Neuraminidase- and benzalkonium chloride-dependent inhibition of basic peptide-induced rat mast cell secretion.

Abstract:

: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.

journal_name

Immunol Lett

journal_title

Immunology letters

authors

Coleman JW

doi

10.1016/0165-2478(82)90134-1

subject

Has Abstract

pub_date

1982-10-01 00:00:00

pages

197-201

issue

4

eissn

0165-2478

issn

1879-0542

pii

0165-2478(82)90134-1

journal_volume

5

pub_type

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