Overexpression of Wild Type and Mutated Human Ferritin H-chain in HeLa Cells
Open accessAbstract
Transfectant HeLa cells were generated that expressed human ferritin H-chain wild type and an H-chain mutant with inactivated ferroxidase activity under the control of the tetracycline-responsive promoter (Tet-off). The clones accumulated exogenous ferritins up to levels 14-16-fold over background, half of which were as H-chain homopolymers. This had no evident effect in the mutant ferritin clone, whereas it induced an iron-deficient phenotype in the H-ferritin wild type clone, manifested by approximately 5-fold increase of IRPs activity, approximately 2.5-fold increase of transferrin receptor, approximately 1.8-fold increase in iron-transferrin iron uptake, and approximately 50% reduction of labile iron pool. Overexpression of the H-ferritin, but not of the mutant ferritin, strongly reduced cell growth and increased resistance to H(2)O(2) toxicity, effects that were reverted by prolonged incubation in iron-supplemented medium. The results show that in HeLa cells H-ferritin regulates the metabolic iron pool with a mechanism dependent on the functionality of the ferroxidase centers, and this affects, in opposite directions, cellular growth and resistance to oxidative damage. This, and the finding that also in vivo H-chain homopolymers are much less efficient than the H/L heteropolymers in taking up iron, indicate that functional activity of H-ferritin in HeLa cells is that predicted from the in vitro data.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Ferritin acts as an antioxidant protein.
“Accumulating evidence shows that ferritin acts as an antioxidant protein (59, 60, 78, 159, 227, 243).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [60]
Ferritin H disruption by siRNA sensitized cells to H2O2-induced oxidative stress.
“ferritin H disruption by siRNA sensitized the cells to H2O2-induced oxidative stress (60)”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [60]
Overexpression or knockdown of ferritin expression in mammalian cells has proven the cytoprotective role of ferritin under prooxidative conditions.
“overexpression or knockdown of ferritin expression in mammalian cells has proven the cytoprotective role of ferritin under prooxidative conditions (59, 60, 78, 159, 227, 243).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [60]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Tight control of gene expression in mammalian cells by tetracycline-responsive promoters.
Gossen, M., & Bujard, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5547 · Cited by 4,943 · see citing works
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667 · see citing works
Self-citationUse of an Aqueous Soluble Tetrazolium/Formazan Assay for Cell Growth Assays in Culture
Cory, A. H., Owen, T. C., Barltrop, J. A., & Cory, J. G. (1991) · Cancer Communications · doi:10.3727/095535491820873191 · Cited by 1,520 · see citing works
Hentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292 · see citing works
Jordan, M., Schallhorn, A., & Wurm, F. M. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.4.596 · Cited by 862 · see citing works
Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts
Lawson, D. M., Artymiuk, P. J., Yewdall, S. J., Smith, J. M. A., Livingstone, J. C., Treffry, A., Luzzago, A., Levi, S., Arosio, P., Cesareni, G., et al. (1991) · Nature · doi:10.1038/349541a0 · Cited by 777 · see citing works
Self-citationLevi, S., Luzzago, A., Cesareni, G., Cozzi, A., Franceschinelli, F., Albertini, A., & Arosio, P. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81326-1 · Cited by 378 · see citing works
Self-citationBeaumont, C., Leneuve, P., Devaux, I., Scoazec, J.-Y., Berthier, M., Loiseau, M.-N., Grandchamp, B., & Bonneau, D. (1995) · Nature Genetics · doi:10.1038/ng1295-444 · Cited by 293 · see citing works
Evidence of H- and L-chains have co-operative roles in the iron-uptake mechanism of human ferritin
Levi, S., Yewdall, S. J., Harrison, P. M., Santambrogio, P., Cozzi, A., Rovida, E., Albertini, A., & Arosio, P. (1992) · Biochemical Journal · doi:10.1042/bj2880591 · Cited by 268 · see citing works
Self-citationIron-sulfur clusters as biosensors of oxidants and iron.
