title: Involvement of a serine protease in mast cell activation.
abstract: To examine the putative role of an endogenous serine esterase in mast cell activation, we have investigated the effect of inhibitors of, and substrates for, alpha-chymotrypsin in normal and permeabilized rat mast cells. These agents effectively blocked histamine release induced by anti-IgE, with an enhanced potency in permeabilized cells, but were ineffective against secretion evoked by compound 48/80. Activation of a chymotryptic enzyme, as evidenced by hydrolysis of a fluorescent substrate, was directly demonstrated following immunologic stimulation of permeabilized mast cells. No such activation was observed with compound 48/80. Immunologic stimulation also led to a significant increase in the total chymotryptic activity recoverable from the cells.
authors.affiliation: Department of Chemistry, University College London, UK.
authors.forename: B
authors.initials: B
authors.lastname: Emadi-Khiav
authors.forename: F L
authors.initials: FL
authors.lastname: Pearce
mesh_terms: D000818:Animals; D002499:Centrifugation, Density Gradient; D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000378:metabolism; D006636:Histamine Release / Q000187:drug effects; D007073:Immunoglobulin E / Q000276:immunology; D066298:In Vitro Techniques; D008407:Mast Cells / Q000201:enzymology / Q000502:physiology*; D010529:Peritoneal Cavity / Q000166:cytology; D051381:Rats; D012697:Serine Endopeptidases / Q000502:physiology*; D003189:p-Methoxy-N-methylphenethylamine / Q000494:pharmacology
chemical_list: D007073:Immunoglobulin E; D003189:p-Methoxy-N-methylphenethylamine; D012697:Serine Endopeptidases; D002918:Chymotrypsin