The DOI matches its Crossref record.
Mechanism of ferritin iron uptake: activity of the H-chain and deletion mapping of the ferro-oxidase site. A study of iron uptake and ferro-oxidase activity of human liver, recombinant H-chain ferritins, and of two H-chain deletion mutants.
Open accessAbstract
To study the functional differences between human ferritin H- and L-chains and the role of the protein shell in the formation and growth of the ferritin iron core, we have compared the kinetics of iron oxidation and uptake of ferritin purified from human liver (90% L) and of the H-chain homopolymer overproduced in Escherichia coli (100% H). As a control for iron autocatalytic activity, we analyzed the effect of Fe(III) on the iron uptake reaction. The results show that the H-chain homopolymer has faster rates of iron uptake and iron oxidation than liver ferritin in all the conditions analyzed and that the difference is reduced in the conditions in which iron autocatalysis in high: i.e. at pH 7 and in presence of iron core. We have also analyzed the properties of two engineered H-chains, one lacking the last 22 amino acids at the carboxyl terminus and the other missing the first 13 residues at the amino terminus. These mutant proteins assemble in ferritin-like proteins and maintain the ability to catalyze iron oxidation. The deletion at the carboxyl terminus, however, prevents the formation of a stable iron core. It is concluded that the ferritin H-chain has an iron oxidation site which is separated from the sites of iron transfer and hydrolysis and that either the integrity of the molecule or the presence of the amino acid sequences forming the hydrophobic channel is necessary for iron core formation.
Overview
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
Verification
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
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
Self-citationMineralization in ferritin: an efficient means of iron storage
Chasteen, N. D., & Harrison, P. M. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4118 · Cited by 815
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
Self-citationSerum ferritin is derived primarily from macrophages through a nonclassical secretory pathway
Cohen, L. A., Gutierrez, L., Weiss, A., Leichtmann-Bardoogo, Y., Zhang, D.-L., Crooks, D. R., Sougrat, R., Morgenstern, A., Galy, B., Hentze, M. W., et al. (2010) · Blood · doi:10.1182/blood-2009-11-253815 · Cited by 452
Brissot, P., Pietrangelo, A., Adams, P. C., de Graaff, B., McLaren, C. E., & Loréal, O. (2018) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2018.16 · Cited by 430
Andrews, S. C. (1998) · Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60134-4 · Cited by 353
Identification of the ferroxidase centre in ferritin
Lawson, D. M., Treffry, A., Artymiuk, P. J., Harrison, P. M., Yewdall, S. J., Luzzago, A., Cesareni, G., Levi, S., & Arosio, P. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81040-3 · Cited by 312
Self-citationUnity in the Biochemistry of the Iron-Storage Proteins Ferritin and Bacterioferritin
Honarmand Ebrahimi, K., Hagedoorn, P.-L., & Hagen, W. R. (2015) · Chemical Reviews · doi:10.1021/cr5004908 · Cited by 297
Heme Degradation and Vascular Injury
Belcher, J. D., Beckman, J. D., Balla, G., Balla, J., & Vercellotti, G. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2822 · Cited by 257
Overexpression of Wild Type and Mutated Human Ferritin H-chain in HeLa Cells
Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Albertini, A., & Arosio, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003797200 · Cited by 242
Self-citationIron-independent induction of ferritin H chain by tumor necrosis factor
Miller, L. L., Miller, S. C., Torti, S. V., Tsuji, Y., & Torti, F. M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.11.4946 · Cited by 213
Role for NF-κB in the regulation of ferritin H by tumor necrosis factor-α
Kwak, E. L., Larochelle, D. A., Beaumont, C., Torti, S. V., & Torti, F. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.15285 · Cited by 189
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
Self-citationFahmy, M., & Young, S. P. (1993) · Biochemical Journal · doi:10.1042/bj2960175 · Cited by 150
Bacterial iron detoxification at the molecular level
Bradley, J. M., Svistunenko, D. A., Wilson, M. T., Hemmings, A. M., Moore, G. R., & Le Brun, N. E. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.007746 · Cited by 140
Tsuji, Y. (2005) · Oncogene · doi:10.1038/sj.onc.1208901 · Cited by 121
Langlois d'Estaintot, B., Santambrogio, P., Granier, T., Gallois, B., Chevalier, J. M., Précigoux, G., Levi, S., & Arosio, P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.04.036 · Cited by 113
Self-citationRegulation, mechanisms and proposed function of ferritin translocation to cell nuclei
Thompson, K. J., Fried, M. G., Ye, Z., Boyer, P., & Connor, J. R. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.10.2165 · Cited by 110
Tsuji, Y., Miller, L. L., Miller, S. C., Torti, S. V., & Torti, F. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89638-0 · Cited by 103
Levi, 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
Self-citationConditional 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
Nandar, W., Neely, E. B., Unger, E., & Connor, J. R. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.02.009 · Cited by 64
Conditional deletion of ferritin H in mice reduces B and T lymphocyte populations
Vanoaica, L., Richman, L., Jaworski, M., Darshan, D., Luther, S. A., & Kühn, L. C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089270 · Cited by 56
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
Self-citationJian, N., Dowle, M., Horniblow, R. D., Tselepis, C., & Palmer, R. E. (2016) · Nanotechnology · doi:10.1088/0957-4484/27/46/46lt02 · Cited by 50
YANG, X., & CHASTEEN, N. D. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3380615 · Cited by 52
Cozzi, A., Santambrogio, P., Privitera, D., Broccoli, V., Rotundo, L. I., Garavaglia, B., Benz, R., Altamura, S., Goede, J. S., Muckenthaler, M. U., et al. (2013) · Journal of Experimental Medicine · doi:10.1084/jem.20130315 · Cited by 47
Self-citationBaraibar, M. A., Barbeito, A. G., Muhoberac, B. B., & Vidal, R. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.015 · Cited by 45
Beaumont, C., Seyhan, A., Yachou, A. K., Grandchamp, B., & Jones, R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31988-9 · Cited by 33
Desmyter, L., Dewaele, S., Reekmans, R., Nystrom, T., Contreras, R., & Chen, C. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.01.008 · Cited by 31
Ferritoid, a Tissue-specific Nuclear Transport Protein for Ferritin in Corneal Epithelial Cells
Millholland, J. M., Fitch, J. M., Cai, C. X., Gibney, E. P., Beazley, K. E., & Linsenmayer, T. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210050200 · Cited by 30
Metadata
- Authors
- Levi, S., Luzzago, A., Cesareni, G., Cozzi, A., Franceschinelli, F., Albertini, A., & Arosio, P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1988-12
- Volume
- 263
- Issue
- 34
- Pages
- 18086-18092
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1556929642
- Cited by
- 380
- References
- 0
- FWCI
- 7.88
- Type
- journal article
- Language
- en
- Open access
- hybrid
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