Rouault, T. A., & Klausner, R. D. (1996) · PubMed · Cited by 238 · see citing works
Epsztejn, S., Glickstein, H., Picard, V., Slotki, I. N., Breuer, W., Beaumont, C., & Cabantchik, Z. I. (1999) · Blood · doi:10.1182/blood.v94.10.3593.422k26_3593_3603 · Cited by 209 · see citing works
Iron-sulfur clusters as biosensors of oxidants and iron
Rouault, T. A., & Klausner, R. D. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10024-4 · Cited by 207 · see citing works
A Short Fe-Fe Distance in Peroxodiferric Ferritin: Control of Fe Substrate Versus Cofactor Decay?
Hwang, J., Krebs, C., Huynh, B. H., Edmondson, D. E., Theil, E. C., & Penner‐Hahn, J. E. (2000) · Science · doi:10.1126/science.287.5450.122 · Cited by 185 · see citing works
The Role of the L-Chain in Ferritin Iron Incorporation
Levi, S., Santambrogio, P., Cozzi, A., Rovida, E., Corsi, B., Tamborini, E., Spada, S., Albertini, A., & Arosio, P. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1325 · Cited by 180 · see citing works
Self-citationProduction and characterization of recombinant heteropolymers of human ferritin H and L chains
Santambrogio, P., Levi, S., Cozzi, A., Rovida, E., Albertini, A., & Arosio, P. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31451-0 · Cited by 161 · see citing works
Self-citationCazzola, M., Bergamaschi, G., Tonon, L., Arbustini, E., Grasso, M., Vercesi, E., Barosi, G., Bianchi, P. E., Cairo, G., & Arosio, P. (1997) · Blood · doi:10.1182/blood.v90.2.814 · Cited by 156 · see citing works
Self-citationThe Cellular Labile Iron Pool and Intracellular Ferritin in K562 Cells
Konijn, A. M., Glickstein, H., Vaisman, B. L., Meyron‐Holtz, E. G., Slotki, I. N., & Cabantchik, Z. I. (1999) · Blood · doi:10.1182/blood.v94.6.2128 · Cited by 156 · see citing works
Santambrogio, P., Levi, S., Arosio, P., Palagi, L., Vecchio, G., Lawson, D. M., Yewdall, S. J., Artymiuk, P. J., Harrison, P. M., & Jappelli, R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49681-6 · Cited by 143 · see citing works
Self-citationReaction Paths of Iron Oxidation and Hydrolysis in Horse Spleen and Recombinant Human Ferritins
Yang, X., Chen-Barrett, Y., Arosio, P., & Chasteen, N. D. (1998) · Biochemistry · doi:10.1021/bi973128a · Cited by 137 · see citing works
Self-citationSantambrogio, P., Levi, S., Cozzi, A., Corsi, B., & Arosio, P. (1996) · Biochemical Journal · doi:10.1042/bj3140139 · Cited by 133 · see citing works
Self-citationRole of Ferritin in the Control of the Labile Iron Pool in Murine Erythroleukemia Cells
Picard, V., Epsztejn, S., Santambrogio, P., Cabantchik, Z. I., & Beaumont, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15382 · Cited by 131 · see citing works
Self-citationExpression and structural and functional properties of human ferritin L-chain from Escherichia coli
Levi, S., Salfeld, J. G., Franceschinelli, F., Cozzi, A., Dörner, M. H., & Arosio, P. (1989) · Biochemistry · doi:10.1021/bi00438a040 · Cited by 127 · see citing works
Self-citationMultiple mechanisms of iron-induced ferritin synthesis in HeLa cells
Cairo, G., Bardella, L., Schiaffonati, L., Arosio, P., Levi, S., & Bernelli‐Zazzera, A. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)91877-7 · Cited by 115 · see citing works
Self-citationLevi, S., Girelli, D., Perrone, F., Pasti, M., Beaumont, C., Corrocher, R., Albertini, A., & Arosio, P. (1998) · Blood · doi:10.1182/blood.v91.11.4180 · Cited by 96 · see citing works
Self-citationLevi, S., Santambrogio, P., Corsi, B., Cozzi, A., & Arosio, P. (1996) · Biochemical Journal · doi:10.1042/bj3170467 · Cited by 90 · see citing works
Self-citationPicard, V., Renaudie, F., Porcher, C., Hentze, M. W., Grandchamp, B., & Beaumont, C. (1996) · Blood · doi:10.1182/blood.v87.5.2057.2057 · Cited by 89 · see citing works
Corsi, B., Levi, S., Cozzi, A., Corti, A., Altimare, D., Albertini, A., & Arosio, P. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01330-7 · Cited by 73 · see citing works
Self-citationFerritin iron kinetics and protein turnover in K562 cells.
