Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-1225
Nat Genet 2005 Nov 01;3711:1258-63. doi: 10.1038/ng1656.
Show Gene links Show Anatomy links

Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1.

Bruce LJ , Robinson HC , Guizouarn H , Borgese F , Harrison P , King MJ , Goede JS , Coles SE , Gore DM , Lutz HU , Ficarella R , Layton DM , Iolascon A , Ellory JC , Stewart GW .


???displayArticle.abstract???
We identified 11 human pedigrees with dominantly inherited hemolytic anemias in both the hereditary stomatocytosis and spherocytosis classes. Affected individuals in these families had an increase in membrane permeability to Na and K that is particularly marked at 0 degrees C. We found that disease in these pedigrees was associated with a series of single amino-acid substitutions in the intramembrane domain of the erythrocyte band 3 anion exchanger, AE1. Anion movements were reduced in the abnormal red cells. The 'leak' cation fluxes were inhibited by SITS, dipyridamole and NS1652, chemically diverse inhibitors of band 3. Expression of the mutated genes in Xenopus laevis oocytes induced abnormal Na and K fluxes in the oocytes, and the induced Cl transport was low. These data are consistent with the suggestion that the substitutions convert the protein from an anion exchanger into an unregulated cation channel.

???displayArticle.pubmedLink??? 16227998
???displayArticle.link??? Nat Genet
???displayArticle.grants??? [+]

Species referenced: Xenopus laevis
Genes referenced: slc4a1