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Role of serine esterases in mast cell activation
Author(s) -
Emadi Khiav B,
Pearce F L.
Publication year - 1998
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1038/sj.bjp.0701724
Subject(s) - histamine , mast cell , prostaglandin d2 , serine protease , biochemistry , cytosol , immunoglobulin e , enzyme , chemistry , protease , serine , stimulation , liberation , biology , prostaglandin , pharmacology , immunology , in vitro , endocrinology , antibody
1 A variety of chymotryptic substrates and inhibitors prevented the release of histamine and prostaglandin D 2 from rat peritoneal mast cells stimulated with anti‐IgE but not the calcium ionophore A23187 or a variety of polyamines. 2 The activity of the compounds was strikingly increased in cells reversibly permeabilized with ATP, indicating the importance of their effective incorporation into the cytosol. 3 The compounds produced a comparable inhibition of immunological, but not pharmacological, histamine release from human mast cells and basophils. 4 Treatment of rat mast cells with anti‐IgE led to a marked increase in the total chymotryptic activity expressed by the cells. 5 Immunological, but not pharmacological, stimulation of permeabilized rat mast cells loaded with a fluorescent chymotryptic substrate led to a pronounced and rapid increase in fluorescence, indicating activation of the enzyme and hydrolysis of the substrate. These changes were attenuated by chymotryptic inhibitors. 6 In total, these data provide compelling evidence for the direct involvement of a serine protease in IgE‐mediated histamine release from mast cells.British Journal of Pharmacology (1998) 123 , 1267–1273; doi: 10.1038/sj.bjp.0701724