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J Membr Biol
1994 May 01;1401:81-8. doi: 10.1007/bf00234488.
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The effects of glycophorin A on the expression of the human red cell anion transporter (band 3) in Xenopus oocytes.
Groves JD
,
Tanner MJ
.
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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.
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