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. 1994 Apr 1;299(Pt 1):191–196. doi: 10.1042/bj2990191

Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D.

N J Hemming 1, D J Anstee 1, W J Mawby 1, M E Reid 1, M J Tanner 1
PMCID: PMC1138040  PMID: 8166640

Abstract

The flexibility of the human erythrocyte membrane is mediated by an underlying network of skeletal proteins which interact with the membrane through ankyrin and protein 4.1. The nature of the membrane attachment site(s) for protein 4.1 has yet to be fully elucidated. In this paper we show that purified protein 4.1 binds much less strongly to alkali-stripped membranes from erythrocytes of individuals with total glycophorin C and D deficiency (Leach phenotype) than to alkali-stripped normal membranes. We further show that a synthetic peptide corresponding to amino acid residues 82-98 of the cytoplasmic domain of glycophorin C specifically binds to purified protein 4.1 and inhibits protein 4.1 binding to alkali-stripped normal membranes. The same synthetic peptide binds directly to membranes from individuals with glycophorin C and D deficiency but not to normal membranes. These results indicate that glycophorins C and D provide major membrane attachment sites for protein 4.1 in normal erythrocytes and that this interaction is mediated by protein 4.1 binding to amino acid residues 82-98 of glycophorin C and 61-77 of glycophorin D.

