Tarro G
Proc Natl Acad Sci U S A. 1973 Feb;70(2):325-7. doi: 10.1073/pnas.70.2.325.
Trypsinization of normal human diploid cells (WI-38 and MRC 5) resulted in the appearance of complement-fixing reactivity with an immunoglobulin (anti-HeLa G globulin), prepared against a purified HeLa (malignant human) cell antigen (G), which reacts with various malignant human cell lines and tumors but not with certain normal human cells. The presence of receptors in the nonreacting, untrypsinized normal human cells and the specificity of the reactive groups that appeared after trypsinization was established by the fact that the antibody could be completely absorbed with large quantities of packed, untrypsinized human cells but not with similar quantities of either rabbit or guinea-pig kidney tissue-culture cells, which did not react with this antibody either before or after treatment with trypsin. The change produced by trypsinization is thus similar to the previously demonstrated appearance of reactive groups with the same anti-HeLa G globulin in normal human cells at certain times after infection with herpes simplex and vaccinia viruses. The fact that the trypsinized WI-38 cells absorbed more antibody than the same number of cells before trypsinization indicated that trypsinization resulted not only in the appearance of reactivity with antibody but also in a greater concentration of combining receptors, which is unlike the situation with lectins producing agglutinability without an increase in the number of receptors. Moreover, the fact that absorption with trypsinized normal cells removed larger amounts not only of the antibody reacting with the trypsin-treated WI-38 cells but also of antibody that reacts with WI-38 cells infected with herpes simplex virus and with the malignant HEp-2 cells, suggests that the combining groups that emerge after trypsinization of the normal human cells are the same or similar to those present in malignant human cells (HEp 2) and to those that emerge after infection of the normal human cells with herpes simplex virus.
对正常人二倍体细胞(WI - 38和MRC 5)进行胰蛋白酶处理后,出现了与一种免疫球蛋白(抗HeLa G球蛋白)的补体结合反应性,该免疫球蛋白是针对纯化的HeLa(人恶性)细胞抗原(G)制备的,它能与多种人恶性细胞系和肿瘤反应,但不与某些正常人细胞反应。未反应的、未经胰蛋白酶处理的正常人细胞中存在受体,且胰蛋白酶处理后出现的反应基团具有特异性,这一点可通过以下事实得以证实:该抗体可被大量密集的、未经胰蛋白酶处理的人细胞完全吸收,但不能被等量的兔或豚鼠肾组织培养细胞吸收,这些肾组织培养细胞无论在胰蛋白酶处理前还是处理后都不与该抗体反应。因此,胰蛋白酶处理所产生的变化类似于先前在单纯疱疹病毒和痘苗病毒感染后的特定时间,正常人细胞中出现的与相同抗HeLa G球蛋白反应的基团。胰蛋白酶处理后的WI - 38细胞比相同数量的未处理细胞吸收更多抗体,这一事实表明,胰蛋白酶处理不仅导致了与抗体反应性的出现,还导致了结合受体的浓度增加,这与凝集素产生凝集性但受体数量不增加的情况不同。此外,用胰蛋白酶处理的正常细胞进行吸收,不仅去除了与经胰蛋白酶处理的WI - 38细胞反应的大量抗体,还去除了与感染单纯疱疹病毒的WI - 38细胞以及恶性HEp - 2细胞反应的抗体,这表明正常人细胞经胰蛋白酶处理后出现的结合基团与人类恶性细胞(HEp 2)中存在的基团相同或相似,也与正常人细胞感染单纯疱疹病毒后出现的基团相同或相似。