The effect of selenium on the function of the anion transporter (Band 3) of erythrocyte membranes.
The transport activity of Band 3 of spectrin-stripped inside-out erythrocyte membrane vesicles (IOVs) or resealed ghosts was enhanced in the presence of trace amounts of Na2SeO3 (0.2-0.5 p.p.m.); however, at higher concentrations of Na2SeO3 (> 4.0 p.p.m.), an inverse result was obtained. Reassociation of spectrin with IOVs has no effect either on the transport activity of Band 3 or on the enhancement of its activity by Na2SeO3. Sulfhydryl reagents (p-chloromercuribenzoic acid and N-ethylmaleimide) could also inhibit Band 3 activity and eliminate the selenium effect. It is suggested that SH groups are involved in anion transport of Band 3 and that the selenium effect is based on the interaction of SH groups of Band 3 with Na2SeO3.
Yang
J
J
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
Yang
F Y
FY
D001457:Anion Exchange Protein 1, Erythrocyte / Q000187:drug effects*; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D017136:Ion Transport / Q000187:drug effects*; D012643:Selenium / Q000494:pharmacology*; D013049:Spectrin / Q000502:physiology; D020245:p-Chloromercuribenzoic Acid
D001457:Anion Exchange Protein 1, Erythrocyte; D002729:Chloromercuribenzoates; D013049:Spectrin; D020245:p-Chloromercuribenzoic Acid; D012643:Selenium