Houri J J, Ogier-Denis E, Trugnan G, Codogno P
INSERM U239, Unité de Recherche sur la Biologie et la Physiopathologie des Cellules Digestives, Paris, France.
Biochem Biophys Res Commun. 1993 Dec 15;197(2):805-11. doi: 10.1006/bbrc.1993.2550.
The aim of the present study was to elucidate the mechanism responsible for the high mannose glycoprotein instability in undifferentiated HT-29 cells (a human colon cancer cell line) reported previously. The results presented here are consistent with lysosomal degradation of these molecular species. In addition inhibitors of the autophagic-lysosomal degradative pathway (3-methyladenine, okadaic acid and asparagine) dramatically block the degradation of proteins and N-linked glycoproteins in undifferentiated HT-29 cells. The main conclusions of this work are: 1- the autophagic-lysosomal pathway is responsible for the high mannose glycoprotein degradation in undifferentiated HT-29 cells; 2- this degradative pathway exists in differentiated cells but is greatly reduced (3.5-4 fold); 3- the HT-29 cell line is a new model to investigate the molecular regulation of autophagy.
本研究的目的是阐明先前报道的未分化HT-29细胞（一种人结肠癌细胞系）中高甘露糖糖蛋白不稳定的机制。此处呈现的结果与这些分子种类的溶酶体降解一致。此外，自噬-溶酶体降解途径的抑制剂（3-甲基腺嘌呤、冈田酸和天冬酰胺）显著阻断未分化HT-29细胞中蛋白质和N-连接糖蛋白的降解。这项工作的主要结论是：1-自噬-溶酶体途径负责未分化HT-29细胞中高甘露糖糖蛋白的降解；2-这种降解途径存在于分化细胞中，但大大减少（3.5-4倍）；3-HT-29细胞系是研究自噬分子调控的新模型。
