Lysosomal proteolysis is the primary degradation pathway for cytosolic ferritin and cytosolic ferritin degradation is necessary for iron exit
Abstract
Cytosolic ferritins sequester and store iron, consequently protecting cells against iron-mediated free radical damage. However, the mechanisms of iron exit from the ferritin cage and reutilization are largely unknown. In a previous study, we found that mitochondrial ferritin (MtFt) expression led to a decrease in cytosolic ferritin. Here we showed that treatment with inhibitors of lysosomal proteases largely blocked cytosolic ferritin loss in both MtFt-expressing and wild-type cells. Moreover, cytosolic ferritin in cells treated with inhibitors of lysosomal proteases was found to store more iron than did cytosolic ferritins in untreated cells. The prevention of cytosolic ferritin degradation in MtFt-expressing cells significantly blocked iron mobilization from the protein cage induced by MtFt expression. These studies also showed that blockage of cytosolic ferritin loss by leupeptin resulted in decreased cytosolic ferritin synthesis and prolonged cytosolic ferritin stability, potentially resulting in diminished iron availability. Lastly, we found that proteasomes were responsible for cytosolic ferritin degradation in cells pretreated with ferric ammonium citrate. Thus, the current studies suggest that cytosolic ferritin degradation precedes the release of iron in MtFt-expressing cells; that MtFt-induced cytosolic ferritin decrease is partially preventable by lysosomal protease inhibitors; and that both lysosomal and proteasomal pathways may be involved in cytosolic ferritin degradation.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
These results are consistent with lysosome-mediated ferritin degradation in MEFs as previously reported.
“These results are consistent with lysosome-mediated ferritin degradation in MEFs as previously reported [51], [54], [55].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [55]
Cites
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
The roles of intracellular protein-degradation pathways in neurodegeneration
Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625 · see citing works
Proteasome inhibitors: valuable new tools for cell biologists.
Lee, D. H., & Goldberg, A. L. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01346-4 · Cited by 1,474 · 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
Leibold, E. A., & Munro, H. N. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.7.2171 · Cited by 671 · see citing works
I RON R EGULATORY P ROTEINS AND THE M OLECULAR C ONTROL OF M AMMALIAN I RON M ETABOLISM
Eisenstein, R. S. (2000) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.20.1.627 · Cited by 652 · see citing works
Ferritins: Dynamic Management of Biological Iron and Oxygen Chemistry
Liu, X., & Theil, E. C. (2005) · Accounts of Chemical Research · doi:10.1021/ar0302336 · Cited by 514 · see citing works
Small molecule regulators of autophagy identified by an image-based high-throughput screen
Zhang, L., Yu, J., Pan, H., Hu, P., Yan, H., Cai, W., Zhu, H., Yu, A. D., Xie, X., Ma, D., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709695104 · Cited by 470 · see citing works
Aisen, P., Wessling‐Resnick, M., & Leibold, E. A. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80033-7 · Cited by 424 · 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
Proteasome Inhibitors Activate Stress Kinases and Induce Hsp72
Meriin, A. B., Gabai, V. L., Yaglom, J., Shifrin, V. I., & Sherman, M. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6373 · Cited by 300 · see citing works
Direct interorganellar transfer of iron from endosome to mitochondrion
Sheftel, A. D., Zhang, A., Brown, C. M., Shirihai, O. S., & Ponka, P. (2007) · Blood · doi:10.1182/blood-2007-01-068148 · Cited by 266 · see citing works
Release of iron from ferritin requires lysosomal activity
Kidane, T. Z., Sauble, E., & Linder, M. C. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00505.2005 · Cited by 263 · see citing works
