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Release of iron from ferritin requires lysosomal activity
Abstract
How ferritin-Fe becomes available for cell functions is unknown. Our previous studies with rat hepatoma cells indicated ferritin had to be degraded to release its Fe. In these studies, we investigated whether this occurs in other cell types and whether lysosomes are required. Release of ferritin-Fe was induced with desferoxamine (DFO) in (59)Fe-preloaded hepatoma, Caco2, and erythroid K562 cells and measured by rocket immunoelectrophoresis and autoradiography. The half-lives for ferritin-(59)Fe and protein were parallel (23, 16, and 11 h for the hepatic, Caco2, and K562 cells, respectively). Co-treatment with 180 microM Fe, leupeptin, chymostatin, or chloroquine markedly decreased rates of ferritin-Fe release and ferritin degradation. Lactacystin had no effect except for a small one in erythroid cells. Fractionation of hepatoma cell lysates on iodixanol gradients showed rapid depletion of cytosolic ferritin by DFO treatment but no accumulation in lysosomes. We conclude that regardless of cell type, release of Fe from ferritin occurs mainly through lysosomal proteolysis.
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“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 [54]
In the citing paper
“Ferritinophagy, the process of ferritin being sequestered into autophagosomes and delivered to lysosomes for degradation, is important for liberating iron from ferritin and thus for maintaining cellular iron homeostasis [51], [53], [54], [55].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [54]
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“Other studies have shown that cytoplasmic ferritin similarly reaches lysosomes and that lysosomes may facilitate the release of iron from ferritin (29, 30).”
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“The mechanism of ferritin iron release in vivo is much more difficult to apprehend and it is currently admitted that ferritin iron is mainly released after proteolytic degradation of the protein through different mechanisms (Truty et al., 2001; De Domenico et al., 2006; Kidane et al., 2006).”
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“As Ft-receptor- (Scara5 or Tim-2) mediated endocytic iron uptake and reutilization of Ft-bound storage iron require lysosomes [50], this pathway may not only export iron but also provide secreted Ft or its degraded product hemosiderin to the CSF/ISF.”
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 329
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“Other arguments for the autophagy hypothesis is that exposure of cells in culture to a panel of inhibitors to lysosomal enzymes prevents the release of iron from ferritin (Kidane et al. 2006), and the finding that exposure of cells to the iron chelator DFO, which is endocytosed and transported into the lysosomal compa…”
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Trivedi, P. C., Bartlett, J. J., & Pulinilkunnil, T. (2020) · Cells · doi:10.3390/cells9051131 · Cited by 309
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Distinct mechanisms of ferritin delivery to lysosomes in iron-depleted and iron-replete cells
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“Several groups have reported that lysosomal degradation of ferritin is crucial for the utilization of ferritin iron stores in a number of different settings (25, 33, 42) and plays a central role in iron extraction from ferritin.”
BackgroundProtein damage, repair and proteolysis
Chondrogianni, N., Petropoulos, I., Grimm, S., Georgila, K., Catalgol, B., Friguet, B., Grune, T., & Gonos, E. S. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.09.001 · Cited by 271
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“Ferritin degradation appears to play an important role in iron release from ferritin in vivo [144–147], which can be stimulated by iron chelators [148] and oxidative stress [149].”
BackgroundFerroportin‐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
“Studies by others have indicated that ferritin can be degraded in the lysosome (Bridges and Hoffman, 1986; Kidane et al, 2006).”
Ultrastructural analysis of autophagosome organization using mammalian autophagy-deficient cells
Kishi‐Itakura, C., Koyama‐Honda, I., Itakura, E., & Mizushima, N. (2014) · Journal of Cell Science · doi:10.1242/jcs.156034 · Cited by 235
“Although autophagic degradation of ferritin has been suggested by the results of previous studies (Asano et al., 2011; De Domenico et al., 2009; Kidane et al., 2006; Ollinger and Roberg, 1997), in the present study we demonstrated that ferritin is a bona fide selective autophagy substrate.”
InfluentialThe 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 211
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“Expression of ferritin is regulated post-transcriptionally by IRPs, and degradation is induced by certain iron chelators and lysosomal activity (108, 227).”
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“The protein component, apoferritin, combined with iron are involved in many important biological processes and play important roles in maintaining the balance of Fe3þ ions in biological systems (Kidane et al., 2006).”
