Cited by 379Neurological diseases and metabolismIron Metabolism and DisordersTrace Elements in Health

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Ceruloplasmin Regulates Iron Levels in the CNS and Prevents Free Radical Injury

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Patel, Bharatkumar N., Dunn, Robert J., Jeong, Suh Young, Zhu, Qinzhang, Julien, Jean-Pierre, David, Samuel·2002·The Journal of Neuroscience

DOI 10.1523/jneurosci.22-15-06578.2002PMC PMC6758125

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Abstract

Ceruloplasmin is a ferroxidase that oxidizes toxic ferrous iron to its nontoxic ferric form. We have previously reported that a glycosylphosphatidylinositol-anchored form of ceruloplasmin is expressed in the mammalian CNS. To better understand the role of ceruloplasmin in iron homeostasis in the CNS, we generated a ceruloplasmin gene-deficient (Cp(-/-)) mouse. Adult Cp(-/-) mice showed increased iron deposition in several regions of the CNS such as the cerebellum and brainstem. Increased lipid peroxidation was also seen in some CNS regions. Cerebellar cells from neonatal Cp(-/-) mice were also more susceptible to oxidative stress in vitro. Cp(-/-) mice showed deficits in motor coordination that were associated with a loss of brainstem dopaminergic neurons. These results indicate that ceruloplasmin plays an important role in maintaining iron homeostasis in the CNS and in protecting the CNS from iron-mediated free radical injury. Therefore, the antioxidant effects of ceruloplasmin could have important implications for various neurodegenerative diseases such as Parkinson's disease and Alzheimer's disease in which iron deposition is known to occur.

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Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667
A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation
McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422
Toxicity of iron and hydrogen peroxide: the Fenton reaction
Winterbourn, C. C. (1995) · Toxicology Letters · doi:10.1016/0378-4274(95)03532-x · Cited by 1,415
Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,365
Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084
A radical hypothesis for neurodegeneration
Olanow, C. W. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90070-3 · Cited by 722
Altered Brain Metabolism of Iron as a Cause of Neurodegenerative Diseases?
Gerlach, M., Ben‐Shachar, D., Riederer, P. F., & Youdim, M. B. H. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63030793.x · Cited by 704
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Frey, D., Schneider, C., Xu, L., Borg, J., Spooren, W. P. J. M., & Caroni, P. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-07-02534.2000 · Cited by 683
The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.
Osaki, S., Johnson, D. A., & Frieden, E. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96527-0 · Cited by 679

