Parczyk K, Koch-Brandt C
Institut für Biochemie, Abteilung Molekulare Genetik, Universität Frankfurt, Germany.
FEBS Lett. 1991 Jan 28;278(2):267-70. doi: 10.1016/0014-5793(91)80132-m.
In the polarized epithelial Madin-Darby canine kidney (MDCK) cell line an 80 kDa glycoprotein complex (gp 80) is sorted into the apical pathway of exocytosis and is secreted constitutively at the apical cell surface. The unglycosylated form of the protein complex is secreted in a nonpolar fashion at both surface domains [(1987) J. Cell. Biol. 105, 2735-2743]. Using ricin-resistant MDCK cells the role of the terminal galactose and sialic acid residues in the sorting of the gp 80 complex was analysed. The results suggest that the carbohydrate cores, rather than the ultimate or penultimate sugar residues, play a critical role in the intracellular transport of this protein.
在极化上皮的犬肾Madin-Darby(MDCK)细胞系中,一种80 kDa糖蛋白复合物(gp 80)被分选到胞吐作用的顶端途径,并在顶端细胞表面组成性分泌。该蛋白复合物的未糖基化形式在两个表面结构域以非极性方式分泌[(1987年)《细胞生物学杂志》105卷,2735 - 2743页]。利用抗蓖麻毒素的MDCK细胞,分析了末端半乳糖和唾液酸残基在gp 80复合物分选中的作用。结果表明,碳水化合物核心而非末端或倒数第二个糖残基在该蛋白的细胞内运输中起关键作用。