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Iron homeostasis in host and gut bacteria – a complex interrelationship
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“Iron may leave ferritin through gated pores or via autophagy and lysosomal degradation of ferritin.(29,30) Iron storage in ferritin is largely determined by the level of ferritin protein, which is tightly regulated by cellular iron levels.”
BackgroundLysosomal Iron, Iron Chelation, and Cell Death
Terman, A., & Kurz, T. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4885 · Cited by 192
“There is evidence that this occurs intralysosomally through the autophagic degradation of ferritin (29, 37, 45).”
Zhao, T., Guo, X., & Sun, Y. (2021) · Aging and Disease · doi:10.14336/ad.2020.0912 · Cited by 180
Specific iron chelators determine the route of ferritin degradation
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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
“On the other hand, there is evidence showing that DFO induces ferritin degradation through the lysosomal pathway (20, 21, 65).”
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Lui, G. Y. L., Kovačević, Ž., Richardson, V., Merlot, A. M., Kalinowski, D. S., & Richardson, D. R. (2015) · Oncotarget · doi:10.18632/oncotarget.4349 · Cited by 165
“Of importance, the iron storage protein, ferritin, is reported to be degraded in the cell via autophagy [314, 315].”
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Ebrahimi‐Fakhari, D., Saffari, A., Wahlster, L., Lu, J., Byrne, S., Hoffmann, G. F., Jungbluth, H., & Şahin, M. (2015) · Brain · doi:10.1093/brain/awv371 · Cited by 165
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Biology of ferritin in mammals: an update on iron storage, oxidative damage and neurodegeneration
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“…iron release has been shown in different cell lines exposed to iron-chelating agents [particularly deferoxamine (DFO) or overexpression of FtMt] (Kidane et al. 2006; Zhang et al. 2010), bacterial infection (larson et al. 2004) and ferroportin activation (Asano et al. 2011). lysosomal inhibitors…”
BackgroundOxidative Stress and Autophagy in the Regulation of Lysosome-Dependent Neuron Death
Pivtoraiko, V. N., Stone, S. L., Roth, K. A., & Shacka, J. J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2263 · Cited by 154
“…agents and protease inhibitors has been shown to increase intralysosomal ferritin stability and decrease the available pools of redox-active iron (75, 82), which, in contrast to macroautophagy induction, may suggest a limited role for redox-active iron and Fenton chemistry in the intralysosomal…”
InfluentialFerritins: furnishing proteins with iron
Bradley, J. M., Brun, N. E. L., & Moore, G. R. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1336-0 · Cited by 150
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“Under healthy conditions, astrocytic iron is believed to be released from ferritin via lysosomal degradation and the resulting free iron is exported with ferroportin (Kidane et al., 2006).”
NCOA4 drives ferritin phase separation to facilitate macroferritinophagy and microferritinophagy
Ohshima, T., Yamamoto, H., Sakamaki, Y., Saito, C., & Mizushima, N. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202203102 · Cited by 148
“During iron deficiency, ferritin particles are transported to lysosomes in order to release the stored iron atoms (Asano et al., 2011; Kidane et al., 2006).”
Ferritin as an important player in neurodegeneration
Friedman, A., Arosio, P., Finazzi, D., Koziorowski, D., & Gałązka-Friedman, J. (2011) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2011.03.016 · Cited by 131
“Previous studies showed that iron exits the shell after protein degradation, which is mediated by lysosomal autophagy and induced by stress conditions such as amino acid starvation [19], bacterial infection [20] and iron chelation with the siderophore DFO [21].”
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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 128
“Experiments monitoring the turnover of ferritin and the release of ferritin iron indicate that most iron release occurs with ferritin degradation (41, 42).”
BackgroundZhang, Y., Mikhael, M., Xu, D., Li, Y., Soe-Lin, S., Ning, B., Li, W., Nie, G., Zhao, Y., & Ponka, P. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3129 · Cited by 120
“For example, inhibitors of lysosomal proteases, but not proteasomal inhibitors, block the degradation induced by iron chelators in different cell lines (22, 52).”
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
“Release of 59Fe from ferritin, studied in three different cell lines, was blocked by inhibitors of lysosomal activity (leupeptin, chymostatin and chloroquine), but not by the proteosomal inhibitor (lactacystin) [69,70].”
