Evidence from oocyte expression that the erythrocyte water channel is distinct from band 3 and the glucose transporter.

Détails

ID Serval
serval:BIB_1A9A66465326
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Evidence from oocyte expression that the erythrocyte water channel is distinct from band 3 and the glucose transporter.
Périodique
Journal of Clinical Investigation
Auteur(s)
Zhang R., Alper S.L., Thorens B., Verkman A.S.
ISSN
0021-9738
Statut éditorial
Publié
Date de publication
11/1991
Peer-reviewed
Oui
Volume
88
Numéro
5
Pages
1553-1558
Langue
anglais
Résumé
It has been proposed that the mercurial-sensitive water transporter in mammalian erythrocytes is the anion exchanger band 3 (AE1) and/or the glucose transporter, band 4.5 (GLUT1). Using a functional assay for water channel expression in Xenopus oocytes (Zhang, R., K. A. Logee, and A. S. Verkman. 1990. J. Biol. Chem. 265:15375-15378), we compared osmotic water permeability (Pf) of oocytes injected with water, reticulocyte mRNA, AE1 mRNA, and GLUT1 mRNA. Injection of oocytes with 5-50 ng of in vitro-transcribed AE1 mRNA had no effect on Pf, but increased trans-stimulated 36Cl uptake greater than fourfold in a dinitro-disulfonic stilbene (DNDS)-inhibitable manner. Injection with 1-50 ng of in vitro-transcribed GLUT1 mRNA increased 3H-methylglucose uptake greater than 15-fold in a cytochalasin B-sensitive manner and increased Pf from (3.7 +/- 0.4) x 10(-4) cm/s (SE, n = 16, 10 degrees C) in water-injected oocytes up to (13 +/- 1) x 10(-4) cm/s (n = 18). Both the increments in sugar and water transport were inhibited by cytochalasin B (25 microM) and phloretin (0.2 mM); neither was inhibited by 0.3 mM HgCl2. In oocytes injected with 50 ng of rabbit reticulocyte mRNA, the Pf of (18 +/- 2) x 10(-4) cm/s (n = 18) was reduced to (4.0 +/- 0.6) x 10(-4) cm/s (n = 10) by HgCl2, but was not inhibited by DNDS (0.4 mM), cytochalasin B or phloretin. Coinjection of reticulocyte mRNA with antisense oligodeoxyribonucleotides against AE1 or GLUT1 did not affect Pf, but inhibited completely the incremental uptake of 36Cl or 3H-methylglucose, respectively. Expression of size-fractionated mRNA from reticulocyte gave a 2-2.5-kb size for water channel mRNA, less than the 4-4.5-kb size for the Cl transporter. These results provide evidence that facilitated water transport in erythrocytes is mediated not by bands 3 or 4.5, but by distinct water transport protein(s).
Mots-clé
Animals, Anion Exchange Protein 1, Erythrocyte, Base Sequence, Body Water, Erythrocytes, Molecular Sequence Data, Monosaccharide Transport Proteins, Oligonucleotides, Antisense, Oocytes, RNA, Messenger, Rabbits, Xenopus laevis
Pubmed
Web of science
Création de la notice
24/01/2008 14:41
Dernière modification de la notice
03/03/2018 14:29
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