ArticlePharmaceutical research2003
Sorting of rat SPNT in renal epithelium is independent of N-glycosylation.
Article in Pharmaceutical research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 18 citations in OpenAlex.
- Human Concentrative Nucleoside Transporter 3 (hCNT3, SLC28A3) Forms a Cyclic Homotrimer.Biochemistry · 2017Article
- Glycosylation of solute carriers: mechanisms and functional consequences.Pflugers Archiv : European journal of physiology · 2016Review
- Role of N-glycosylation in trafficking of apical membrane proteins in epithelia.American journal of physiology. Renal physiology · 2009Review
- A mouse model of sitosterolemia: absence of Abcg8/sterolin-2 results in failure to secrete biliary cholesterol.BMC medicine · 2004Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
purposeThe sodium-dependent, purine-selective nucleoside transporter, SPNT, has a unique steady-state expression pattern in renal epithelial cells. In comparison with the concentrative nucleoside transporter, CNTI, which is confined to the apical membrane, SPNT is expressed predominantly on the apical membrane but with significant expression on the basolateral membrane as well. Alternate surface expression indicates that SPNT likely has different sorting and trafficking mechanisms from CNTI. Because glycosylation has been reported to be essential for apical targeting of other transporters, and SPNT contains three unique glycosylation sites, we examined the importance of glycosylation in sorting of SPNT. Preliminary studies suggested that glycosylation affects surface expression of SPNT but not CNT1.
methodsAll three unique glycosylation sites were mutated alone and in tandem. Wild-type and mutant SPNT, tagged with green fluorescence protein, were stably transfected into MDCK. Positive clones were assayed for polarized surface expression by immunofluorescence and functional analysis.
resultsMutation at all three sites alone or in tandem resulted in functional proteins. Removal of sites N606 and N625 resulted in proteins of reduced molecular mass. None of the unglycosylated mutants localized differently than wild-type SPNT.
conclusionN-linked glycosylation is not essential for polarized sorting.
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Registered trials
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