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Clinical and Experimental Immunology logoLink to Clinical and Experimental Immunology
. 1984 Jun;56(3):701–708.

Purified plasminogen activating factor produced by malignant lymphoid cells abrogates lymphocyte cytotoxicity.

S K Sundar, J Bergeron, J Menezes
PMCID: PMC1536014  PMID: 6430612

Abstract

Immunosuppression is a generally observed phenomenon in patients with malignancies. Here we report that plasminogen activating factor (PAF) produced by human (P3HR-1) and simian (B95-8) lymphoid cells of malignant origin abrogates lymphocyte cytotoxicity. PAF has been purified from Epstein-Barr (EB) virus genome carrying lymphocyte cytotoxicity. PAF has been purified from Epstein-Barr (EB) virus genome carrying lymphoid lines by affinity chromatography using lysine-Sepharose columns. Purified PAF consistently inhibited Killer cell activity against the following targets: K-562, EB virus superinfected Raji cells and in vitro EB virus transformed autologous B lymphocytes. Furthermore PAF also inhibited the antibody-dependent cellular cytotoxicity. The results presented also indicate that PAF affects the effector lymphocytes and not the target cells. Taken together, these observations emphasize the importance of factors such as PAF, released by malignant cells, as inhibitors/modulators of immune mechanisms effective against tumour cells.

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Selected References

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  1. Allison A. C. Cell-mediated immune responses to virus infections and virus-induced tumours. Br Med Bull. 1967 Jan;23(1):60–65. doi: 10.1093/oxfordjournals.bmb.a070518. [DOI] [PubMed] [Google Scholar]
  2. Bluming A. Z., Ziegler J. L., Fass L., Herberman R. B. Delayed cutaneous sensitivity reactions to autologous Burkitt lymphoma protein extract. Results of a prospective two and a half year study. Clin Exp Immunol. 1971 Dec;9(6):713–719. [PMC free article] [PubMed] [Google Scholar]
  3. Fass L., Herberman R. B., Ziegler J. Delayed cutaneous hypersensitivity reactions to autologous extracts of Burkitt-lymphoma cells. N Engl J Med. 1970 Apr 2;282(14):776–780. doi: 10.1056/NEJM197004022821404. [DOI] [PubMed] [Google Scholar]
  4. Hatcher V. B., Oberman M. S., Lazarus G. S., Grayzel A. I. A cytotoxic proteinase isolated from human lymphocytes. J Immunol. 1978 Feb;120(2):665–670. [PubMed] [Google Scholar]
  5. Hewetson J. F., Golub S. H., Klien G., Singh S. Cellular reactions against Burkitt Lymphoma cells. I. Colony inhibition with effector cells from patients with Burkitt's lymphoma. Int J Cancer. 1972 Jul 15;10(1):142–149. doi: 10.1002/ijc.2910100119. [DOI] [PubMed] [Google Scholar]
  6. Kok P., Astrup T. Isolation and purification of a tissue plasminogen activator and its comparison with urokinase. Biochemistry. 1969 Jan;8(1):79–86. doi: 10.1021/bi00829a013. [DOI] [PubMed] [Google Scholar]
  7. Lai P. K., Mackay-Scollay E. M., Fimmel P. J., Alpers M. P., Keast D. Cell-mediated immunity to Epstein-Barr virus and a blocking factor in patients with infectious mononucleosis. Nature. 1974 Dec 13;252(5484):608–610. doi: 10.1038/252608a0. [DOI] [PubMed] [Google Scholar]
  8. Magrath I. T. Immunosuppression in Burkitt's lymphoma. I. Cutaneous reactivity to recall antigens: alterations induced by a tumour burden and by BCG administration. Int J Cancer. 1974 Jun 15;13(6):839–849. doi: 10.1002/ijc.2910130611. [DOI] [PubMed] [Google Scholar]
  9. Matsuo O., Rijken D. C., Collen D. Comparison of the relative fibrinogenolytic, fibrinolytic and thrombolytic properties of tissue plasminogen activator and urokinase in vitro. Thromb Haemost. 1981 Jun 30;45(3):225–229. [PubMed] [Google Scholar]
  10. Newcomb E. W., Silverstein S. C., Silagi S. Malignant mouse melanoma cells do not form tumors when mixed with cells of a non-malignant subclone: relationships between plasminogen activator expression by the tumor cells and the host's immune response. J Cell Physiol. 1978 May;95(2):169–177. doi: 10.1002/jcp.1040950206. [DOI] [PubMed] [Google Scholar]
  11. Patel P. C., Menezes J. Epstein-Barr virus (EBV)--lymphoid cell interactions. II. The influence of the EBV replication cycle on natural killing and antibody-dependent cellular cytotoxicity against EBV-infected cells. Clin Exp Immunol. 1982 Jun;48(3):589–601. [PMC free article] [PubMed] [Google Scholar]
  12. Radcliffe R., Heinze T. Isolation of plasminogen activator from human plasma by chromatography on lysine-sepharose. Arch Biochem Biophys. 1978 Jul;189(1):185–194. doi: 10.1016/0003-9861(78)90131-5. [DOI] [PubMed] [Google Scholar]
  13. Rijken D. C., Wijngaards G., Welbergen J. Immunological characterization of plasminogen activator activities in human tissues and body fluids. J Lab Clin Med. 1981 Apr;97(4):477–486. [PubMed] [Google Scholar]
  14. Sundar S. K., Ablashi D. V., Kamaraju L. S., Levine P. H., Faggioni A., Armstrong G. R., Pearson G. R., Krueger G. R., Hewetson J. F., Bertram G. Sera from patients with undifferentiated nasopharyngeal carcinoma contain a factor which abrogates specific Epstein-Barr virus antigen-induced lymphocyte response. Int J Cancer. 1982 Apr 15;29(4):407–412. doi: 10.1002/ijc.2910290408. [DOI] [PubMed] [Google Scholar]
  15. Thorsen S., Glas-Greenwalt P., Astrup T. Differences in the binding to fibrin of urokinase and tissue plasminogen activator. Thromb Diath Haemorrh. 1972 Aug 31;28(1):65–74. [PubMed] [Google Scholar]
  16. Unkeless J. C., Tobia A., Ossowski L., Quigley J. P., Rifkin D. B., Reich E. An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. I. Chick embryo fibroblast cultures transformed by avian RNA tumor viruses. J Exp Med. 1973 Jan 1;137(1):85–111. doi: 10.1084/jem.137.1.85. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Wainberg M. A., Israel E., Margolese R. G. Further studies on the mitogenic and immune-modulating effects of plasminogen activator. Immunology. 1982 Apr;45(4):715–720. [PMC free article] [PubMed] [Google Scholar]

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