Yokota T, Otsuji E, Noguchi A, Yamaguchi T, Sawai K, Takahashi T
First Department of Surgery, Kyoto Prefectural University of Medicine, Japan.
Int J Cancer. 1989 Dec 15;44(6):1095-9. doi: 10.1002/ijc.2910440626.
We studied antigenic modulation and internalization of monoclonal antibody (MAb) A7 using the enzyme-linked immunosorbent assay (ELISA) and biotin-labelled antibody-staining techniques. Incubation of the colonic SW1116 cell line with an excess of MAb A7 induced modulation of the cell-surface antigen. When the line was assayed by ELISA, a change in cellular reactivity with MAb A7 was seen after 1 hr. After 24 hr, the cellular reactivity showed a 52% decrease in absorbance. Modulation was inhibited by 0.1% sodium azide and acetone fixation, suggesting that this is an energy-dependent phenomenon. The internalization of biotinylated MAb A7 was examined. Internalized biotinylated MAb A7 was detected in cells fixed before labelling with avidin-biotin peroxidase complex. It was observed that the amount of MAb A7 which remained associated with the cell surface had decreased since A7 was internalized.
我们使用酶联免疫吸附测定（ELISA）和生物素标记抗体染色技术研究了单克隆抗体（MAb）A7的抗原调变和内化。用过量的MAb A7孵育结肠SW1116细胞系可诱导细胞表面抗原的调变。当用ELISA检测该细胞系时，1小时后可见细胞与MAb A7的反应性发生变化。24小时后，细胞反应性的吸光度下降了52%。0.1%叠氮化钠和丙酮固定可抑制调变，提示这是一种能量依赖现象。我们检测了生物素化MAb A7的内化。在用抗生物素蛋白-生物素过氧化物酶复合物标记之前固定的细胞中检测到了内化的生物素化MAb A7。观察到，由于A7被内化，与细胞表面保持结合的MAb A7量减少。
