Uher F, Dobronyi I, Gergel J
Immunology. 1981 Mar;42(3):419-25.
The features and function of IgM-FcR of rat peritoneal macrophages were studied. Macrophages specifically bind and phagocytose ox red blood cells coated with rat IgM (EA-IgM) through a specific receptor. This receptor is trypsin sensitive and its activity requires Ca++ ions. Both sodium azide and low temperature (4 degrees) inhibit the bindings as well as ingestion of EA-IgM by macrophages, suggesting the metabolically dependent character of the interaction between EA-IgM and macrophages. Colchicine inhibits the binding of EA-IgM by macrophages. Similarly, the ingestion of EA-IgM was also inhibited when peritoneal exudate cells (PEC) were pre-treated with colchicine or vinblastine or cytochalasin B. It is suggested that cytoskeletal elements of macrophages play an important role both in the binding of EA-IgM to their receptors and in the subsequent internalization of the receptor-ligand complexes. Ingestion of soluble IgM antibodies containing immune complexes (IC) resulted in a release of beta-glucuronidase from macrophages.
对大鼠腹腔巨噬细胞的IgM - FcR的特征和功能进行了研究。巨噬细胞通过一种特异性受体特异性结合并吞噬包被有大鼠IgM的氧合红细胞（EA - IgM）。该受体对胰蛋白酶敏感，其活性需要Ca++离子。叠氮化钠和低温（4℃）均抑制巨噬细胞对EA - IgM的结合以及摄取，提示EA - IgM与巨噬细胞之间相互作用具有代谢依赖性。秋水仙碱抑制巨噬细胞对EA - IgM的结合。同样，当腹腔渗出细胞（PEC）用秋水仙碱、长春碱或细胞松弛素B预处理时，EA - IgM的摄取也受到抑制。提示巨噬细胞的细胞骨架成分在EA - IgM与其受体的结合以及随后受体 - 配体复合物的内化过程中均起重要作用。摄取含有免疫复合物（IC）的可溶性IgM抗体导致巨噬细胞释放β - 葡萄糖醛酸酶。
