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The role of carbohydrates in vectorial exocytosis The secretion of the gp 80 glycoprotein complex in a ricin‐resistant mutant of MDCK cells
Author(s) -
Parczyk Karsten,
Koch-Brandt Claudia
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80132-m
Subject(s) - exocytosis , glycoprotein , secretion , ricin , microbiology and biotechnology , sialic acid , mutant , biochemistry , chemistry , golgi apparatus , biology , cell , gene , toxin
In the polarized epithelial Madin‐Darby canine kidney (MDCK) cell line an 80 kDa glycoprotein complex (gp 80) is sorted into the spical pathway or exocytosis and is secreted constitutively at the apical cell surface. The unglycosylated form or 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 slalic 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.

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