Cruchaud A, Berney M, Balant L
J Immunol. 1975 Jan;114(1 Pt 1):102-9.
The catabolism of completely endocytosed isologous and heterologous gamma-globulins by mouse macrophages was studied in vitro. Mouse, human, and rabbit 125-I-IgG were coupled to mouse, human, or sheep erythrocytes either as antibodies or by covalent binding. They were exposed to macrophages for 1 hr and the non-endocytosed erythrocytes were then removed with a Ficoll gradient centrifugation. Catabolism was evaluated after 2, 5, and 18 hr in culture by measuring the radioactivity released into the culture medium as well as the radioactivity that remained associated with cells. It was found that all iota-globulins were catabolized in a similar fashion, and that the type of carrier erythrocytes (isologous or heterologous) had no influence on catabolism. Some of the material that remained associated with macrophages was on the cell membrane and could be removed by trypsin. Some of the material that was released by macrophages was completely degraded but some was either not degraded or only partially degraded. Sucrose density gradient analysis and SDS-polyacrylamide gel electrophoresis showed that this material had kept some physical properties of native iota-globulins. It was also found with the antigen-binding inhibition test and incubation with erythrocytes that the released material contained molecules carrying Fab determinants and was able to bind specifically to erythrocytic antigens. Taken together, these observations show that iota-globulins phagocytosed in the form of antigen-antibody complexes are only incompletely degraded and that the material associated with plasma membrane of macrophages or found in the culture medium is a product of cell catabolism.
在体外研究了小鼠巨噬细胞对完全内吞的同源和异源γ-球蛋白的分解代谢。将小鼠、人及兔的125-I-IgG作为抗体或以共价结合的方式与小鼠、人或绵羊红细胞偶联。将它们与巨噬细胞接触1小时,然后用Ficoll梯度离心法去除未内吞的红细胞。通过测量释放到培养基中的放射性以及与细胞相关的放射性,在培养2、5和18小时后评估分解代谢情况。发现所有的iota-球蛋白均以相似的方式被分解代谢,并且载体红细胞的类型(同源或异源)对分解代谢没有影响。一些与巨噬细胞相关的物质位于细胞膜上,可被胰蛋白酶去除。巨噬细胞释放的一些物质被完全降解,但有些未被降解或仅部分降解。蔗糖密度梯度分析和SDS-聚丙烯酰胺凝胶电泳表明,该物质保留了天然iota-球蛋白的一些物理特性。通过抗原结合抑制试验以及与红细胞孵育还发现,释放的物质含有携带Fab决定簇的分子,并且能够特异性结合红细胞抗原。综上所述,这些观察结果表明,以抗原-抗体复合物形式吞噬的iota-球蛋白仅被不完全降解,并且与巨噬细胞质膜相关或存在于培养基中的物质是细胞分解代谢的产物。