Expression and role of heat-shock protein 65 (HSP65) in macrophages during Trypanosoma cruzi infection: Involvement of HSP65 in prevention of apoptosis of macrophages

Microbes and Infection

Volumn 1, Issue 6, 1999, Pages 419-427

  Sakai, Tohru ^a   Hisaeda, Hajime ^a   Ishikawa, Hiroyuki ^a   Maekawa, Yoichi ^a   Zhang, Manxin ^a   Nakao, Yoko ^a   Takeuchi, Tsutomu ^b   Matsumoto, Kozo ^a   Good, Robert A ^c   Himeno, Kunisuke ^a  

^a UNIVERSITY OF TOKUSHIMA   (Japan)

^b KEIO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c UNIVERSITY OF SOUTH FLORIDA   (United States)

Author keywords

Apoptosis; Heat shock protein; Trypanosoma cruzi

Indexed keywords

ANTISENSE OLIGONUCLEOTIDE; GAMMA INTERFERON; HEAT SHOCK PROTEIN 65; MESSENGER RNA; NITRIC OXIDE; TUMOR NECROSIS FACTOR ALPHA;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; APOPTOSIS; ARTICLE; CELL INTERACTION; CONTROLLED STUDY; FEMALE; INFECTION RESISTANCE; LYMPHOCYTE DIFFERENTIATION; LYMPHOCYTE FUNCTION; MACROPHAGE; MOUSE; NATURAL KILLER CELL; NONHUMAN; PARASITEMIA; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRAIN DIFFERENCE; SURVIVAL; T LYMPHOCYTE SUBPOPULATION; TRYPANOSOMA CRUZI; TRYPANOSOMIASIS;

ANIMALIA; PROTOZOA; TRYPANOSOMA; TRYPANOSOMA CRUZI;

EID: 0032721659     PISSN: 12864579     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1286-4579(99)80045-8     Document Type: Article

References (40)

