Håkansson L, Venge P
Immunology. 1982 Dec;47(4):687-94.
The co-operation between the Fc and C3b receptors of PMNs (neutrophil granulocytes) during phagocytosis has been studied by the effect of interference with either of the receptors. The significance of the Fc receptor for the mediation of internalization proposed by previous investigators was confirmed by the inhibition of both Fc- and C3b-mediated phagocytosis by Fc fragments of IgG and by Fab fragments of antiserum against the Fc part of IgG. C3b-receptor-mediated phagocytosis was inhibited by trypsin, granulocyte elastase, myeloperoxidase and HO. High concentrations of elastase and the combined action of HO and myeloperoxidase generated a C3b-receptor dysfunction, which implied that the destruction of C3b-receptor function also disturbed Fc-receptor function. The demonstrated C3b receptor dysfunction indicated that the Fc and C3b receptors were closely situated in the cellular membrane of the PMN. A hypothesis for co-operation between the two receptor types would be that the C3b receptor initially facilitates the adherence of an IgG-C3b-coated particle. Secondly, the C3b receptor would facilitate the IgG-Fc-receptor contact either by some kind of structural derangement to permit the entrance of the IgG-C3b complex or by removal of C3b from the Fc part of IgG.
通过干扰多形核白细胞（中性粒细胞）的Fc受体和C3b受体中的任何一种，研究了吞噬作用期间这两种受体之间的合作。IgG的Fc片段以及抗IgG Fc部分的抗血清Fab片段对Fc介导和C3b介导的吞噬作用均有抑制，这证实了先前研究者提出的Fc受体在介导内化过程中的重要性。胰蛋白酶、粒细胞弹性蛋白酶、髓过氧化物酶和HO可抑制C3b受体介导的吞噬作用。高浓度的弹性蛋白酶以及HO和髓过氧化物酶的联合作用会导致C3b受体功能障碍，这意味着C3b受体功能的破坏也会干扰Fc受体功能。所证实的C3b受体功能障碍表明，Fc受体和C3b受体在多形核白细胞的细胞膜中紧密相邻。两种受体类型之间合作的一种假设是，C3b受体首先促进IgG-C3b包被颗粒的黏附。其次，C3b受体将通过某种结构紊乱以允许IgG-C3b复合物进入，或者通过从IgG的Fc部分去除C3b来促进IgG-Fc受体接触。
