Nutrient Deprivation of Cultured Rat Hepatocytes Increases the Desferrioxamine-available Iron Pool and Augments the Sensitivity to Hydrogen Peroxide
Open accessAbstract
Primary cultures of rat hepatocytes were subjected to amino acid and serum deprivation for 4 h. This treatment augmented the sensitivity to ensuing hydrogen peroxide exposure for 30 min. The by nutrient deprivation-increased autophagocytosis was confirmed by transmission electron microscopy and uptake of the lysosomotropic weak base acridine orange within the intracellular acidic vacuolar apparatus. The desferrioxamine-available pool of iron increased 2.5-fold during deprivation, compared with control cells. Furthermore, amino acid deprivation increased the cellular protein turnover, measured by radioactive labeling with -3H-Leu. Exposure to 40 microM ascorbic acid specifically decreased the turnover of ferritin, as estimated by enzyme-linked immunosorbent assay, and prevented an increase of the desferrioxamine-available iron pool, resulting in protection against hydrogen peroxide-induced cell killing. Thus, hepatocytes with nutrient deprivation-enhanced autophagocytosis contain a larger pool of catalytically active iron than control cells. This iron pool is mainly derived from the turnover (autophagocytosis) of cytosolic ferritin and is probably situated in the lysosomes. Furthermore, nutrient-deprived cells show augmented sensitivity to hydrogen peroxide-induced oxidative stress, since the enhanced availability of iron in low molecular weight form results in an increased potential of intralysosomal Fenton chemistry, that may cause lysosomal rupture with release of potent hydrolytic enzymes.
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HFE2 is expressed mainly in skeletal muscle, cardiac tissue, and liver.
“HFE2 is expressed mainly in skeletal muscle, cardiac tissue, and liver.”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [230]
HFE2 is a GPI-anchored protein that appears to be a sensor of dietary iron levels.
“HFE2 is a GPI-anchored protein that appears to be a sensor of dietary iron levels (230).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [230]
Type 2 HH is associated with a mutation mapped via positional cloning to chromosome 1q in a gene encoding hemojuvelin (HFE2).
“This particular type of HH is associated with a mutation that was mapped via positional cloning to chromosome 1q (230). The mutation occurs in a gene encoding hemojuvelin (HFE2).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [230]
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Ohkuma, S., & Poole, B. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.7.3327 · Cited by 2,185 · see citing works
Ferritin: a cytoprotective antioxidant strategem of endothelium.
Balla, G., Jacob, H., Balla, J., Rosenberg, M. E., Nath, K. A., Apple, F., Eaton, J. W., & Vercellotti, G. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37165-0 · Cited by 1,097 · see citing works
Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site.
Graf, E., Mahoney, J. R., Bryant, R. G., & Eaton, J. W. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43139-5 · Cited by 855 · see citing works
Hyslop, P. A., Hinshaw, D. B., Halsey, W. A., Schraufstätter, I. U., Sauerheber, R., Spragg, R. G., Jackson, J. H., & Cochrane, C. G. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77928-9 · Cited by 616 · see citing works
The Biochemistry of Desferrioxamine and its Relation to Iron Metabolism
Keberle, H. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1965.tb54077.x · Cited by 615 · see citing works
Jakoby, W. B., & Ziegler, D. M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45272-0 · Cited by 415 · see citing works
Ferritin as a source of iron for oxidative damage
Reif, D. W. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90091-t · Cited by 357 · see citing works
Starke-Reed, P. E., & Farber, J. L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39218-9 · Cited by 298 · see citing works
Cellular injury induced by oxidative stress is mediated through lysosomal damage
Öllinger, K., & Brunk, U. T. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00062-3 · Cited by 243 · see citing works
Self-citationHydroxyl free radical formation from hydrogen peroxide by ferrous iron-nucleotide complexes
Floyd, R. A., & Lewis, C. A. (1983) · Biochemistry · doi:10.1021/bi00280a008 · Cited by 179 · see citing works
Aust, S. D., Chignell, C. F., Bray, T. Μ., Kalyanaraman, B., & Mason, R. P. (1993) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1993.1100 · Cited by 174 · see citing works
Mechanisms of the killing of cultured hepatocytes by hydrogen peroxide
Rubin, R., & Farber, J. L. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90010-9 · Cited by 169 · see citing works
Evidence that desferrioxamine cannot enter cells by passive diffusion
Lloyd, J. B., Cable, H. C., & Rice-Evans, C. A. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90109-i · Cited by 163 · see citing works
HISTOCHEMICAL INDICATIONS FOR LYSOSOMAL LOCALIZATION OF HEAVY METALS IN NORMAL RAT BRAIN AND LIVER
Brun, A. E., & Brunk, U. T. (1970) · Journal of Histochemistry & Cytochemistry · doi:10.1177/18.11.820 · Cited by 123 · see citing works
Low molecular weight iron and the oxygen paradox in isolated rat hearts.