1. Lindquist S. The heat-shock response. Annu. Rev. Biochem. 55:1986;1151-1191.
2. Pelham H. Heat-shock proteins: coming in from the cold. Nature. 332:1988;776-777.
3. Schlesinger M.J. Heat-shock proteins: the search for functions. J. Cell. Biol. 103:1986;321-325.
4. Jindal S., Dudani A.K., Singh B.S., Harley C.B., Gupta R.S. Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65 Kd mycobacterial antigen. Mol. Cell. Biol. 9:1989;2279-2283.
5. Garsia R.J., Hellqvist L., Booth R.J., Radford A.J., Britton W.J., Astbury L., Trent R.J., Basten A. Homology of the 80-kilodalton antigens from Mycobacterium leprae and Mycobacterium bovis with the Mycobacterium tuberculosis 71-kilodalton antigen and with the conserved heat-shock protein 70 of eukaryotes. Infect. Immun. 57:1989;204-212.
6. Birk O.S., Douek D.C., Elias D., Takacs K., Dewchand H., Gur S.L., Walker M.D., van der Zee R., Cohen I.R., Altmann D.M. A role of Hsp60 in autoimmune diabetes: analysis in a transgenic model. Proc. Natl. Acad. Sci. USA. 93:1996;1032-1037.
7. Prakken B.J., van der Zee R., Anderton S.M., van Kooten P.J.S., Kuis W., van den W. Peptide-induced nasal tolerance for a mycobacterial heat-shock protein 60 T cell epitope in rats suppresses both ajuvant arthritis and nonmicrobially induced experimental arthritis. Proc. Natl. Acad. Sci. USA. 94:1997;3284-3289.
8. Tascon R.E., Colston M.J., Ragno S., Stavropoulos E., Gregory D., Lowrie D.B. Vaccination against tuberculosis by DNA injection. Nat. M. 2:1996;888-892.
9. Brener Z. Immunity to Trypanosoma cruzi. Adv. Parasitiol. 18:1980;247-292.
10. Takle G.G., Snary D., Warren K.S. Immunology and Molecular Biology of Parasitic Infections. Warren K.S. Immunology and Molecular Biology of Parasitic Infections. 1992;213-236 Blackwell Scientific Publications, Oxford.
11. Pottenberg M.E., Sporrong L., Persson I., Wigzell H., Örn A. Cytokine gene expression during infection of mice lacking CD4 and/or CD8 with Trypanosoma cruzi, Scand. J. Immunol. 41:1995;164-170.
12. Rottenberg M., Cardoni R.L., Anderson R., Segura E.L., Örn A. Role of T helper/inducer cells as well as natural killer cells in resistance to Trypanosoma cruzi infection. Scand. J. Immunol. 28:1988;573-582.
13. + T cells increases susceptibility and reverses vaccine-induced immunity in mice infected with Trypanosoma cruzi. J. Immunol. 144:1990;717-724.
14. Cardillo F., Voltarelli J.C., Reed S.G., Silva J. Regulation of Trypanosoma cruzi infection in mice by gamma interferon and IL-10: role of NK cells. Infect. Immun. 64:1996;128-134.
15. Nagasawa H., Oka M., Maeda K., Jian-Guo C., Hisaeda H., Ito Y., Good R.A., Himeno K. Induction of heat-shock protein closely correlates with protection against Toxoplasma gondii infection. Proc. Natl. Acad. Sci. USA. 89:1992;3155-3158.
16. Himeno K., Nagasawa H., Hisaeda H. Role of 65-kDa heat-shock protein in protective immunity against Toxoplasma infection. J. Protozool. Res. 3:1993;72-80.
17. Nagasawa H., Hisaeda H., Maekawa Y., Fujioka H., Ito Y., Aikawa M., Himeno K. γδ T cells play a crucial role in the expression of 65000 MW heat-shock protein in mice immunized with Toxoplasma antigen. Immunology. 83:1994;347-352.
18. Hisaeda H., Nagasawa H., Maeda K., Maekawa Y., Ishikawa H., Ito Y., Good R.A., Himeno K. γδ T cells play an important role in hsp65 expression and in acquiring protective immune responses against infection with Toxoplasma gondii. J. Immunol. 154:1995;244-251.
19. Hisaeda H., Sakai T., Nagasawa H., Ishikawa H., Yasutomo K., Maekawa Y., Himeno K. Contribution of extrathymic γδgd T cells to the expression of heat-shock protein and to protective immunity in mice infected with Toxoplasma gongii. Immunology. 88:1996;551-557.
20. Hisaeda H., Sakai T., Ishikawa H., Maekawa Y., Yasutomo K., Good R.A., Himeno K. Heat-shock protein 65 induced by γδ T cells prevents apoptosis of macrophages and contributes to host defense in mice infected with Toxoplasma gondii. J. Immunol. 159:1997;2375-2381.
21. Steinhoff U., Zügel U., Wand-Württenberger A., Hengel H., Rösch R., Munk M.E., Kaufmann S.H.E. Prevention of autoimmune lysis by T cells with specificity for a heat-shock protein by antisense oligonucleotide treatment. Proc. Natl. Acad. Sci. USA. 91:1994;5085-5088.
22. Green L.C., Wagner D.A., Glogowski J., Skipper P.L., Wishnok J.S., Tannenbaum S.T. Analysis of nitrate nitrite, and (15N) nitrate in biological fluids. Anal. Biochem. 126:1982;131-138.
23. Ishikawa H., Hisaeda H., Maekawa Y., Nagasawa H., Sakai T., Ota F., Himeno K. Expression of heat-shock protein in host macrophages correlates with a protective potential against infection with Leishmania major in mice. Parasitol. Int. 46:1997;263-269.
24. Koga T., Wand-Württenberger A., Debruyn J., Munk M.E., Schoel B., Kaufmann S.H.E. T cells against a bacterial heat-shock protein recognize stressed macrophages. Science. 245:1989;1112-1115.
25. Ferm M.T., Söderström K., Jindal S., Gröngerg A., Ivanyi J., Young R., Kiessling R. Induction human hsp65 expression in monocytic cell lines. Int. Immunol. 4:1992;305-311.
26. Muñoz-Fernández M.A., Fernández M.A., Fresno M. Synergism between tumor necrosis factor-α and interferon-γ on macrophage activation for the killing of intracellular Trypanosoma cruzi through a nitric oxide-dependent mechanism. Eur. J. Immunol. 22:1992;301-307.
27. Gazzinelli R.T., Oswald I.P., Hieny S., James S.L., Sher A. The microbicidal activity of interferon-γ-treated macrophages against Trypanosoma cruzi involves an L-ariginine-dependent, nitrogen oxide- mediated mechanism inhibitable by interleukin-10 and transforming growth factor-β Eur. J. Immunol. 22:1992;2501-2506.
28. Mehlen P., Schulze-Osthoff K., Arrigo A.P. Small stress proteins as novel regulators of apoptosis: heat-shock protein 27 blocks Fas/Apo-1- and staurosporine-induced cell death. J. Biol. Chem. 271:1996;16510-16514.
29. Samali A., Cotter T.G. Heat-shock proteins increase resistance to apoptosis. Exp. Cell. Res. 223:1996;163-170.
30. Wei Y.Q., Zhao X., Kariya Y., Teshigawara K., Uchida A. Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells. Cancer Immunol. Immunother. 40:1995;73-78.
31. Dix D.J., Allen J.W., Collins B.W., Mori C., Nakamura N., Poorman-Allen P., Goulding E.H., Eddy E. Targeted gene disruption of Hsp70-2 results in failed meiosis germ cell apoptosis, and male infertility. Proc. Natl. Acad. Sci. USA. 93:1996;3264-3268.
32. Galea-Lauri J., Richardson A.J., Latchman D.S., Katz D.R. Increased heat-shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid cell line U937 following induction with TNF-alpha and cycloheximide: a possible role in immunopathology. J. Immunol. 157:1996;4109-4118.
33. Albina J.E., Cui S., Mateo R.B., Reichner J.S. Nitric oxide-mediated apoptosis in murine peritoneal macrophages. J. Immunol. 150:1993;5080-5085.
34. Rojas M., Barrera L.F., Puzo G., Garcia L.F. Differential induction of apoptosis by virulent Mycobacterium tuberculosis in resistant and susceptible murine macrophages. J. Immunol. 159:1997;1352-1361.
35. Kato S., Muro M., Akifusa S., Hanada N., Semba I., Fukii T., Kowashi Y., Kowashi Y., Nishihara T. Evidence for apoptosis of murine macrophages by Actinobacillus actinomycetemcomtans infection. Infect. Immun. 63:1995;3914-3919.
36. Zychlinsky A., Prevost M.C., Sansonetti P.J. Shigella flexneri induces apoptosis in infected macrophages. Nature. 358:1992;167-169.
37. Monack D.M., Raupach B., Hromockyj A.E., Falkow S. Salmonella typhimurium invation induces apoptosis in infected macrophages. Proc. Natl. Acad. Sci. USA. 93:1996;9833-9838.
38. Gupta R.S. Sequence and structural homology between a mouse T-complex protein TCP-1 and the 'chaperonin' family of bacterial (GroEL, 60-65 kDa heat-shock antigen) and eukaryotic proteins. Biochem. Int. 20:1990;833-841.
39. Kroemer G., Zamzami N., Susin S.A. Mitochondrial control of apoptosis. Immunol. Today. 18:1997;44-51.
40. Kroemer G. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat. M. 3:1997;614-620.