Ferroportin‐mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome
De Domenico, I., Vaughn, M. B., Li, L., Bagley, D., Musci, G., Ward, D. M., & Kaplan, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601409 · Cited by 235 · see citing works
Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
Cazzola, M., Invernizzi, R., Bergamaschi, G., Levi, S., Corsi, B., Travaglino, E., Rolandi, V., Biasiotto, G., Drysdale, J., & Arosio, P. (2003) · Blood · doi:10.1182/blood-2002-07-2006 · Cited by 205 · see citing works
Girelli, D., Corrocher, R., Bisceglia, L., Olivieri, O., De Franceschi, L., Zelante, L., & Gasparini, P. (1995) · Blood · doi:10.1182/blood.v86.11.4050.bloodjournal86114050 · Cited by 196 · see citing works
Poňka, P., Borová, J., Neuwirt, J., Fuchs, O., & Nečas, E. (1979) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(79)90100-4 · Cited by 183 · 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
Mitochondrial Ferritin: A New Player in Iron Metabolism
Drysdale, J., Arosio, P., Invernizzi, R., Cazzola, M., Volz, A., Corsi, B., Biasiotto, G., & Levi, S. (2002) · Blood Cells, Molecules, and Diseases · doi:10.1006/bcmd.2002.0577 · Cited by 180 · see citing works
Nie, G., Sheftel, A. D., Kim, S. F., & Ponka, P. (2004) · Blood · doi:10.1182/blood-2004-07-2722 · Cited by 179 · see citing works
Specific iron chelators determine the route of ferritin degradation
De Domenico, I., Ward, D. M., & Kaplan, J. (2009) · Blood · doi:10.1182/blood-2009-05-224188 · Cited by 176 · 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
Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts
Radisky, D. C., & Kaplan, J. (1998) · Biochemical Journal · doi:10.1042/bj3360201 · Cited by 163 · see citing works
Production 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
Ferritin iron uptake and release. Structure–function relationships
Harrison, P. M., Hoy, T. G., Macara, I. G., & Hoare, R. J. (1974) · Biochemical Journal · doi:10.1042/bj1430445 · Cited by 133 · see citing works
Localized Unfolding at the Junction of Three Ferritin Subunits
Takagi, H., Shi, D., Ha, Y., Allewell, N. M., & Theil, E. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18685 · Cited by 130 · see citing works
Richardson, D. R., Ponka, P., & Vyoral, D. (1996) · Blood · doi:10.1182/blood.v87.8.3477.bloodjournal8783477 · Cited by 128 · see citing works
Jin, W., Takagi, H., Pancorbo, B., & Theil, E. C. (2001) · Biochemistry · doi:10.1021/bi002509c · Cited by 98 · see citing works
Acquisition of iron from transferrin regulates reticulocyte heme synthesis.
Poňka, P., & Schulman, H. M. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38631-3 · Cited by 94 · see citing works
Wistow, G. J., Bernstein, S. L., Wyatt, M. K., Behal, A., Touchman, J. W., Bouffard, G., Smith, D., & Peterson, K. (2002) · PubMed · Cited by 91 · see citing works
The genetics of inherited sideroblastic anemias
Fleming, M. D. (2002) · Seminars in Hematology · doi:10.1053/shem.2002.35637 · Cited by 86 · see citing works
Oxidation-induced ferritin turnover in microglial cells: role of proteasome
Mehlhase, J., Sandig, G., Pantopoulos, K., & Grune, T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.025 · Cited by 84 · see citing works
Alcindor, T., & Bridges, K. R. (2002) · British Journal of Haematology · doi:10.1046/j.0007-1048.2002.03378.x · Cited by 84 · see citing works
Kwok, J., & Richardson, D. R. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.4.849 · Cited by 82 · see citing works
Endogenous ferritin protects cells with iron-laden lysosomes against oxidative stress
Garner, B., Roberg, K. B., & Brunk, U. T. (1998) · Free Radical Research · doi:10.1080/10715769800300121 · Cited by 74 · see citing works
Kwok, J., & Richardson, D. R. (2004) · Molecular Pharmacology · doi:10.1124/mol.65.1.181 · Cited by 71 · see citing works
Ferritin 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
Ascorbic acid inhibits lysosomal autophagy of ferritin.
