Skip to main content
NCBI home page
Clinical and Experimental Immunology logoLink to Clinical and Experimental Immunology
. 1988 Aug;73(2):186–190.

Tumour necrosis factor (cachectin) production during experimental Chagas' disease.

R L Tarleton 1
PMCID: PMC1541603  PMID: 3141092

Abstract

Mice infected with the protozoan parasite Trypanosoma cruzi are primed for the production of tumour necrosis factor/cachectin. Active infection is not required for stimulation of TNF production as formalin-fixed, but not heat-killed, parasites can act as a priming stimulus. Both epimastigote and trypomastigote stages of the parasite can prime for TNF production but on a per cell basis, trypomastigotes are more potent stimulators than epimastigotes and live parasites prime more efficiently than killed preparations. Although the priming effect of epimastigotes and trypomastigotes is dose-dependent when assayed 10 days after parasite injection, parasitemia levels in the infected mice do not correlate with the level of TNF production. Spleen cells from infected mice are also primed for the production in vitro of TNF in response to LPS or T. cruzi. These results suggest that TNF may be constitutively produced in vivo and that the priming for TNF production, or the production itself, may be regulated during the course of the infection in mice.

Full text

PDF
186

Selected References

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

  1. Beutler B. A., Milsark I. W., Cerami A. Cachectin/tumor necrosis factor: production, distribution, and metabolic fate in vivo. J Immunol. 1985 Dec;135(6):3972–3977. [PubMed] [Google Scholar]
  2. Beutler B., Cerami A. Cachectin and tumour necrosis factor as two sides of the same biological coin. Nature. 1986 Apr 17;320(6063):584–588. doi: 10.1038/320584a0. [DOI] [PubMed] [Google Scholar]
  3. Beutler B., Greenwald D., Hulmes J. D., Chang M., Pan Y. C., Mathison J., Ulevitch R., Cerami A. Identity of tumour necrosis factor and the macrophage-secreted factor cachectin. Nature. 1985 Aug 8;316(6028):552–554. doi: 10.1038/316552a0. [DOI] [PubMed] [Google Scholar]
  4. Beutler B., Mahoney J., Le Trang N., Pekala P., Cerami A. Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced RAW 264.7 cells. J Exp Med. 1985 May 1;161(5):984–995. doi: 10.1084/jem.161.5.984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Clark I. A., Virelizier J. L., Carswell E. A., Wood P. R. Possible importance of macrophage-derived mediators in acute malaria. Infect Immun. 1981 Jun;32(3):1058–1066. doi: 10.1128/iai.32.3.1058-1066.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cunningham D. S., Kuhn R. E. Lymphoblast transformation as a measure of immune competence during experimental Chagas' disease. J Parasitol. 1980 Jun;66(3):390–398. [PubMed] [Google Scholar]
  7. Cunningham D. S., Kuhn R. E., Rowland E. C. Suppression of humoral responses during Trypanosoma cruzi infections in mice. Infect Immun. 1978 Oct;22(1):155–160. doi: 10.1128/iai.22.1.155-160.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cunningham D. S., Kuhn R. E. Trypanosoma cruzi-induced suppression of the primary immune response in murine cell cultures to T-cell-dependent and -independent antigens. J Parasitol. 1980 Feb;66(1):16–27. [PubMed] [Google Scholar]
  9. Dayer J. M., Beutler B., Cerami A. Cachectin/tumor necrosis factor stimulates collagenase and prostaglandin E2 production by human synovial cells and dermal fibroblasts. J Exp Med. 1985 Dec 1;162(6):2163–2168. doi: 10.1084/jem.162.6.2163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Dinarello C. A. An update on human interleukin-1: from molecular biology to clinical relevance. J Clin Immunol. 1985 Sep;5(5):287–297. doi: 10.1007/BF00918247. [DOI] [PubMed] [Google Scholar]
  11. Dinarello C. A., Cannon J. G., Wolff S. M., Bernheim H. A., Beutler B., Cerami A., Figari I. S., Palladino M. A., Jr, O'Connor J. V. Tumor necrosis factor (cachectin) is an endogenous pyrogen and induces production of interleukin 1. J Exp Med. 1986 Jun 1;163(6):1433–1450. doi: 10.1084/jem.163.6.1433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Flick D. A., Gifford G. E. Comparison of in vitro cell cytotoxic assays for tumor necrosis factor. J Immunol Methods. 1984 Mar 30;68(1-2):167–175. doi: 10.1016/0022-1759(84)90147-9. [DOI] [PubMed] [Google Scholar]