Roberts, S., & Bomford, A. B. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37407-6 · Cited by 68 · see citing works
YANG, X., & CHASTEEN, N. D. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3380615 · Cited by 52 · see citing works
Transient overexpression of human H- and L-ferritin chains in COS cells
Corsi, B., Perrone, F., Bourgeois, M., Beaumont, C., Panzeri, C., Cozzi, A., Sangregorio, R., Santambrogio, P., Albertini, A., Arosio, P., et al. (1998) · Biochemical Journal · doi:10.1042/bj3300315 · Cited by 43 · see citing works
Self-citationConstruction of a ferroxidase center in human ferritin L-chain.
Levi, S., Corsi, B., Rovida, E., Cozzi, A., Santambrogio, P., Albertini, A., & Arosio, P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43817-3 · Cited by 38 · see citing works
Self-citationCozzi, A., Levi, S., Bazzigaluppi, E., Ruggeri, G., & Arosio, P. (1989) · Clinica Chimica Acta · doi:10.1016/0009-8981(89)90052-1 · Cited by 34 · see citing works
Self-citationStudies on the Interaction between Ferritin and Ceruloplasmin
Juan, S., & Aust, S. D. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0722 · Cited by 22 · see citing works
Fan, H., Villegas, C., & Wright, J. A. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00143-3 · Cited by 15 · see citing works
Louache, F., Pelosi, E., Titeux, M., Peschle, C., & Testa, U. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80781-x · Cited by 14 · see citing works
Mechanism of Fe(II) Oxidation and Core Formation in Ferritin
Harrison, P. M., Bauminger, E. R., Hechel, D., Hodson, N. W., Nowik, I., Treffry, A., & Yewdall, S. J. (1994) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-2554-7_1 · Cited by 7 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- Hentze, M. W., and Kuhn, L. C. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 8175-8182
- Gossen, M., and Bujard, H. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 5547-5551
Cited by
Sorted by citations
Iron and cancer: more ore to be mined
Torti, S. V., & Torti, F. M. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3495 · Cited by 1,621 · see citing works
Regulation of ferritin genes and protein
Torti, F. M., & Torti, S. V. (2002) · Blood · doi:10.1182/blood.v99.10.3505 · Cited by 1,173 · see citing works
Ferritins: A family of molecules for iron storage, antioxidation and more
Arosio, P., Ingrassia, R., & Cavadini, P. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.004 · Cited by 886 · see citing works
Self-citationKakhlon, O., & Cabantchik, Z. I. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01006-7 · Cited by 839 · see citing works
Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo
Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., Viswanath, V., Jacobs, R., Yang, L., Beal, M. F., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00126-0 · Cited by 620 · see citing works
Arosio, P., & Levi, S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00842-0 · Cited by 543 · see citing works
Self-citationLabile iron pool: the main determinant of cellular response to oxidative stress
Kruszewski, M. K. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.004 · Cited by 529 · see citing works
Ferritin and the response to oxidative stress
Orino, K., Lehman, L. J., Tsuji, Y., Ayaki, H., Torti, S. V., & Torti, F. M. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3570241 · Cited by 535 · see citing works
Intracellular iron transport and storage: from molecular mechanisms to health implications
Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526 · see citing works
LaVaute, T., Smith, S., Cooperman, S., Iwai, K., Land, W., Meyron-Holtz, E., Drake, S. K., Miller, G., Abu-Asab, M., Tsokos, M., et al. (2001) · Nature Genetics · doi:10.1038/84859 · Cited by 509 · see citing works
Mammalian iron metabolism and its control by iron regulatory proteins
Anderson, C. P., Shen, M., Eisenstein, R. S., & Leibold, E. A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.010 · Cited by 493 · see citing works
A new transgene reporter for in vivo magnetic resonance imaging
Genové, G., DeMarco, U., Xu, H., Goins, W. F., & Ahrens, E. T. (2005) · Nature Medicine · doi:10.1038/nm1208 · Cited by 423 · see citing works
Meyron‐Holtz, E. G., Ghosh, M. C., Iwai, K., LaVaute, T., Brazzolotto, X., Berger, U. V., Land, W., Ollivierre‐Wilson, H., Grinberg, A., Love, P., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600041 · Cited by 408 · see citing works
A human mitochondrial ferritin encoded by an intronless gene
Levi, S., Corsi, B., Bosisio, M., Invernizzi, R., Volz, A., Sanford, D., Arosio, P., & Drysdale, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100141200 · Cited by 400 · see citing works
Self-citationFerritin and the response to oxidative stress
ORINO, K., LEHMAN, L., TSUJI, Y., AYAKI, H., TORTI, S. V., & TORTI, F. M. (2001) · Biochemical Journal · doi:10.1042/bj3570241 · Cited by 535 · see citing works
Oxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects
Galaris, D., & Pantopoulos, K. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701713104 · Cited by 352 · see citing works
Cohen, B., Dafni, H., Meir, G., Harmelin, A., & Neeman, M. (2005) · Neoplasia · doi:10.1593/neo.04436 · Cited by 322 · see citing works
Arosio, P., & Levi, S. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.02.005 · Cited by 320 · see citing works
Self-citationThe Redox Basis of Epigenetic Modifications: From Mechanisms to Functional Consequences
Cyr, A. R., & Domann, F. E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3492 · Cited by 294 · see citing works
Singh, S., Vrishni, S., Singh, B. K., Rahman, I., & Kakkar, P. (2010) · Free Radical Research · doi:10.3109/10715762.2010.507670 · Cited by 294 · see citing works
Pietsch, E. C., Chan, J. Y., Torti, F. M., & Torti, S. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210664200 · Cited by 284 · see citing works
Heme oxygenase-1 is a modulator of inflammation and vaso-occlusion in transgenic sickle mice
Belcher, J. D. (2006) · Journal of Clinical Investigation · doi:10.1172/jci26857 · Cited by 265 · see citing works
Iron homeostasis and toxicity in retinal degeneration
He, X., Hahn, P., Iacovelli, J., Wong, R., King, C., Bhisitkul, R., Massaro-Giordano, M., & Dunaief, J. L. (2007) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2007.07.004 · Cited by 260 · see citing works
Heme oxygenase-1: from biology to therapeutic potential
Soares, M. P., & Bach, F. H. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.12.004 · Cited by 257 · see citing works
The significance of ferritin in cancer: Anti-oxidation, inflammation and tumorigenesis
Alkhateeb, A. A., & Connor, J. R. (2013) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2013.07.002 · Cited by 247 · see citing works
Cooperman, S. S., Meyron-Holtz, E. G., Olivierre-Wilson, H., Ghosh, M. C., McConnell, J. P., & Rouault, T. A. (2005) · Blood · doi:10.1182/blood-2004-12-4703 · Cited by 235 · see citing works
A central role for free heme in the pathogenesis of severe malaria: the missing link?
