کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2048637 | 1074086 | 2011 | 5 صفحه PDF | دانلود رایگان |
Nucleotide sugar transporters deliver substrates for glycosyltransferases into the endoplasmic reticulum and the Golgi apparatus. We demonstrated that overexpression of UDP-GlcNAc transporter (NGT) in MDCK-RCAr and CHO-Lec8 mutant cells defective in UDP-Gal transporter (UGT) restored galactosylation of N-glycans. NGT overexpression resulted in decreased transport of UDP-GlcNAc into the Golgi vesicles. This effect resembled the phenotype of mutant cells corrected by UGT1 overexpression. The transport of UDP-Gal was not significantly changed. Our data suggest that the biological function of UGT and NGT in galactosylation of macromolecules may be coupled.
► UDP-GlcNAc transporter (NGT) expression analyzed in cells defective in UDP-Gal transporter (UGT).
► Surprisingly overexpression of NGT partially restores galactosylation in UGT mutant cells.
► Biological function of UGT and NGT in galactosylation may be coupled.
Journal: FEBS Letters - Volume 585, Issue 19, 3 October 2011, Pages 3090–3094