BackgroundEmerging and Dynamic Biomedical Uses of Ferritin
Chiou, B., & Connor, J. R. (2018) · Pharmaceuticals · doi:10.3390/ph11040124 · Cited by 119
“Some studies suggest that intracellular ferritin is transported to the lysosome to be degraded and the iron inside the ferritin core to be recycled [27].”
BackgroundMobilization of Stored Iron in Mammals: A Review
Linder, M. C. (2013) · Nutrients · doi:10.3390/nu5104022 · Cited by 114
“Degradation was also measured by following loss of 35S-radioactivity from labeled ferritin in cells exposed to FAC or made iron deficient by exposure to DFO, which enters lysosomes, or with another chelator (bathophenanthroline disulfonate) that stays outside the cell.”
BackgroundInfluentialBrain iron accumulation in aging and neurodegenerative disorders
Hagemeier, J., Geurts, J. J. G., & Zivadinov, R. (2012) · Expert Review of Neurotherapeutics · doi:10.1586/ern.12.128 · Cited by 114
Zhang, D., Meyron‐Holtz, E. G., & Rouault, T. A. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006080908 · Cited by 110
“graded in the lysosome (7) or through a pore in the ferritin shell (8).”
BackgroundIron-sensitive fluorescent probes: monitoring intracellular iron pools
Ma, Y., Abbate, V., & Hider, R. C. (2014) · Metallomics · doi:10.1039/c4mt00214h · Cited by 106
Ferritin self-assembly, structure, function, and biotechnological applications
Sudarev, V. V., Dolotova, S. M., Bukhalovich, S. M., Bazhenov, S. V., Ryzhykau, Y. L., Uversky, V. N., Bondarev, N. A., Osipov, S. D., Mikhailov, A. E., Kuklina, D. D., et al. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.10.126 · Cited by 106
Iron and Neurodegeneration: Is Ferritinophagy the Link?
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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 111
“28 Notably, both iron release and ferritin degradation are reportedly dependent on functional lysosome; this is due to the critical involvement of the The physiological role of NCOA4.”
BackgroundThe many faces of the octahedral ferritin protein
Watt, R. K. (2011) · BioMetals · doi:10.1007/s10534-011-9415-8 · Cited by 98
Lin, Y., Epstein, D. L., & Liton, P. B. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-5410 · Cited by 97
Macroautophagy is impaired in old murine brain tissue as well as in senescent human fibroblasts
Ott, C., König, J., Höhn, A., Jung, T., & Grune, T. (2016) · Redox Biology · doi:10.1016/j.redox.2016.10.015 · Cited by 96
“Protein concentrations were determined by the Bradford assay (BioRad, 5000006) and immunoblot analyses were performed as described below.”
Proteasome activation delays aging in vitro and in vivo
Chondrogianni, N., Sakellari, M., Lefaki, M., Papaevgeniou, N., & Gonos, E. S. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.031 · Cited by 94
“The two mechanisms share a lot of common substrates for degradation [160–163], and they have a common recognition signal, namely the ubiquitin chains.”
BackgroundRole of Endolysosomes in HIV-1 Tat-Induced Neurotoxicity
Hui, L., Chen, X., Haughey, N. J., & Geiger, J. D. (2012) · ASN NEURO · doi:10.1042/an20120017 · Cited by 94
“…system that contains hydrolases that degrade macromolecules, high concentrations of readily releasable calcium (Christensen et al., 2002; Moreno and Docampo, 2009; Patel and Docampo, 2010), and high concentrations of potentially redox-active iron (Brun and Brunk, 1970; Kidane et al., 2006).”
BackgroundFerroptosis: Biological Rust of Lipid Membranes
Hassannia, B., Coillie, S. V., & Berghe, T. V. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8175 · Cited by 93
“Utilization of iron stored in ferritin requires the release of iron by lysosomal degradation of ferritin (83).”
The Mucosal Immune System and Its Regulation by Autophagy
Kabat, A. M., Pott, J., & Maloy, K. J. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00240 · Cited by 95
“To date, there is evidence for the targeted sequestration and selective autophagy of a diverse array of cytosolic cargos, including aggregate-prone or misfolded proteins (aggrephagy) (22, 24–26), protein complexes in signaling cascades (27–29), peroxisomes (pexophagy) (30, 31), mitochondria (mitophagy) (32–38), surplu…”
BackgroundAdvances in iron chelation: an update
Heli, H., Mirtorabi, S., & Karimian, K. (2011) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2011.569493 · Cited by 92
“Ferritin is hydrolyzed in lysosomes of cells, where it is converted to low molecular weight iron pools that are principal source of iron for chelating agents (proved by chloroquine inhibition of lysosomal catabolism and decrease in iron removal by chelating agents) [43].”