Ferreira, A., Balla, J., Jeney, V., Balla, G., & Soares, M. P. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0368-5 · Cited by 205 · see citing works
Balla, J., Vercellotti, G. M., Jeney, V., Yachie, A., Varga, Z., Jacob, H. S., Eaton, J. W., & Balla, G. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1787 · Cited by 212 · see citing works
Ferritin – from iron, through inflammation and autoimmunity, to COVID-19
Mahroum, N., Alghory, A., Kiyak, Z., Alwani, A., Seida, R., Alrais, M., & Shoenfeld, Y. (2021) · Journal of Autoimmunity · doi:10.1016/j.jaut.2021.102778 · Cited by 208 · see citing works
Role of ferritin alterations in human breast cancer cells
Shpyleva, S., Tryndyak, V., Kovalchuk, O., Starlard‐Davenport, A., Chekhun, V. F., Beland, F. A., & Pogribny, I. P. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-010-0849-4 · Cited by 206 · see citing works
MRI detection of transcriptional regulation of gene expression in transgenic mice
Cohen, B., Ziv, K., Plaks, V., Israely, T., Kalchenko, V., Harmelin, A., Benjamin, L. E., & Neeman, M. (2007) · Nature Medicine · doi:10.1038/nm1497 · Cited by 194 · see citing works
Regulation of tissue iron homeostasis: the macrophage “ferrostat”
Winn, N. C., Volk, K. M., & Hasty, A. H. (2020) · JCI Insight · doi:10.1172/jci.insight.132964 · Cited by 177 · see citing works
Cairo, G., Recalcati, S., Pietrangelo, A., & Minotti, G. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00825-0 · Cited by 176 · see citing works
Yang, N., Tan, S.-H., Ng, S., Shi, Y. P., Zhou, J., Tan, K. S. W., Wong, W. S. F., & Shen, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564567 · Cited by 175 · see citing works
Widespread distribution of encapsulin nanocompartments reveals functional diversity
Giessen, T. W., & Silver, P. A. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.29 · Cited by 169 · see citing works
Biology of ferritin in mammals: an update on iron storage, oxidative damage and neurodegeneration
Finazzi, D., & Arosio, P. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1329-0 · Cited by 166 · see citing works
Self-citationIron transport proteins: Gateways of cellular and systemic iron homeostasis
Knutson, M. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.786632 · Cited by 163 · see citing works
Corsi, B., Cozzi, A., Arosio, P., Drysdale, J., Santambrogio, P., Campanella, A., Biasiotto, G., Albertini, A., & Levi, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m105372200 · Cited by 164 · see citing works
Self-citationKoorts, A. M., & Viljoen, M. (2007) · Archives of Physiology and Biochemistry · doi:10.1080/13813450701318583 · Cited by 164 · see citing works
Campanella, A., Rovelli, E., Santambrogio, P., Cozzi, A., Taroni, F., & Levi, S. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn308 · Cited by 162 · see citing works
Self-citationPhytoferritin and its implications for human health and nutrition
Zhao, G. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.01.009 · Cited by 143 · see citing works
Seldon, M. P., Silva, G. P. D. L., Pejanovic, N., Larsen, R., Grégoire, I. P., Filipe, J. C.-R., Anrather, J., & Soares, M. P. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.11.7840 · Cited by 132 · see citing works
Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Biasiotto, G., & Arosio, P. (2004) · Blood · doi:10.1182/blood-2003-06-1842 · Cited by 132 · see citing works
Self-citationMissirlis, F., Kosmidis, S., Brody, T., Mavrakis, M., Holmberg, S. K. S., Odenwald, W. F., Skoulakis, E. M. C., & Rouault, T. A. (2007) · Genetics · doi:10.1534/genetics.107.075150 · Cited by 131 · see citing works
Nuclear ferritin: A new role for ferritin in cell biology
Alkhateeb, A. A., & Connor, J. R. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.03.017 · Cited by 125 · see citing works
Iron-regulatory proteins: molecular biology and pathophysiological implications
Cairo, G., & Recalcati, S. (2007) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399407000531 · Cited by 124 · see citing works
Heme, heme oxygenase and ferritin in vascular endothelial cell injury
Balla, J., Vercellotti, G. M., Jeney, V., Yachie, A., Varga, Z., Eaton, J. W., & Balla, G. (2005) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200500076 · Cited by 123 · see citing works
Tsuji, Y. (2005) · Oncogene · doi:10.1038/sj.onc.1208901 · Cited by 121 · see citing works
Iron Regulatory Proteins: From Molecular Mechanisms to Drug Development
Recalcati, S., Minotti, G., & Cairo, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2983 · Cited by 123 · see citing works
Insect ferritins: Typical or atypical?
Pham, D. Q. ‐., & Winzerling, J. J. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.03.004 · Cited by 120 · see citing works
Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus)
Hu, Y., Zheng, W., & Sun, L. (2010) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2010.01.001 · Cited by 115 · see citing works
Iwasaki, K., MacKenzie, E. L., Hailemariam, K., Sakamoto, K., & Tsuji, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2845-2856.2006 · Cited by 112 · see citing works
Zhang, D., Meyron‐Holtz, E. G., & Rouault, T. A. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006080908 · Cited by 109 · see citing works
The role of labile iron pool in cardiovascular diseases.
