Cited by 558Neurological diseases and metabolismTrace Elements in HealthIron Metabolism and Disorders

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Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.

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Harris, Z L, Takahashi, Y, Miyajima, H, Serizawa, M, MacGillivray, R T, Gitlin, J D·1995·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.92.7.2539PMC PMC42253

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Abstract

Ceruloplasmin is an abundant alpha 2-serum glycoprotein that contains 95% of the copper found in the plasma of vertebrate species. We report here on the identification of a genetic defect in the ceruloplasmin gene in a patient previously noted to have a total absence of circulating serum ceruloplasmin in association with late-onset retinal and basal ganglia degeneration. In this patient T2 (transverse relaxation time)-weighted magnetic resonance imaging of the brain revealed basal ganglia densities consistent with iron deposition, and liver biopsy confirmed the presence of excess iron. Although Southern blot analysis of the patient's DNA was normal, PCR amplification of 18 of the 19 exons composing the human ceruloplasmin gene revealed a distinct size difference in exon 7. DNA sequence analysis of this exon revealed a 5-bp insertion at amino acid 410, resulting in a frame-shift mutation and a truncated open reading frame. The validity of this mutation was confirmed by analysis of DNA from the patient's daughter, which revealed heterozygosity for this same 5-bp insertion. The presence of this mutation in conjunction with the clinical and pathologic findings demonstrates an essential role for ceruloplasmin in human biology and identifies aceruloplasminemia as an autosomal recessive disorder of iron metabolism. These findings support previous studies that identified ceruloplasmin as a ferroxidase and are remarkably consistent with recent studies on the essential role of a homologous copper oxidase in iron metabolism in yeast. The clinical and laboratory findings suggest that additional patients with movement disorders and nonclassical Wilson disease should be examined for ceruloplasmin gene mutations.

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DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
The Wilson disease gene is a putative copper transporting P–type ATPase similar to the Menkes gene
Bull, P. C., Thomas, G. R., Rommens, J. M., Forbes, J., & Cox, D. W. (1993) · Nature Genetics · doi:10.1038/ng1293-327 · Cited by 1,939
The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene
Tanzi, R. E., Petrukhin, K. E., Чернов, И. П., Pellequer, J., Wasco, W., Ross, B., Romano, D., Parano, E., Pavone, P., Brzustowicz, L. M., et al. (1993) · Nature Genetics · doi:10.1038/ng1293-344 · Cited by 1,367
Increased nigral iron content and alterations in other metal ions occurring in brain in Parkinson's disease
Dexter, D. T., Wells, F. R., Lee, A. J., Agid, F., Agid, Y., Jenner, P., & Marsden, C. D. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb07264.x · Cited by 1,149
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
The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.
Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., Sipe, D. M., & Kaplan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90346-8 · Cited by 670
Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport
Dancis, A., Yuan, D. S., Haile, D., Askwith, C., Eide, D., Moehle, C., Kaplan, J., & Klausner, R. D. (1994) · Cell · doi:10.1016/0092-8674(94)90345-x · Cited by 659
Isolation and Characterization of a Human Liver cDNA as a Candidate Gene for Wilson Disease
Yamaguchi, Y., Heiny, M. E., & Gitlin, J. D. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2471 · Cited by 508
Deficiency of Ceruloplasmin in Patients with Hepatolenticular Degeneration (Wilson's Disease)
Scheinberg, I. H., & Gitlin, D. (1952) · Science · doi:10.1126/science.116.3018.484 · Cited by 444
The role of ceruloplasmin in iron metabolism.
Roeser, H. P., Lee, G. R., Nacht, S., & Cartwright, G. E. (1970) · Journal of Clinical Investigation · doi:10.1172/jci106460 · Cited by 365

