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  4. Human Mutations in SLC2A9 (Glut9) Affect Transport Capacity for Urate.
 
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Titre

Human Mutations in SLC2A9 (Glut9) Affect Transport Capacity for Urate.

Type
article
Institution
UNIL/CHUV/Unisanté + institutions partenaires
Périodique
Frontiers in Physiology  
Auteur(s)
Ruiz, A.
Auteure/Auteur
Gautschi, I.
Auteure/Auteur
Schild, L.
Auteure/Auteur
Bonny, O.
Auteure/Auteur
Liens vers les personnes
Schild, Laurent  
Gautschi, Ivan  
Bonny, Olivier  
Liens vers les unités
DPT- Dpt pharmacologie et de toxicologie  
Néphrologie  
Dép. des Sciences Biomédicales  
ISSN
1664-042X
Statut éditorial
Publié
Date de publication
2018
Volume
9
Première page
476
Peer-reviewed
Oui
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: epublish
Résumé
SLC2A9 or Glut9 is a voltage sensitive urate transporter, mainly expressed in the kidneys, the liver, and the intestine. Human Glut9 loss-of-function mutations were identified in familial hypouricemia, and several single nucleotide polymorphisms (SNPs) were associated with lower serum urate, further indicating that Glut9 is a major determinant of serum uric acid level. To get insights in Glut9 transport characteristics, we systematically analyzed the function of known human Glut9 mutants using <sup>14</sup> C-urate uptake assay and two-electrode voltage clamp (TEVC) in the <i>Xenopus laevis</i> oocyte expression system. Surface expression was assessed by immunostaining and biotinylation. We found decreased urate transport by flux studies for most of the variants. No variant was permissive for glucose transport. We could further differentiate two behaviors among the mutants: those harboring poor overall and cell-surface expression leading to low activity and those fully expressed at the cell surface, but presenting decreased activity. We studied the latter by TEVC and observed, in depolarized conditions, decreased inward currents measured in presence of 400 μM urate, partially reversed in 1 mM urate. In addition, we showed that C210F displays lower transport ability. By contrast, N333S showed decreased urate transport activity and urate affinity, suggesting that it may belong to the urate binding pocket. Systematic analysis of Glut9 mutants confirms Glut9 as putative target for the treatment of hyperuricemia and brings new insights in Glut9 structure - function.
Sujets

SLC2A9

site directed mutagen...

structure-function re...

transporters

uric acid

PID Serval
serval:BIB_A7AF8FC6F949
DOI
10.3389/fphys.2018.00476
PMID
29967582
WOS
000435499800001
Permalien
https://iris.unil.ch/handle/iris/221238
Open Access
Oui
Date de création
2018-07-09T15:56:06.954Z
Date de création dans IRIS
2025-05-21T04:18:01Z
Fichier(s)
En cours de chargement...
Vignette d'image
Nom

29967582_BIB_A7AF8FC6F949.pdf

Version du manuscrit

published

Licence

https://creativecommons.org/licenses/by/4.0

Taille

3.88 MB

Format

Adobe PDF

PID Serval

serval:BIB_A7AF8FC6F949.P001

URN

urn:nbn:ch:serval-BIB_A7AF8FC6F9494

Somme de contrôle

(MD5):8051808de16880ee3a413efdd19a191f

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