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Characterization of macrophage proteases involved in the ingestion of antigen—antibody complexes by the use of protease inhibitors
Author(s) -
Nagai Kenji,
Nakamura Tohoru,
Koyama Jiro
Publication year - 1978
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(78)80774-1
Subject(s) - chemistry , library science , computer science
The ingestion of antigen-antibody complexes preceding the intracellular digestion by phagocytes can be inhibited by potent inhibitors of serine esterases such as diisopropylphosphofluoridate (DFP), p-nitrophenyl phosphonates, cyclohexyl alkylphosphonofluoridates, and cyclohexyl phenylalkylphosphonofluoridates [ 1,2] . The available evidence suggests that active and/or stimulus-activated serine esterases are required for the process of ingestion. In order to characterize the serine esterases involved, it was attempted to study effects of various protease inhibitors with known specificities on the ingestive activity of guinea pig peritoneal macrophages against sensitized sheep erythrocytes [EA] . Among the inhibitors tested, DFP, 1-L-tosylamido-2-phenylethylchloromethylketone (TPCK), and chymostatin alone were found to reduce the ingestive activity of macrophages. These results are reported in this paper, indicating that the esterases required for the ingestion are presumably chymotrypsin-like proteases.