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. 1981 Dec;1(12):1150–1162. doi: 10.1128/mcb.1.12.1150

Membrane protein redistribution during differentiation of cultured human erythroleukemic cells.

R C Hunt, L M Marshall
PMCID: PMC369741  PMID: 6955588

Abstract

Human erythroleukemic (K562) cells differentiate along the erythroid differentiation pathway in vitro when 0.05 mM hemin is included in the growth medium. In the presence of the inducer the cells continue to proliferate and, after a delay of 24 to 48 h, start to synthesize hemoglobin. However, during differentiation, no changes in the major cell surface proteins were detected using lactoperoxidase-catalyzed iodination, and no change in the synthesis of spectrin, the major cytoskeletal protein of the mature erythrocyte, was detected by specific immune precipitation. Despite this absence of major changes in cell surface proteins, profound changes take place in the organization of the cell membranes. A process similar but not identical to the enucleation observed in erythroid differentiation in vivo occurs in which a smooth-surfaced cell, about 10 micrometers in diameter, is divided from the nucleus-containing part of the cell. With the exception of ribosomes, these reticulocyte-like cells contain no organelles when examined by transmission electron microscopy, but contain much of the parent cell's hemoglobin, spectrin, and glycophorin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andersson L. C., Jokinen M., Gahmberg C. G. Induction of erythroid differentiation in the human leukaemia cell line K562. Nature. 1979 Mar 22;278(5702):364–365. doi: 10.1038/278364a0. [DOI] [PubMed] [Google Scholar]
  2. Andersson L. C., Nilsson K., Gahmberg C. G. K562--a human erythroleukemic cell line. Int J Cancer. 1979 Feb;23(2):143–147. doi: 10.1002/ijc.2910230202. [DOI] [PubMed] [Google Scholar]
  3. Bretscher M. S. Directed lipid flow in cell membranes. Nature. 1976 Mar 4;260(5546):21–23. doi: 10.1038/260021a0. [DOI] [PubMed] [Google Scholar]
  4. Bretscher M. S. Major human erythrocyte glycoprotein spans the cell membrane. Nat New Biol. 1971 Jun 23;231(25):229–232. doi: 10.1038/newbio231229a0. [DOI] [PubMed] [Google Scholar]
  5. Bretscher M. S., Thomson J. N., Pearse B. M. Coated pits act as molecular filters. Proc Natl Acad Sci U S A. 1980 Jul;77(7):4156–4159. doi: 10.1073/pnas.77.7.4156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cabantchik Z. I., Rothstein A. Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation. J Membr Biol. 1974;15(3):207–226. doi: 10.1007/BF01870088. [DOI] [PubMed] [Google Scholar]
  7. Cherry R. J., Bürkli A., Busslinger M., Schneider G., Parish G. R. Rotational diffusion of band 3 proteins in the human erythrocyte membrane. Nature. 1976 Sep 30;263(5576):389–393. doi: 10.1038/263389a0. [DOI] [PubMed] [Google Scholar]
  8. Eisen H., Bach R., Emery R. Induction of spectrin in erythroleukemic cells transformed by Friend virus. Proc Natl Acad Sci U S A. 1977 Sep;74(9):3898–3902. doi: 10.1073/pnas.74.9.3898. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Eisen H. Terminal erythroid differentiation in normal and leukemic mouse cells. Blood Cells. 1978;4(1-2):177–188. [PubMed] [Google Scholar]
  10. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  11. Friend C., Scher W., Holland J. G., Sato T. Hemoglobin synthesis in murine virus-induced leukemic cells in vitro: stimulation of erythroid differentiation by dimethyl sulfoxide. Proc Natl Acad Sci U S A. 1971 Feb;68(2):378–382. doi: 10.1073/pnas.68.2.378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Geiduschek J. B., Singer S. J. Molecular changes in the membranes of mouse erythroid cells accompanying differentiation. Cell. 1979 Jan;16(1):149–163. doi: 10.1016/0092-8674(79)90196-x. [DOI] [PubMed] [Google Scholar]
  13. Hamaguchi H., Cleve H. Solubilization and comparative analysis of mammalian erythrocyte membrane glycoproteins. Biochem Biophys Res Commun. 1972 Apr 28;47(2):459–464. doi: 10.1016/0006-291x(72)90736-x. [DOI] [PubMed] [Google Scholar]
  14. Hunt R. C., Marshall L. M. The interaction of lectins with the surface of differentiating erythroleukaemic cells. J Cell Sci. 1979 Aug;38:315–329. doi: 10.1242/jcs.38.1.315. [DOI] [PubMed] [Google Scholar]
  15. Hynes R. O. Alteration of cell-surface proteins by viral transformation and by proteolysis. Proc Natl Acad Sci U S A. 1973 Nov;70(11):3170–3174. doi: 10.1073/pnas.70.11.3170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  17. Lozzio C. B., Lozzio B. B. Human chronic myelogenous leukemia cell-line with positive Philadelphia chromosome. Blood. 1975 Mar;45(3):321–334. [PubMed] [Google Scholar]
  18. Lux S. E. Spectrin-actin membrane skeleton of normal and abnormal red blood cells. Semin Hematol. 1979 Jan;16(1):21–51. [PubMed] [Google Scholar]
  19. Marchesi V. T., Furthmayr H., Tomita M. The red cell membrane. Annu Rev Biochem. 1976;45:667–698. doi: 10.1146/annurev.bi.45.070176.003315. [DOI] [PubMed] [Google Scholar]
  20. Marchesi V. T. Isolation of spectrin from erythrocyte membranes. Methods Enzymol. 1974;32:275–277. doi: 10.1016/0076-6879(74)32028-9. [DOI] [PubMed] [Google Scholar]
  21. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  22. Rutherford T. R., Clegg J. B., Weatherall D. J. K562 human leukaemic cells synthesise embryonic haemoglobin in response to haemin. Nature. 1979 Jul 12;280(5718):164–165. doi: 10.1038/280164a0. [DOI] [PubMed] [Google Scholar]
  23. Skutelsky E., Farquhar M. G. Variations in distribution of con A receptor sites and anionic groups during red blood cell differentiation in the rat. J Cell Biol. 1976 Oct;71(1):218–231. doi: 10.1083/jcb.71.1.218. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Steck T. L., Koziarz J. J., Singh M. K., Reddy G., Köhler H. Preparation and analysis of seven major, topographically defined fragments of band 3, the predominant transmembrane polypeptide of human erythrocyte membranes. Biochemistry. 1978 Apr 4;17(7):1216–1222. doi: 10.1021/bi00600a013. [DOI] [PubMed] [Google Scholar]
  25. Stern P. L., Bretscher M. S. Capping of exogenous Forssman glycolipid on cells. J Cell Biol. 1979 Sep;82(3):829–833. doi: 10.1083/jcb.82.3.829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Turco S. J., Rush J. S., Laine R. A. Presence of erythroglycan on human K-562 chronic myelogenous leukemia-derived cells. J Biol Chem. 1980 Apr 25;255(8):3266–3269. [PubMed] [Google Scholar]
  27. Walter R. J., Berlin R. D., Pfeiffer J. R., Oliver J. M. Polarization of endocytosis and receptor topography on cultured macrophages. J Cell Biol. 1980 Jul;86(1):199–211. doi: 10.1083/jcb.86.1.199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wang E., Goldberg A. R. Binding of deoxyribonuclease I to actin: a new way to visualize microfilament bundles in nonmuscle cells. J Histochem Cytochem. 1978 Sep;26(9):745–749. doi: 10.1177/26.9.361884. [DOI] [PubMed] [Google Scholar]

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