Redox state regulates HIF-1α and its DNA binding and phosphorylation in salmonid cells

Journal of Cell Science

Volumn 117, Issue 15, 2004, Pages 3201-3206

  Nikinmaa, Mikko ^a   Pursiheimo, Saijaliisa ^a   Soitamo, Arto J ^a  

^a UNIVERSITY OF TURKU   (Finland)

Author keywords

Hypoxia; Hypoxia inducible factor; Oxidative stress; Phosphorylation; Rainbow trout

Indexed keywords

ACETYLCYSTEINE; BUTHIONINE SULFOXIMINE; CELL DNA; COBALT; GALLIC ACID PROPYL ESTER; HYPOXIA INDUCIBLE FACTOR 1ALPHA; OXYGEN; PROLINE DERIVATIVE; REDUCING AGENT;

ANIMAL CELL; ARTICLE; CELL HYPOXIA; CELL LINE; CONTROLLED STUDY; DNA BINDING; GENETIC CONSERVATION; HYDROXYLATION; NONHUMAN; OXIDATION; OXIDATION REDUCTION STATE; OXYGENATION; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; REDUCTION; REGULATORY MECHANISM; SALMONID;

ACETYLCYSTEINE; ANIMALS; ANOXIA; ANTIMETABOLITES; ANTIOXIDANTS; BUTHIONINE SULFOXIMINE; CELL LINE; CYSTEINE; DIMERIZATION; DNA; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME INHIBITORS; HYDROXYLATION; HYPOXIA-INDUCIBLE FACTOR 1, ALPHA SUBUNIT; IMMUNOBLOTTING; IMMUNOPRECIPITATION; ONCORHYNCHUS MYKISS; OXIDATION-REDUCTION; OXIDATIVE STRESS; OXYGEN; PHOSPHORYLATION; PROLINE; PROPYL GALLATE; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RNA; TIME FACTORS; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTORS;

ANIMALIA; MAMMALIA; ONCORHYNCHUS; ONCORHYNCHUS MYKISS; SALMONIDAE;

EID: 2642536298     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01192     Document Type: Article

References (33)

