id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
work_kzfqzopqtvdp3no6b4op34jxgi	Saminathan Muthusamy	N-glycosylation is essential for ileal ASBT function and protection against proteases	2015.0	8	.pdf	application/pdf	7024	833	65	N-glycosylation is essential for ileal ASBT function and protection against proteases HEK-293 cells stably transfected with ASBT-V5 fusion protein. Further, ASBT function and expression are increased in diseases that are associated with bile acid The current studies were focused at investigating the mechanisms by which glycosylation affects ASBT function and data suggest that hyperglycemia-induced changes in the glycosylation may underlie the increase in ASBT function and bile We have generated HEK-293 cells that express ASBT-V5 fusion protein in higher band is the mature N-acetylglucosamine rich glycosylated ASBT protein. glycosylated ASBT protein (upper band). A: HEK-293 cells stably expressing wild-type ASBT-V5 fusion protein were stably expressing glycosylation deficient mutant ASBT (N10Q)-V5 total protein was extracted and separated by SDS-PAGE followed by Western blotting with glycosylated ASBT protein was significantly increased in response to incubation with 25 mM glucose. evidence showing that complex glycosylation of ASBT increases its protein stability on the plasma membrane.	./cache/work_kzfqzopqtvdp3no6b4op34jxgi.pdf	./txt/work_kzfqzopqtvdp3no6b4op34jxgi.txt