Receptors for the Fc fragment of IgG on natural killer cells.
Receptors for the Fc fragment of IgG on natural killer cells.
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发表时间：
1993-07
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通讯作者：
G. Trinchieri;N. Valiante
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作者：
G. Trinchieri;N. Valiante
自然杀伤（NK）细胞能够通过其表面的CD16 - FcγRIIIA分子与免疫复合物IgG结合。这种相互作用激活NK细胞的裂解机制，并诱导活化细胞产生淋巴因子。CD16介导的NK细胞激活的确切分子基础仍不清楚；然而，近期的一些研究为未来的研究提供了框架。研究表明，NK细胞上的CD16受扰会引发这些细胞中的多种早期信号转导事件，例如多磷酸磷脂酰肌醇水解、[Ca2+]i升高和蛋白酪氨酸激酶激活。此外，在NK细胞中鉴定出与CD16复合的CD3 - ζ/η和/或FcεRI - γ多肽，这表明存在一种类似于针对T细胞受体和Fcε受体复合物所研究的信号转导机制。因此，现在应该从一种潜在的共同信号转导机制的角度来看待对这些受体复合物各自的研究。对所观察到的相似性和差异性进行比较，应该会对CD16介导的NK细胞激活显然所必需的复杂分子相互作用网络产生有价值的见解。
Natural killer (NK) cells are capable of binding to immune-complexed IgG via CD16-Fc gamma RIIIA molecules on their surface. This interaction activates the NK cell lytic mechanism and induces production of lymphokines by the activated cells. The exact molecular basis for CD16-mediated NK cell activation remains unclear; however, a number of recent studies have provided a framework for future research. It has been shown that CD16 perturbation on NK cells evokes a variety of early signal transduction events in these cells, such as polyphosphatidylinositol hydrolysis, [Ca2+]i increases and protein tyrosine kinase activation. Furthermore, the identification, of CD3-zeta/eta and/or Fc epsilon RI-gamma polypeptides complexed with CD16 in NK cells suggests a signal transduction mechanism analogous to those studied for the T cell receptor and Fc epsilon-receptor complexes. Therefore, research on each of these receptor complexes should now be viewed in light of a potential common signal transduction mechanism. Comparison of the similarities and differences observed should yield valuable insight into the complex network of molecular interactions apparently necessary for CD16-mediated NK cell activation.