Voogd, A., Sluiter, W. J., van Eijk, H. G., & Koster, J. F. (1992) · Journal of Clinical Investigation · doi:10.1172/jci116086 · Cited by 122 · see citing works
On the limited ability of superoxide to release iron from ferritin
Bolann, B. J., & Ulvik, R. J. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19415.x · Cited by 111 · see citing works
The effects of ascorbic acid on the intracellular metabolism of iron and ferritin.
Bridges, K. R., & Hoffman, K. E. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67014-0 · Cited by 105 · see citing works
Myers, B. M., Prendergast, F. G., Holman, R. T., Kuntz, S. M., & LaRusso, N. F. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115423 · Cited by 97 · see citing works
Sakaida, I., Kyle, M. E., & Farber, J. L. (1990) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10830-4 · Cited by 86 · see citing works
Lethal hydrogen peroxide toxicity involves lysosomal iron-catalyzed reactions with membrane damage
Brunk, U. T., Zhang, H., Roberg, K. B., & Öllinger, K. M. (1995) · Redox Report · doi:10.1080/13510002.1995.11746997 · Cited by 85 · see citing works
Self-citationAscorbic 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
Lysosomal origin of the ferric iron required for cell killing by hydrogen peroxide
Starke-Reed, P. E., Gilbertson, J. D., & Farber, J. L. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)90916-7 · Cited by 62 · see citing works
Insulinoma cells in culture show pronounced sensitivity to alloxan-induced oxidative stress
Zhang, H., �llinger, K., & Brunk, U. T. (1995) · Diabetologia · doi:10.1007/bf00401832 · Cited by 60 · see citing works
Self-citationCramer, S. M., Nathanael, B., & Horvath, C. G. (1984) · Journal of Chromatography A · doi:10.1016/s0021-9673(01)87642-1 · Cited by 59 · see citing works
Liquid chromatographic determination of common water-soluble antioxidants in biological samples
Honegger, C. G., Langemann, H., Krenger, W., & Kempf, A. (1989) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(00)83056-x · Cited by 55 · see citing works
Effect of ferric iron and desferrioxamine on lipofuscin accumulation in cultured rat heart myocytes
Marzabadi, M. R., Sohal, R. S., & Brunk, U. T. (1988) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(88)90122-4 · Cited by 51 · see citing works
Gower, J. D., Healing, G., & Green, C. J. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90099-7 · Cited by 42 · see citing works
Gower, J. D., Healing, G., & Green, C. R. (1989) · Free Radical Research Communications · doi:10.3109/10715768909074713 · Cited by 31 · see citing works
Energy depletion and autophagy. Cytochemical and biochemical studies in isolated rat hepatocytes
Schellens, J. P. M., & Meijer, A. J. (1991) · The Histochemical Journal · doi:10.1007/bf01041376 · Cited by 26 · see citing works
An experimental model system for leishmaniasis
Abok, K., Fredriksson, B. ‐., & Brunk, U. T. (1988) · Apmis · doi:10.1111/j.1699-0463.1988.tb00915.x · Cited by 24 · see citing works
Superoxide-mediated release of iron from ferritin by some flavoenzymes
Bando, Y., & Aki, K. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)92333-u · Cited by 19 · see citing works
Latour, I., Prégaldien, J.-L., & Calderón, P. B. (1992) · Archives of Toxicology · doi:10.1007/bf01972625 · Cited by 18 · see citing works
Zhang, H., & Brunk, U. T. (1993) · Diabetologia · doi:10.1007/bf00401140 · Cited by 18 · see citing works