Bridges, K. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47862-3 · Cited by 65 · see citing works
Persson, H. L., Nilsson, K., & Brunk, U. T. (2001) · Redox Report · doi:10.1179/135100001101536049 · 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
Ferritin Oxidation in Vitro: Implication of Iron Release and Degradation by the 20S Proteasome
Rudeck, M., Volk, T. J., Sitte, N., & Grune, T. (2000) · IUBMB Life · doi:10.1080/152165400410317 · Cited by 51 · see citing works
On the Cytoprotective Role of Ferritin in Macrophages and its Ability to Enhance Lysosomal Stability
Garner, B., Li, W., Roberg, K. B., & Brunk, U. T. (1997) · Free Radical Research · doi:10.3109/10715769709065788 · Cited by 50 · see citing works
Iron Prevents Ferritin Turnover in Hepatic Cells
Truty, J., Malpe, R., & Linder, M. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105392200 · Cited by 49 · see citing works
Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form
Kurz, T., & Brunk, U. T. (2009) · Autophagy · doi:10.4161/auto.5.1.7248 · Cited by 48 · see citing works
Mikulits, W., Schranzhofer, M., Beug, H., & Müllner, E. W. (1999) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(99)00085-x · Cited by 41 · see citing works
Cozzi, A., Santambrogio, P., Corsi, B., Campanella, A., Arosio, P., & Levi, S. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.05.004 · Cited by 38 · see citing works
May, A. M., & Fitzsimons, E. J. (1994) · Baillière s Clinical Haematology · doi:10.1016/s0950-3536(05)80128-3 · Cited by 29 · see citing works
Goralska, M., Nagar, S., Fleisher, L. N., & McGahan, M. C. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-0358 · Cited by 28 · see citing works
Lu, Z., Nie, G., Li, Y., Soe-Lin, S., Tao, Y., Cao, Y., Zhang, Z., Liu, N., Ponka, P., & Zhao, B. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2306 · Cited by 28 · see citing works
Vyoral, D., & Petrák, J. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(98)00039-1 · Cited by 27 · see citing works
Can Ferritin Provide Iron for Hemoglobin Synthesis?
Ponka, P., & Richardson, D. R. (1997) · Blood · doi:10.1182/blood.v89.7.2611 · Cited by 27 · see citing works
Burdon, K. P., Sharma, S., Chen, C. S., Dimasi, D. P., Mackey, D. A., & Craig, J. E. (2007) · Human Mutation · doi:10.1002/humu.9501 · Cited by 26 · see citing works
Hereditary Hyperferritinemia Cataract Syndrome: Ocular, Genetic, and Biochemical Findings
Ismail, A. R., Lachlan, K. L., Mumford, A. D., Temple, I. K., & Hodgkins, P. R. (2006) · European Journal of Ophthalmology · doi:10.1177/112067210601600125 · Cited by 19 · see citing works
Olejnicka, B. T., Dalen, H., Baranowski, M., & Brunk, U. T. (1997) · Redox Report · doi:10.1080/13510002.1997.11747128 · Cited by 12 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986 · see citing works
Regulators of Iron Homeostasis: New Players in Metabolism, Cell Death, and Disease
Bogdan, A. R., Miyazawa, M., Hashimoto, K., & Tsuji, Y. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.11.012 · Cited by 897 · see citing works
Kell, D. B., & Pretorius, E. (2014) · Metallomics · doi:10.1039/c3mt00347g · Cited by 667 · see citing works
Mechanisms of mammalian iron homeostasis
Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598 · see citing works
Regulation of iron transport and the role of transferrin
Gkouvatsos, K., Papanikolaou, G., & Pantopoulos, K. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.10.013 · Cited by 518 · see citing works
A Dual Role of Heme Oxygenase-1 in Cancer Cells
Chiang, S.-K., Chen, S., & Chang, L. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010039 · Cited by 466 · see citing works
Masaldan, S., Clatworthy, S. A. S., Gamell, C., Meggyesy, P. M., Rigopoulos, A.-T., Haupt, S., Haupt, Y., Denoyer, D., Adlard, P. A., Bush, A. I., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2017.08.015 · Cited by 452 · see citing works
The role of NCOA4-mediated ferritinophagy in health and disease
Santana-Codina, N., & Mancias, J. D. (2018) · Pharmaceuticals · doi:10.3390/ph11040114 · Cited by 410 · see citing works
Molecular mechanisms underlying chemical liver injury
Gu, X., & Manautou, J. E. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411002110 · Cited by 389 · see citing works
