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Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.
Open accessAbstract
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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“As reported by Harris and colleagues, 184 iron deficiency results from lack of ferroxidase activity needed to mobilize iron from storage.”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [184]
In the citing paper
“In iron-replete cells, IRP1, which has ∼30% homology to mitochondrial aconitase based on amino acid alignments, loses its affinity for the IRE, and converts to a cytosolic aconitase (127, 263).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [127]
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“Several mutations have been reported in this exceptional autosomal recessive disease (OMIM 604290) (85), whose main clinical peculiarities are the presence of neurological symptoms, the intolerance to phlebotomies (due to the anemic trend), and the efficacy of desferrioxamine therapy (86, 87).”
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“This blue, multi-copper oxidase appears to have pleotropic functions and has been referred to as a prototypic ‘‘moonlighting’’ protein (Bielli and Calabrese 2002), capable of oxidizing a variety of substrates—from amines to Fe(II) ( Harris 2000; Linder 1991, 2002); scavenging radicals (Linder 2001, 2002); and deliveri…”
BackgroundInfluentialCOMPARATIVE NUTRITIONOF IRON AND COPPER
Winzerling, J. J., & Law, A. J. H. (1997) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.17.1.501 · Cited by 64
Ferroptosis is Involved in Hypoxic-ischemic Brain Damage in Neonatal Rats
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Sternlieb, I. (2000) · Clinics in Liver Disease · doi:10.1016/s1089-3261(05)70105-7 · Cited by 64
Expression and function of iron‐regulatory proteins in retina
Gnana‐Prakasam, J. P., Martin, P. M., Smith, S. B., & Ganapathy, V. (2010) · IUBMB Life · doi:10.1002/iub.326 · Cited by 62
“Aceruloplasminemia is caused by mutations in ceruloplasmin (48).”
BackgroundPantothenate Kinase-Associated Neurodegeneration
Hartig, M., Prokisch, H., Meitinger, T., & Klopstock, T. (2012) · Current Drug Targets · doi:10.2174/138945012802002384 · Cited by 63
“/primer/testing/genetictesting • Genetic Testing Registry: Hypoprebetalipoproteinemia, acanthocytosis, retinitis pigmentosa, and pallidal degeneration https://www.ncbi.nlm.nih.gov/gtr/conditions/C1846582/ • Genetic Testing Registry: Neurodegeneration with brain iron accumulation https://www.ncbi.nlm.nih.gov/gtr/condit…”
BackgroundInfluentialEffects of development and iron status on ceruloplasmin expression in rat brain
Chang, Y. Z., Qian, Z., Wang, K., Zhu, L., Yang, X. D., Du, J. R., Jiang, L. H., Ho, K. P., Wang, Q., & Ke, Y. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20321 · Cited by 64
“…from the brain cells based on observations on aceruloplasminemia (a disorder of iron metabolism resulting from inherited mutations in the CP gene) (Harris et al., 1995; Yoshida et al., 1995; Kaplan and O’Halloran, 1996; Takahashi et al., 1996; Gitlin, 1998) and studies using an animal model of…”
Background"Metal elements and pesticides as risk factors for Parkinson's disease - A review"
Ullah, I., Zhao, L., Yang, H. T., Muhammad, F., Alwayli, D., Wang, X., & Li, H. (2021) · Toxicology Reports · doi:10.1016/j.toxrep.2021.03.009 · Cited by 72
Kaneko, K., Yoshida, K., Arima, K., Ohara, S., Miyajima, H., Kato, T., Ohta, M., & Ikeda, S.-I. (2002) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/61.12.1069 · Cited by 61
