Reduced DIDS-sensitive chloride conductance in Ae1−/− mouse erythrocytes
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- 作者：Seth L. Alper ; David H. V ; orpe ; Luanne L. Peters ; Carlo Brugnara
- 关键词：Cl− ; /HCO3− ; exchange ; Patch cl Isotopic flux ; Light scattering ; Ionophore
- 刊名：Blood Cells, Molecules, and Diseases
- 出版年：2008
- 出版时间：July-August 2008
- 年：2008
- 卷：41
- 期：1
- 页码：22-34
- 全文大小：1098 K
文摘
The resting membrane potential of the human erythrocyte is largely determined by a constitutive Cl− conductance ![]()
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−/HCO3− 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.