Zhang, H., Olejnicka, B. T., Öllinger, K. M., & Brunk, U. T. (1996) · Redox Report · doi:10.1080/13510002.1996.11747056 · Cited by 14 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Reactive oxygen and mechanisms of inflammatory liver injury: Present concepts
Jaeschke, H. (2011) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2010.06592.x · Cited by 594 · see citing works
Methods for Monitoring Autophagy from Yeast to Human
Klionsky, D. J., Cuervo, A. M., & Seglen, P. O. (2007) · Autophagy · doi:10.4161/auto.3678 · Cited by 656 · 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
Oxidative Stress and Autophagy
Kiffin, R., Bandyopadhyay, U., & Cuervo, A. M. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.152 · Cited by 527 · see citing works
NF-κB Activation Represses Tumor Necrosis Factor-α-induced Autophagy
Djavaheri‐Mergny, M., Amelotti, M., Mathieu, J., Besançon, F., Bauvy, C., Souquère, S., Pierron, G., & Codogno, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602097200 · Cited by 467 · see citing works
The Roles of Therapy-Induced Autophagy and Necrosis in Cancer Treatment
Amaravadi, R. K., & Thompson, C. B. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-1595 · Cited by 469 · 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
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
Roberg, K. B., & Öllinger, K. M. (1998) · Europe PMC (PubMed Central) · Cited by 261 · see citing works
Self-citationFerroportin‐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
The Chelatable Iron Pool in Living Cells: A Methodically Defined Quantity
Petrat, F. M., de GROOT, H., Sustmann, R., & Rauen, U. (2002) · Biological Chemistry · doi:10.1515/bc.2002.051 · Cited by 230 · see citing works
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 227 · see citing works
Petrat, F., de GROOT, H., & Rauen, U. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560061 · Cited by 215 · see citing works
Petrat, F., Rauen, U., & de GROOT, H. (1999) · Hepatology · doi:10.1002/hep.510290435 · Cited by 202 · see citing works
Rauen, U., Petrat, F., Li, T., & de GROOT, H. (2000) · The FASEB Journal · doi:10.1096/fj.00-0071com · Cited by 189 · see citing works
PI3K/p110δ is a novel therapeutic target in multiple myeloma
Ikeda, H., Hideshima, T., Fulciniti, M., Perrone, G., Miura, N., Yasui, H., Okawa, Y., Kiziltepe, T., Santo, L., Vallet, S., et al. (2010) · Blood · doi:10.1182/blood-2009-06-222943 · Cited by 188 · 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
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
Petrat, F., Weisheit, D., LENSEN, M., de GROOT, H., Sustmann, R., & Rauen, U. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620137 · Cited by 143 · see citing works
Diverse Functions of Autophagy in Liver Physiology and Liver Diseases
Ke, P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020300 · Cited by 115 · see citing works
Induction and Regulation of Hepatocyte Apoptosis by Oxidative Stress
Czaja, M. J. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602760598909 · Cited by 113 · see citing works
Determination of the Chelatable Iron Pool of Single Intact Cells by Laser Scanning Microscopy
Petrat, F., de GROOT, H., & Rauen, U. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1711 · Cited by 112 · 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
Activation of autophagy in mesenchymal stem cells provides tumor stromal support.
