Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 374, Issue 1, Pages 123-127Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2008.06.120
Keywords
hSVCT1; hSVCT2; transport; ascorbic acid
Categories
Funding
- NIH [DK 056061, DK-73032, DK-71538, NS046783]
- NSF [0237946]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0237946] Funding Source: National Science Foundation
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The human sodium-dependent vitamin C transporters (hSVCT1 and hSVCT2) mediate cellular uptake of ascorbic acid. Both these transporters contain potential sites for N-glycosylation in their extracellular domains (Asn-138, Asn-144 [hSVCT1]; Asn-188, Asn-196 [hSVC-r2]), however the role of N-glycosylation in transporter function is unexplored. Oil the basis of the result that tunicamycin decreased C-14-ascorbic acid uptake in HepG2 cells, we systematically ablated all consensus N-glycosylation sites in hSVCT1 and hSVCT2 to resolve any effects on ascorbic acid uptake, transporter expression and targeting. We show that removal of individual N-glycosylation sites significantly impairs protein expression and consequently ascorbic acid uptake for hSVCT1 mutants (N138Q is retained intracellularly) and for hSVCT2 mutants (all of which reach the cell surface). N-Glycosylation is therefore essential for vitamin C transporter functionality. (C) 2008 Elsevier Inc. All rights reserved.
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