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Human cell-surface glycoprotein with unusual properties

Nature volume 286, pages 888891 (28 August 1980) | Download Citation

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Abstract

We report here the identification of human cell-surface glycoprotein with unusual and interesting properties. We initially detected this glycoprotein on the surface of cultured human haematopoietic cell lines by means of a monoclonal antibody. Although it is expressed on all cultured human haematopoietic cell lines tested, including the inducible promyelocytic tumour cell line HL-60 (ref. 1), it is not present in readily detectable amounts on most normal or leukaemic human haematopoietic cells. HL-60 cells, on exposure in vitro to appropriate chemical inducers, undergo morphological and functional differentiation along the granulocytic pathway or into macrophage-like cells2–6. One consequence of in vitro induction is the specific loss of the glycoprotein from the surface of HL-60 cells. The molecule does not, however, seem to be a highly tissue-specific differentiation antigen because it is also found on human tumour cell lines derived from non-haematopoietic tissues. Rather, its expression seems to be related to cell proliferation. Preliminary chemical characterization suggests that the glycoprotein may be identical to the abnormal glycoprotein previously reported by Bramwell and Harris to be associated with malignancy7,8.

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References

  1. 1.

    et al. Blood 54, 713–733 (1979).

  2. 2.

    , , & Proc. natn. Acad. Sci. U.S.A. 75, 2458–2462 (1978).

  3. 3.

    , , & J. exp. Med. 149, 969–973 (1979).

  4. 4.

    , & Proc. natn. Acad. Sci. U.S.A. 76, 2779–2783 (1979).

  5. 5.

    & Proc. natn. Acad. Sci. U.S.A. 76, 1293–1297 (1979).

  6. 6.

    , & Proc. natn. Acad. Sci. U.S.A. 76, 4087–4091 (1979).

  7. 7.

    & Proc. R. Soc. A201, 87–106 (1978).

  8. 8.

    & Proc. R. Soc. A203, 93–96 (1979).

  9. 9.

    & Blood 45, 321–334 (1975).

  10. 10.

    & Nature 256, 495–497 (1975).

  11. 11.

    J. exp. Med. 148, 313–323 (1978).

  12. 12.

    & Eur. J. Immun. 5, 274–281 (1974).

  13. 13.

    , & Nature 284, 69–70 (1980).

  14. 14.

    , & Blood 54, 95–104 (1979).

  15. 15.

    , , & Biochim. biophys. Acta 355, 260–299 (1974).

  16. 16.

    , & J. cell. Physiol. 102, 217–222 (1980).

  17. 17.

    & Biochim. biophys. Acta 516, 129–166 (1978).

  18. 18.

    , & Proc. natn. Acad. Sci. U.S.A. 72, 157–161 (1975).

  19. 19.

    & J. biol. Chem. 255, 1662–1669 (1980).

  20. 20.

    in Methods in Virology Vol. 5 (eds Maramorosch, K. & Koprowski, H.) 179–246 (Academic, New York, 1971).

  21. 21.

    & FEBS Lett. 82, 314–316 (1977).

  22. 22.

    & Science 184, 1297–1298 (1974).

  23. 23.

    Proc. natn. Acad. Sci. U.S.A. 70, 3650–3654 (1973).

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Author information

Affiliations

  1. Department of Cancer Biology, The Salk Institute for Biological Studies, Post Office Box 85800, San Diego, California 92138

    • M. Bishr Omary
    •  & Ian S. Trowbridge
  2. Cell Culture Laboratory, Department of Immunology and Immunochemistry Research, Roswell Park Memorial Institute, New York State Department of Health, 666 Elm Street, Buffalo, New York 14623

    • Jun Minowada

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https://doi.org/10.1038/286888a0

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