Zn2+ inhibits the anion transport activity of band 3 by binding to its cytoplasmic tail.
نویسندگان
چکیده
Zn2+ can induce a conformational change of Band 3 with concomitant inhibition of its anion transport activity of human erythrocyte membrane vesicles only from the cytoplasmic side. The Zn2+ inhibition exhibits a dose-dependent manner with an apparent half maximal concentration of 50 microM ZnCl2 and can be reversed by 0.5 mM EDTA, but not by 1 mM dithiothreitol. The Zn2+ effect is specific and no similar inhibitory action could be observed by other divalent cations (Cu2+, Mn2+, Mg2+ or Sr2+).
منابع مشابه
Persistence of external chloride and DIDS binding after chemical modification of Glu-681 in human band 3.
Although its primary function is monovalent anion exchange, the band 3 protein also cotransports divalent anions together with protons at low pH. The putative proton binding site, Glu-681 in human erythrocyte band 3, is conserved throughout the anion exchanger family (AE family). To determine whether or not the monovalent anion binding site is located near Glu-681, we modified this residue with...
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The extracellular lysine residues in the human erythrocyte anion transport protein (band 3) have been investigated using chemical modification with the impermeant homobifunctional active ester bis(sulfosuccinimidyl)-suberate (BSSS). This agent forms covalent intra- and intermolecular cross-links in human band 3 in intact cells (Staros and Kakkad. 1983. J. Membr. Biol. 74:247). We have found tha...
متن کاملTransmembrane effects of irreversible inhibitors of anion transport in red blood cells. Evidence for mobile transport sites
Experiments were designed to determine whether band 3, the anion transport protein of the red cell membrane, contains a mobile element that acts as a carrier to move the anions across a permeability barrier. The transport site-specific, nonpenetrating irreversible inhibitor 4,4'-diisothiocyano-2,2'-stilbene disulfonate (DIDS) was found to be effective only when applied extracellularly. It was u...
متن کاملNaturally occurring anti-band 3 antibodies in clearance of senescent and oxidatively stressed human red blood cells.
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متن کاملACELL October 46/4
Bahar, Sonya, Christopher T. Gunter, Cheryl Wu, Scott D. Kennedy, and Philip A. Knauf. Persistence of external chloride and DIDS binding after chemical modification of Glu-681 in human band 3. Am. J. Physiol. 277 (Cell Physiol. 46): C791–C799, 1999.—Although its primary function is monovalent anion exchange, the band 3 protein also cotransports divalent anions together with protons at low pH. T...
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ورودعنوان ژورنال:
- Bioscience reports
دوره 14 4 شماره
صفحات -
تاریخ انتشار 1994