THE FC-GAMMA RECEPTOR OF NATURAL-KILLER CELLS IS A PHOSPHOLIPID-LINKED MEMBRANE-PROTEIN
THE FC-GAMMA RECEPTOR OF NATURAL-KILLER CELLS IS A PHOSPHOLIPID-LINKED MEMBRANE-PROTEIN
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DOI：
10.1038/333568a0
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发表时间：
1988-06-09
期刊：
影响因子：
64.8
通讯作者：
SEED, B
中科院分区：
文献类型：
--
作者：
SIMMONS, D;SEED, B
Fc的三种受体已经描述了人免疫球蛋白G的（恒定）区1，2; FcRI，一种高亲和力的（Ka 108 M −1）受体在单核细胞上表达3 -5; FcRII（CD 32），一种低亲和力的在B细胞、粒细胞、巨噬细胞和血小板上表达的（Ka 106 M −1）受体6 -9;和FcRIII（CD 16，FcR 10），一种在巨噬细胞、嗜中性粒细胞、嗜酸性粒细胞、自然杀伤细胞和被认为包含抑制细胞的T细胞亚群上表达的低亲和力受体10 -13。抗CD 16抗体阻断天然宿主细胞介导的抗体依赖性细胞毒性（ADCC）14，15。聚集的IgG与自然杀伤细胞上的CD 16的结合导致淋巴细胞活化抗原的表达、介质释放、形态学变化和溶解活性16 -18。我们在这里报告的分离的互补DNA克隆编码CD 16决定簇，产生预期的亲和力和亚型特异性的IgG结合在COS细胞中，并证明编码磷脂锚定蛋白。在所有阳性RNA样品中均发现单个信使RNA转录物，N-聚糖酶处理显示COS细胞中发现的形式与外周血单核细胞（PBMC）上存在的形式相同。我们还发现CD 16与鼠IgG 2b/l受体的α-形式关系最密切，并提出细胞外接触介导IgG结合引发的信号。
Three types of receptor for the Fc (constant) region of human immunoglobulin G have been described1,2; FcRI, a high-affinity (Ka≈108M−1) receptor expressed on monocytes3–5; FcRII (CD32), a low-affinity (Ka≈106M−1) receptor expressed on B cells, granulocytes, macrophages and platelets6–9; and FcRIII (CD 16, FcR10), a low-affinity receptor expressed on macrophages, neutrophils, eosinophils, natural killer cells and a subset of T cells believed to comprise the suppresssor cells10–13. Anti-CD 16 anti-bodies block natural killer-cell mediated antibody dependent cellular cytotoxicity (ADCC)14,15. Binding of aggregated IgG to CD 16 on natural killer cells leads to the expression of lymphocyte activation antigens, mediator release, morphological changes and lytic activity16–18. We report here the isolation of a complementary DNA clone encoding CD 16 determinants which gave rise to IgG binding of the expected affinity and subtype specificity in COS cells, and which proved to encode a phospholipid anchored protein. A single messenger RNA transcript was found in all positive RNA samples, and N-glycanase treatment showed the form found in COS cells was identical to the form present on peripheral blood mononuclear cells (PBMCs). We also show that CD 16 is most closely related to the α-form of the murine IgG 2b/l receptor and propose that extracellular contacts mediate the signal initiated by IgG binding.