Perussia B, Ravetch J V
Wistar Institute of Anatomy and Biology, Philadelphia, PA 19104.
Eur J Immunol. 1991 Feb;21(2):425-9. doi: 10.1002/eji.1830210226.
The low-affinity Fc receptor for immune-complexed IgG (Fc gamma RIII; CD16) present on in vitro cultured human monocytes are encoded by an Fc gamma RIII-2 gene that, by cDNA sequence analysis, is identical to that expressed on tissue macrophages and on natural killer cells. In macrophages, Fc gamma RIII-2 encodes a glycoprotein of 52-62 kDa, with a peptide backbone of 33 kDa identical to that of the homologous receptor on natural killer cells. Like this and unlike in polymorphonuclear neutrophils, Fc gamma RIII (CD16) on cultured monocytes is insensitive to phosphatidylinositol-specific phospholipase C, is not allelic for the neutrophil NA alloantigens NA-1/NA-2, is not recognized by a monoclonal antibody (1D3) detecting an epitope present only on neutrophil Fc gamma RIII (CD16) and functions to trigger cytotoxicity upon ligand binding.
体外培养的人单核细胞上存在的免疫复合物IgG低亲和力Fc受体（FcγRIII；CD16）由FcγRIII-2基因编码，通过cDNA序列分析，该基因与组织巨噬细胞和自然杀伤细胞上表达的基因相同。在巨噬细胞中，FcγRIII-2编码一种52-62 kDa的糖蛋白，其33 kDa的肽骨架与自然杀伤细胞上同源受体的肽骨架相同。与自然杀伤细胞上的情况一样且与多形核中性粒细胞不同，培养的单核细胞上的FcγRIII（CD16）对磷脂酰肌醇特异性磷脂酶C不敏感，不是中性粒细胞NA同种异体抗原NA-1/NA-2的等位基因，不被检测仅存在于中性粒细胞FcγRIII（CD16）上的表位的单克隆抗体（1D3）识别，并且在配体结合时具有触发细胞毒性的功能。
