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.
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