Coupland K, Leslie R G
Immunology. 1983 Apr;48(4):647-56.
The equilibrium binding of soluble complexes of guinea-pig anti-dinitrophenyl IgG1 or IgG2 and dinitrophenylated bovine serum albumin (DNPBSA) to homologous peritoneal macrophages and neutrophils has been compared. The immunoglobulin receptors on these phagocytes were found to differ in two major respects. Macrophages express specific binding activity for both IgG1 and IgG2 complexes whereas neutrophils possess specificity only for the IgG2 subclass. Furthermore, the number of receptors for IgG2 on macrophages (0.8-1 x 10(6)) is fifty- to seventy-fold greater than the number on neutrophils (1.3-2.6 x 10(4)). The phagocytes also displayed differences in their avidity for soluble IgG2-containing complexes which could either reflect the disparity in receptor densities on their membranes or indicate differences in the structure of their Fc receptors. Inhibition of complex binding by immunoglobulin fragments indicated that, at least, the macrophages and neutrophils recognize the same portion of the IgG2 molecule.
已对豚鼠抗二硝基苯基IgG1或IgG2与二硝基苯基化牛血清白蛋白(DNPBSA)的可溶性复合物与同源腹膜巨噬细胞和中性粒细胞的平衡结合进行了比较。发现这些吞噬细胞上的免疫球蛋白受体在两个主要方面存在差异。巨噬细胞对IgG1和IgG2复合物均表现出特异性结合活性,而中性粒细胞仅对IgG2亚类具有特异性。此外,巨噬细胞上IgG2受体的数量(0.8 - 1×10⁶)比中性粒细胞上的数量(1.3 - 2.6×10⁴)大五十至七十倍。吞噬细胞对含可溶性IgG2复合物的亲和力也存在差异,这可能反映了其膜上受体密度的差异,或者表明其Fc受体结构存在差异。免疫球蛋白片段对复合物结合的抑制表明,至少巨噬细胞和中性粒细胞识别IgG2分子的同一部分。