Evidence for the presence of three different anion exchangers in a red cell. functional expression studies in xenopus oocytes

Evidence for the presence of three different anion exchangers in a red cell. functional... Anion exchangers (AE) are transmembrane proteins catalyzing electroneutral exchange of Cl- for HCO 3 - . To date, three different genes coding for this protein, AE1, AE2 and AE3, have been identified in many species. AE1 is considered to be the unique anion exchanger expressed in erythrocytes. In this paper we propose the presence of three different AEs in skate erythrocytes, a skAE1, a skAE2 and a skAE3, cloned by RT-PCR (reverse-transcriptase polymerase chain reaction). These three skAE have a similar predicted secondary structure. All three skAE are divided in two main domains: a hydrophilic cytoplasmic N-terminal domain and a C-terminal domain crossing the lipid bilayer at least 12 times. The greatest similarity is found in the membrane-spanning domain of the three skAE. The size as well as the amino-acid sequence of the cytoplasmic domain differ significantly among three anion exchangers. Functional expression studies in Xenopus oocytes led to the conclusion that skAE-1 and -2 share some functional features (Cl-dependence and DIDS sensitivity). The skAE3 could not be expressed in Xenopus oocytes. These data are in agreement with expression data obtained with AEs of different species utilizing the oocyte system. It is highly probable that these three new AE sequences come from three different genes, thus suggesting for the first time the presence of the three AE genes in Chondrichthyes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Evidence for the presence of three different anion exchangers in a red cell. functional expression studies in xenopus oocytes

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Publisher
Springer-Verlag
Copyright
Copyright © 2003 by Springer-Verlag
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-002-2012-6
Publisher site
See Article on Publisher Site

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