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Background
The blue copper ceruloplasmin induces aggregation of newly differentiated neurons: a potential modulator of nervous system organization
Maltais, D. B., Desroches, D., Aouffen, M., Mateescu, M. A., Wang, R., & Paquin, J. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00325-7 · Cited by 25
“Aceruloplasminemia, a genetic deficiency of functional CP, causes iron accumulation and degeneration in brain and other organs (Harris et al., 1995; Klomp and Gitlin, 1996; David and Patel, 2000).”
Stimulation of the Ferroxidase Activity of Ceruloplasmin during Iron Loading into Ferritin
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Background
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Method
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Background
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Background
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Method
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Background
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BackgroundResult
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Background
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Background
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Background
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“Aceruloplasminemia is caused by mutations in the CP gene, which encodes CP (5).”
Background
Evaluation of serum ceruloplasmin in aggressive and chronic periodontitis patients
Harshavardhana, B., Rath, S., & Mukherjee, M. (2013) · Journal of Indian Society of Periodontology · doi:10.4103/0972-124x.115659 · Cited by 14
“[16,17] It thus leads to a state of hypoferremia.”
Systematic Identification of Proteins Binding with Cisplatin in Blood by Affinity Chromatography and a Four-Dimensional Proteomic Method
Tao, J., Jia, S., Wang, M., Huang, Z., Wang, B., Zhang, W., Wei, Y., Li, W., Jiang, H., & Du, Z. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00535 · Cited by 14
Ceruloplasmin expression and its role in iron transport in C6 cells
Chang, Y. Z., Qian, Z., Du, J. R., Zhu, L., Xu, Y., Li, L., Wang, C., Wang, Q., Ge, X. H., Ho, K. P., et al. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.01.004 · Cited by 14
The effect of copper deficiency on the formation of hemosiderin in sprague-dawley rats
Welch, K. D., Hall, J. O., Davis, T. Z., & Aust, S. D. (2007) · BioMetals · doi:10.1007/s10534-006-9046-7 · Cited by 15
“Excessive iron deposition resembling hemosiderosis in liver, brain, and pancreas has been observed upon histological examination of tissues from patients diagnosed with aceruloplasminemia (Harris et al. 1995; Harris et al. 1998; Harris and Gitlin 1996; Yoshida et al. 1995).”
Background
Atypical haemochromatosis: phenotypic spectrum and beta2-microglobulin candidate gene analysis.
Walker, A. P., Wallace, D. F., Partridge, J., Bomford, A. B., & Dooley, J. S. (1999) · PubMed Central · Cited by 14
Copper in mammals: mechanisms of homeostasis and pathophysiology
Cater, M. A., & Mercer, J. F. B. (2005) · Topics in current genetics · doi:10.1007/4735_101 · Cited by 15
“However, aceruloplasminemia patients display an iron accumulation phenotype and do not show any symptoms of disturbed copper homeostasis, which is strong evidence that ceruloplasmin is not an essential copper transport protein (Harris et al. 1995; Yoshida et al. 1995; Meyer et al. 2001).”
Background
Therapeutic applications of chelating drugs in iron metabolic disorders of the brain and retina
Shahandeh, A., Bui, B. V., Finkelstein, D. I., & Nguyen, C. T. O. (2020) · Journal of Neuroscience Research · doi:10.1002/jnr.24685 · Cited by 13
“Aceruloplasminemia is an uncommon adult-onset autosomal recessive disorder caused by disruption in a gene that encodes ceruloplasmin, an enzyme that plays role in cellular iron homeostasis (Harris et al., 1995).”
Background
Non-HFE hemochromatosis
Herruzo, J. A. S., & Muñoz, P. S. (2005) · Revista Española de Enfermedades Digestivas · doi:10.4321/s1130-01082005000400007 · Cited by 13
Neurobehavioural deficits following postnatal iron overload: II instrumental learning performance
Archer, T., Schoröder, N., & Fredriksson, A. (2003) · Neurotoxicity Research · doi:10.1007/bf03033374 · Cited by 13
Early onset insulin‐dependent diabetes mellitus as an initial manifestation of aceruloplasminaemia
MUROI, R., Yagyu, H., Kobayashi, H., Nagata, M., Sato, N. S., Ideno, J., Fujita, N., Ando, A., Okada, K., Takiyama, Y., et al. (2006) · Diabetic Medicine · doi:10.1111/j.1464-5491.2006.01883.x · Cited by 13
Identification andin silicocharacterization of a novel compound heterozygosity associated with hereditary aceruloplasminemia
Hofmann, W. P., Hofmann, W. P., Welsch, C., Takahashi, Y., Miyajima, H., Mihm, U., Krick, C. M., Zeuzem, S., & Sarrazin, C. (2007) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365520701278810 · Cited by 13
“Cp catalyzes the oxidation of ferrous iron to ferric iron, a step required for iron coupling to transferrin [4].”
Background
Hypocaeruloplasminaemia with heteroallelic caeruloplasmin gene mutation: MRI of the brain
Daimon, M., Moriai, S., Susa, S., Yamatani, K., Hosoya, T., & Kato, T. (1999) · Neuroradiology · doi:10.1007/s002340050730 · Cited by 13
Hémochromatose HFE : approche pathogénique et diagnostique
Brissot, P., Lan, C. L., Troadec, M., Lorho, R., Ropert, M., Lescoat, G., & Loréal, O. (2005) · Transfusion Clinique et Biologique · doi:10.1016/j.tracli.2005.04.040 · Cited by 14
Other autosomal recessive and childhood ataxias