Kruszewski, M. K. (2004) · Acta Biochimica Polonica · doi:10.18388/abp.2004_3585 · Cited by 104 · see citing works
The importance of eukaryotic ferritins in iron handling and cytoprotection
Arosio, P., Carmona, F., Gozzelino, R., Maccarinelli, F., & Poli, M. (2015) · Biochemical Journal · doi:10.1042/bj20150787 · Cited by 104 · see citing works
Self-citationFerritin L and H Subunits Are Differentially Regulated on a Post-transcriptional Level
Sammarco, M. C., Ditch, S., Banerjee, A., & Grabczyk, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703456200 · Cited by 102 · see citing works
Kakhlon, O., Gruenbaum, Y., & Cabantchik, Z. I. (2001) · Blood · doi:10.1182/blood.v97.9.2863 · Cited by 97 · see citing works
In vivo magnetic resonance imaging of ferritin-based reporter visualizes native neuroblast migration
Iordanova, B. E., & Ahrens, E. T. (2011) · NeuroImage · doi:10.1016/j.neuroimage.2011.08.068 · Cited by 97 · see citing works
Iron(II) and Hydrogen Peroxide Detoxification by Human H-Chain Ferritin. An EPR Spin-Trapping Study
Zhao, G., Arosio, P., & Chasteen, N. D. (2006) · Biochemistry · doi:10.1021/bi052443r · Cited by 95 · see citing works
Self-citationSakamoto, K., Iwasaki, K., Sugiyama, H., & Tsuji, Y. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0762 · Cited by 92 · see citing works
H ferritin knockout mice: a model of hyperferritinemia in the absence of iron overload
Ferreira, C., Santambrogio, P., Martin, M.-E., Andrieu, V., Feldmann, G., Hénin, D., & Beaumont, C. (2001) · Blood · doi:10.1182/blood.v98.3.525 · Cited by 90 · see citing works
Self-citationPost-transcriptional Modulation of Iron Homeostasis during p53-dependent Growth Arrest
Zhang, F., Wang, W., Tsuji, Y., Torti, S. V., & Torti, F. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806432200 · Cited by 90 · see citing works
Alli, A. A., Desai, D. N., Elshika, A., Conrad, M., Proneth, B., Clapp, W. L., Atkinson, C., Segal, M. S., Searcy, L. A., Denslow, N. D., et al. (2022) · Clinical Immunology · doi:10.1016/j.clim.2022.109213 · Cited by 86 · see citing works
Oxidative stress and cell death in cells expressing L-ferritin variants causing neuroferritinopathy
Cozzi, A., Rovelli, E., Frizzale, G., Campanella, A., Amendola, M., Arosio, P., & Levi, S. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.09.009 · Cited by 78 · see citing works
Self-citationShvartsman, M., Kikkeri, R. V., Shanzer, A., & Cabantchik, Z. I. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00054.2007 · Cited by 78 · see citing works
Naumova, A. V., Reinecke, H., Yarnykh, V. L., Deem, J. D., Yuan, C., & Murry, C. E. (2010) · Molecular Imaging · doi:10.2310/7290.2010.00020 · Cited by 77 · see citing works
Role of iron and ferritin in TNFα‐induced apoptosis in HeLa cells
Cozzi, A., Levi, S., Corsi, B., Santambrogio, P., Campanella, A., Gerardi, G., & Arosio, P. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00114-5 · Cited by 76 · see citing works
Self-citationCampan, M., Lionetti, V., Aquaro, G. D., Forini, F., Matteucci, M., Vannucci, L., Chiuppesi, F., Cristofano, C. D., Faggioni, M., Maioli, M., et al. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00935.2010 · Cited by 76 · see citing works
Excess Capacity of the Iron Regulatory Protein System
Wang, W., Di, X., D'Agostino, R. B., Torti, S. V., & Torti, F. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703167200 · Cited by 75 · see citing works
Zhang, J., Chen, X., Hong, J., Tang, A., Liu, Y., Xie, N., Nie, G., Yan, X., & Liang, M. (2020) · Science China Life Sciences · doi:10.1007/s11427-020-1795-4 · Cited by 76 · see citing works
Mechanisms of iron metabolism in Caenorhabditis elegans
Anderson, C. P., & Leibold, E. A. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00113 · Cited by 74 · see citing works
Iron, oxidative stress and the example of solar ultraviolet a radiation.
