Walsh SB, Borgese F, Gabillat N, Unwin RJ, Guizouarn H. Cation transport activity of anion exchanger 1 mutations found in inherited distal renal tubular acidosis. Am J Physiol Renal Physiol 295: F343–F350, 2008. First published June 4, 2008; doi:10.1152/ajprenal.00587.2007.—Anion exchanger 1 (AE1) is encoded by SLC4A1 and mediates electroneutral anion exchange across cell membranes. It is the m...

On bases of previous observations on the band 3 anion exchange inhibition by the electrophilic reagent 1-fluoro-2,4-dinitrobenzene in resealed ghosts and a previously proposed band 3-based mechanism of control of the erythrocyte shape, it is suggested that stomatocytoses by 1-chloro-2,4-dinitrobenzene and other electrophilic reagents are due to an inhibition of the band 3 anion exchange by a co...

Erythrocytes are very susceptible to oxidative stress, having a high content of intracellular oxygen and hemoglobin. In the present study, exposure to oxidative stress resulted in a significant impairment of erythrocyte membrane functions, such as deformability and anion exchange. Band 3 protein, also known as anion exchanger-1, plays an important role in these two functions. We show that oxida...

Although many polarized proteins are sorted to the same membrane domain in all epithelial tissues, there are some that exhibit a cell type-specific polarity. We recently found that band 3 (the anion exchanger AE1) was present in the apical membrane of a renal intercalated cell line when these cells were seeded at low density, but its targeting was reversed to the basolateral membrane under the ...

Anion exchanger 1 (AE1) is encoded by SLC4A1 and mediates electroneutral anion exchange across cell membranes. It is the most abundant protein in the red cell membrane, but it is also found in the basolateral membrane of renal alpha-intercalated cells, where it is required for normal urinary acidification. Recently, four point mutations in red cell AE1 have been described that convert the anion...

Folding and oligomerization of most plasma membrane glycoproteins, including those involved in ion transport, occur in the ER and are frequently required for their exit from this organelle. It is currently unknown, however, where or when in the biosynthetic pathway these proteins become functionally active. AE1 and AE2 are tissue-specific, plasma membrane anion transport proteins. Transient exp...