Olsen I, Abraham D, Shelton I, Bou-Gharios G, Muir H, Winchester B
Kennedy Institute of Rheumatology, London, U.K.
Biochim Biophys Acta. 1988 Mar 11;968(3):312-22. doi: 10.1016/0167-4889(88)90022-5.
The activity of a lysosomal enzyme, alpha-D-mannosidase (EC 3.2.1.24), increased markedly in normal lymphocytes when they were cultured together with fibroblasts from a patient with an inherited deficiency of this enzyme. Cell-to-cell contact was obligatory for this increase in activity, which also required new protein synthesis. The enzyme induced in the co-cultured lymphocytes was a high molecular weight form of alpha-D-mannosidase that was not detected in lymphocytes cultured alone, which had only the low molecular weight mature enzyme. It was this precursor form alone that was directly transferred to the mannosidosis fibroblasts, where it was present initially in organelles of low density. When the culture period was extended the lymphocyte precursor enzyme was transported to the heavy lysosomes in the recipient cells, and correctly processed to the functionally effective mature enzyme.
当正常淋巴细胞与一名患有遗传性α-D-甘露糖苷酶（EC 3.2.1.24）缺乏症患者的成纤维细胞共同培养时，溶酶体酶α-D-甘露糖苷酶的活性显著增加。细胞间接触对于这种活性增加是必不可少的，这也需要新的蛋白质合成。在共培养的淋巴细胞中诱导产生的酶是α-D-甘露糖苷酶的高分子量形式，在单独培养的淋巴细胞中未检测到，单独培养的淋巴细胞中只有低分子量的成熟酶。正是这种前体形式直接转移到了甘露糖苷贮积症成纤维细胞中，最初它存在于低密度细胞器中。当培养期延长时，淋巴细胞前体酶被转运到受体细胞的重溶酶体中，并正确加工成功能有效的成熟酶。
