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Lectin Receptors and Lectin Resistance in Chinese Hamster Ovary Cells

  • Pamela Stanley
  • Jeremy P. Carver
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 84)

Abstract

Chinese hamster ovary (CHO) cells previously selected in a single-step for resistance to one or two different lectins and assigned to individual phenotyp-ic groups on the basis of their unique patterns of lectin resistance, have been examined for their lectin-binding abilities. The lectin-binding parameters of CHO cells were shown to be very complex in a detailed study of the binding of 125I-WGA to wild-type (WT) cells. On the basis of these results, standard assay conditions were established and comparative binding studies between the twenty-two WT and lectin-resistant (LecR) clones were performed. A general correlation of lectin resistance with decreased lectin-binding ability and of lectin sensitivity with increased lectinbinding ability was found, although several exceptions to this trend were observed.

Keywords

Chinese Hamster Ovary Cell Chinese Hamster Ovary Wheat Germ Agglutinin Lectin Binding Scatchard Plot 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    ADAIR, W. L and KORNFELD, S.: Isolation of the receptors for wheat germ agglutinin and the Ricinus communis lectins from human erythrocytes using affinity chromatography. J. Biol. Chem. 249 (1974) 4696.Google Scholar
  2. 2.
    BETEL, I. and van den BERG, K.J.: Interaction of concanavalin A with rat lymphocytes. Europ. J. Biochem. 30 (1972) 571.PubMedCrossRefGoogle Scholar
  3. 3.
    CUATRECASAS, P.: Interaction of wheat germ agglutinin and concanavalin A with isolated fat cells. Biochem. 12 (1973) 1312.CrossRefGoogle Scholar
  4. 4.
    DERANLEAU, D. A.: Theory of the measurement of weak molecular complexes. I. General considerations. J. Am. Chem. Soc. 91 (1969) 4044.CrossRefGoogle Scholar
  5. 5.
    GOTTLIEB, C., SKINNER, A.M. and KORNFELD, S.: Isolation of a clone of Chinese hamster ovary cells deficient in plant lectin-binding sites. Proc. Nat. Acad. Sci. (U.S.) 71 (1974) 1078.CrossRefGoogle Scholar
  6. 6.
    GOTTLIEB, C., BAENZIGER, J. and KORNFELD, S.: Deficient uridine diphosphate-N-acetylglucosamine glycoprotein N-acetylglucosamin-yltransferase activity in a clone of Chinese hamster ovary cells with altered surface glycoproteins. J. Biol. Chem. 250 (1975) 3303.PubMedGoogle Scholar
  7. 7.
    GUERINI, C., ZACHOWSKI, A., PRIGENT, B., PARAF, A., DUNIA, I., DIAWARA, M. -A. and BENEDETTI, E. L: Correlation between the mobility of inner plasma membrane structure and agglutination by concanaval-in A in two cell lines of MOPC 173 plasmacytoma cells. Proc. Nat. Acad. Sci. (U.S.) 71 (1974) 114.CrossRefGoogle Scholar
  8. 8.
    HUNTER, W.M. and GREENWOOD, F.C.: Preparation of lodine-131 labelled human growth hormone of high specific activity. Nature 194 (1962)495.PubMedCrossRefGoogle Scholar
  9. 9.
    HYMAN, R., LACORBIERE, M., STAVAREK, S- and NICOLSON, G.: Derivation of lymphoma variants with reduced sensitivity to plant lectins. J. Nat. Cancer Inst. 52 (1974) 963.PubMedGoogle Scholar
  10. 10.
    JULIANO, R. L. and STANLEY, P.: Altered cell surface glycoproteins in phytohemagglutinin-resistant mutants of Chinese hamster ovary cells. Bio-chim. Biophys. Acta 389 (1975) 401.CrossRefGoogle Scholar
  11. 11.
    LOWRY, O. H., ROSEBROUGH, N.J., FARR, A. L and RANDALL, R.J.: Protein measurements with the fol in phenol reagent. J. Biol. Chem. 193 (1951)265.PubMedGoogle Scholar
