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. 1975 Jul 1;66(1):76–85. doi: 10.1083/jcb.66.1.76

Receptor mobility and the binding of cells to lectin-coated fibers

PMCID: PMC2109514  PMID: 167030

Abstract

The ability of cells to bind to nylon fibers coated with lectin molecules interspaced with varying numbers of albumin molecules has been analyzed. The cells used were lymphoma cells, normal lymphocytes, myeloid leukemia cells, and normal and transformed fibroblasts, and the fibers were coated with different densities of concanavalin A or the lectins from soybean or wheat germ. Cells fixed with glutaraldehyde did not bind to lectin-coated fibers. The number of cells bound to fibers could be increased by increasing the density of lectin molecules on the fiber, the density of specific receptors on the cell, or the mobility of the receptors. It is suggested that binding of cells to fibers involves alignment and binding of specific cell surface receptors with lectin molecules immobilized on the fibers, and that this alignment requires short-range rapid lateral mobility (RLM) of the receptors. The titration of cell binding to fibers coated with different densities of lectin and albumin has been used to measure the relative RLM of unoccupied cell surface receptors for the lectin. The results indicate a relationship of RLM to lectin-induced cell-to-cell binding. The RLM or receptors for concanavalin A (Con A) was generally found to be higher than that of receptors for the lectins from wheat germ or soybean. Receptor RLM could be decreased by use of metabolic inhibitors or by lowering the temperature. Receptors for Con A had a lower RLM on normal fibroblasts than on SV40-transformed fibroblasts, and trypsinization of normal fibroblasts increased Con A receptor RLM. Normal lymphocytes, lymphoma cells, and lines of myeloid leukemia cells that can be induced to differentiate had a high receptor RLM, whereas lines of myeloid leukemia cells that could not be induced to differentiate had a low receptor RLM. These results suggest that the RLM of Con A receptors is related to the transformation of fibroblasts and the ability of myeloid leukemia cells to undergo differentiation

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Selected References

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

  1. Burger M. M. A difference in the architecture of the surface membrane of normal and virally transformed cells. Proc Natl Acad Sci U S A. 1969 Mar;62(3):994–1001. doi: 10.1073/pnas.62.3.994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. De Petris S., Raff M. C., Mallucci L. Ligand-induced redistribution of concanavalin A receptors on normal, trypsinized and transformed fibroblasts. Nat New Biol. 1973 Aug 29;244(139):275–278. doi: 10.1038/newbio244275a0. [DOI] [PubMed] [Google Scholar]
  3. Edelman G. M., Rutishauser U., Millette C. F. Cell fractionation and arrangement on fibers, beads, and surfaces. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2153–2157. doi: 10.1073/pnas.68.9.2153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Edelman G. M., Rutishauser U. Specific fractionation and manipulation of cells with chemically derivatized fibers and surfaces. Methods Enzymol. 1974;34:195–225. doi: 10.1016/s0076-6879(74)34018-9. [DOI] [PubMed] [Google Scholar]
  5. Edelman G. M., Yahara I., Wang J. L. Receptor mobility and receptor-cytoplasmic interactions in lymphocytes. Proc Natl Acad Sci U S A. 1973 May;70(5):1442–1446. doi: 10.1073/pnas.70.5.1442. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fibach E., Hayashi M., Sachs L. Control of normal differentiation of myeloid leukemic cells to macrophages and granulocytes. Proc Natl Acad Sci U S A. 1973 Feb;70(2):343–346. doi: 10.1073/pnas.70.2.343. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Inbar M., Ben-Bassat H., Sachs L. Difference in the mobility of lectin sites on the surfact membrane of normal lymphocytes and malignant lymphoma cells. Int J Cancer. 1973 Jul 15;12(1):93–99. doi: 10.1002/ijc.2910120110. [DOI] [PubMed] [Google Scholar]
  8. Inbar M., Huet C., Oseroff A. R., Ben-Bassat H., Sachs L. Inhibition of lectin agglutinability by fixation of the cell surface membrane. Biochim Biophys Acta. 1973 Jul 18;311(4):594–599. doi: 10.1016/0005-2736(73)90132-6. [DOI] [PubMed] [Google Scholar]
  9. Inbar M., Sachs L. Interaction of the carbohydrate-binding protein concanavalin A with normal and transformed cells. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1418–1425. doi: 10.1073/pnas.63.4.1418. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Inbar M., Shinitzky M., Sachs L. Rotational relaxation time of concanavalin A bound to the surface membrane of normal and malignant transformed cells. J Mol Biol. 1973 Dec 5;81(2):245–253. doi: 10.1016/0022-2836(73)90192-7. [DOI] [PubMed] [Google Scholar]
  11. KLEIN E., KLEIN G. ANTIGENIC PROPERTIES OF LYMPHOMAS INDUCED BY THE MOLONEY AGENT. J Natl Cancer Inst. 1964 Mar;32:547–568. [PubMed] [Google Scholar]
  12. Lis H., Sharon N. The biochemistry of plant lectins (phytohemagglutinins). Annu Rev Biochem. 1973;42(0):541–574. doi: 10.1146/annurev.bi.42.070173.002545. [DOI] [PubMed] [Google Scholar]
  13. Loor F., Forni L., Pernis B. The dynamic state of the lymphocyte membrane. Factors affecting the distribution and turnover of surface immunoglobulins. Eur J Immunol. 1972 Jun;2(3):203–212. doi: 10.1002/eji.1830020304. [DOI] [PubMed] [Google Scholar]
  14. Lotem J., Sachs L. Different blocks in the differentiation of myeloid leukemic cells. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3507–3511. doi: 10.1073/pnas.71.9.3507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Nagata Y., Burger M. M. Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding. J Biol Chem. 1974 May 25;249(10):3116–3122. [PubMed] [Google Scholar]
  16. Nicolson G. L. Temperature-dependent mobility of concanavalin A sites on tumour cell surfaces. Nat New Biol. 1973 Jun 13;243(128):218–220. doi: 10.1038/newbio243218a0. [DOI] [PubMed] [Google Scholar]
  17. Rosenblith J. Z., Ukena T. E., Yin H. H., Berlin R. D., Karnovsky M. J. A comparative evaluation of the distribution of concanavalin A-binding sites on the surfaces of normal, virally-transformed, and protease-treated fibroblasts. Proc Natl Acad Sci U S A. 1973 Jun;70(6):1625–1629. doi: 10.1073/pnas.70.6.1625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Rutishauser U., Sachs L. Cell-to-cell binding induced by different lectins. J Cell Biol. 1975 May;65(2):247–257. doi: 10.1083/jcb.65.2.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Rutishauser U., Sachs L. Receptor mobility and the mechanism of cell-cell binding induced by concanavalin A. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2456–2460. doi: 10.1073/pnas.71.6.2456. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sachs L. Regulation of membrane changes, differentiation, and malignancy in carcinogenesis. Harvey Lect. 1974;68:1–35. [PubMed] [Google Scholar]
  21. Shevach E. M., Stobo J. D., Green I. Immunoglobulin and theta-bearing murine leukemias and lymphomas. J Immunol. 1972 May;108(5):1146–1151. [PubMed] [Google Scholar]
  22. Vlodavsky I., Inbar M., Sachs L. Membrane changes and adenosine triphosphate content in normal and malignant transformed cells. Proc Natl Acad Sci U S A. 1973 Jun;70(6):1780–1784. doi: 10.1073/pnas.70.6.1780. [DOI] [PMC free article] [PubMed] [Google Scholar]

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