Inhibitory Effects of Sialic Acid- or N-Acetylglucosamine-Specific Lectins on Histamine Release Induced by Compound 48/80, Bradykinin and a Polyethylenimine in Rat Peritoneal Mast Cells

Abstract

ABSTRACT-The effects of seven lectins with various sugar-specificities on histamine release from rat peritoneal mast cells induced by non-immunologic stimuli were studied. The non-immunologic stimuli used were three basic secretagogues, compound 48/80, bradykinin and PEI6 (polyethylenimine with a molecular weight of 600). In this study, we observed inhibition of the histamine release by Macckia amurensis mitogen and Solanum tuberosum agglutinin (100 tg/ml at 371C for 10 min), which are specific for sialic acid-a2,3 N-acetyl galactosamine (Siaa2,3Ga1NAc) and N-acetyl glucosamine (G1cNAc) oligomers, respectively. The effects of Phytolacca americana mitogen and Sambucus sieboldiana agglutinin were different. Three lectins specific for mucin type oligosaccharides inhibited the histamine release induced by compound 48/80 but not that induced by bradykinin or PEI6. Since bradykinin and PEI6 additively enhanced the histamine release in duced by compound 48/80, they partially shared the same signalling pathways. Glycoproteins with bisecting GIcNAc and Sia residues, as described previously (Jpn. J. Pharmacol. 57, 79-90, 1991), seemed to be one of the action sites for compound 48/80, bradykinin and PEI6. In addition to the direct activation of the per tussis toxin-sensitive G proteins, we propose another mechanism of non-immunologic stimuli via specific glycoproteins on rat peritoneal mast cells. The apparent sugar residues involved were asparagine-linked oligosaccharides with Sia (especially Siaa2,3Gal), G1cNAc oligomers and/or bisecting G1cNAc.

Datura stramonium Agglutinin Released Histamine from Rat Peritoneal Mast Cells That Was Inhibited by Pertussis Toxin, Haptenic Sugar and N-Acetylglucosamine-Specific Lectins: Involvement of Glycoproteins with A-Acetylglucosamine Residues

“…In this study, we proposed that the binding of DSA to the corresponding glyco proteins resulted in histamine release and that WGA, STA and PWM inhibited it. These results were consistent with the inhibitory effects of lectins on the histamine release in duced by basic secretagogues (9,10). The binding of Con A to the glycoproteins including the IgE-IgE receptor complex, however, did not inhibit the histamine release induced by DSA, and a-MM, a haptenic sugar of Con A, was not inhibitory.…”

“…The cells were washed twice or three times and resuspended in fresh HEPES buffered Tyrode solution containing 0.3 mM Ca 2' and ex posed to DSA. Neuraminidase-treated mast cells were still active because they released histamine in the presence of Ca 21 ionophore A23187 as described previously (10). There was no detectable protease activity in the neuramini dase, using BZ-Arg-MCA (benzyl-L-arginine 4-methyl coumaryl-7-amide; Peptide Institute, Inc., Osaka) as a substrate.…”

“…They lack responsiveness to non-immunologic stimuli, although they begin to respond to compound 48/80 after co-cul ture with fibroblasts (8). Recently we reported that a 10 min incubation of specific lectins with rat peritoneal mast cells resulted in the inhibition of the histamine release in duced by compound 48/80, bradykinin and PEI6 (9,10). The inhibitory lectins for the histamine release induced by compound 48/80, bradykinin or PEI6 were WGA (9), PHA-E4 (9) and STA (10), as well as MAM (10).…”

“…Recently we reported that a 10 min incubation of specific lectins with rat peritoneal mast cells resulted in the inhibition of the histamine release in duced by compound 48/80, bradykinin and PEI6 (9,10). The inhibitory lectins for the histamine release induced by compound 48/80, bradykinin or PEI6 were WGA (9), PHA-E4 (9) and STA (10), as well as MAM (10). On the other hand Con A that recognizes sugar residues rich in mannose but not G1cNAc did not inhibit the histamine release induced by compound 48/80, bradykinin or PEI6.…”

An Initial Signal of Activation of Rat Peritoneal Mast Cells Stimulated by Datura stramonium Agglutinin: A Confocal Fluorescence Microscopic Analysis of Intracellular Calcium Ion and Cytoskeletal Assembly

“…They may occupy sugar residues of glycoproteins that serve as binding sites for DSA, which overlap one of the binding sites of compound 48/80, prevent access of DSA and compound 48/80 to the binding sites and inhibit the histamine release induced by DSA and compound 48/80 (1-3). Con A, however, did not interfere with the inter actions and did not inhibit the histamine release, since it recognizes high-mannose sugar-residues but not G1cNAc oligomer (1, 3).…”