The identification of ferritin in the nucleus of K562 cells, and investigation of a possible role in the transcriptional regulation of adult β-globin gene expression

Journal of Cell Science

Volumn 112, Issue 6, 1999, Pages 825-831

  Pountney, David ^a   Trugnan, Germain ^a   Bourgeois, Monique ^a   Beaumont, Carole ^a  

^a INSERM   (France)

Author keywords

Confocal microscopy; Ferritin; Gene expression; Nucleus; globin

Indexed keywords

BETA GLOBIN; FERRITIN; IRON BINDING PROTEIN; MONOCLONAL ANTIBODY; OLIGONUCLEOTIDE;

ARTICLE; CELL NUCLEUS; CELL STRAIN K 562; CELLULAR DISTRIBUTION; CONFOCAL MICROSCOPY; CROSS REACTION; CYTOPLASM; CYTOSOL; FREEZING; GEL MOBILITY SHIFT ASSAY; HEAT SENSITIVITY; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; PRIORITY JOURNAL; PROMOTER REGION; THAWING; TRANSCRIPTION REGULATION;

EID: 0032900602     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (27)

1. Andrews, N. C. and Faller, D. V. (1991). A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian cells Nucleic. Acids. Res. 19, 2499.
2. Blair, F. C., Kyker, K. D., Kurein, B. T., Stewart, D. R., Halnisz, H, Berg, P. E., Schechter, A. N. and Broyles, R. H. (1994). Conference on Haemoglobin Switching, Washington DC, p6.
3. Cai, C. X., Birk, D. E. and Linsenmayer, T. F. (1997). Ferritin is a developmentally regulated nuclear protein of avian corneal epithelial cells. J. Biol. Chem. 272, 12831-12839.
4. Cai, C. X., Birk, D. E. and Linsenmayer, T. F. (1998). Nuclear ferritin protects DNA from UV damage in corneal epithelial cells. Mol. Biol. Cell. 9, 1037-1051.
5. Cairo, G., Tacchini, L., Pogliaghi, G., Anzon, E., Tomasi, A. and Bernelli-Zazzera, A. (1995). Induction of ferritin synthesis by oxidative stress. Transcriptional and post-transcriptional regulation by expansion of the 'free' iron pool. J. Biol. Chem. 270, 700-703.
6. Cermak, J., Balla, J., Jacob, H. S., Balla, G., Enright, H., Nath, K. and Vercellotti, G. M. (1993). Tumor cell heme uptake induces ferritin synthesis resulting in altered oxidant sensitivity: possible role in chemotherapy efficacy. Cancer Res. 53, 5308-5313.
7. Chang, K., Fan, Y., Andreeff, M., Liu, J. and Mu, Z. T. (1995). The PML gene encodes a phosphoprotein associated with the nuclear matrix. blood 85, 3646-3653.
8. Coy, M. and Neilands, J. B. (1991). Structural dynamics and functional domains of the Fur protein. Biochemistry 30, 8201-8210.
9. Grant, R. A., Filman, D. J., Finkel, S. E., Kolter, R. and Hogle, J. M. (1998). The crystal structure of Dps. a ferritin homolog that binds and protects DNA. Nature Struct. Biol. 5, 294-303.
10. Gray, N. K. and Hentze, M. W. (1994). Iron regulatory protein prevents binding ot the 43S translation pre-initiation complex to ferritin and eALAS mRNAs. EMBO J. 13, 3882-3891.
11. Grosveld, F., Bloom van Assendelft, G., Greaves, D. and Kollias, G. (1987). Position-independent, high-level expression of the human β-globin gene in transgenic mice. Cell 57, 975-985.
12. Klausner, R. D., Rouault, T A. and Harford, J. B. (1993). Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72, 19-28.
13. Levi, S., Luzzago A., Cesarini, G., Cozzi, A., Franceschinelli, F., Albertini, A. and Arosio, P. (1988). Mechanism of ferritin iron uptake: activity of the H-chain deletion mapping of the ferroxidase site J. Biol. Chem. 263, 18086-18092.
14. Macleod, K. and Plumb, M. (1991). Derepression of mouse β-major-globin gene transcription during erythroid differentiation. Mol. Cell. Biol. 11, 4324-4332.
15. Okada, S. (1996). Iron-induced tissue damage and cancer: the role of reactive oxygen species-free radicals. Pathol. Int. 46, 311-332.
16. Picard, V., Renaudie, P., Porcher, C., Hentze, M. W., Grandchamp, B. and Beaumont, C. (1996). Overexpression of the ferritin H subunit in cultured erythroid cells changes the intracellular iron distribution. Blood 87, 2207-2064.
17. Picard, V., Epsztejn, S., Santambrogio, P. and Cabantchik, I. Z. (1998). Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells. J. Biol. Chem. (in press).
18. Ponka, P. (1997). Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanism in erythroid cells. Blood 89, 1-25.
19. Porcu, S., Kitamura, M., Witkowska, E., Zhang, Z., Mutero, A., Lin, C., Chang, J. and Gaensler, K. M. L. (1997). The human (globin locus introduced by YAC transfer exhibits a specific and reproducible pattern of developmental regulation in transgenic mice. Blood 90, 4602-4609.
20. Richter, G. W. (1961). Intranuclear aggregates of ferritin in liver cells of mice treated with saccharated iron oxide. Their possible relation to nuclear protein synthesis. J. Biophys. Biochem. Cytol. 9, 263-270.
21. Santambrogio, P., Levi, S., Cozzi, A., Rovida, E., Albertini, A. and Arosio, P. (1993). Production and characterization of recombinant heteropolymers of human ferritin H and L chains. J. Biol. Chem. 268, 12744-12748.
22. Smith, A. G., Cartherw, P., Francis, J. E., Edwards, R. E. and Dinsdale, d. (1990). Characterisation and accumulation of ferritin in hepatocyte nuclei of mice with iron overload. Hepatology 12, 1399-1405.
23. Verma, I. M., Stevenson, J. K., Schwarz, E. M., Van Antwerp, D. and Miyamoto, S. (1995). Rel/NK-κB/lκB family: intimate tales of association and dissociation. Genes Dev. 9, 2723-2735.
24. Voisard, C., Wang, J., McEvoy, J. L., Xu, P. and Leong, S. A. (1993). Urbs-1, a gene regulating siderophore biosynthesis in Ustilago maydis. encodes a protein similar to the erythroid transcription factor GATA-1. Mol. Cell. Biol. 13, 7091-7100.
25. Wiseman, H. and Halliwell, B. (1996). Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer Biochem. J. 313, 17-29.
26. Wu, V. and Noguchi, C. T. (1991). Activation of globin gene expression by cDNAs from induced K562 cells. Evidence for involvement of ferritin in globin gene expression. J. Biol. Chem. 266, 17566-17572.
27. Yamaguchi-Iwai, V., Dancis, A. and Klausner, R. D. (1995). AFT1: a mediator of iron regulated transcriptional control in Sacharomyes cerevisiae. EMBO. J. 14, 1231-1239.