Iron chelation decreases human immunodeficiency virus-1 Tat potentiated tumor necrosis factor-induced NF-κB activation in Jurkat cells

European Cytokine Network

Volumn 8, Issue 1, 1997, Pages 37-43

  Shatrov, Vladimir A ^a,c,d   Boelaert, Johan R ^b   Chouaib, Salem ^a   Dröge, Wulf ^c   Lehmann, Volker ^c  

^a INSTITUT GUSTAVE ROUSSY   (France)

^b General Hospital St Jan   (Belgium)

^c GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

^d INSERM   (France)

Author keywords

HIV 1; Iron chelation; NF b activation; Tat; TNF

Indexed keywords

CHELATING AGENT; DEFEROXAMINE; GLUTATHIONE; GLUTATHIONE DISULFIDE; HYDROXYL RADICAL; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IRON; TRANSACTIVATOR PROTEIN; TUMOR NECROSIS FACTOR ALPHA;

ARTICLE; CONTROLLED STUDY; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; IRON CHELATION; LEUKEMIA CELL LINE; PROTEIN DNA BINDING; TRANSACTIVATION;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0030891134     PISSN: 11485493     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (32)

1. Duh E. J., Maury W. J., Folks T. M., Fauci A. S., and Rabson A. B. 1989. Tumor necrosis factor a activates HIV type 1 through inductions of nuclear factor binding to NF-κB sites in the long terminal repeat. Proc. Natl. Acad. Sci. USA 86:5974.
2. Folks T. M., Clouse K. A., Justement J., Rabson A., Duh E. J., Kehrl J. H., and Fauci A. S. 1989. Tumor necrosis factor oc induces expression of immunodeficiency virus in a chronically infected T cell clone. Proc. Natl. Acad. Sci. USA 86:2365.
3. Oakes J. W., Bagasra O., Duan L., and Pomerantz R.J. 1994. Association of alterations in NF-αB moieties with HIV type 1 proviral latency in certain monocytic cells. AIDS Res. and Human Retrovir. 10:1213.
4. Baeuerle P. A. and Henkel T. 1994. Function and activation of NF-κB in the immune system. Annu. Rev. Imnumol. 12: 141.
5. Thanos D. and Maniatis T. 1995. NF-κB: a lesson in family values. Cell 80:529.
6. Schreck R., Rieber P., and Baeuerle P. A. 1991. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J. 10:2247.
7. Israel N., Gouderot-Pocidalo M. A., Aillet F., and Virelizier J. L. 1992. Redox status of cells influences constitutive or induced NF-κB translocation and HIV long terminal repeat activity in human T and monocytic cell lines. J. Immunol. 149:3386.
8. Schulze-Osthoff K., Beyaert R., Vandervoorde V., Haegeman G., and Fiers, W. 1993. Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene inductive effects of TNF. EMBO J 12:3095.
9. Legrand-Poels S., Vaira D., Pincemail J., Van de Vorst A., and Piette J. 1990. Activation of human immunodeficiency virus type 1 by oxidative stress. AIDS Res and Human Retrovir. 6: 1389.
10. Roederer M., Staal F. J. T., Raju P. A., Ela S. W., Herzenberg L. A., and Herzenber L. A. 1990. Cytokine stimulated HIV replication is inhibited by N-acctyl-L-cysteine. Proc. Natl. Acad. Sci USA 87:4884.
11. Schreck R., Meier B., Mannel D. N., Droge W., and Baeuerle P. A. 1992. Dithiocarbamates as potent inhibitors of nuclear factor KB activation in intact cells. J. Exp. Med. 175:1181.
12. Bergmann S., Shatrov V., Ratter F., Schiemann S., Schulze-Osthoff K., and Lehmann V. 1994. Adenosine and homocysteine together enhance TNF-mediated cytotoxicity but do not alter activation of nuclear factor κB. J Immunol. 153:1736.
13. Cullen B. R: 1990. The HIV-1 Tat protein: An RNA sequence-specific progressivity factor. Cell 63:655.
14. Rosen C. A. and Pavlakis G. N. 1990. Tat and Rev: Positive regulators of HIV gene expression. AIDS 4:499.
15. Vaishnav Y. N. and Wong-Staal F. 1991. The biochemistry of AIDS. Annu. Rev. Biochem. 60:577.
16. Dingwall C., Emberg I., Gait M. J., Green S. M., Heaphy S., Kam J., Lowe A. D., Singh M., Skimmer M. A., and Valerio R. 1989. Human immunodeficiency virus 1 Tat protein binds transactivation-responsive region (TAR)RNA in vitro. Proc. Natl. Acad. Sci. USA 86:6925.
17. Westendorp M. O., Shatrov V. A., Schulze-Osthoff K., Frank R., Kraft M., Los M., Krammer P. H., Droge W., and Lehmann V. 1995. HIV-1 Tat potentiates TNF-induced NF-κB activtion and cytotoxicity by altering the cellular redox state. EMBO J. 14:546.
18. Sappey C., Boelaert J. R., Legrand-Poels S., Forceille C., Favier A., and Piette J. 1995. Iron chelation decreases NF-κB and HIV type 1 activation due to oxidative stress. AIDS Res. and Human Retrovir. 11:1049.
19. Brittenham G. M. 1992. Development of iron-chelating agents for clinical use. Blood 80:569.
20. Zabel U., Schreck R., and Baeuerle P. 1991. DNA binding of purified transcription factor NF-κB. J. Biol. Chem. 266:252.
21. Hsu H., Xiong J., and Goeddel D. V. 1995 The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell 81:495.
22. Mimnaugh E. G., Dusve L., Atwell J., and Myers C. L. 1989 Differential oxygen radical susceptibility of Adriamycin-sensitive and - resistant MCF-7 human breast tumor cells. Cancer Res. 49:8.
23. Zauli G., Davis B. R., Re M. C., Visani G., Furlini G., and La Placa M. 1992. Tat protein stimulates production of transfomming growth factor-β1 by marrow macrophages: a potential mechanism for HIV-1 induced hematopoietic suppression. Blood 80:3036.
24. Staal F. J. T., Roederer M., Raju P. A., Anderson M. T., Ela S. W., Herzenberg L. A., and Herzenberg L. A. 1993. Antioxidants inhibit stimulation of HIV transcription. AIDS Res. and Human Retrovir. 9:299.
25. Li S. and Sedivy J. M. 1993. Raf-1 protein kinase activates the NF-κB transcription factor by dissociating the cytoplasmic NF-κB-IκB complex. Proc. Natl. Acad. Sci USA 90:947.
26. Henkel T., Machleldt T., Alkalay I., Kronke M., Ben-Nerlah Y., and Baeuerle P. A. 1993. Rapid proteolysis of IκB is necessary for activation of transcription factor NF-κB. Nature 365: 182.
27. Fridovich I. 1978. The biology of oxygen radicals. Science 201:875.
28. Halliwell B. and Gutteridge J. M. C.1989. Free Radicals in Biology and Medicine. Second Edition. Clarendon Press, Oxford.
29. Hassan H. M. 1988. Biosynthesis and regulation of Superoxide dismutases. Free Radical Biol. Med. 5:377.
30. Haber F. and Weiss J. 1934. The catalytic decomposition of hydrogen peroxide by iron salts. Proc. Roy. Soc. London A 147:322.
31. Shapiro B. M. 1991. The control of oxidant stress at fertilization. Science 252:533.
32. Brown R. H. 1995. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell 80:687.