ABSTRACT-The histamine release induced by compound 48/80, bradykinin or polyethylenimine with a molecular weight of 600 (PEI6) was inhibited by wheat germ agglutinin (WGA) and phytohemagglutinin E-subunits (PHA-E4), and the inhibition was specifically reversed by N-acetyl glucosamine and N-acetyl galactosamine, respec tively. Concanavalin A (Con A) and phytohemagglutinin L-subunits (PHA-L4) did not inhibit the histamine release induced by compound 48/80, bradykinin or PEI6. The histamine release induced by substance P was also inhibited sugar-specifically by WGA and PHA-E4. The binding sites for compound 48/80, bradykinin, PEI6 and sub stance P, therefore, seemed to especially overlap each other. These binding sites were found to be glycoproteins having affinities to WGA and PHA-E4, but not to Con A and PHA-L4. The binding of WGA and PHA-E4 to the glycoproteins resulted in inhibition of the interaction between the basic secretagogues including bradykinin and substance P and their binding sites on the mast cells. The bindings of five lectins to mast cell glycoproteins were examined by lectin-blotting. Several glycoproteins, which had specific affinities to WGA and PHA-E4, but not to Con A and PHA-L4 were de tected. We assumed that the binding sites for basic secretagogues which are coupled with histamine-releasing mechanisms exist among these glycoproteins. A 41-kDa pro tein (a-subunit of pertussis toxin-sensitive G protein) was not detected by WGA, sug gesting that the binding sites for the basic secretagogues were not G proteins.Stimulus-secretion coupling mechanisms in rat peritoneal mast cells are thought to involve G proteins, because GTP-analogues enhanced histamine release (1). Moreover, histamine re lease induced by compound 48/80 or brady kinin is inhibited by pertussis toxin, but that induced by antigen or anti-IgE is not (2-4). We found that the histamine release induced by polyethylenimine (MW = 600, PEI6) was inhibited by pertussis toxin (5). Compound 48/80, bradykinin and polyethylenimine are all basic secretagogues. There is, however, no similarity in their chemical structures. The ac tion sites for compound 48/80 on the plasma