scholarly journals Interaction of the human erythrocyte Band 3 anion exchanger 1 (AE1, SLC4A1) with lipids and glycophorin A: Molecular organization of the Wright (Wr) blood group antigen

2018 ◽  
Vol 14 (7) ◽  
pp. e1006284 ◽  
Author(s):  
Antreas C. Kalli ◽  
Reinhart A. F. Reithmeier
Keyword(s):  
Blood Group ◽  
Anion Exchanger ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Blood Group Antigen ◽  
Molecular Organization ◽  
Glycophorin A ◽  
Anion Exchanger 1

The Low-Incidence Blood Group Antigen, Wda, Is Associated with the Substitution Val557→ Met in Human Erythrocyte Band 3 (AE1)

Vox Sanguinis ◽  
1996 ◽  
Vol 71 (2) ◽  
pp. 118-120 ◽  
Author(s):  
Lesley J. Bruce ◽  
Teresa Zelinski ◽  
Kay Ridgwell ◽  
Michael J. A. Tanner
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Blood Group Antigen ◽  
Low Incidence

The Low-Incidence Blood Group Antigen, Wda, Is Associated with Substitution Val(557-> Met in Human Erythrocyte Band 3 (AE1)

Vox Sanguinis ◽  
1996 ◽  
Vol 71 (2) ◽  
pp. 118-120
Author(s):  
Lesley J. Bruce ◽  
Teresa Zelinski ◽  
Kay Ridgwell ◽  
Michael J. A. Tanner
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Blood Group Antigen ◽  
Low Incidence

Interaction of anion exchanger 1 and glycophorin A in human erythroleukaemic K562 cells

2009 ◽  
Vol 421 (3) ◽  
pp. 345-356 ◽  
Author(s):  
Allison J. Pang ◽  
Reinhart A. F. Reithmeier
Keyword(s):  
Cell Surface ◽  
Anion Exchanger ◽  
K562 Cells ◽  
Surface Expression ◽  
Protein Band ◽  
Band 3 ◽  
Cell Surface Expression ◽  
Glycophorin A ◽  
Anion Exchanger 1 ◽  
Integral Proteins

AE1 [anion exchanger 1, also known as SLC4A1 (solute carrier family 4, anion exchanger, member 1) and band 3 (erythrocyte membrane protein band 3)] is a major membrane glycoprotein expressed in human erythrocytes where it mediates the exchange of chloride and bicarbonate across the plasma membrane. Glycophorin A (GPA) is a sialoglycoprotein that associates with AE1 in erythrocytes forming the Wrb (Wright b) blood group antigen. These two integral proteins may also form a complex during biosynthesis, with GPA facilitating the cell surface expression of AE1. This study investigates the interaction of GPA with AE1 in K562 cells, a human erythroleukaemic cell line that expresses GPA, and the role of GPA in the cell surface expression of AE1. In K562 cells, GPA was dimeric and N- and O-glycosylated similar to erythroid GPA. GPA was localized at the cell surface, but also localized to the Golgi. AE1 expressed in K562 cells contained both complex and high-mannose oligosaccharides, and co-localized with GPA at the cell surface and in the endoplasmic reticulum (ER). The Wrb antigen was detected at the cell surface of AE1-transfected K562 cells, indicating the existence of an AE1–GPA complex. Immunofluorescence and co-immunoprecipitation studies using AE1 and an ER-localized hereditary spherocytosis mutant (R760Q AE1) showed that GPA and AE1 could interact in the ER. GPA knockdown by shRNAs (small-hairpin RNAs), however, had no effect on the level of cell surface expression of AE1. The results indicate that AE1 and GPA form a complex in the ER of human K562 cells, but that both proteins can also traffic to the cell surface independently of each other.

scholarly journals Miltenberger blood group antigen type III (Mi.III) enhances the expression of band 3

Blood ◽  
2009 ◽  
Vol 114 (9) ◽  
pp. 1919-1928 ◽  
Author(s):  
Kate Hsu ◽  
Naiwen Chi ◽  
Marjan Gucek ◽  
Jennifer E. Van Eyk ◽  
Robert N. Cole ◽  
...  
Keyword(s):  
Blood Group ◽  
Surface Expression ◽  
Hybrid Structure ◽  
Blood Group Antigen ◽  
Hek293 Cells ◽  
Erythrocyte Membranes ◽  
Glycophorin A ◽  
Ph Homeostasis ◽  
Anion Exchanger 1 ◽  
Glycophorin B

The special blood group antigen Mi.III exhibits a characteristic hybrid structure of glycophorin A (GPA) and glycophorin B, termed Gp.Mur. This phenotype has exceptionally high occurrence rates in several indigenous tribes in Taiwan (∼21.2%-88.4%). Because glycophorin/Miltenberger begins interaction with anion exchanger-1 (AE1) in the endoplasmic reticulum, we hypothesized that the AE1-based macrocomplexes on erythrocyte membranes obtained from Mi.III+ people could be differentiated from those obtained from non-Miltenberger people. Quantitative mass spectrometric comparison of the AE1-based complexes by iTRAQ™ (Applied Biosystems) revealed 25% to 67% higher expression of AE1 in Mi.III+ erythrocytes. In accordance with the higher AE1 level, the Mi.III+ erythrocytes exhibited superior HCO3− capacities, pH homeostasis, and osmotic resistance. Cotransfection experiments in HEK293 cells showed that Gp.Mur, like GPA, enhanced trafficking of AE1 to the plasma membrane. In summary, the increased surface expression of AE1 in Mi.III+ erythrocytes could be attributed to the additive effect of GPA and Gp.Mur coexpression.

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