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Barbariga, M., Curnis, F., Spitaleri, A., Andolfo, A., Zucchelli, C., Lazzaro, M., Magnani, G., Musco, G., Corti, A., & Alessio, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.520981 · Cited by 35
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Lee, C. M., Lo, H., Shao, R., Wang, S., Xia, W., Gershenson, D. M., & Hung, M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2551 · Cited by 35
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Tello, C., Darling, A., Lupo, V., Pérez‐Dueñas, B., & Espinós, C. (2017) · Clinical Genetics · doi:10.1111/cge.13057 · Cited by 34
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Ferroxidase Hephaestin's Cell-Autonomous Role in the Retinal Pigment Epithelium
Wolkow, N., Song, D., Song, Y., Chu, S., Hadziahmetovic, M., Lee, J. C., Iacovelli, J., Grieco, S. F., & Dunaief, J. L. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.12.041 · Cited by 34
Ceruloplasmin, a moonlighting protein in fish
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Ceruloplasmin Upregulation in Retina of Murine and Human Glaucomatous Eyes
Stasi, K., Nagel, D., Yang, X., Ren, L., Mittag, T. W., & Danias, J. (2007) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.06-0497 · Cited by 33
Differential expression of ceruloplasmin isoforms in the cerebrospinal fluid of amyotrophic lateral sclerosis patients
Conti, A., Iannaccone, S., Sferrazza, B., Monte, L. B. D., Cappa, S. F., Franciotta, D. M., Olivieri, S., & Alessio, M. (2008) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200780081 · Cited by 33
Molecular targets and therapeutic interventions for iron induced neurodegeneration
Bagwe‐Parab, S., & Kaur, G. (2019) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2019.12.011 · Cited by 33
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Texel, S. J., Zhang, J., Camandola, S., Unger, E. L., Taub, D. D., Koehler, R. C., Harris, Z. L., & Mattson, M. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025077 · Cited by 33
Deciphering glycomics and neuroproteomic alterations in experimental traumatic brain injury: Comparative analysis of aspirin and clopidogrel treatment
Abou‐Abbass, H., Bahmad, H. F., Abou‐El‐Hassan, H., Zhu, R., Zhou, S., Dong, X., Hamade, E., Mallah, K., Zebian, A., Ramadan, N., et al. (2016) · Electrophoresis · doi:10.1002/elps.201500583 · Cited by 32
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Song, X., Li, B., Li, Z., Wang, J., & Zhang, D. (2017) · Nutrition Research · doi:10.1016/j.nutres.2017.01.004 · Cited by 31
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Mani, K., Cheng, F., Havsmark, B., David, S., & Fransson, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313678200 · Cited by 30
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Activity and content of antioxidant enzymes in prostate tumors.
Kotrikadze, N., Alibegashvili, M., Zibzibadze, M., Abashidze, N., Chigogidze, T., Managadze, L., & Arcivadze, K. (2008) · PubMed · Cited by 29
Role of soluble ceruloplasmin in iron uptake by midbrain and hippocampus neurons
Ke, Y., Ho, K., Jin-rong, D., Zhu, L., Xu, Y., Wang, Q., Wang, C. Y., Li, L., Ge, X., Chang, Y. Z., et al. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20740 · Cited by 27
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Yui, K., Imataka, G., & Yoshihara, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179803 · Cited by 27
Presence of an acute phase response in sheep with clinical classical scrapie
Meling, S., Bårdsen, K., & Ulvund, M. J. (2012) · BMC Veterinary Research · doi:10.1186/1746-6148-8-113 · Cited by 27
Extrapyramidal and cerebellar movement disorder in association with heterozygous ceruloplasmin gene mutation
Kuhn, J., Miyajima, H., Takahashi, Y., Kunath, B., Hartmann-Klosterkoetter, U., Cooper-Mahkorn, D., Schaefer, M. C., & Bewermeyer, H. (2005) · Journal of Neurology · doi:10.1007/s00415-005-0608-3 · Cited by 27
Systems genetic analysis of peripheral iron parameters in the mouse
Jones, B. C., Beard, J. L., Gibson, J. N., Unger, E. L., Allen, R. P., Mccarthy, K., & Earley, C. J. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00608.2006 · Cited by 27
High Dietary Iron Disrupts Iron Homeostasis and Induces Amyloid-β and Phospho-τ Expression in the Hippocampus of Adult Wild-Type and APP/PS1 Transgenic Mice
Chen, M., Zheng, J., Liu, G., Zeng, C., Xu, E., Zhu, W., Anderson, G. J., & Chen, H. (2019) · Journal of Nutrition · doi:10.1093/jn/nxz168 · Cited by 26
Transcriptional regulation of ceruloplasmin by an IL-6 response element pathway
Conley, L., Geurs, T. L., & Levin, L. A. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.05.027 · Cited by 27
Structure-Function Analysis of the Cuprous Oxidase Activity in Fet3p from Saccharomyces cerevisiae
Stoj, C. S., Augustine, A. J., Solomon, E. I., & Kosman, D. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609766200 · Cited by 26
Serum concentrations of acute phase proteins in goats and ewes with naturally acquired Staphylococcus aureus mastitis
Simplício, K. M. M. G., Rocha, T. G., Sánchez, D. C. C., Cotrim, F., Silva, P. C., & Fagliari, J. J. (2017) · Arquivo Brasileiro de Medicina Veterinária e Zootecnia · doi:10.1590/1678-4162-8722 · Cited by 25
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Jouini, N., Saied, Z., Sassi, S. B., Nebli, F., Messaoud, T. B., Hentati, F., & Belal, S. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201250 · Cited by 25

Authors: Patel, B. N., Dunn, R. J., Jeong, S. Y., Zhu, Q., Julien, J.-P., & David, S.
Affiliations: Montreal General Hospital (CA)
ORCID: Jeong, Suh Young
Julien, Jean-Pierre
David, Samuel
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2002-08-01
Volume: 22
Issue: 15
Pages: 6578-6586
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.22-15-06578.2002
PMC: PMC6758125
OpenAlex: W1595395957
Cited by: 379
References: 51
Citations by year: 2026: 5 · 2025: 12 · 2024: 10 · 2023: 12 · 2022: 16 · 2021: 14 · 2020: 12 · 2019: 11 · 2018: 22 · 2017: 17 · 2016: 11 · 2015: 24 · 2014: 24 · 2013: 15 · 2012: 22
FWCI: 10.71
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Neuroscience (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Parkinson's Disease Foundation
Canadian Institutes of Health Research
Topics: Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords: ceruloplasmin, iron homeostasis, central nervous system, ferroxidase, oxidative damage, oxidative stress, lipid peroxidation, cerebellum, brainstem, dopaminergic neurons, motor coordination deficits, neurodegenerative diseases, Parkinson's disease, Alzheimer's disease, iron accumulation
MeSH terms: Animals, Astrocytes, Brain Stem, Cell Survival, Cells, Cultured, Central Nervous System, Ceruloplasmin, Disease Models, Animal, Free Radicals, Iron, Liver, Neurons, Transferrin, Lipid Peroxidation, Mice, Knockout, Oxidative Stress, Gene Targeting, Motor Skills Disorders, Mice

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Ceruloplasmin Regulates Iron Levels in the CNS and Prevents Free Radical Injury

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