Stoyanovsky, D. A., Tyurina, Y. Y., Shrivastava, I. H., Bahar, İ., Tyurin, V. A., Protchenko, O. V., Jadhav, S., Bolevich, S., Kozlov, A. V., Vladimirov, Y. A., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.008 · Cited by 374 · see citing works
The Role of NCOA4-Mediated Ferritinophagy in Ferroptosis
Santana-Codina, N., Gikandi, A., & Mancias, J. D. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_4 · Cited by 315 · see citing works
The function and mechanism of ferroptosis in cancer
Wang, Y., Wei, Z., Pan, K., Li, J., & Chen, Q. (2020) · APOPTOSIS · doi:10.1007/s10495-020-01638-w · Cited by 262 · see citing works
Lane, D. J. R., & Richardson, D. R. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.007 · Cited by 264 · see citing works
Homeostasis and metabolism of iron and other metal ions in neurodegenerative diseases
Chen, L., Shen, Q.-Q., Liu, Y.-J., Zhang, Y., Sun, L., Ma, X.-Z., Song, N., & Xie, J.-X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02071-0 · Cited by 261 · see citing works
Oxidative Stress and the Homeodynamics of Iron Metabolism
Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5020808 · Cited by 247 · see citing works
The long history of iron in the Universe and in health and disease
Sheftel, A. D., Mason, A. B., & Ponka, P. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.08.002 · Cited by 234 · see citing works
Antioxidants Mediate Both Iron Homeostasis and Oxidative Stress
Imam, M. U., Zhang, S., Ma, J., Wang, H., & Wang, F. (2017) · Nutrients · doi:10.3390/nu9070671 · Cited by 226 · see citing works
New Insights into the Role of Ferritin in Iron Homeostasis and Neurodegenerative Diseases
Zhang, N., Yu, X., Xie, J., & Xu, H. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02277-7 · Cited by 218 · see citing works
The role of lysosomes in iron metabolism and recycling
Kurz, T., Eaton, J. W., & Brunk, U. T. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.08.016 · Cited by 207 · see citing works
Lysosomal Iron, Iron Chelation, and Cell Death
Terman, A., & Kurz, T. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4885 · Cited by 191 · see citing works
Brain Iron Metabolism Dysfunction in Parkinson’s Disease
Jiang, H. F., Wang, J., Rogers, J. T., & Xie, J. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9879-1 · Cited by 183 · see citing works
Iron Metabolism in Oligodendrocytes and Astrocytes, Implications for Myelination and Remyelination
Cheli, V. T., Correale, J. D., Paez, P. M., & Pasquini, J. M. (2020) · ASN NEURO · doi:10.1177/1759091420962681 · Cited by 182 · see citing works
Iron dysregulation in movement disorders
Dušek, P., Jankovic, J. J., & Le, W. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.054 · Cited by 172 · 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
Morris, G., Berk, M., Carvalho, A. F., Maes, M. H. J., Walker, A. J., & Puri, B. K. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.12.036 · Cited by 154 · see citing works
SPION primes THP1 derived M2 macrophages towards M1-like macrophages
Laskar, A., Eilertsen, J., Li, W., & Yuan, X.-M. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.10.115 · Cited by 138 · see citing works
Iron chelation in the treatment of neurodegenerative diseases
Dušek, P., Schneider, S. A., & Aaseth, J. (2016) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2016.03.010 · Cited by 133 · see citing works
Kalinowski, D. S., Stefani, C., Toyokuni, S., Ganz, T., Anderson, G. J., Subramaniam, V. N., Trinder, D., Olynyk, J. K., Chua, A. C. G., Jansson, P. J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.026 · Cited by 129 · see citing works
Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells
Philpott, C. C., Ryu, M., Frey, A. G., & Patel, S. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.791962 · Cited by 125 · see citing works
Emerging and Dynamic Biomedical Uses of Ferritin
Chiou, B., & Connor, J. R. (2018) · Pharmaceuticals · doi:10.3390/ph11040124 · Cited by 119 · see citing works
Mobilization of Stored Iron in Mammals: A Review
Linder, M. C. (2013) · Nutrients · doi:10.3390/nu5104022 · Cited by 111 · see citing works
Iron and Neurodegeneration: Is Ferritinophagy the Link?
