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The effects of human red cell glycophorin A (GPA) on the expression of the human erythrocyte anion transporter (band 3, AE1) has been examined in Xenopus oocytes. The coexpression of GPA with band 3 increased stilbene disulfonate-sensitive chloride transport into the oocytes. The effect of GPA was particularly noticeable at low band 3 concentrations and(More)
The human erythrocyte anion transporter (band 3; AE1) has a single N-linked glycosylation site at amino residue Asn-642. To investigate the functional role of the N-glycan in band 3 (b3) we have constructed mutant b3 cDNAs in which this residue has been replaced by Gly, Ser or Thr, and the expression of these mutants was examined in Xenopus oocytes.(More)
South-East Asian ovalocytosis (SAO) is caused by the heterozygous presence of a variant form of the human erythrocyte anion transporter (band 3; AE1). The expression of band 3 SAO has been studied in Xenopus oocytes. Band 3 SAO is not functional as an anion transporter but is inserted stably into the plasma membrane of oocytes. Band 3 SAO translocation to(More)
We constructed cDNA clones encoding N-terminal, C-terminal and internal polypeptide fragments of the human red cell anion exchanger (band 3; AE1). The internal fragments comprised between one and seven putative transmembrane spans with two or more spans deleted from both termini of the membrane domain of band 3. Sets of three, four or five complementary(More)
The anion transport activity of the human erythrocyte anion transporter (band 3; AE1) has been examined in both normal and glycophorin A (GPA)-deficient (MkMk) human red blood cells (RBCs). The sulfate transport activity of MkMk cells (from two ethnically diverse sources) was approximately 60% that of normal erythrocytes under the transport assay conditions(More)
We expressed the 52-kDa integral membrane domain (B3mem) of the human erythrocyte anion transporter (band 3; AE1) in a protease-deficient strain of the yeast Saccharomyces cerevisiae under the control of the inducible GAL10-CYC1 promoter. Immunoblots of total protein from transformed yeast cells confirmed that the B3mem polypeptide was overexpressed shortly(More)
We have examined the functional co-assembly of non-complementary pairs of N- and C-terminal polypeptide fragments of the anion transport domain (b3mem) of human red-cell band 3. cDNA clones encoding non-contiguous pairs of fragments with one transmembrane (TM) region omitted, or overlapping pairs of fragments with between one and ten TM regions duplicated,(More)
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(More)
The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642. We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes. We used an N-glycosylation mutagenesis approach to examine(More)