Involvement of a serine protease in mast cell activation.
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.
Emadi-Khiav
B
B
Department of Chemistry, University College London, UK.
Pearce
F L
FL
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
D007073:Immunoglobulin E; D003189:p-Methoxy-N-methylphenethylamine; D012697:Serine Endopeptidases; D002918:Chymotrypsin