Synthesis of lysosomal α-mannosidase in normal and mannosidosis fibroblasts
Synthesis of lysosomal α-mannosidase in normal and mannosidosis fibroblasts
复制标题
正常和甘露糖苷沉积症成纤维细胞中溶酶体 α-甘露糖苷酶的合成
DOI：
10.1016/s0006-291x(83)80046-1
复制
发表时间：
1983
影响因子：
3.1
通讯作者：
K. Figura
中科院分区：
文献类型：
--
作者：
R. Pohlmann;A. Hasilik;S. Cheng;S. Pemble;B. Winchester;K. Figura
在代谢标记的成纤维细胞中，研究了两名甘露糖症患者和对照组的溶酶体α-甘露糖苷酶的合成和分泌。正常成纤维细胞分泌110 kDa的α-甘露糖苷酶。细胞内α-甘露糖苷酶由多个多肽组成，表观MRS在40~67 kDa之间。在两个甘露糖症细胞系中均未检测到α-甘露糖苷酶的胞内和胞外多肽。甘露糖症成纤维细胞分泌酸性α-甘露糖苷酶活性是正常的三分之一。与正常细胞相比，NH4Cl不能促进细胞分泌α-甘露糖苷酶，分泌的活性也不能免疫沉淀，说明甘露聚糖症成纤维细胞分泌的酸性α-甘露糖苷酶活性与溶酶体的DNA-甘露糖苷酶无关。
The biosynthesis and secretion of lysosomal α-mannosidase was studied in metabolically labelled fibroblasts from controls and two patients with manosidosis. Normal fibroblasts secrete α-mannosidase as a 110kDa polypeptide. Intracellularly α-mannosidase is represented by several polypeptides with apparent Mrs ranging from 40 to 67kDa. In two mannosidosis cell lines none of intra- and extracellular polypeptides of α-mannosidase were detectable. The mannosidosis fibroblasts secreted acid α-mannosidase activity at one third of the normal rate. In contrast to normal cells the secretion was not enhanced by NH4Cl and the secreted activity was not immunoprecipitable, indicating that the acid α-mannosidase activity secreted by mannosidosis fibroblasts is not related to the lysosomal α-mannosidase.