Trinchieri G, Valiante N
Wistar Institute of Anatomy and Biology, Philadelphia, Pa 19104.
Nat Immun. 1993 Jul-Oct;12(4-5):218-34.
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.
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细胞活化的确切分子基础尚不清楚；然而，最近的一些研究为未来的研究提供了一个框架。研究表明，NK细胞上的CD16扰动会在这些细胞中引发多种早期信号转导事件，如多磷酸肌醇水解、[Ca2+]i增加和蛋白酪氨酸激酶活化。此外，在NK细胞中鉴定出与CD16复合的CD3-ζ/η和/或FcεRI-γ多肽，提示了一种类似于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的研究。对观察到的异同进行比较，应该能够对CD16介导的NK细胞活化显然所需的复杂分子相互作用网络产生有价值的见解。