Biasiotto, G., Lorenzo, D. D., Archetti, S., & Zanella, I. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9473-y · Cited by 104 · see citing works
The role of lysosome in regulated necrosis
Alu, A., Han, X., Ma, X., Wu, M., Wei, Y., & Wei, X. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.07.003 · Cited by 104 · see citing works
Li, J., Feng, Y., Li, Y., He, P., Zhou, Q.-Y., Tian, Y., Yao, R.-Q., & Yao, Y.-M. (2024) · Cell Proliferation · doi:10.1111/cpr.13621 · Cited by 102 · see citing works
Hirayama, T., Niwa, M., Hirosawa, S., & Nagasawa, H. (2020) · ACS Sensors · doi:10.1021/acssensors.0c01445 · Cited by 90 · see citing works
Iron stimulates plasma-activated medium-induced A549 cell injury
Adachi, T., Nonomura, S., Horiba, M., Hirayama, T., Kamiya, T., Nagasawa, H., & Hara, H. (2016) · Scientific Reports · doi:10.1038/srep20928 · Cited by 84 · see citing works
NCOA4 is Regulated by HIF and Mediates Mobilization of Murine Hepatic Iron Stores After Blood Loss
Li, X., Lozovatsky, L., Sukumaran, A., Gonzalez, L. A., Jain, A., Liu, D., Ayala‐Lopez, N., & Finberg, K. E. (2020) · Blood · doi:10.1182/blood.2020006321 · Cited by 76 · 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
Laskar, A., Ghosh, M., Khattak, S. I., Li, W., & Yuan, X. (2012) · Nanomedicine · doi:10.2217/nnm.11.148 · Cited by 75 · see citing works
Görg, B., Karababa, A., Schütz, E., Paluschinski, M., Schrimpf, A., Shafigullina, A. K., Castoldi, M., Bidmon, H. J., & Häussinger, D. (2019) · Journal of Hepatology · doi:10.1016/j.jhep.2019.06.020 · 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
Lysosome signaling in cell survival and programmed cell death for cellular homeostasis
Patra, S., Patil, S., Klionsky, D., & Bhutia, S. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30928 · Cited by 55 · see citing works
Caco-2 Cell Acquisition of Dietary Iron(III) Invokes a Nanoparticulate Endocytic Pathway
Pereira, D. I. A., Mergler, B. I., Faria, N., Bruggraber, S. F. A., Aslam, M. F., Poots, L. K., Prassmayer, L., Lönnerdal, B. L., Brown, A., & Powell, J. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081250 · Cited by 68 · see citing works
WDR45 , one gene associated with multiple neurodevelopmental disorders
Cong, Y., So, V., Tijssen, M. A. J., Verbeek, D. S., Reggiori, F., & Mauthe, M. (2021) · Autophagy · doi:10.1080/15548627.2021.1899669 · Cited by 68 · see citing works
Mobilization of iron from ferritin: New steps and details
La, A., Nguyen, T., Tran, K., Sauble, E., Tu, D., Gonzalez, A., Kidane, T. Z., Soriano, C., Morgan, J., Doan, M., et al. (2018) · Metallomics · doi:10.1039/c7mt00284j · Cited by 56 · see citing works
Perturbed iron biology in the prefrontal cortex of people with schizophrenia
Lotan, A., Luza, S., Opazo, C., Ayton, S., Lane, D. J. R., Mancuso, S. G., Pereira, A. M., Sundram, S., Weickert, C. S., Bousman, C., et al. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-01979-3 · 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
Iron robbery by intracellular pathogen via bacterial effector–induced ferritinophagy
Yan, Q., Zhang, W., Lin, M., Teymournejad, O., Budachetri, K., Lakritz, J., & Rikihisa, Y. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2026598118 · Cited by 54 · see citing works
Nasrollahi, F., Sana, B., Paramelle, D., Ahadian, S., Khademhosseini, A., & Lim, S. (2020) · Advanced Therapeutics · doi:10.1002/adtp.201900183 · Cited by 52 · see citing works
Mechanism of Ferroptosis and Its Role in Spinal Cord Injury
Li, F., Wang, H., Chen, H., Guo, J., Dang, X., Ru, Y., & Wang, H. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.926780 · Cited by 49 · see citing works
Iron Dysregulation in Parkinson’s Disease: Focused on the Autophagy–Lysosome Pathway
Chen, L., Huang, Y., Cui, J., Song, N., & Xie, J. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00390 · Cited by 46 · see citing works
Lactoferrin: from the structure to the functional orchestration of iron homeostasis
Ianiro, G., Rosa, L., di Patti, M. C. B., Valenti, P., Musci, G., & Cutone, A. (2022) · BioMetals · doi:10.1007/s10534-022-00453-x · Cited by 42 · see citing works
Tai, Y. K., Chew, K. C. M., Tan, B. W. Q., Lim, K., & Soong, T. W. (2016) · Scientific Reports · doi:10.1038/srep21113 · Cited by 39 · see citing works
