Crago S S, Kulhavy R, Prince S J, Mestecky J
J Exp Med. 1978 Jun 1;147(6):1832-7. doi: 10.1084/jem.147.6.1832.
Epithelial cells of human fetal intestines and of a colonic carcinoma cell line (HT-29) exhibited intracellular and surface binding of polymeric immunoglobulins of IgA and IgM classes; monomeric IgA and IgG did not bind to these cells. Secretory component was identified as the receptor involved in the immunoglobulin binding. This conclusion was confirmed by the following experiments: trypsin abrogated the surface binding of polymeric immunoglobulin, reappearance of surface secretory component (SC) restored immunoglobulin binding; the appearance of SC in developing fetal tissues coincided with their potential to bind polymeric immunoglobulin; anti-SC reagents inhibited the binding of immunoglobulins to epithelial cells; and SC-containing secretory IgA did not bind to the surface of HT-29 cells.
人胎儿肠道上皮细胞和结肠癌细胞系(HT - 29)表现出细胞内和表面对IgA和IgM类聚合免疫球蛋白的结合;单体IgA和IgG不与这些细胞结合。分泌成分被鉴定为参与免疫球蛋白结合的受体。以下实验证实了这一结论:胰蛋白酶消除了聚合免疫球蛋白的表面结合,表面分泌成分(SC)的重新出现恢复了免疫球蛋白结合;发育中的胎儿组织中SC的出现与其结合聚合免疫球蛋白的潜力相一致;抗SC试剂抑制免疫球蛋白与上皮细胞的结合;含SC的分泌型IgA不与HT - 29细胞表面结合。