Yamamoto K, Sugita N, Kobayashi T, Okuda K, Van De Winkel J G, Yoshie H
Department of Periodontology, Faculty of Dentistry, Niigata University, Niigata, Japan.
Tissue Antigens. 2001 Apr;57(4):363-6. doi: 10.1034/j.1399-0039.2001.057004363.x.
Immunoglobulin G Fc receptor IIIb (FcgammaRIIIb) is constitutively expressed on neutrophils, and has three allelic forms: FcgammaRIIIb-NA1, FcgammaRIIIb-NA2, and FcgammaRIIIb-SH. We identified two Japanese subjects in whom an A to G substitution at nt 221 changes asparagine (N) to serine (S) at amino acid position 45 in the FcgammaRIIIb-NA2 gene. FcgammaRIIIb-NA2-specific monoclonal antibodies (GRM1 and PEN1) did not bind to mutant neutrophils, which lack an N-linked glycosylation site. Furthermore, IgG3-mediated neutrophil phagocytosis by mutant was slightly increased as compared to wild-type donors (Note).
免疫球蛋白G Fc受体IIIb（FcγRIIIb）在中性粒细胞上组成性表达，有三种等位基因形式：FcγRIIIb-NA1、FcγRIIIb-NA2和FcγRIIIb-SH。我们在两名日本受试者中发现，FcγRIIIb-NA2基因中第221位核苷酸处的A到G替换导致第45位氨基酸处的天冬酰胺（N）变为丝氨酸（S）。FcγRIIIb-NA2特异性单克隆抗体（GRM1和PEN1）不与缺乏N-连接糖基化位点的突变中性粒细胞结合。此外，与野生型供体相比，突变体中IgG3介导的中性粒细胞吞噬作用略有增加（注）。
