Sano S, Okazaki K, Yamamoto Y
First Department of Internal Medicine, Kochi Medical School, Japan.
J Gastroenterol. 1994 Oct;29(5):569-76. doi: 10.1007/BF02365437.
We have previously studied the biosynthesis and secretion of mucin in the normal human stomach and reported that the tetramer of the 60-kDa subunit of mucin core protein was synthesized and highly glycosylated, and that only high molecular weight mucin was secreted. In this study, we investigated the mucin-related products of a gastric cancer cell line (Hs746T). Analysis of intracellular and extracellular products immunoprecipitated with an anti-apomucin monoclonal antibody revealed that a 110-kDa protein, the dimer of the 55-kDa subunit, was synthesized and secreted. Tunicamycin treatment inhibited the secretion of the 110-kDa protein. These findings suggest that N-glycosylation may be involved in the secretory mechanism of the mucin-related product.
我们之前研究了正常人胃中粘蛋白的生物合成与分泌，并报道粘蛋白核心蛋白60-kDa亚基的四聚体被合成且高度糖基化，并且仅分泌高分子量的粘蛋白。在本研究中，我们调查了一种胃癌细胞系（Hs746T）的粘蛋白相关产物。用抗脱辅基粘蛋白单克隆抗体免疫沉淀的细胞内和细胞外产物分析显示，一种110-kDa蛋白，即55-kDa亚基的二聚体，被合成并分泌。衣霉素处理抑制了110-kDa蛋白的分泌。这些发现表明N-糖基化可能参与了粘蛋白相关产物的分泌机制。