1. Arrigo, A. P. (1999). Gene expression and the thiol redox state. Free Radic. Biol. Med. 27, 936-944.
2. Eriksson, J. E., Toivola, D. M., Sahlgren, C., Mikhailov, A. and Härmälä-Brasken, A. S. (1998). Strategies to assess phosphoprotein phosphatase and protein kinase-mediated regulation of the cytoskeleton. Methods Enzymol. 298, 542-569.
3. Gradin, K., Takasaki, C., Fujii-Kuriyama, Y. and Sogawa, K. (2002). The transcriptional activation function of the HIF-like factor requires phosphorylation at a conserved threonine. J. Biol. Chem. 277, 23508-23514.
4. 2-evoked regulation of HIF-1α and NF-κB in perinatal lung epithelium requires glutathione biosynthesis. Am. J. Physiol. Lung Cell. Mol. Physiol. 278, L492-L503.
5. Haddad, J. J. E., Olver, R. E. and Land, S. C. (2000). Antioxidant/pro-oxidant equilibrium regulates HIF-1α and NF-κ B redox sensitivity - evidence for inhibition by glutathione oxidation in alveolar epithelial cells. J. Biol. Chem. 275, 21130-21139.
6. Hirsila, M., Koivunen, P., Gunzler, V., Kivirikko, K. I. and Myllyharju, J. (2003). Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J. Biol. Chem. 278, 30772-30780.
7. Hofer, T., Desbaillets, I., Hopfl, G., Gassmann, M. and Wenger, R. H. (2001). Dissecting hypoxia-dependent and hypoxia-independent steps in the HIF-1α activation cascade: implications for HIF-1α gene therapy. FASEB J. 15, 2715-2717.
8. Hossain, M. A., Bouton, C. M., Pevsner, J. and Laterra, J. (2000). Induction of vascular endothelial growth factor in human astrocytes by lead. Involvement of a protein kinase C/activator protein-1 complex-dependent and hypoxia-inducible factor 1-independent signaling pathway. J. Biol. Chem. 275, 27874-27882.
9. Huang, J. H., Zhao, Q., Mooney, S. M. and Lee, F. S. (2002). Sequence determinants in hypoxia-inducible factor-1 alpha for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3. J. Biol. Chem. 277, 39792-39800.
10. 2 sensing. Science 292, 464-468.
11. 2-regulated prolyl hydroxylation. Science 292, 468-472.
12. Jiang, B. H., Rue, E., Wang, G. L., Roe, R. and Semenza, G. L. (1996). Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. J. Biol. Chem. 271, 17771-17778.
13. Jiang, B. H., Zheng, J. Z., Leung, S. W., Roe, R. and Semenza, G. L. (1997). Transactivation and inhibitory domains of hypoxia-inducible factor 1α. Modulation of transcriptional activity by oxygen tension. J. Biol. Chem. 272, 19253-19260.
14. Kvietikova, I., Wenger, R. H., Marti, H. H. and Gassmann, M. (1995). The transcription factors ATF-1 and CREB-1 bind constitutively to the hypoxia-inducible factor-1 (HIF-1) DNA recognition site. Nucleic Acids Res. 23, 4542-4550.
15. Lando, D., Pongratz, I., Poellinger, L. and Whitelaw, M. L. (2000). A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1alpha and the HIF-like factor. J. Biol. Chem. 275, 4618-4627.
16. Lundstrom, J., Carney, B., Amcoff, P., Pettersson, A., Borjeson, H., Forlin, L. and Norrgren, L. (1999). Antioxidative systems, detoxifying enzymes and thiamine levels in Baltic salmon (Salmo salar) that develop M74. Ambio 28, 24-29.
17. Mottet, D., Michel, G., Renard, P., Ninane, N., Raes, M. and Michiels, C. (2003). Role of ERK and calcium in the hypoxia-induced activation of HIF-1. J. Cell. Physiol. 194, 30-44.
18. Obin, M., Shang, F., Gong, X., Handelman, G., Blumberg, J. and Taylor, A. (1998). Redox regulation of ubiquitin-conjugating enzymes: mechanistic insights using the thiol-specific oxidant diamide. FASEB J. 12, 561-569.
19. Powis, G. and Montfort, W. R. (2001). Properties and biological activities of thioredoxins. Annu. Rev. Pharmacol. Toxicol. 41, 261-295.
20. 2 insult. Exp. Eye Res. 76, 49-59.
21. Richard, D. E., Berra, E., Gothie, E., Roux, D. and Pouyssegur, J. (1999). p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α(HIF-1α) and enhance the transcriptional activity of HEF-1. J. Biol. Chem. 274, 32631-32637.
22. Rolfs, A., Kvietikova, I., Gassmann, M. and Wenger, R. H. (1997). Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1. J. Biol. Chem. 272, 2055-2062.
23. 2, and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell 107, 1-3.
24. Semenza, G. L., Agani, F., Booth, G., Forsythe, J., Iyer, N., Jiang, B. H., Leung, S., Roe, R., Wiener, C. and Yu, A. (1997). Structural and functional analysis of hypoxia-inducible factor 1. Kidney Int. 51, 553-555.
25. Soitamo, A. J., Rabergh, C. M. I., Gassmann, M., Sistonen, L. and Nikinmaa, M. (2001). Characterization of a hypoxia-inducible factor (HIF-1α) from rainbow trout. Accumulation of protein occurs at normal venous oxygen tension. J. Biol. Chem. 276, 19699-19705.
26. Srinivas, V., Leshchinsky, I., Sang, N., King, M. P., Minchenko, A. and Caro, J. (2001). Oxygen sensing and HIF-1 activation does not require an active mitochondrial respiratory chain electron-transfer pathway. J. Biol. Chem. 276, 21995-21998.
27. Vuori, K. A. M., Soitamo, A., Vuorinen, P. J. and Nikinmaa, M. (2004). Baltic salmon (Salmo salar) yolk-sac fry mortality is associated with disturbances in the function of hypoxia-inducible transcription factor (HIF-1α) and consecutive gene expression. Aquat. Toxicol. 68, 301-313.
28. Wang, G. L. and Semenza, G. L. (1995). Purification and characterization of hypoxia-inducible factor 1. J. Biol. Chem. 270, 1230-1237.
29. Wang, G. L., Jiang, B. H. and Semenza, G. L. (1995). Effect of protein kinase and phosphatase inhibitors on expression of hypoxia-inducible factor 1. Biochem. Biophys. Res. Commun. 216, 669-675.
30. Welsh, S. J., Williams, R. R., Birmingham, A., Newman, D. J., Kirkpatrick, D. L. and Powis, G. (2003). The thioredoxin redox inhibitors 1-methylpropyl 2-imidazolyl disulfide and pleurotin inhibit hypoxia-induced factor 1 alpha and vascular endothelial growth factor formation. Mol. Cancer Ther. 2, 235-243.
31. Wenger, R. H. (2000). Mammalian oxygen sensing, signalling and gene regulation. J. Exp. Biol. 203, 1253-1263.
32. Yang, Z. Z., Zhang, A. Y., Yi, F. X., Li, P. L. and Zou, A. P. (2003). Redox regulation of HIF-1 alpha levels and HO-1 expression in renal medullary interstitial cells. Am. J. Physiol. Renal Physiol. 284, F1207-F1215.
33. Yuan, Y., Hilliard, G., Ferguson, T. and Millhorn, D. E. (2003). Cobalt inbibits the interaction between hypoxia-inducible factor-alpha and von Hippel-Lindau protein by direct binding to hypoxia-inducible factor-alpha. J. Biol. Chem. 278, 15911-15916.