Abstract
Heme oxygenase (HO)-l is a stress response protein that is induced by a variety of stimuli associated with oxidative stress.1 HO-1 catalyzes the degradation of heme to generate biliverdin, carbon monoxide, and iron.2 Biliverdin is subsequently converted to bilirubin, a potent endogenous antioxidant.3 Carbon monoxide shares many similarities with nitric oxide, such as its ability to increase cGMP levels and promote vasodilation, thereby modulating tissue perfusion.4,5 The induction of HO-1 in response to cellular stress is an important protective mechanism, since mice lacking HO-1 show reduced survival when subjected to endotoxemia,6 chronic hypoxia,7 or transplantation of cardiac xenografts.8
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References
Keyse S.M. and Tyrrel R.: Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA irradiation, hydrogen peroxide, and sodium arsenite, Proc. Natl. Acad. Sci. USA., 86:99–103, 1989.
Maines M.D.: Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications, FASEB J., 2:2557–2568, 1988.
Stocker R., Yamamoto Y., McDonagh A.F., Glazer A.N., and Ames B.N.: Bilirubin is an anti-oxidant of possible physiological importance, Science., 235:1042–1046, 1987.
Morita T., Perrella M.A., Lee M.-E., and Kourembanas S.: Smooth muscle cell-derived carbon monoxide is a regulator of vascular cGMP., Proc. Natl. Acad. Sci. USA., 92:1475–1479, 1995.
Christodoulides N., Durante W., Kroll M.H., and Schafer A.I.: Vascular smooth muscle cell heme oxygenases generate guanylyl cyclase-stimulatory carbon monoxide., Circulation., 91:2306–2309, 1995.
Poss K.D. and Tonegawa S.: Reduced stress defense in heme oxygenase 1-deficient cells, Proc. Natl. Acad. Sci. U.S.A., 94:10925–10930, 1997.
Yet S.-F., Perrella M.A., Layne M.D., Hsieh C.-M., Maemura K., Kobzik L., Wiesel P., Christou H., Kourembanas S., and Lee M.-E.: Hypoxia induces severe right ventricular dilatation and infarction in heme oxygenase-1 null mice, J. Clin. Invest., 103:R23–R29, 1999.
Soares M.P., Lin Y.L., Csizmadia E., Takigami K., Sato K., Grey S.T., Colvin R.B., Choi A.M., Poss K.D., and Bach F.H.: Expression of heme oxygenase-1 can determine cardiac xenograft survival., Nat. Med., 4:1073–1077, 1998.
Camhi S.L., Alam J., Otterbein L., Sylvester S.L., and Choi A.M.K.: Induction of heme oxygenase-1 gene expression by lipopolysaccharide is mediated by AP-1 activation., Am. J. Respir. Cell Mol. Biol., 13:387–398, 1995.
Yet S.-F., Pellacani A., Patterson C., Tan L., Folta S.C., Foster L., Lee W.-S., Hsieh C.-M., and Perrella M.A.: Induction of heme oxygenase-1 expression in vascular smooth muscle cells. A link to endotoxic shock., J. Biol. Chem., 272:4295–4301, 1997.
Camhi S., Alam J., Wiegand G., Yoke Chin B., and Choi A.M.K.: Transcriptional activation of the HO-1 gene by lipopolysaccharide is mediated by 5’ distal enhancers: Role of reactive oxygen intermediates and AP-1, Am. J. Respir. Cell Mol. Biol., 18:226–234, 1998.
Karin M. and Barnes P.J.: Nuclear factor NF-B-a pivotal transcription factor in chronic inflammatory disease, N. Engl. J. Med., 336:1066–1071, 1997.
Dinarello C.A.: Biological basis for interleukin-1 in disease, Blood., 87:2095–2147, 1996.
Friedrichs B., Muller C., and Brigelius-Flohe R: Inhibition of tumor necrosis factor-alpha- and interleukin-1-induced endothelial E-selectin expression by thiol-modifying agents, Arterioscler. Thromb. Vasc. Biol., 18:1829–1837, 1998.
Karin M., Liu Z.-g, and Zandi E.: AP-1 function and regulation, Curr. Opin. Cell Biol., 9:240–246, 1997.
Abate C., Patel L., Rauscher III F.J., and Curran T.: Redox regulation of Fos and Jun DNA-binding activity in vitro, Science., 249:1157–1161, 1990.
