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Complete Deficiency of Glycophorin A in Red Blood Cells From Mice
With Targeted Inactivation of the Band 3 (AE1) Gene
Hani Hassoun,
Toshihiko Hanada,
Mohini Lutchman,
Kenneth E. Sahr,
Jiri Palek,
Manjit Hanspal, and
Athar H. Chishti
From the Laboratory of Tumor Cell Biology, Department of Biomedical
Research, St. Elizabeth's Medical Center, Tufts University School of
Medicine, Boston, MA.
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.
Blood, Vol. 91 No. 6 (March 15), 1998:
pp. 2146-2151
© 1998 by The American Society of Hematology.
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