Unkeless J C, Wright S D
Contemp Top Immunobiol. 1984;14:171-87. doi: 10.1007/978-1-4757-4862-8_6.
Recent experiments have revealed the structure of some phagocytosis-promoting receptors. The C3b receptor is a single-chain membrane glycoprotein of Mr 205,000, while the C3bi receptor is composed of two surface glycoprotein chains, of Mr 180,000 and 100,000. Fc receptors all appear to be single-chain glycoproteins of approximately Mr 50,000. Despite this structural similarity, Fc receptors display a broad range of heterogeneity with respect to ligand specificity. One type of Fc receptor (Fc gamma 2b/gamma 1R) appears to function as a ligand-dependent ion channel; the ion flux initiated by the ligation of this receptor may represent the proximal signal sent by this Fc receptor. The second signal sent by other Fc receptors and by the C3 receptors is uncharacterized, except for the observation that the second signal generated by C3 receptors is distinct from that of Fc gamma 2b/gamma 1R.
最近的实验揭示了一些促进吞噬作用的受体的结构。C3b受体是一种分子量为205,000的单链膜糖蛋白,而C3bi受体由两条表面糖蛋白链组成,分子量分别为180,000和100,000。Fc受体似乎都是分子量约为50,000的单链糖蛋白。尽管结构相似,但Fc受体在配体特异性方面表现出广泛的异质性。一种类型的Fc受体(Fcγ2b/γ1R)似乎作为配体依赖性离子通道发挥作用;该受体的结合引发的离子通量可能代表该Fc受体发出的近端信号。除了观察到C3受体产生的第二信号与Fcγ2b/γ1R的不同之外,其他Fc受体和C3受体发出的第二信号尚未明确。