Sánchez, C. G., Penfornis, P., Oskowitz, A., Boonjindasup, A., Cai, D. Z., Dhule, S., Rowan, B., Kelekar, A., Krause, D., & Pochampally, R. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr029 · Cited by 105 · see citing works
Chiang, M.-C., Chen, H.-M., Lee, Y.-H., Chang, H.-H., Wu, Y.-C., Soong, B.-W., Chen, C.-M., Wu, Y.-R., Liu, C.-S., Niu, D.-M., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddl481 · Cited by 95 · see citing works
Mitophagy in the Pathogenesis of Liver Diseases
Ke, P. (2020) · Cells · doi:10.3390/cells9040831 · Cited by 89 · see citing works
Larson, J. A., Howie, H. L., & So, M. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04169.x · Cited by 85 · see citing works
Iron-Induced Liver Injury: A Critical Reappraisal
Bloomer, S. A., & Brown, K. E. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092132 · Cited by 84 · see citing works
Selectively sensing first-row transition metal ions through fluorescence enhancement
Pal, S., Chatterjee, N., & Bharadwaj, P. K. (2014) · RSC Advances · doi:10.1039/c4ra02054e · Cited by 82 · see citing works
Autophagy, Redox Signaling, and Ventricular Remodeling
Gurusamy, N., & Das, D. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2524 · Cited by 81 · see citing works
Petrat, F., Paluch, S., Dogruöz, E., Dörfler, P., Kirsch, M., Korth, H., Sustmann, R., & de GROOT, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305291200 · Cited by 76 · 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
Self-citationLipiński, P., Drapier, J., Oliveira, L., Retmańska, H., Sochanowicz, B., & Kruszewski, M. K. (2000) · Blood · doi:10.1182/blood.v95.9.2960.009k13_2960_2966 · Cited by 73 · see citing works
Nagy, T. A., Moreland, S. M., Andrews-Polymenis, H., & Detweiler, C. S. (2013) · Infection and Immunity · doi:10.1128/iai.00412-13 · Cited by 72 · see citing works
Chougala, M. B., Bhaskar, J. J., Rajan, M. G. R., & Salimath, P. V. (2012) · Clinical Nutrition · doi:10.1016/j.clnu.2012.02.003 · Cited by 68 · see citing works
Chelation and determination of labile iron in primary hepatocytes by pyridinone fluorescent probes
Ma, Y., de GROOT, H., Liu, Z. D., Hider, R. C., & Petrat, F. (2006) · Biochemical Journal · doi:10.1042/bj20051496 · Cited by 68 · see citing works
Temporal responses in the disruption of iron regulation by manganese
Kwik-Uribe, C. L., & Smith, D. R. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20836 · Cited by 64 · 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
Fixing frataxin: ‘ironing out’ the metabolic defect in Friedreich's ataxia
Anzovino, A., Lane, D., Huang, L.-H. M., & Richardson, D. R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12470 · Cited by 54 · see citing works
Emerging Roles of Impaired Autophagy in Fatty Liver Disease and Hepatocellular Carcinoma
Niture, S. K., Lin, M., Ríos-Colón, L., Qi, Q., Moore, J. T., & Kumar, D. (2021) · International Journal of Hepatology · doi:10.1155/2021/6675762 · Cited by 46 · see citing works
Xu, X., Zhang, L., Shen, D., Wu, H., & Liu, Q. (2007) · Journal of Fluorescence · doi:10.1007/s10895-007-0263-4 · Cited by 44 · see citing works
Kwik-Uribe, C. L., Reaney, S. H., Zhu, Z., & Smith, D. R. (2003) · Brain Research · doi:10.1016/s0006-8993(03)02457-0 · Cited by 44 · see citing works
P66Shc mediated ferritin degradation—A novel mechanism of ROS formation
Borkowska, A., Sielicka-Dudzin, A., Herman-Antosiewicz, A., Hałoń, M., Woźniak, M., & Antosiewicz, J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.045 · Cited by 33 · see citing works
Enhancement of iron toxicity in L929 cells by d-glucose: accelerated(re-)reduction
Lehnen-Beyel, I., de GROOT, H., & Rauen, U. (2002) · Biochemical Journal · doi:10.1042/bj20020639 · Cited by 30 · see citing works