The flux of iron through ferritin in erythrocyte development
Philpott, C. C. (2018) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000417 · Cited by 38 · see citing works
Wan, R., Cheli, V. T., González, D. A. S., Rosenblum, S. L., Wan, Q., & Paez, P. M. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1281-20.2020 · Cited by 38 · see citing works
Role of ferritinophagy in cystine deprivation-induced cell death in glioblastoma cells
Hayashima, K., Kimura, I., & Katoh, H. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.12.075 · Cited by 38 · see citing works
Savliwala, S., Chiu‐Lam, A., Unni, M., Rivera‐Rodriguez, A., Fuller, E. G., Sen, K., Threadcraft, M. A., & Rinaldi, C. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816662-8.00013-8 · Cited by 37 · see citing works
The mechanistic role of chemically diverse metal ions in the induction of autophagy
Sahni, S., Bae, D.-H., Jansson, P. J., & Richardson, D. R. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.01.009 · Cited by 31 · see citing works
Reduced autophagy leads to an impaired ferritin turnover in senescent fibroblasts
Ott, C., König, J., Höhn, A., Jung, T., & Grune, T. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.492 · Cited by 29 · see citing works
Karlsson, M., Frennesson, C. I., Gustafsson, T., Brunk, U. T., NILSSON, S. E. G., & Kurz, T. (2013) · Experimental Eye Research · doi:10.1016/j.exer.2013.10.014 · Cited by 29 · see citing works
Helicobacter pylori infection perturbs iron homeostasis in gastric epithelial cells
Flores, S. E., Aitchison, A., Day, A. S., & Keenan, J. I. (2017) · PLoS ONE · doi:10.1371/journal.pone.0184026 · Cited by 28 · see citing works
Krishan, S., Jansson, P. J., Gutierrez, E., Lane, D. J. R., Richardson, D. R., & Sahni, S. (2015) · PubMed Central · doi:10.18999/nagjms.77.1-2.1 · Cited by 28 · see citing works
Li, X., Xie, W., Zhang, Z., Kansara, S., Jankovic, J. J., & Le, W. (2012) · Neurosignals · doi:10.1159/000332954 · Cited by 26 · see citing works
Hor, C. H. H., & Tang, B. L. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2018-0045 · Cited by 23 · see citing works
Sun, Q., Wang, Y., Hou, L., Li, S., Hong, J.-S., Wang, Q., & Zhao, J. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.12.045 · Cited by 23 · see citing works
Iordanova, B. E., Hitchens, T. K., Robison, C. S., & Ahrens, E. T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072720 · Cited by 22 · see citing works
Jiang, Y., Pang, X., Wang, X., Leung, A. W., Luan, Y., Zhao, G., Wang, P., & Xu, C. (2017) · Journal of Materials Chemistry B · doi:10.1039/c6tb02860h · Cited by 22 · see citing works
Phenothiazines and phenoxazines: as electron transfer mediators for ferritin iron release
Koochana, P. K., Mohanty, A., Subhadarshanee, B., Satpati, S., Naskar, R., Dixit, A., & Behera, R. K. (2019) · Dalton Transactions · doi:10.1039/c8dt04383c · Cited by 22 · see citing works
Transferrin receptor is necessary for proper oligodendrocyte iron homeostasis and development
Cheli, V. T., González, D. A. S., Wan, R., Rosenblum, S. L., Denaroso, G., Angeliu, C. G., Smith, Z. I., Wang, C., & Paez, P. M. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1383-22.2023 · Cited by 21 · see citing works
To Boost or to Reset: The Role of Lactoferrin in Energy Metabolism
Ianiro, G., Niro, A., Rosa, L., Valenti, P., Musci, G., & Cutone, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115925 · Cited by 21 · see citing works
Non-canonical vs. Canonical Functions of Heme Oxygenase-1 in Cancer
Jagadeesh, A., Fang, X., Kim, S. H., Quispe, Y. N. G., Zheng, J., Surh, Y., & Kim, S. (2022) · Journal of Cancer Prevention · doi:10.15430/jcp.2022.27.1.7 · Cited by 20 · see citing works
Deferiprone attenuates neuropathology and improves outcome following traumatic brain injury
Daglas, M., Truong, P. H., Miles, L. Q., Juan, S. M. A., Rao, S. S., & Adlard, P. A. (2022) · British Journal of Pharmacology · doi:10.1111/bph.15950 · Cited by 20 · see citing works
The role of lysosomes in airborne particulate matter-induced pulmonary toxicity
Nie, B., Liu, X., Lei, C., Liang, X., Zhang, D., & Zhang, J. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.170893 · Cited by 19 · see citing works
Review of ferroptosis in colorectal cancer: Friends or foes?
