Protease inhibition of natural killer (NK) and antibody-dependent cell-mediated cytoxicity (ADCC) activities.
The ability of protease inhibitors to modulate NK and ADCC cell activities was studied. NK and ADCC cell activities were suppressed by 1,10 phenanthroline (PHE), N-alpha-p-tosyl-L-lysine chloromethyl ketone (TLCK), L-1-tosylamide-2-phenylethylchoromethyl ketone (TPCK), N-benzoyl-DL-tyrosine ethyl ester (BTEE), and phenylethylchoromethyl fluoride (PMSF). The effect of these protease inhibitors on ADCC was not mediated through the early phase of cytotoxicity involving Fc-receptor binding, since they failed to alter EoxA rosetting of effector cells. The results suggest that an activated esterase system might play a role in the later phase of the cytotoxic mechanism by ADCC cells and perhaps NK cells.
D000818:Animals; D000920:Antibody-Dependent Cell Cytotoxicity / Q000187:drug effects*; D004121:Dimethyl Sulfoxide / Q000494:pharmacology; D000431:Ethanol / Q000494:pharmacology; D005260:Female; D006801:Humans; D066298:In Vitro Techniques; D007694:Killer Cells, Natural / Q000187:drug effects*; D011480:Protease Inhibitors / Q000494:pharmacology*; D051381:Rats; D011915:Rats, Inbred BUF; D011961:Receptors, Fc / Q000187:drug effects / Q000378:metabolism; D012397:Rosette Formation; D013154:Spleen / Q000187:drug effects
D011480:Protease Inhibitors; D011961:Receptors, Fc; D000431:Ethanol; D004121:Dimethyl Sulfoxide