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The effect of serine and thiol protease inhibitors on the chemiluminescence of human neutrophils in investigationsIn Vitro

✍ Scribed by Kantorski, J. ;Tchórzewski, H.

Publisher
John Wiley and Sons
Year
1992
Weight
563 KB
Volume
7
Category
Article
ISSN
0884-3996

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✦ Synopsis

We have studied an indirect role of serine and thiol proteases in the activation of human neutrophils in vitro. Stimulation was evaluated using a chemiluminescence (CL) generation system. Receptor-dependent and receptor-independent stimuli were studied, e.g. opsonized zymosan, formyl-methionyl-leucyl-phenylalanine, platelet activating factor, phorbol myristate acetate, and calcium ionophore A231 87. The serine protease inhibitors TPCK and TLCK, and thiol protease inhibitor PHMB, diminished the CL with different potencies and in a dose-dependent manner after treatment of cells with the various stimuli. Non-specific serine protease inhibitor, PMSF. and trypsin substrate TAME, showed a low inhibitory potency with respect t o CL generation. Synthetic substrates for chymotrypsin (BTEE. ATEE) significantly inhibited CL with the various stimuli used with some differences in susceptibility t o their inhibition. Specific chymotrypsin inhibitors diminished both the resting and activator-induced CL. We suggest that cell-bound chymotrypsin-like protease(s) is involved in the activation of signal transduction in human neutrophils after both receptor-dependent and receptorindependent stimulation.

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