scholarly journals Inverse effects of dansylation of red blood cell membrane on band 3 protein-mediated transport of sulphate and chloride

1982 ◽  
Vol 328 (1) ◽  
pp. 27-48 ◽  
Author(s):  
Sigrid Lepke ◽  
Hermann Passow
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Band 3 ◽  
Band 3 Protein ◽  
Red Blood Cell Membrane

Modeling of band-3 protein diffusion in the normal and defective red blood cell membrane

Soft Matter ◽  
2016 ◽  
Vol 12 (15) ◽  
pp. 3643-3653 ◽  
Author(s):  
He Li ◽  
Yihao Zhang ◽  
Vi Ha ◽  
George Lykotrafitis
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Band 3 ◽  
Protein Diffusion ◽  
Band 3 Protein ◽  
Red Blood Cell Membrane

scholarly journals Complete Deficiency of Glycophorin A in Red Blood Cells From Mice With Targeted Inactivation of the Band 3 (AE1) Gene

Blood ◽  
1998 ◽  
Vol 91 (6) ◽  
pp. 2146-2151 ◽  
Author(s):  
Hani Hassoun ◽  
Toshihiko Hanada ◽  
Mohini Lutchman ◽  
Kenneth E. Sahr ◽  
Jiri Palek ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Blood Cells ◽  
Band 3 ◽  
Glycophorin A ◽  
Blood Group Antigens ◽  
Red Blood Cell Membrane ◽  
Anion Transporter

Abstract Glycophorin A is the major transmembrane sialoglycoprotein of red blood cells. It has been shown to contribute to the expression of the MN and Wright blood group antigens, to act as a receptor for the malaria parasite Plasmodium falciparum and Sendai virus, and along with the anion transporter, band 3, may contribute to the mechanical properties of the red blood cell membrane. Several lines of evidence suggest a close interaction between glycophorin A and band 3 during their biosynthesis. Recently, we have generated mice where the band 3 expression was completely eliminated by selective inactivation of the AE1 anion exchanger gene, thus allowing us to study the effect of band 3 on the expression of red blood cell membrane proteins. In this report, we show that the band 3 −/− red blood cells contain protein 4.1, adducin, dematin, p55, and glycophorin C. In contrast, the band 3 −/− red blood cells are completely devoid of glycophorin A (GPA), as assessed by Western blot and immunocytochemistry techniques, whereas the polymerase chain reaction (PCR) confirmed the presence of GPA mRNA. Pulse-label and pulse-chase experiments show that GPA is not incorporated in the membrane and is rapidly degraded in the cytoplasm. Based on these findings and other published evidence, we propose that band 3 plays a chaperone-like role, which is necessary for the recruitment of GPA to the red blood cell plasma membrane.

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