Aroun, A., Zhong, J. L., Tyrrell, R. M., & Pourzand, C. (2012) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05204g · Cited by 74 · see citing works
Effects of brevetoxin exposure on the immune system of loggerhead sea turtles
Walsh, C. J., Leggett, S. R., Carter, B. J., & Colle, C. F. (2009) · Aquatic Toxicology · doi:10.1016/j.aquatox.2009.12.014 · Cited by 73 · see citing works
Cell sensitivity to oxidative stress is influenced by ferritin autophagy
Kurz, T., Gustafsson, B., & Brunk, U. T. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.014 · Cited by 73 · see citing works
Velde, G. V., Rangarajan, J. R., Toelen, J., Dresselaers, T., Ibrahimi, A., Krylychkina, O., Vreys, R., der Linden, A. V., Maes, F., Debyser, Z., et al. (2011) · Gene Therapy · doi:10.1038/gt.2011.2 · Cited by 71 · see citing works
Iron Metabolism of the Skeletal Muscle and Neurodegeneration
Hałoń, M., Borkowska, A., Herman-Antosiewicz, A., & Antosiewicz, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00165 · Cited by 69 · see citing works
Noninvasive Monitoring of Embryonic Stem Cells In Vivo with MRI Transgene Reporter
Liu, J., Cheng, E., Long, R. C., Yang, S., Wang, L., Cheng, P., Yang, J., Wu, D., Mao, H. Z., & Chan, A. W. S. (2009) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2008.0678 · Cited by 66 · see citing works
Iron Oxidation and Core Formation in Recombinant Heteropolymeric Human Ferritins
Mehlenbacher, M. R., Poli, M., Arosio, P., Santambrogio, P., Levi, S., Chasteen, N. D., & Bou‐Abdallah, F. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00024 · Cited by 64 · see citing works
Self-citationOxidative stress caused by lead (Pb) induces iron deficiency in Drosophila melanogaster
Liu, Z.-H., Shang, J., Yan, L., Tian, W., Xiang, L., Wang, H.-L., Cheng, J., & Xiao, G. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.125428 · Cited by 64 · see citing works
Modulation of iron homeostasis with hepcidin ameliorates spontaneous murine lupus nephritis
Scindia, Y. M., Wlazlo, E., Ghias, E., Cechova, S., Loi, V., Leeds, J. T., Ledesma, J., Helen, C., & Swaminathan, S. (2020) · Kidney International · doi:10.1016/j.kint.2020.01.025 · Cited by 61 · see citing works
Aung, W., Hasegawa, S., Furukawa, T., & Saga, T. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm090 · Cited by 62 · see citing works
Geiser, D. L., Chavez, C. A., Flores-Munguia, R., Winzerling, J. J., & Pham, D. Q. ‐. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03709.x · Cited by 62 · see citing works
Iron‐siRNA Nanohybrids for Enhanced Chemodynamic Therapy via Ferritin Heavy Chain Downregulation
Wang, J., Ding, H., Zhu, Y., Liu, Y., Yu, M., Cai, H., Ao, R., Huang, H., Gong, P., Liao, Y., et al. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202302255 · Cited by 61 · see citing works
Iordanova, B. E., Robison, C. S., & Ahrens, E. T. (2010) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-010-0657-7 · Cited by 61 · see citing works
Velde, G. V., Rangarajan, J. R., Vreys, R., Guglielmetti, C., Dresselaers, T., Verhoye, M., der Linden, A. V., Debyser, Z., Baekelandt, V., Maes, F., et al. (2012) · NeuroImage · doi:10.1016/j.neuroimage.2012.04.040 · Cited by 60 · see citing works
Repression of the heavy ferritin chain increases the labile iron pool of human K562 cells
Kakhlon, O., Gruenbaum, Y., & Cabantchik, Z. I. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560311 · Cited by 59 · see citing works
Ferritin binds and activates p53 under oxidative stress
Lee, J., Jang, H., Cho, E., & Youn, H. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.08.125 · Cited by 58 · see citing works
Post-Transcriptional Regulation of Human Iron Metabolism by Iron Regulatory Proteins
Rouault, T. A. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0571 · Cited by 58 · see citing works
