Target-effector interaction in the human and murine natural killer system: specificity and xenogeneic reactivity of the solubilized natural killer-target structure complex and its loss in a somatic cell hybrid.
Target-effector interaction in the human and murine natural killer system: specificity and xenogeneic reactivity of the solubilized natural killer-target structure complex and its loss in a somatic cell hybrid.
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人和鼠类天然杀手级系统中的靶向效应相互作用:溶解的天然杀手靶结构复合物的特异性和异类反应性及其在体细胞杂种中的损失。
DOI:
10.1084/jem.150.3.471
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发表时间:
1979-09-19
期刊:
影响因子:
--
通讯作者:
Jondal M
中科院分区:
文献类型:
--
作者:
Roder JC;Ahrlund-Richter L;Jondal M
Preincubation of natural killer (NK) cells with electrophoresis purified proteins from a variety of NK-sensitive murine and human tumor cells specifically prevented subsequent binding to the intact, homologous target cell. The NK-target structures (NK-TS) consisted of some or all of four characteristic molecular species, tentatively assigned molecular weights of 140K, 160K, 190K, and 240K (+/-10K) based on electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gels. When these NK-TS molecules were compared in cross-inhibition assays, the large 240K molecule most often carried the unique NK specificity, whereas the smaller 140K molecules cross-reacted between YAC, 136-6 and X-63 in the mouse and between Molt-4 and K562 in the human. Mouse NK cells recognised a different spectrum of NK-TS molecules than human NK cells. The control of NK-TS expression was partially revealed in a cloned, somatic cell hybrid bwtween an NK sensitive (YAC-IR) and insensitive (A9HT) cell line. The hybrid did not express NK-TS and did not bind to NK cells which is in accordance with negative NK cytolytic results previously reported. Although unique specificities are carried by some of the multiple NK-TS protein molecules, cross-reactions were widespread. These observations taken together suggest that the NK cell is polyspecific and has some heterogeneity in the recognition structure although much less than would be expected of an antibody-combining site.