The expression of the abnormal human red cell anion transporter from South-East Asian ovalocytes (band 3 SAO) in Xenopus oocytes

• Published in: FEBS letters Vol. 330; no. 2; pp. 186 - 190
• Main Authors: Groves, Jonathan D., Ring, Susan M., Schofield, Ann E., Tanner, Michael J.A.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 13.09.1993; Elsevier
• Subjects: Anemias. Hemoglobinopathies; Animals; Anion Exchange Protein 1, Erythrocyte - genetics; Anion Exchange Protein 1, Erythrocyte - metabolism; Anion transporter; BADS, 4-benzamido-4'-aminostilbene-2,2'-disulphonate; Band 3; Base Sequence; Biological and medical sciences; Biological Transport; Cell Membrane - metabolism; Cloning, Molecular; DIDS, 4,4'-diisothiocyanato-2,2'-stilbene disulphonate; Diseases of red blood cells; DNA; DNDS, 4,4'-dinitrostilbene-2,2'-disulphonate; Elliptocytosis, Hereditary - genetics; Freshwater; Glycophorin - genetics; Glycophorin - metabolism; Glycophorin A; GPA, glycophorin A; Hematologic and hematopoietic diseases; Hereditary ovalocytosis; Humans; Medical sciences; Molecular Sequence Data; Oocytes; Precipitin Tests; RNA - genetics; RNA - metabolism; RNA, Complementary; SAO, South-East Asian hereditary ovalocytosis; Sequence Deletion; Xenopus; Xenopus oocyte; Asia; South east Asia; Glycophorin A; DNDS, 4,4'-dinitrostilbene-2,2'-disulphonate; Band 3; GPA, glycophorin A; BADS, 4-benzamido-4'-aminostilbene-2,2'-disulphonate; SAO, South-East Asian hereditary ovalocytosis; DIDS, 4,4'-diisothiocyanato-2,2'-stilbene disulphonate; Anion transporter; Xenopus oocyte; Hereditary ovalocytosis; Human; Erythrocytic membrane disease; Molecular form; Band 3 protein; Heterologous system; Pathophysiology; Xenopus laevis; Amphibia; Ion transport; Hemopathy; Salientia; Biological activity; Hereditary elliptocytosis; Genetic disease; Vertebrata; Hemolytic anemia; Glycophorin; Carrier protein; Oocyte
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(93)80270-5

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 the cell surface does not require co-expression of normal band 3. Co-expression of glycophorin A (GPA) increases the rate of translocation of band 3 SAO to the oocyte membrane but is not essential for this process. We suggest that the increased tendency of band 3 SAO to form oligomers may facilitate its translocation to the cell surface.