Weber E, Günther D, Laube F, Wiederanders B, Kirschke H
Institute of Physiological Chemistry, Medical Faculty, Martin-Luther-University, Halle (Saale), Germany.
J Cancer Res Clin Oncol. 1994;120(9):564-7. doi: 10.1007/BF01221037.
Several tumour-forming cell lines are known to secrete the precursor of a lysosomal cysteine proteinase, procathepsin L. The function in tumour growth and proliferation of this neutral-pH-labile proteinase or its precursor outside lysosomes is as yet unknown. Murine myeloma cells (P3X63Ag8.653) secrete procathepsin L and exhibit a high potential for malignant tumour growth and metastasis. Such cells were fused with spleen cells of mice immunized with cathepsin L. Clones of the resulting hybridoma cells continued to secrete procathepsin L, but also secreted the antibody to cathepsin L. Here we show that the hybridoma cells producing an antibody to cathepsin L have, to a great extent, lost the potential that they otherwise exhibit for inducing solid tumours after implantation into mice.
已知几种肿瘤形成细胞系会分泌溶酶体半胱氨酸蛋白酶组织蛋白酶L的前体。这种在中性pH值下不稳定的蛋白酶或其在溶酶体外的前体在肿瘤生长和增殖中的作用尚不清楚。小鼠骨髓瘤细胞（P3X63Ag8.653）分泌组织蛋白酶L的前体，并具有很高的恶性肿瘤生长和转移潜力。将此类细胞与用组织蛋白酶L免疫的小鼠脾细胞融合。所得杂交瘤细胞的克隆继续分泌组织蛋白酶L的前体，同时也分泌抗组织蛋白酶L的抗体。在此我们表明，产生抗组织蛋白酶L抗体的杂交瘤细胞在很大程度上丧失了它们在植入小鼠后诱导实体瘤的能力。
