| Literature DB >> 21889501 |
Dorota Maszczak-Seneczko1, Teresa Olczak, Piotr Jakimowicz, Mariusz Olczak.
Abstract
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-RCA(r) 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.Entities:
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Year: 2011 PMID: 21889501 DOI: 10.1016/j.febslet.2011.08.038
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124