Michele, G. D., & Filla, A. (2011) · Handbook of clinical neurology · doi:10.1016/b978-0-444-51892-7.00021-8 · Cited by 12
Ceruloplasmin
Harris, Z. L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-810532-0.00009-4 · Cited by 15
Rethinking ‘rare’ PINK1 Parkinson's disease: A meta-analysis of geographical prevalence, phenotypic diversity, and α-synuclein pathology
Yin, E. P., & Dieriks, B. V. (2025) · Journal of Parkinson s Disease · doi:10.1177/1877718x241304814 · Cited by 12
“…include increased sub-stantia nigra echogenicity, which is indicative of higher iron levels and posited as a vulnerability marker for PD. 164,165 In animal studies, heterozygote PINK1 knockout mice were unabletoproducelong-termpotentiationdespite repetitivecor-tical inputs to striatal…”
Effects of graded levels of cupric citrate on growth performance, antioxidant status, serum lipid metabolites and immunity, and tissue residues of trace elements in weaned pigs
Peng, C. C., Yan, J. Y., Dong, B., Zhu, L., Tian, Y., & Gong, L. M. (2016) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.16.0182 · Cited by 11
“Cu affects a wide spectrum of biological activities such as catalyzing the formation of hydroxyl radicals, which can lead to lipid peroxidation [9], and it plays a critical role in iron and zinc homeostasis [6,10].”
Background
Biometals and Alzheimer’s Disease
Mot, A. I., & Crouch, P. J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804562-6.00001-4 · Cited by 11
Aceruloplasminemia and putaminal cavitation
Riboldi, G. M., Anstett, K., Jain, R., Lau, H., & Swope, D. (2018) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2018.03.003 · Cited by 11
Aceruloplasminemia: a case report
Raimondo, D. D., Pinto, A. V., Tuttolomondo, A., Fernández, P., Camaschella, C., & Licata, G. (2008) · Internal and Emergency Medicine · doi:10.1007/s11739-008-0150-2 · Cited by 11
“Aceruloplasminemia, after the first description, has been reported mainly in Japanese patients [1, 2, 9–18] and rarely in whites [10, 19].”
Background
Divalent cation binding to ceruloplasmin
Musci, G., di Patti, M. C. B., Petruzzelli, R., GIARTOSIO, A., & Calabrese, L. (1996) · BioMetals · doi:10.1007/bf00188092 · Cited by 11
“A role for ceruloplasmin in iron metabolism, mediated by its ferroxidase activity, has recently received a confirmation (Harris et al. 1995).”
Background
Serúlópasmín og járn. Tengsl við Alzheimersjúkdóm og Parkinsonsjúkdóm
Jóhannesson, Þ., Kristinsson, J., Þórsdóttir, G., Snædal, J., & Snædal, J. (2012) · Læknablaðið · doi:10.17992/lbl.2012.10.457 · Cited by 11
Inherited iron overload disorders
Andrews, N. C. (2000) · Current Opinion in Pediatrics · doi:10.1097/00008480-200012000-00015 · Cited by 11
Iron: More than Meets the Eye
Naquin, E. R., Garg, R., Chen, W. J., Karmakar, E., Prasad, A., Mandadi, S., Depala, K. S., Gopianand, J. S., & Gnana‐Prakasam, J. P. (2025) · Nutrients · doi:10.3390/nu17182964 · Cited by 10
Haemolysis and Perturbations in the Systemic Iron Metabolism of Suckling, Copper-Deficient Mosaic Mutant Mice – An Animal Model of Menkes Disease
Lenartowicz, M., Starzyński, R. R., Krzeptowski, W., Grzmil, P., Bednarz, A., Ogórek, M., Pierzchała, O., Staroń, R., Gajowiak, A., & Lipiński, P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107641 · Cited by 10
“The role of Cp in iron metabolism has been reported in the congenital human disease acaeruloplasminemia, in which mutations in the caeruloplasmin gene lead to hypoferraemia and iron loading in the liver [12,13].”
Background
Zinc mediates the interaction between ceruloplasmin and apo-transferrin for the efficient transfer of Fe(III) ions
Sakajiri, T., Nakatsuji, M., Teraoka, Y., Furuta, K., Ikuta, K., Shibusa, K., Sugano, E., Tomita, H., Inui, T., & Yamamura, T. (2021) · Metallomics · doi:10.1093/mtomcs/mfab065 · Cited by 11
Animal Models of Hereditary Iron Transport Disorders
Andrews, N. C. (2002) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0593-8_1 · Cited by 10
New view of aceruloplasminemia: Systematic review and meta-analysis tracking dots from onset to disease development and iron-related features
Ketata, I., & Ellouz, E. (2023) · Rare · doi:10.1016/j.rare.2023.100010 · Cited by 9
Age-dependent expression of hephaestin in the brain of ceruloplasmin-deficient mice
Cui, R., Duan, X., Anderson, G. J., Qiao, Y.-T., Yu, P., Qian, Z., Yoshida, K., Takeda, S., Guo, P., Yang, Z.-L., et al. (2009) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2009.05.004 · Cited by 9
“All patients eventually succumb to the effects of increased iron accumulation within the basal ganglia [3–6].”
Background
Molecular analysis of Ceruloplasmin in a South African cohort presenting with oesophageal cancer
Strickland, N. J., Matsha, T. E., Erasmus, R., & Zaahl, M. G. (2011) · International Journal of Cancer · doi:10.1002/ijc.26418 · Cited by 10
Functional Characterization of Rare RAB12 Variants and Their Role in Musician’s and Other Dystonias
Hebert, E., Borngräber, F., Schmidt, A., Raković, A., Brænne, I., Weißbach, A., Hampf, J., Vollstedt, E., Größer, L., Schaake, S., et al. (2017) · Genes · doi:10.3390/genes8100276 · Cited by 9
“Furthermore, in several genetic forms of neurodegeneration with brain iron accumulation (NBIA), dystonia (DYT) is a prominent feature of the disease such as in NBIA/DYT-PANK2 [37], NBIA/DYT/PARK-PLA2G6 [38], NBIA/DYT/PARK-CP [39], and NBIA/DYT-DCAF17 [31,40].”
Background
Gene regulation by copper and the basis for copper homeostasis
Mercer, J. F. B. (1997) · Nutrition · doi:10.1016/s0899-9007(96)00323-1 · Cited by 9