Klatt P., Molina E.P., De Lacoba M.G., Padilla C.A., Martinez-Galisteo E., Barcena J.A., and Lamas S.: Redox regulation of c-Jun DNA binding by reversibel S-glutathiolation., FASEB J., 13:1481–1490, 1999.
Schenk H., Klein M., Erdebrügger W., Dröge W., and Schulze-Osthoff K.: Distinct effects of thiore- doxin and antioxidants on the activation of transcription factors NF-B and AP-1, Proc. Natl. Acad. Sci. USA., 91:1672–1676, 1994.
Hirota K., Matsui M., Iwata S., Nishiyama A., Mori K., and Yodoi J.: AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1, Proc. Natl. Acad. Sci. USA., 94:3633–3638, 1997.
Hirota K., Murata M., Sachi Y., Nakamura H., Takeuchi J., Mori K., and Yodoi J.: Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-B., J. Biol. Chem., 274:27891–27897, 1999.
Nikitovic D., Holmgren A., and Spyrou G: Inhibition of AP-1 DNA binding by nitric oxide involving conserved cysteine residures in Jun and Fos., Biochem. Biophys. Res. Commun., 242:109–112, 1998.
Qin J, M. C.G., Kennedy W.P., Kuszewski J., and Gronenborn A.M.: The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal, Structure., 4:613–620, 1996.
Xanthoudakis S., Miao G., Wang F., Pan Y.-C., and Curran T.: Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme, EMBO J., 11:3323–3335, 1992.
Holmgren A. and Luthman M.: Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay, Biochemistry, 17:4071–4077, 1978.
Inamdar N.M., Ahn Y.I., and Alam J.: The heme-responsive element of the mouse heme oxygenase gene is an extended AP-1 binding site that resembles the recognition sequences for MAF and NF-E2 transcription factors, Biochem. Biophys. Res. Com., 221:570–576, 1996.
Xanthoudakis S. and Curran T.: Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity, EMBO J., 11:653–665, 1992.
Schenk H., Vogt M., Droge W., and Schulze-Osthoff K.: Thioredoxin as a potent costimulus of cytokine expression, J. Immunol., 156:765–771, 1996.
Biguet C., Wakasugi N., Mishal Z., Holmgren A., Chouaib S., Tursz T., and Wakasugi H.: Thioredoxin increases the proliferation of human B-cell lines through a proteine kinase C-dependent mechanism, J. Biol. Chem., 269:28865–28870, 1994.
Makino Y., Yoshikawa N., Okamoto K., Hirota K., Yodoi J., Makino I., and Tanaka H.: Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function, J. Biol. Chem., 274:3182–3188, 1999.
Nathan C.F.: Secretory products of macrophages., J. Clin. Invest., 79:319–326, 1987.
Tanaka T., Nishiyama Y., Okada K., Matsui M., Yodoi J., Hiai H., and Toyokuni S.: Induction and nuclear translocation of thioredoxin by oxidative damage in the mouse kidney: independence of tubular necrosis and sulfhydryl depletion, Lab. Invest., 77:145–155, 1997.
Masutani H., Hirota K., Sasada T., Ueda-Tanigushu Y., Tanigushi Y., Matsui M., and Yodoi J.: Transactivation of an inducible anti-oxidative stress protein, human thioredoxin by HTLV-I tax., Immunol. Lett., 54:67–71, 1996.
Ema M., Hirota K., Mimura J., Abe H., Yodoi J., Sogawa K., Poellinger L., and Fjii-Kuriyama Y: Molecular mechanisms of transcription activation by HLF and HIFlα in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300, EMBO J., 18:1905–1914, 1999.
Arnér E.S.J., Björnstedt M., and Holmgren A.: l-chloro-2,4-dinitrobenzene is an irreversible inhibitor of human thioredoxin reductase, J. Biol. Chem., 270:3473–3482, 1995.
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Perrella, M.A., Yet, SF. (2002). Thioredoxin Facilitates the Induction of Heme Oxygenase-1 in Response to Inflammatory Mediators. In: Abraham, N.G. (eds) Heme Oxygenase in Biology and Medicine. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0741-3_19
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DOI: https://doi.org/10.1007/978-1-4615-0741-3_19
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