The effects of glycophorin A on the expression of the human red cell anion transporter (band 3) in Xenopus oocytes.
The effects of human red cell glycophorin A (GPA) on the translocation to the plasma membrane and anion transport activity of the human erythrocyte anion transporter (band 3; AE1) have been examined using the Xenopus oocyte expression system. We show that band 3 accumulates steadily at the oocyte surface with time in the presence or absence of GPA, but this occurs more quickly when GPA is coexpressed. The amount of band 3 at the surface is determined by the concentrations of band 3 and GPA cRNA that are injected, with a higher proportion of total band 3 being translocated to the surface in the presence of GPA cRNA. The increased expression of DNDS-sensitive chloride transport is highly specific to GPA, and is not observed when the cRNA to the putative glycophorin E or a very high concentration of the cRNA to glycophorin C are coexpressed with band 3 in oocytes.
Groves
J D
JD
Department of Biochemistry, School of Medical Sciences, University of Bristol, United Kingdom.
Tanner
M J
MJ
D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002712:Chlorides / Q000378:metabolism; D015870:Gene Expression; D006021:Glycophorins / Q000235:genetics / Q000378:metabolism*; D009865:Oocytes / Q000378:metabolism*; D018075:RNA, Complementary / Q000235:genetics / Q000378:metabolism; D014981:Xenopus
D001457:Anion Exchange Protein 1, Erythrocyte; D002712:Chlorides; D006021:Glycophorins; D018075:RNA, Complementary