ArticleBlood cells, molecules & diseases
Reduced DIDS-sensitive chloride conductance in Ae1-/- mouse erythrocytes.
Article in Blood cells, molecules & diseases. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Critical role of Babesia bovis spherical body protein 3 in ridge formation on infected red blood cells.PLoS pathogens · 2024Article
- Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S.American journal of physiology. Cell physiology · 2011Article
- Hydrogen ion dynamics in human red blood cells.The Journal of physiology · 2010Article
- Article
- Acid-sensitive outwardly rectifying anion channels in human erythrocytes.The Journal of membrane biology · 2009Article
- Molecular physiology and genetics of Na+-independent SLC4 anion exchangers.The Journal of experimental biology · 2009Review
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Authors and funding
4 authors at 4 institutions in 1 country.
Funding
Abstract
The resting membrane potential of the human erythrocyte is largely determined by a constitutive Cl(-) conductance approximately 100-fold greater than the resting cation conductance. The 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS)-sensitive electroneutral Cl(-) transport mediated by the human erythroid Cl(-)/HCO(3)(-) exchanger, AE1 (SLC4A1, band 3) is >10,000-fold greater than can be accounted for by the Cl(-) conductance of the red cell. The molecular identities of conductive anion pathways across the red cell membrane remain poorly defined. We have examined red cell Cl(-) conductance in the Ae1(-/-) mouse as a genetic test of the hypothesis that Ae1 mediates DIDS-sensitive Cl(-) conductance in mouse red cells. We report here that wildtype mouse red cell membrane potential resembles that of human red cells in the predominance of its Cl(-) conductance. We show with four technical approaches that the DIDS-sensitive component of erythroid Cl(-) conductance is reduced or absent from Ae1(-/-) red cells. These results are consistent with the hypothesis that the Ae1 anion exchanger polypeptide can operate infrequently in a conductive mode. However, the fragile red cell membrane of the Ae1(-/-) mouse red cell exhibits reduced abundance or loss of multiple polypeptides. Thus, loss of one or more distinct, DIDS-sensitive anion channel polypeptide(s) from the Ae1(-/-) red cell membrane cannot be ruled out as an explanation for the reduced DIDS-sensitive anion conductance.
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