Bloomer, S. A., Brown, K. E., Buettner, G. R., & Kregel, K. C. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00719.2007 · Cited by 28 · see citing works
Zieger, M. A. J., & Gupta, M. P. (2006) · Cell Transplantation · doi:10.3727/000000006783981756 · Cited by 22 · see citing works
Iron-binding drugs targeted to lysosomes: a potential strategy to treat inflammatory lung disorders
Persson, H. L., & Richardson, D. R. (2005) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.14.8.997 · Cited by 21 · see citing works
Novel iron-specific fluorescent probes
Ma, Y., Luo, W., Camplo, M., Liu, Z. D., & Hider, R. C. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.05.010 · Cited by 20 · see citing works
Modulation of N-Ethylmaleimide-sensitive Factor Activity upon Amino Acid Deprivation
Shorer, H., Amar, N., Meerson, A., & Elazar, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500554200 · Cited by 18 · see citing works
Response to iron overload in cultured hepatocytes
Chen, H.-J., Sugiyama, M., Shimokawa, F., Murakami, M., Hashimoto, O., Matsui, T., & Funaba, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-78026-6 · Cited by 19 · see citing works
Martı́nez, R., Quintana, K., Navarro, R., Martı́n, C., Hernández, M., Aurrekoetxea, I., Ruiz-Sanz, J. I., Lacort, M., & Ruiz‐Larrea, M. B. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(02)00207-x · Cited by 18 · see citing works
Radiation-induced lysosomal iron reactivity: Implications for radioprotective therapy
Persson, H. (2006) · IUBMB Life · doi:10.1080/15216540600755998 · Cited by 16 · see citing works
Hagen, K., Zhu, C., Melefors, Ö., & Hultcrantz, R. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(98)00115-0 · Cited by 14 · see citing works
Kim, H. J., & Kim, S. G. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00877-2 · Cited by 13 · 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
Hagen, K., Eckes, K., Melefors, Ö., & Hultcrantz, R. (2002) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365520212494 · Cited by 9 · see citing works
Dabrosin, C., & Öllinger, K. M. (1998) · Free Radical Research · doi:10.1080/10715769800300261 · Cited by 8 · see citing works
Self-citationDev, 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
Stewart, C. D., Mamori, M., Arman, H. D., & Musie, G. T. (2021) · ChemistrySelect · doi:10.1002/slct.202102315 · Cited by 2 · see citing works
Soft x-ray tomographic study or iron deposits under iron-overload condition in human SK-Hep-1
Hua, M. D.-S., Hsieh, C.-C., Lin, Y.-H., Lin, Z., & Lai, L. (2023) · AIP conference proceedings · doi:10.1063/5.0168149 · Cited by 1 · see citing works
The Regulation of TonB-dependent Transporters in Neisseria gnorrhoeae
Hollander, A. M. (2011) · VCU Scholars Compass (Virginia Commonwealth University) · doi:10.25772/5jsv-wt28
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- Authors
- Öllinger, K., & Roberg, K.
- Affiliations
- Linköping University (SE)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-09
- Volume
- 272
- Issue
- 38
- Pages
- 23707-23711
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2046663690
- Cited by
- 65
- References
- 35
- Citations by year
- 2025: 1 · 2023: 1 · 2021: 3 · 2020: 2 · 2019: 2 · 2017: 1 · 2015: 2 · 2014: 2 · 2013: 3 · 2012: 1
- FWCI
- 3.12
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Keywords
- nutrient deprivation, hepatocytes, amino acid starvation, serum deprivation, hydrogen peroxide sensitivity, oxidative stress, autophagy, lysosomes, Fenton reaction, vitamin C, lysosomal rupture, protein turnover
- MeSH terms
- Animals, Autophagy, Cells, Cultured, Culture Media, Deferoxamine, Hydrogen Peroxide, Liver, Microscopy, Electron, Oxidation-Reduction, Rats
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 ›
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