BackgroundA general map of iron metabolism and tissue-specific subnetworks
Hower, V., Mendes, P., Torti, F. M., Laubenbacher, R., Akman, S. A., Shulaev, V., & Torti, S. V. (2009) · Molecular BioSystems · doi:10.1039/b816714c · Cited by 97
Conditional deletion of ferritin H in mice induces loss of iron storage and liver damage #
Darshan, D., Vanoaica, L., Richman, L., Beermann, F., & Kühn, L. C. (2009) · Hepatology · doi:10.1002/hep.23058 · Cited by 86
“This agrees with reports of ferritin half-lives of 3 days in rat liver(29) and <24 h in tissue culture cells.(30) Thus, iron stores are dynamic making the metal continuously available for the biosynthesis of iron-containing proteins.”
BackgroundIron Supply via NCOA4-Mediated Ferritin Degradation Maintains Mitochondrial Functions
Fujimaki, M., Furuya, N., Saiki, S., Amo, T., Imamichi, Y., & Hattori, N. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00010-19 · Cited by 85
Alzheimer’s disease: as it was in the beginning
Kozlov, S. O., Afonin, A. М., Evsyukov, I., & Бондаренко, А. Б. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0006 · Cited by 87
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Powell, J. J., Bruggraber, S. F. A., Faria, N., Poots, L. K., Hondow, N., Pennycook, T. J., Latunde-Dada, G. O., Simpson, R. J., Brown, A., & Pereira, D. I. A. (2014) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2013.12.011 · Cited by 83
“However, it is a matter of debate as to whether the protein shell and ferrihydrite-like core of ferritin control the slow release of Fe(III) ions from the gastric environment, or, if ferritin as a whole or as a protein-denuded mineral nanoparticle is rapidly emptied from the stomach and endocytosed by the intestinal e…”
BackgroundNCOA4 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 75
Laskar, A., Ghosh, M., Khattak, S. I., Li, W., & Yuan, X. (2012) · Nanomedicine · doi:10.2217/nnm.11.148 · Cited by 75
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 75
Coordination of autophagy with other cellular activities
Wang, Y., & Qin, Z. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.194 · Cited by 71
Liu, X. S., Patterson, L. D., Miller, M. J., & Theil, E. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700153200 · Cited by 70
Li, W., Xu, L.-H., Forssell, C., Sullivan, J. L., & Yuan, X.-M. (2008) · Experimental Biology and Medicine · doi:10.3181/0711-rm-320 · Cited by 69
“Under certain conditions ferritin can even release redox-active iron and thus may also function as a prooxidant (12, 30, 31).”
BackgroundMolecular and biochemical changes of the cardiovascular system due to smoking exposure
Armani, C., Landini Jr., L., & Leone, A. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787846973 · Cited by 68
Castino, R., Fiorentino, I., Cagnin, M., Giovia, A., & Isidoro, C. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr179 · Cited by 69
“Iron accumulates in lysosomes following the continuous delivery to this organelle of ironcontaining proteins via endocytosis and macroautophagy (Kidane et al., 2006; Kurz et al., 2008).”
BackgroundDoulias, P., Kotoglou, P., Τενοπούλου, Μ., Keramisanou, D., Tzavaras, T., Brunk, U. T., Galaris, D., & Angelidis, C. E. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.11.022 · Cited by 65
Baksi, S., & Singh, N. (2017) · Scientific Reports · doi:10.1038/s41598-017-12862-x · Cited by 64
Ferroptosis in Parkinson's disease —— The iron-related degenerative disease
Yao, Z., Jiao, Q., Du, X., Jia, F., Chen, X., Yan, C., & Jiang, H. F. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102477 · Cited by 65
Autophagy-dependent versus autophagy-independent ferroptosis
Zhu, Y., Fujimaki, M., & Rubinsztein, D. C. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.01.005 · Cited by 64
Iron-mediated oxidative stress plays an essential role in ferritin-induced cell death
Bresgen, N., Jaksch, H., Lacher, H., Ohlenschläger, I., Uchida, K., & Eckl, P. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.019 · Cited by 62
Reductive Mobilization of Iron from Intact Ferritin: Mechanisms and Physiological Implication
Bou‐Abdallah, F., Paliakkara, J. J., Melman, G. I., & Melman, A. (2018) · Pharmaceuticals · doi:10.3390/ph11040120 · Cited by 63
“It is well established that the major pathway of iron mobilization from ferritin is based on proteolytic degradation, which involves transport of ferritin molecules into the lysosomes, followed by dissolution of the exposed iron hydroxide core [22,27,28].”
