Cited by 568Iron Metabolism and DisordersNeurological diseases and metabolismTrace Elements in Health

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Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux

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Harris, Z. Leah, Durley, Alison P., Man, Tsz Kwong, Gitlin, Jonathan D.·1999·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.96.19.10812PMC PMC17965

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Abstract

Aceruloplasminemia is an autosomal recessive disorder of iron metabolism. Affected individuals evidence iron accumulation in tissue parenchyma in association with absent serum ceruloplasmin. Genetic studies of such patients reveal inherited mutations in the ceruloplasmin gene. To elucidate the role of ceruloplasmin in iron homeostasis, we created an animal model of aceruloplasminemia by disrupting the murine ceruloplasmin ( Cp ) gene. Although normal at birth, Cp −/− mice demonstrate progressive accumulation of iron such that by one year of age all animals have a prominent elevation in serum ferritin and a 3- to 6-fold increase in the iron content of the liver and spleen. Histological analysis of affected tissues in these mice shows abundant iron stores within reticuloendothelial cells and hepatocytes. Ferrokinetic studies in Cp +/+ and Cp −/− mice reveal equivalent rates of iron absorption and plasma iron turnover, suggesting that iron accumulation results from altered compartmentalization within the iron cycle. Consistent with this concept, Cp −/− mice showed no abnormalities in cellular iron uptake but a striking impairment in the movement of iron out of reticuloendothelial cells and hepatocytes. Our findings reveal an essential physiologic role for ceruloplasmin in determining the rate of iron efflux from cells with mobilizable iron stores.

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Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166
Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
Tybulewicz, V. L. J., Crawford, C. E., Jackson, P. K., Bronson, R. T., & Mulligan, R. C. (1991) · Cell · doi:10.1016/0092-8674(91)90011-m · Cited by 1,281
Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C. (1997) · Nature Genetics · doi:10.1038/ng0897-383 · Cited by 1,159
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
Heme oxygenase 1 is required for mammalian iron reutilization
Poss, K. D., & Tonegawa, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10919 · Cited by 1,016
Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin
Babcock, M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M., & Kaplan, J. (1997) · Science · doi:10.1126/science.276.5319.1709 · Cited by 921
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
Transferrin receptor is necessary for development of erythrocytes and the nervous system
Levy, J. E., Jin, O., Fujiwara, Y., Kuo, F., & Andrews, N. (1999) · Nature Genetics · doi:10.1038/7727 · Cited by 574
Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.
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.92.7.2539 · Cited by 558
Self-citation
HFE gene knockout produces mouse model of hereditary hemochromatosis
Zhou, X. Y., Tomatsu, S., Fleming, R. E., Parkkila, S., Waheed, A., Jiang, J., Fei, Y., Brunt, E. M., Ruddy, D. A., Prass, C. E., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2492 · Cited by 519

Show all 40 references

Research works printed but not linked: 4

P Ponka, C Beaumont, D R Richardson Semin Hematol 35, 35–54 (1998).
B R Bacon, M L Schilsky Adv Intern Med 44, 91–116 (1999).
J I Logan, K B Harveyson, G B Wisdom, A E Hughes, G P R Archbold Q J Med 87, 663–670 (1994).
J D Torrance, T H Bothwell Methods in Hematology: Iron, ed J D Cook (Churchill Livingstone, New York), pp. 104–109 (1980).

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Authors: Harris, Z. L., Durley, A. P., Man, T. K., & Gitlin, J. D.
Affiliations: Washington University in St. Louis (US)
ORCID: Harris, Z. Leah
Man, Tsz Kwong
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1999-09-14
Volume: 96
Issue: 19
Pages: 10812-10817
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.96.19.10812
PMC: PMC17965
OpenAlex: W2104657893
Cited by: 568
References: 40
Citations by year: 2026: 6 · 2025: 3 · 2024: 10 · 2023: 13 · 2022: 16 · 2021: 17 · 2020: 20 · 2019: 17 · 2018: 20 · 2017: 14 · 2016: 17 · 2015: 14 · 2014: 18 · 2013: 13 · 2012: 24
FWCI: 15.54
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (1p30hd033688-01, 5r01hl041536-13, 5k08dk002464-04, DK02464, HL41536)
National Heart, Lung, and Blood Institute (HL41536)
National Institute of Diabetes and Digestive and Kidney Diseases (DK02464)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD 33688)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords: ceruloplasmin, aceruloplasminemia, iron efflux, cellular iron homeostasis, iron accumulation, iron metabolism, ferrokinetics, reticuloendothelial cells, hepatocytes, serum ferritin, iron storage
MeSH terms: Animals, Apoproteins, Ceruloplasmin, Disease Models, Animal, Homeostasis, Iron, Liver, Metal Metabolism, Inborn Errors, Models, Genetic, Phenotype, Spleen, Time Factors, Mutagenesis, Insertional, Neurodegenerative Diseases, Mice

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Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux

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