“5 (pancreatic cancer) 15 dementia (IQ 80), blepharospasm, ataxia 5-bp (TACAC) insertion nt 1287 (exon 7) (14) 4 (16) 60/M/2 (cardiac failure) 4 dementia (IQ 68), ataxia 1-bp (A) insertion nt 607 (exon 3) (16) 5 (7) 58/M/20 (unknown) 2 dementia (IQ 69), oral dyskinesia G→A transition nt 2630 (exon15) (17)”
Lower serum ceruloplasmin levels correlate with younger age of onset in Parkinson’s disease
Bharucha, K. J., Friedman, J. H., Vincent, A. S., & Ross, E. D. (2008) · Journal of Neurology · doi:10.1007/s00415-009-0063-7 · Cited by 62
Aceruloplasminemia: A novel mutation in a family with marked phenotypic variability
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Value of an enzymatic assay for the determination of serum ceruloplasmin
MacIntyre, G., Gutfreund, K. S., Martin, W. R. W., Camicioli, R. M., & Cox, D. W. (2004) · Journal of Laboratory and Clinical Medicine · doi:10.1016/j.lab.2004.08.005 · Cited by 63
Anemia and iron overload due to compound heterozygosity for novel ceruloplasmin mutations
Bosio, S., Gobbi, M. D., Roetto, A., Zecchina, G., Leonardo, E., Rizzetto, M., Lucetti, C., Petrozzi, L., Bonuccelli, U., & Camaschella, C. (2002) · Blood · doi:10.1182/blood-2002-02-0584 · Cited by 63
Increased Lipid Peroxidation and Mitochondrial Dysfunction in Aceruloplasminemia Brains
Miyajima, H., Kono, S., Takahashi, Y., & Sugimoto, M. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0561 · Cited by 61
Tseng, H. H., Chang, J., Hwang, Y., Yeh, K., Chen, Y., & Yu, H. (2009) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-009-0585-5 · Cited by 60
“In addition, patients with aceruloplasminemia usually present with microcytic anemia (Harris et al. 1995; Loreal et al. 2002), and patients with atransferrinemia commonly suVer from severe anemia (Beutler et al. 2000; Hayashi et al. 1993).”
BackgroundProtective role of macrophage-derived ceruloplasmin in inflammatory bowel disease
Bakhautdin, B., Febbraio, M., Goksoy, E., de la Motte, C. A., Gulen, M. F., Childers, E. P., Hazen, S. L., Li, X., & Fox, P. L. (2012) · Gut · doi:10.1136/gutjnl-2011-300694 · Cited by 65
Harazono, A., Kawasaki, N., Itoh, S., Hashii, N., Ishii‐Watabe, A., Kawanishi, T., & Hayakawa, T. (2005) · Analytical Biochemistry · doi:10.1016/j.ab.2005.10.036 · Cited by 61
Oligodendroglial survival factors, PDGF-AA and CNTF, activate similar JAK/STAT signaling pathways
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Recent advances in understanding haemochromatosis: a transition state
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Hephaestin and Ceruloplasmin Play Distinct but Interrelated Roles in Iron Homeostasis in Mouse Brain
Jiang, R., Hua, C., Wan, Y., Jiang, B., Hu, H., Zheng, J., Fuqua, B. K., Dunaief, J. L., Anderson, G. J., David, S., et al. (2015) · Journal of Nutrition · doi:10.3945/jn.114.207316 · Cited by 60
“In humans, mutations in the Cp gene that result in loss of functional CP (aceruloplasminemia) lead to iron accumulation and neurodegeneration, particularly in the motor regions of the brain and in the retina (15, 23, 24).”
BackgroundMitochondrial Membrane Protein-Associated Neurodegeneration (MPAN)
Hartig, M., Prokisch, H., Meitinger, T., & Klopstock, T. (2013) · International review of neurobiology · doi:10.1016/b978-0-12-410502-7.00004-1 · Cited by 60
Metadata
- Authors
- Harris, Z. L., Takahashi, Y., Miyajima, H., Serizawa, M., MacGillivray, R. T., & Gitlin, J. D.
- Affiliations
- Washington University in St. Louis (US)
- 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
- 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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