BackgroundLi, J., Yuan, J., Li, Y., Wang, J., Xie, Q., Ma, R., Wang, J., Ren, M., Lu, D., & Xu, Z. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154411 · Cited by 60
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
Self-citationPerturbed 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 58
“While ferritin-bound iron is “ nanocaged ” and largely excluded from participating in such intracellular signalling, part of the excessive PFC iron that we noted may fi nd its way into lysosomes, where ferritin is degraded and iron is released [168].”
BackgroundIdentification of autophagy as a longevity-assurance mechanism in the aging modelPodospora anserina
Knuppertz, L., Hamann, A., Pampaloni, F., Stelzer, E. H. K., & Osiewacz, H. D. (2014) · Autophagy · doi:10.4161/auto.28148 · Cited by 57
“While macroautophagy and the ubiquitinproteasome system were formerly regarded as 2 separate cellular pathways with distinct functions, it is now clear that a number of proteins can be degraded by both autophagy and the proteasome.(76-79) Recent work suggests that the 2 systems “communicate” with each other under cert…”
BackgroundIron 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 53
“Iron must be released from ferritin and reduced back to Fe 2+ for utilization via shuttling of ironbound ferritin to the lysosome, a process termed ferriti-nophagy (a form of selective autophagy) (39).”
Fibrillar α-synuclein toxicity depends on functional lysosomes
Guiney, S. J., Adlard, P. A., Lei, P., Mawal, C., Bush, A. I., Finkelstein, D. I., & Ayton, S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013428 · Cited by 52
“Membranes were probed with primary antibodies for proteins commonly associated with autophagosomes, p62 and LC3-II (43), ferritin, which is degraded by the autophagy-lysosomal pathway (44-47), and LAMP-1.”
MethodNasrollahi, F., Sana, B., Paramelle, D., Ahadian, S., Khademhosseini, A., & Lim, S. (2020) · Advanced Therapeutics · doi:10.1002/adtp.201900183 · Cited by 52
Ferritinophagy in the etiopathogenic mechanism of related diseases
Jin, X., Jiang, C., Zou, Z., Huang, H., Li, X., Xu, S., & Tan, R. (2023) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2023.109339 · Cited by 55
Sheftel, A. D., & Lill, R. (2008) · Annals of Medicine · doi:10.1080/07853890802322229 · Cited by 49
“In vivo experiments have demonstrated that iron release from Ft may precede lysosomal and/or proteasomal degradation of the protein (27,28).”
Background
Metadata
- Authors
- Kidane, T. Z., Sauble, E., & Linder, M. C.
- Affiliations
- California State University, Fullerton (US)
- ORCID
- Linder, Maria C.
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2006-09
- Volume
- 291
- Issue
- 3
- Pages
- C445-C455
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2136891799
- Cited by
- 263
- References
- 51
- Citations by year
- 2026: 6 · 2025: 13 · 2024: 17 · 2023: 13 · 2022: 12 · 2021: 17 · 2020: 13 · 2019: 10 · 2018: 16 · 2017: 16 · 2016: 12 · 2015: 12 · 2014: 17 · 2013: 13 · 2012: 9
- FWCI
- 7.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk053080-04)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK-53080)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Keywords
- ferritin, iron release, lysosomal proteolysis, deferoxamine, ferritin degradation, lysosomes, hepatoma cells, Caco-2 cells, iron metabolism, leupeptin, chymostatin, chloroquine, lactacystin
- MeSH terms
- Animals, Chloroquine, Deferoxamine, Ferritins, Humans, Immunoelectrophoresis, Iron, Leupeptins, Lysosomes, Oligopeptides, Peptide Hydrolases, Protease Inhibitors, Caco-2 Cells, K562 Cells, Enterocytes, Hepatocytes, Erythroid Cells, Rats
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