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Selected References

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  1. Alloisio N., Morlé L., Bachir D., Guetarni D., Colonna P., Delaunay J. Red cell membrane sialoglycoprotein beta in homozygous and heterozygous 4.1(-) hereditary elliptocytosis. Biochim Biophys Acta. 1985 Jun 11;816(1):57–62. doi: 10.1016/0005-2736(85)90392-x. [DOI] [PubMed] [Google Scholar]
  2. Anstee D. J., Parsons S. F., Ridgwell K., Tanner M. J., Merry A. H., Thomson E. E., Judson P. A., Johnson P., Bates S., Fraser I. D. Two individuals with elliptocytic red cells apparently lack three minor erythrocyte membrane sialoglycoproteins. Biochem J. 1984 Mar 1;218(2):615–619. doi: 10.1042/bj2180615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bennett V. The membrane skeleton of human erythrocytes and its implications for more complex cells. Annu Rev Biochem. 1985;54:273–304. doi: 10.1146/annurev.bi.54.070185.001421. [DOI] [PubMed] [Google Scholar]
  4. Cohen A. M., Liu S. C., Lawler J., Derick L., Palek J. Identification of the protein 4.1 binding site to phosphatidylserine vesicles. Biochemistry. 1988 Jan 26;27(2):614–619. doi: 10.1021/bi00402a018. [DOI] [PubMed] [Google Scholar]
  5. Cohen C. M., Foley S. F. The role of band 4.1 in the association of actin with erythrocyte membranes. Biochim Biophys Acta. 1982 Jun 28;688(3):691–701. doi: 10.1016/0005-2736(82)90281-4. [DOI] [PubMed] [Google Scholar]
  6. Conboy J., Mohandas N., Tchernia G., Kan Y. W. Molecular basis of hereditary elliptocytosis due to protein 4.1 deficiency. N Engl J Med. 1986 Sep 11;315(11):680–685. doi: 10.1056/NEJM198609113151105. [DOI] [PubMed] [Google Scholar]
  7. DODGE J. T., MITCHELL C., HANAHAN D. J. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys. 1963 Jan;100:119–130. doi: 10.1016/0003-9861(63)90042-0. [DOI] [PubMed] [Google Scholar]
  8. Daniels G. L., Shaw M. A., Judson P. A., Reid M. E., Anstee D. J., Colpitts P., Cornwall S., Moore B. P., Lee S. A family demonstrating inheritance of the Leach phenotype: a Gerbich-negative phenotype associated with elliptocytosis. Vox Sang. 1986;50(2):117–121. doi: 10.1111/j.1423-0410.1986.tb04860.x. [DOI] [PubMed] [Google Scholar]
  9. Danilov Y. N., Fennell R., Ling E., Cohen C. M. Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase C. J Biol Chem. 1990 Feb 15;265(5):2556–2562. [PubMed] [Google Scholar]
  10. Gardner B., Anstee D. J., Mawby W. J., Tanner M. J., von dem Borne A. E. The abundance and organization of polypeptides associated with antigens of the Rh blood group system. Transfus Med. 1991 Jun;1(2):77–85. doi: 10.1111/j.1365-3148.1991.tb00013.x. [DOI] [PubMed] [Google Scholar]
  11. Green N., Alexander H., Olson A., Alexander S., Shinnick T. M., Sutcliffe J. G., Lerner R. A. Immunogenic structure of the influenza virus hemagglutinin. Cell. 1982 Mar;28(3):477–487. doi: 10.1016/0092-8674(82)90202-1. [DOI] [PubMed] [Google Scholar]
  12. Jöns T., Drenckhahn D. Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger. EMBO J. 1992 Aug;11(8):2863–2867. doi: 10.1002/j.1460-2075.1992.tb05354.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lombardo C. R., Willardson B. M., Low P. S. Localization of the protein 4.1-binding site on the cytoplasmic domain of erythrocyte membrane band 3. J Biol Chem. 1992 May 15;267(14):9540–9546. [PubMed] [Google Scholar]
  14. Lovrien R. E., Anderson R. A. Stoichiometry of wheat germ agglutinin as a morphology controlling agent and as a morphology controlling agent and as a morphology protective agent for the human erythrocyte. J Cell Biol. 1980 Jun;85(3):534–548. doi: 10.1083/jcb.85.3.534. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Mallinson G., Martin P. G., Anstee D. J., Tanner M. J., Merry A. H., Tills D., Sonneborn H. H. Identification and partial characterization of the human erythrocyte membrane component(s) that express the antigens of the LW blood-group system. Biochem J. 1986 Mar 15;234(3):649–652. doi: 10.1042/bj2340649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. McGuire M., Smith B. L., Agre P. Distinct variants of erythrocyte protein 4.1 inherited in linkage with elliptocytosis and Rh type in three white families. Blood. 1988 Jul;72(1):287–293. [PubMed] [Google Scholar]
  17. Pasternack G. R., Anderson R. A., Leto T. L., Marchesi V. T. Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton. J Biol Chem. 1985 Mar 25;260(6):3676–3683. [PubMed] [Google Scholar]
  18. Pinder J. C. Red cell membrane cytoskeleton and the control of membrane properties. Biochem Soc Trans. 1991 Nov;19(4):1039–1041. doi: 10.1042/bst0191039. [DOI] [PubMed] [Google Scholar]
  19. Presant C. A., Kornfeld S. Characterization of the cell surface receptor for the Agaricus bisporus hemagglutinin. J Biol Chem. 1972 Nov 10;247(21):6937–6945. [PubMed] [Google Scholar]
  20. Reid M. E., Anstee D. J., Tanner M. J., Ridgwell K., Nurse G. T. Structural relationships between human erythrocyte sialoglycoproteins beta and gamma and abnormal sialoglycoproteins found in certain rare human erythrocyte variants lacking the Gerbich blood-group antigen(s). Biochem J. 1987 May 15;244(1):123–128. doi: 10.1042/bj2440123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Reid M. E., Takakuwa Y., Conboy J., Tchernia G., Mohandas N. Glycophorin C content of human erythrocyte membrane is regulated by protein 4.1. Blood. 1990 Jun 1;75(11):2229–2234. [PubMed] [Google Scholar]
  22. Sato S. B., Ohnishi S. Interaction of a peripheral protein of the erythrocyte membrane, band 4.1, with phosphatidylserine-containing liposomes and erythrocyte inside-out vesicles. Eur J Biochem. 1983 Jan 17;130(1):19–25. doi: 10.1111/j.1432-1033.1983.tb07111.x. [DOI] [PubMed] [Google Scholar]
  23. Steck T. L. The organization of proteins in the human red blood cell membrane. A review. J Cell Biol. 1974 Jul;62(1):1–19. doi: 10.1083/jcb.62.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Walder J. A., Walder R. Y., Heller M. J., Freier S. M., Letsinger R. L., Klotz I. M. Complementary carrier peptide synthesis: general strategy and implications for prebiotic origin of peptide synthesis. Proc Natl Acad Sci U S A. 1979 Jan;76(1):51–55. doi: 10.1073/pnas.76.1.51. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Yannoukakos D., Vasseur C., Driancourt C., Blouquit Y., Delaunay J., Wajcman H., Bursaux E. Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56----Glu) by protein chemistry methods. Blood. 1991 Aug 15;78(4):1117–1120. [PubMed] [Google Scholar]

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