Wu, Z., Fang, Z.-X., Hou, Y.-Y., Wu, B., Deng, Y., Wu, H.-T., & Liu, J. (2023) · World Journal of Gastroenterology · doi:10.3748/wjg.v29.i3.469 · Cited by 18 · see citing works
García-Beltrán, O., Urrutia, P. J., & Núñez, M. (2023) · Antioxidants · doi:10.3390/antiox12020214 · Cited by 15 · see citing works
Acute Phase Proteins: Ferritin and Ferritin Isoforms
Maria, A., & Viljoe, M. (2011) · InTech eBooks · doi:10.5772/20586 · Cited by 16 · see citing works
Phagocytic intracellular digestion in amphioxus ( Branchiostoma )
He, C., Han, T., Liao, X., Zhou, Y., Wang, X., Guan, R., Tian, T., Li, Y., Bi, C., Lü, N., et al. (2018) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2018.0438 · Cited by 16 · see citing works
Shi, Z., Yuan, H., Cao, L., & Lin, Y. (2023) · Biochemistry and Cell Biology · doi:10.1139/bcb-2022-0361 · Cited by 16 · see citing works
Ferroptosis: The functions of Nrf2 in human embryonic stem cells
Abraki, S. B., Karamali, F., & Nasr‐Esfahani, M. H. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110654 · Cited by 15 · see citing works
Melanoma bone metastasis-induced osteocyte ferroptosis via the HIF1α-HMOX1 axis
Jia, Y., Li, R., Li, Y., Kachler, K., Meng, X., Gießl, A., Qin, Y., Zhang, F., Liu, N., Andreev, D., et al. (2025) · Bone Research · doi:10.1038/s41413-024-00384-y · Cited by 15 · see citing works
Ashok, A., Chaudhary, S., Wise, A. S., Rana, N. A., McDonald, D., Kritikos, A. E., Lindner, E., & Singh, N. (2021) · Antioxidants · doi:10.3390/antiox10081253 · Cited by 14 · see citing works
Masison, J., & Mendes, P. (2023) · PLoS ONE · doi:10.1371/journal.pone.0281401 · Cited by 14 · see citing works
Co‐regulation of hepatic steatosis by ferritinophagy and unsaturated fatty acid supply
Li, N., Liao, Y., Huang, H., & Fu, S. (2022) · Hepatology Communications · doi:10.1002/hep4.2040 · Cited by 12 · see citing works
Sala, D., Musiani, F., & Rosato, A. (2018) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201800602 · Cited by 13 · see citing works
Xiong, Q., Sun, H., Xing, W., Li, X., Chen, G., Zhao, Z., Wu, C., & Li, P. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.03.012 · Cited by 12 · see citing works
Zhen, C., Zhang, G., Wang, S., Wang, J., Fang, Y., & Shang, P. (2024) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2024.03.001 · Cited by 12 · see citing works
Bi, C., Lü, N., Han, T., Huang, Z., Chen, J.-Y., He, C., & Lu, Z. (2020) · BioMed Research International · doi:10.1155/2020/3697342 · Cited by 12 · see citing works
Lysosomal Storage Disorders and Iron
Brás, J. (2013) · International review of neurobiology · doi:10.1016/b978-0-12-410502-7.00012-0 · Cited by 11 · see citing works
Yu, N., Wang, N., Zhang, W., Xue, J., Zhou, Q., Hu, F., Bai, X., & Liu, N. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e27276 · Cited by 8 · see citing works
Zhang, R., Xin, L., Guo, X., & Ding, Z. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26083482 · Cited by 8 · see citing works
Encapsulins: Nanotechnology’s future in a shell