Zheng, W., Hu, Y., & Sun, L. (2010) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2010.03.012 · Cited by 56 · see citing works
Nie, G., Chen, G., Sheftel, A. D., Pantopoulos, K., & Ponka, P. (2006) · Blood · doi:10.1182/blood-2006-04-018341 · Cited by 56 · see citing works
Iron increases the susceptibility of multiple myeloma cells to bortezomib
Campanella, A., Santambrogio, P., Fontana, F., Frenquelli, M., Cenci, S., Marcatti, M., Sitia, R., Tonon, G., & Camaschella, C. (2012) · Haematologica · doi:10.3324/haematol.2012.074872 · Cited by 55 · see citing works
Self-citationVasculotoxic and Proinflammatory Effects of Plasma Heme: Cell Signaling and Cytoprotective Responses
Belcher, J. D., Nath, K. A., & Vercellotti, G. M. (2013) · ISRN Oxidative Medicine · doi:10.1155/2013/831596 · Cited by 54 · see citing works
Luscieti, S., Santambrogio, P., Langlois d'Estaintot, B., Granier, T., Cozzi, A., Poli, M., Gallois, B., Finazzi, D., Cattaneo, A., Levi, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.096404 · Cited by 51 · see citing works
Self-citationProtective Role of Hepcidin in Polymicrobial Sepsis and Acute Kidney Injury
Scindia, Y. M., Wlazlo, E., Leeds, J. T., Loi, V., Ledesma, J., Cechova, S., Ghias, E., & Swaminathan, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00615 · Cited by 52 · see citing works
Visualization of exosomes from mesenchymal stem cells in vivo by magnetic resonance imaging
Liu, T., Zhu, Y., Zhao, R., Wei, X., & Xin, X. (2020) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2020.02.001 · Cited by 52 · see citing works
Xie, C., Zhang, N., Zhou, H., Li, J., Li, Q., Zarubin, T., Lin, S., & Han, J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.15.6673-6681.2005 · Cited by 52 · see citing works
Pereira, S. M., Moss, D., Williams, S. R., Murray, P. A., & Taylor, A. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160715481 · Cited by 51 · see citing works
Maccarinelli, F., Pagani, A., Cozzi, A., Codazzi, F., Giacomo, G. D., Capoccia, S., Rapino, S., Finazzi, D., Politi, L. S., Cirulli, F., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.10.023 · Cited by 52 · see citing works
Self-citationActis, C., Muzio, G., & Autelli, R. (2021) · Cancers · doi:10.3390/cancers13061252 · Cited by 48 · see citing works
Cytoprotective effects of ferritin on doxorubicin-induced breast cancer cell death
Buranrat, B., & Connor, J. R. (2015) · Oncology Reports · doi:10.3892/or.2015.4250 · Cited by 48 · see citing works
- Authors
- Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Albertini, A., & Arosio, P.
- Affiliations
- IRCCS Ospedale San Raffaele (IT)
- University of Brescia (IT)
- Corresponding author
- Arosio, Paolo
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-08
- Volume
- 275
- Issue
- 33
- Pages
- 25122-25129
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2030928461
- Cited by
- 242
- References
- 36
- Citations by year
- 2025: 4 · 2024: 5 · 2023: 8 · 2022: 4 · 2021: 8 · 2020: 9 · 2019: 7 · 2018: 3 · 2017: 8 · 2016: 7 · 2015: 8 · 2014: 14 · 2013: 9 · 2012: 10
- FWCI
- 6.27
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, cc-by)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Keywords
- ferroxidase activity, iron metabolism, iron regulatory proteins, transferrin receptor, iron absorption, labile iron pool, oxidative stress resistance, cell growth, HeLa cells, tetracycline-responsive promoter
- MeSH terms
- Anti-Bacterial Agents, Apoferritins, Cell Division, Ceruloplasmin, Doxycycline, Enzyme-Linked Immunosorbent Assay, Ferritins, HeLa Cells, Humans, Hydrogen Peroxide, Iron, Mutation, Plasmids, Precipitin Tests, Promoter Regions, Genetic, Tetracycline, Time Factors, Transfection, Immunoblotting, Mutagenesis, DNA, Complementary, Oxidative Stress
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review