Journal
BIOLOGICAL CHEMISTRY
Volume 385, Issue 1, Pages 49-57Publisher
WALTER DE GRUYTER & CO
DOI: 10.1515/BC.2004.007
Keywords
CHO cells; G-protein coupled receptor; receptor internalization; signal transduction
Categories
Ask authors/readers for more resources
To investigate the glycosylation of the human bradykinin B-2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells. Western blot experiments demonstrated that all three extracellular asparagines are glycosylated. The kinetics of bradykinin binding and receptor sequestration remained unchanged after glycosylation had been suppressed. However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation. These results indicate that, for the human bradykinin B-2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available