-derived peptides C3a
and C5a has been known for a long time; however, it has also been rep
orted that serosal- and mucosal-type mast cells respond differently to
peptidergic stimuli. The mechanism of mast cell activation by cross-l
inking of Fc epsilon RI has been the subject of intensive studies in t
he past few years, while the action mode of the anaphylatoxic compleme
nt peptides has been revealed only recently. We report about a novel f
unction of C3a: its inhibitory activity on IgE-mediated triggering of
the mucosal RBL-2H3 cells. Surprisingly, the other anaphylatoxic pepti
de C5a, which has been shown to be significantly more effective in sev
eral biological assays, did not influence antigen-induced triggering o
f the RBL-2H3 cell line at all.