Authors: Harris, Z. L., Takahashi, Y., Miyajima, H., Serizawa, M., MacGillivray, R. T., & Gitlin, J. D.
Affiliations: Washington University in St. Louis (US)
ORCID: Harris, Z L
Miyajima, H
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1995-03-28
Volume: 92
Issue: 7
Pages: 2539-2543
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.92.7.2539
PMC: PMC42253
OpenAlex: W2132544275
Cited by: 558
References: 29
Citations by year: 2026: 3 · 2025: 7 · 2024: 3 · 2023: 6 · 2022: 6 · 2021: 15 · 2020: 9 · 2019: 12 · 2018: 17 · 2017: 10 · 2016: 13 · 2015: 16 · 2014: 16 · 2013: 22 · 2012: 20
FWCI: 16.77
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01hl041536-13)
National Heart, Lung, and Blood Institute (HL41536)
Topics: Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Keywords: aceruloplasminemia, ceruloplasmin, frameshift mutation, iron metabolism, iron accumulation, basal ganglia degeneration, retinal degeneration, ferroxidase, copper oxidase, autosomal recessive disorder, movement disorders, heterozygosity
MeSH terms: Amino Acid Sequence, Animals, Basal Ganglia, Base Sequence, Blepharospasm, Ceruloplasmin, DNA, Exons, Female, Humans, Iron, Magnetic Resonance Imaging, Metal Metabolism, Inborn Errors, Middle Aged, Molecular Sequence Data, Reference Values, Retinal Degeneration, Vertebrates, Polymerase Chain Reaction, DNA Primers

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Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.

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