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N ‐glycans are not the signal for apical sorting of corticosteroid binding globulin in MDCK cells
Author(s) -
Larsen Jakob E.,
Avvakumov George V.,
Hammond Geoffrey L.,
Vogel Lotte K.
Publication year - 1999
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/s0014-5793(99)00526-8
Subject(s) - glycosylation , glycan , mutant , biology , n linked glycosylation , glycoprotein , microbiology and biotechnology , biochemistry , gene
It has been suggested that N ‐glycans act as a general sorting signal for secretory proteins in MDCK cells [Scheiffele et al. (1995) Nature 378, 96–98]. Human corticosteroid binding globulin contains six consensus sites for N ‐glycosylation and is known to be secreted to the apical side of MDCK cells. Our results show that wild‐type corticosteroid binding globulin is N ‐glycosylated when it is recombinantly expressed in MDCK cells. Six mutants, each lacking one of the N ‐glycosylation sites, and a mutant lacking all six N ‐glycosylation sites were also secreted to the apical side of MDCK cells in a polarized manner. Thus, the N ‐glycans on corticosteroid binding globulin do not act as an apical sorting signal in MDCK cells.