Quinton, A. R., McDowell, H. B., & Hoiczyk, E. (2023) · Advances in applied microbiology · doi:10.1016/bs.aambs.2023.09.001 · Cited by 8 · see citing works
Cui, F., Mi, H., Wang, R., Du, Y., Li, F., Chang, S., Su, Y., Liu, A., & Shi, M. (2023) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-023-02860-6 · Cited by 7 · see citing works
Iron kinetics and laboratory assessment
Doig, K. (2020) · Elsevier eBooks · doi:10.1016/b978-0-323-53045-3.00017-9 · Cited by 7 · see citing works
Ye, X., Liu, R., Qiao, Z., Chai, X., & Wang, Y. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1273342 · Cited by 6 · see citing works
Vulinović, M. P., Turčić, P., Micek, V., & Ljubojević, M. (2022) · Archives of Industrial Hygiene and Toxicology · doi:10.2478/aiht-2022-73-3621 · Cited by 6 · see citing works
Dev, S., Asthana, S., Singh, P., Seth, P., Banerjee, C., & Mukhopadhyay, C. K. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.01.021 · Cited by 5 · see citing works
Iron‐inhibited autophagy via transcription factor ZFP27 in Parkinson's disease
Wang, Y., Wen, Q., Chen, R., Gan, Z., Huang, X., Wang, P., Cao, X., Zhao, N., Yang, Z., & Yan, J. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17946 · Cited by 4 · see citing works
Microbial Degradation of Proteins
Bustamante-Torres, M., Romero-Fierro, D., Estrella-Nuñez, J., & Bucio, E. (2021) · Environmental and microbial biotechnology · doi:10.1007/978-981-16-0518-5_13 · Cited by 4 · see citing works
A ferritin protein is involved in the development and reproduction of the whitefly, Bemisia tabaci
Yu, H., Wang, K., Yang, Z., Li, X., Liu, S., Wang, L., & Zhang, H. (2023) · Environmental Entomology · doi:10.1093/ee/nvad056 · Cited by 3 · see citing works
Adachi, T. (2022) · Thermal Medicine · doi:10.3191/thermalmed.38.1 · Cited by 3 · see citing works
- Authors
- Zhang, Y., Mikhael, M., Xu, D., Li, Y., Soe-Lin, S., Ning, B., Li, W., Nie, G., Zhao, Y., & Ponka, P.
- Affiliations
- Xizang Minzu University (CN)
- Jewish General Hospital (CA)
- Jilin University (CN)
- Chinese Academy of Sciences (CN)
- Corresponding author
- Nie, Guangjun
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2010-10
- Volume
- 13
- Issue
- 7
- Pages
- 999-1009
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2022266635
- Cited by
- 120
- References
- 55
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 6 · 2023: 14 · 2022: 10 · 2021: 8 · 2020: 10 · 2019: 3 · 2018: 10 · 2017: 12 · 2016: 6 · 2015: 6 · 2014: 5 · 2013: 10 · 2012: 7
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Chinese Academy of Sciences
- Canadian Institutes of Health Research
- 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
- ferritin degradation, lysosomal proteolysis, proteasome, mitochondrial ferritin, iron mobilization, iron storage, leupeptin, ferric ammonium citrate, iron availability
- MeSH terms
- Quaternary Ammonium Compounds, Cell Line, Cytosol, Ferric Compounds, Ferritins, Humans, Iron, Leupeptins, Lysosomes, Mitochondria, Peptide Hydrolases, Protease Inhibitors, Proteasome Endopeptidase Complex
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