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Direct evidence for release of pore‐forming protein during NK cellular lysis
Author(s) -
Ortaldo John R.,
WinklerPickett Robin T.,
Nagashima Kunio,
Yagita Hideo,
Okumura Kb
Publication year - 1992
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.52.5.483
Subject(s) - exocytosis , effector , biology , cytotoxicity , lysis , microbiology and biotechnology , cytolysis , secretion , monoclonal antibody , k562 cells , cell , lymphokine activated killer cell , natural killer cell , antibody , biophysics , immunology , cytotoxic t cell , biochemistry , in vitro , interleukin 21
In the present study, we have examined the exocytosis model for cellular lysis. Using monoclonal antibodies reactive with human pore‐forming protein (PFP), we examined the localization of PFP at the interaction site of natural killer (NK) cells and the NK tumor targets K562 and Molt‐4 as well as during antibody‐ dependent cellular cytotoxicity. Following the interaction of effector‐target cell contact, an increased frequency of PFP was detected on the effector surface, in the micro‐ environment, and on the target surface of the interaction site. This temporal deposition of PFP was paralleled by loss of target cell integrity and release of chromium. In addition, selective deposition of PFP was seen at the interaction site of the target cell compared to other target cell regions. Collectively, these results are consistent with the exocytosis model and further support the hypothesis that PFP is one of the secreted moieties involved in NK cellular cytotoxicity