  13. Gamble J. R., Harlan J. M., Klebanoff S. J., Vadas M. A. Stimulation of the adherence of neutrophils to umbilical vein endothelium by human recombinant tumor necrosis factor. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8667–8671. doi: 10.1073/pnas.82.24.8667. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Haidaris C. G., Haynes J. D., Meltzer M. S., Allison A. C. Serum containing tumor necrosis factor is cytotoxic for the human malaria parasite Plasmodium falciparum. Infect Immun. 1983 Oct;42(1):385–393. doi: 10.1128/iai.42.1.385-393.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Hotez P. J., Le Trang N., Fairlamb A. H., Cerami A. Lipoprotein lipase suppression in 3T3-L1 cells by a haematoprotozoan-induced mediator from peritoneal exudate cells. Parasite Immunol. 1984 May;6(3):203–209. doi: 10.1111/j.1365-3024.1984.tb00793.x. [DOI] [PubMed] [Google Scholar]
  16. Krassner S. M., Granger B., Morrow C., Granger G. In vitro release of lymphotoxin by spleen cells from C3H/HEJ and C57BL/6 mice infected with Trypanosoma cruzi. Am J Trop Med Hyg. 1982 Nov;31(6):1080–1089. doi: 10.4269/ajtmh.1982.31.1080. [DOI] [PubMed] [Google Scholar]
  17. Landegren U. Measurement of cell numbers by means of the endogenous enzyme hexosaminidase. Applications to detection of lymphokines and cell surface antigens. J Immunol Methods. 1984 Mar 16;67(2):379–388. doi: 10.1016/0022-1759(84)90477-0. [DOI] [PubMed] [Google Scholar]
  18. Nedwin G. E., Svedersky L. P., Bringman T. S., Palladino M. A., Jr, Goeddel D. V. Effect of interleukin 2, interferon-gamma, and mitogens on the production of tumor necrosis factors alpha and beta. J Immunol. 1985 Oct;135(4):2492–2497. [PubMed] [Google Scholar]
  19. Nogueira N., Gordon S., Cohn Z. Trypanosoma cruzi: modification of macrophage function during infection. J Exp Med. 1977 Jul 1;146(1):157–171. doi: 10.1084/jem.146.1.157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Old L. J. Tumor necrosis factor (TNF). Science. 1985 Nov 8;230(4726):630–632. doi: 10.1126/science.2413547. [DOI] [PubMed] [Google Scholar]
  21. Plata F., Garcia Pons F., Eisen H. Antigenic polymorphism of Trypanosoma cruzi: clonal analysis of trypomastigote surface antigens. Eur J Immunol. 1984 May;14(5):392–399. doi: 10.1002/eji.1830140503. [DOI] [PubMed] [Google Scholar]
  22. Powell M. R., Kuhn R. E. Measurement of cytolytic antibody in experimental Chagas' disease using a terminal radiolabelling procedure. J Parasitol. 1980 Jun;66(3):399–406. [PubMed] [Google Scholar]
  23. Rouzer C. A., Cerami A. Hypertriglyceridemia associated with Trypanosoma brucei brucei infection in rabbits: role of defective triglyceride removal. Mol Biochem Parasitol. 1980 Oct;2(1):31–38. doi: 10.1016/0166-6851(80)90046-8. [DOI] [PubMed] [Google Scholar]
  24. Silberstein D. S., David J. R. Tumor necrosis factor enhances eosinophil toxicity to Schistosoma mansoni larvae. Proc Natl Acad Sci U S A. 1986 Feb;83(4):1055–1059. doi: 10.1073/pnas.83.4.1055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Sugarman B. J., Aggarwal B. B., Hass P. E., Figari I. S., Palladino M. A., Jr, Shepard H. M. Recombinant human tumor necrosis factor-alpha: effects on proliferation of normal and transformed cells in vitro. Science. 1985 Nov 22;230(4728):943–945. doi: 10.1126/science.3933111. [DOI] [PubMed] [Google Scholar]
  26. Tarleton R. L., Kuhn R. E. Changes in cell populations and immunoglobulin-producing cells in the spleens of mice infected with Trypanosoma cruzi: correlations with parasite-specific antibody response. Cell Immunol. 1983 Sep;80(2):392–404. doi: 10.1016/0008-8749(83)90126-0. [DOI] [PubMed] [Google Scholar]
  27. Tarleton R. L., Kuhn R. E. Measurement of parasite-specific immune responses in vitro: evidence for suppression of the antibody response to Trypanosoma cruzi. Eur J Immunol. 1985 Aug;15(8):845–850. doi: 10.1002/eji.1830150820. [DOI] [PubMed] [Google Scholar]
  28. Tarleton R. L., Kuhn R. E. Restoration of in vitro immune responses of spleen cells from mice infected with Trypanosoma cruzi by supernatants containing interleukin 2. J Immunol. 1984 Sep;133(3):1570–1575. [PubMed] [Google Scholar]
  29. Taverne J., Dockrell H. M., Playfair J. H. Endotoxin-induced serum factor kills malarial parasites in vitro. Infect Immun. 1981 Jul;33(1):83–89. doi: 10.1128/iai.33.1.83-89.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Wood P. R., Clark I. A. Macrophages from Babesia and malaria infected mice are primed for monokine release. Parasite Immunol. 1984 Jul;6(4):309–317. doi: 10.1111/j.1365-3024.1984.tb00803.x. [DOI] [PubMed] [Google Scholar]
  31. Wozencraft A. O., Dockrell H. M., Taverne J., Targett G. A., Playfair J. H. Killing of human malaria parasites by macrophage secretory products. Infect Immun. 1984 Feb;43(2):664–669. doi: 10.1128/iai.43.2.664-669.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Clinical and Experimental Immunology are provided here courtesy of British Society for Immunology

RESOURCES