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Effects of DDT and triclosan on tumor‐cell binding capacity and cell‐surface protein expression of human natural killer cells
Author(s) -
HurdBrown Tasia,
Udoji Felicia,
Martin Tamara,
Whalen Margaret M.
Publication year - 2013
Publication title -
journal of applied toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.784
H-Index - 87
eISSN - 1099-1263
pISSN - 0260-437X
DOI - 10.1002/jat.2767
Subject(s) - lytic cycle , cd16 , cell , cytotoxicity , function (biology) , natural killer cell , chemistry , cell function , microbiology and biotechnology , biology , biochemistry , immunology , in vitro , antigen , cd8 , virus , cd3
ABSTRACT 1,1,1‐trichloro‐2,2‐bis(4‐chlorophenyl)ethane (DDT) and triclosan (TCS) are organochlorine (OC) compounds that contaminate the environment, are found in human blood and have been shown to decrease the tumor‐cell killing (lytic) function of human natural killer (NK) cells. NK cells defend against tumor cells and virally infected cells. They bind to these targets, utilizing a variety of cell surface proteins. The present study examined concentrations of DDT and TCS that decrease lytic function for alteration of NK binding to tumor targets. Levels of either compound that caused loss of binding function were then examined for effects on expression of cell‐surface proteins needed for binding. NK cells exposed to 2.5 μM DDT for 24 h (which caused a greater than 55% loss of lytic function) showed a decrease in NK binding function of about 22%, and a decrease in CD16 cell‐surface protein of 20%. NK cells exposed to 5 μM TCS for 24 h showed a decrease in ability to bind tumor cells of 37% and a decrease in expression of CD56 of about 34%. This same treatment caused a decrease in lytic function of greater than 87%. These results indicated that only a portion of the loss of NK lytic function seen with exposures to these compounds could be accounted for by loss of binding function. They also showed that loss of binding function is accompanied by a loss of cell‐surface proteins important in binding function. Copyright © 2012 John Wiley & Sons, Ltd.