  12. 12.
    MEAGER, A., UNGKITCHANUKIT, A. and NAIRN, R.: Ricin resistance in baby hamster kidney cells. Nature 257 (1975) 137.PubMedCrossRefGoogle Scholar
  13. 13.
    MEAGER, A., UNGKITCHANUKIT, A. and HUGHES, R. C.: Variants of hamster fibroblasts resistant to Ricinus communis toxin (Ricin). Biochem. J. 154 (1976) 113.PubMedGoogle Scholar
  14. 14.
    NASPITZ, CH. K. and RICHTER, M.: The action of phytohemagglutinin in vivo and in vitro, a review. Progr. Allergy 12 (1968) 1.Google Scholar
  15. 15.
    NICOLSON, G. L.: The interactions of lectins with animal cell surfaces. Internat. Rev. Cytol. 39 (1974) 89.CrossRefGoogle Scholar
  16. 16.
    NICOLSON, G. L., BLAUSTEIN, J. and ETZLER, M. E.: Characterization of two plant lectins from Ricinus communis and their quantitative interaction with a murine lymphoma. Biochem. 13 (1974) 196.CrossRefGoogle Scholar
  17. 17.
    NICOLSON, G. L., ROBBINS, J.C. and HYMAN, R.: Cell surface receptors and their dynamics on toxin-treated malignant cells. J. Supra-molec. Struct. 4 (1976) 15.CrossRefGoogle Scholar
  18. 18.
    OZANNE, B.: Variants of Simian virus-40 transformed 3T3 cells that are resistant to concanavalin A. J. Virol. 12 (1973) 79.PubMedGoogle Scholar
  19. 19.
    REFSNES, K., OLSNES, S. and PIHL, A.: On the toxic proteins abrin and ricin. Studies of their binding to and entry into Ehrlich ascites cells. J. Biol. Chem. 249 (1974) 3557.PubMedGoogle Scholar
  20. 20.
    SCHNEBLI, H. P. and BACHI, T.: Reaction of lectins with human erythrocytes. Exptl. Cell Res. 91 (1975) 175.PubMedCrossRefGoogle Scholar
  21. 21.
    STAGG, B.H., TEMPERLEY, JOHN M. and ROCHMAN, H.: lodination and the biological activity of gastrin. Nature 228 (1970) 58.PubMedCrossRefGoogle Scholar
  22. 22.
    STANLEY, P., CAILLIBOT, V. and SIMINOVITCH, L.: Stable alterations at the cell membrane of Chinese hamster ovary cells resistant to the cytotoxicity of phytohemagglutinin. Somatic Cell Genetics 1 (1975) 3.PubMedCrossRefGoogle Scholar
  23. 23.
    STANLEY, P., CAILLIBOT, V. and SIMINOVITCH, L.: Selection and characterization of eight phenotypically distinct lines of lectin-resistant Chinese hamster ovary cells. Cell 6 (1975) 121.PubMedCrossRefGoogle Scholar
  24. 24.
    STANLEY, P., NARASIMHAN, S., SIMINOVITCH, L and SCHACHTER, H.: Chinese hamster ovary cells selected for resistance to the cytor-toxicity of phytohemagglutinin are deficient in a UDP-N-acetylgluco-samine:glycoprotein N-acetylglucosaminyltransferase activity. Proc. Nat. Acad. Sci. (U.S.) 72 (1975) 3323.CrossRefGoogle Scholar
  25. 25.
    STANLEY, P. and SIMINOVITCH, L.: Selection and characterization of Chinese hamster ovary cells resistant to the cytotoxicity of lectins. In Vitro 12 (1976) 208.PubMedCrossRefGoogle Scholar
  26. 26.
    YOUNG, N.M., LEON, M.A., TAKAHASHI, T., HOWARD, I. K. and SAGE, H.J.: Studies on a phytohemagglutinin from the lentil Ml. Reaction of Lens culinaris hemagglutinin with polysaccharides, glycoproteins, and lymphocytes. J. Biol. Chem. 246 (1971) 1596.PubMedGoogle Scholar
  27. 27.
    ZACHOWSKl, A., PRIGENT, B., MONSIGNY, M. and PARAF, A.: Susceptible and non-susceptible phenotypes of MOPC 173 plasmacytoma to the killing effect of concanavalin A: Study on the concanavalin A sites. Biochimie 56 (1974). 1621.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Pamela Stanley
    • 1
  • Jeremy P. Carver
    • 1
  1. 1.Department of Medical GeneticsUniversity of TorontoTorontoCanada

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