Neuraminidase- and benzalkonium chloride-dependent inhibition of basic peptide-induced rat mast cell secretion.
Two types of inhibition of basic peptide-induced rat mast cell secretion are reported. Pretreatment of rat peritoneal mast cells with Vibrio comma neuraminidase, an enzyme which cleaves sialic acid from oligosaccharides, led to inhibition of 5-hydroxytryptamine release induced by the basic peptides polylysine, corticotropin 1-24 and a decapeptide sequence of human IgE. Inhibition was similarly observed when mast cells were challenged in the presence of the cationic cell membrane-active substance benzalkonium chloride. It is postulated that both of these experimental procedures inhibit basic peptide-induced secretion by depletion of cell surface negative charge. Sialic acid itself does not act as a specific receptor for basic peptides, since a molar excess of sialic acid in free solution failed to inhibit secretion by binding to basic peptides in the fluid phase.
D000818:Animals; D001548:Benzalkonium Compounds / Q000494:pharmacology*; D003366:Cosyntropin / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007073:Immunoglobulin E / Q000494:pharmacology; D008407:Mast Cells / Q000378:metabolism*; D009439:Neuraminidase / Q000494:pharmacology*; D010455:Peptides / Q000494:pharmacology*; D011107:Polylysine / Q000494:pharmacology; D051381:Rats; D012701:Serotonin / Q000378:metabolism*; D012794:Sialic Acids / Q000494:pharmacology
D001548:Benzalkonium Compounds; D010455:Peptides; D012794:Sialic Acids; D003366:Cosyntropin; D011107:Polylysine; D012701:Serotonin; D007073:Immunoglobulin E; D009439:Neuraminidase