A Novel Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin Is Expressed by Mammalian Astrocytes

Patel, Bharatkumar N.; David, Samuel

doi:10.1074/jbc.272.32.20185

Cited by 327Neurological diseases and metabolismTrace Elements in HealthIron Metabolism and Disorders

A Novel Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin Is Expressed by Mammalian Astrocytes

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Patel, Bharatkumar N., David, Samuel·1997·Journal of Biological Chemistry

DOI 10.1074/jbc.272.32.20185

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Abstract

Ceruloplasmin is a copper-binding protein, which is the major ferroxidase in plasma of hepatic origin. We now provide evidence for a novel membrane-bound form of ceruloplasmin expressed by astrocytes in the mammalian central nervous system. Using a monoclonal antibody (1A1), we show that the cell surface antigen recognized by this antibody is ceruloplasmin and that it is directly anchored to the cell surface via a glycosylphosphatidylinositol (GPI) anchor. Our peptide mapping and other immunochemical studies indicate that, except for the GPI anchor, the membrane-bound and secreted plasma forms are similar. We also show that the membrane-bound form of ceruloplasmin has oxidase activity. These studies therefore suggest that the GPI-anchored form of ceruloplasmin may play a role similar to the secreted form in oxidizing ferrous iron. The GPI-anchored form of ceruloplasmin expressed by astrocytes is likely to be the major form of this molecule in the central nervous system because serum ceruloplasmin does not cross the blood-brain barrier. Lack of this form of ceruloplasmin in the central nervous system could lead to the generation of highly toxic free radicals, which can cause neuronal degeneration as seen in aceruloplasminemia and other neurodegenerative diseases such as Parkinson's and Alzheimer's disease.

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Recent evidence has implicated abnormal iron metabolism in the pathogenesis of neurodegeneration.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669 · see citing works
Antibodies, a laboratory manual
(1989) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(89)90130-3 · Cited by 12,318 · see citing works
Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
Cleveland, D. W., Fischer, S. G., Kirschner, M. W., & Laemmli, U. K. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75212-0 · Cited by 5,556 · see citing works
Basal Lipid Peroxidation in Substantia Nigra Is Increased in Parkinson's Disease
Dexter, D. T., Carter, C. J., Wells, F. R., Javoy-Agid, F., Agid, Y., Lees, A. J., Jenner, P. G., & MARSDEN, C. D. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb09133.x · Cited by 1,397 · see citing works
CELL-SURFACE ANCHORING OF PROTEINS VIA GLYCOSYL-PHOSPHATIDYLINOSITOL STRUCTURES
Ferguson, M. A. J., & Williams, A. F. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.001441 · Cited by 1,290 · see citing works
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 · see citing works
A permease-oxidase complex involved in high-affinity iron uptake in yeast.
Stearman, R., Yuan, D. S., Yamaguchi-Iwai, Y., Klausner, R. D., & Dancis, A. (1996) · Science · doi:10.1126/science.271.5255.1552 · Cited by 683 · see citing works
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 · see citing works
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 · see citing works
Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease
Lovell, M. A., Ehmann, W. D., Butler, S. M., & Markesbery, W. R. (1995) · Neurology · doi:10.1212/wnl.45.8.1594 · Cited by 644 · see citing works
THE STRUCTURE AND BIOSYNTHESIS OF GLYCOSYL PHOSPHATIDYLINOSITOL PROTEIN ANCHORS
Englund, P. T. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.001005 · Cited by 585 · see citing works
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 · see citing works
Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: an X-ray microanalysis
Hirsch, E. C., Brandel, J. ‐., Galle, P., Javoy‐Agid, F., & Agid, Y. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb08170.x · Cited by 537 · see citing works
Selective Increase of Iron in Substantia Nigra Zona Compacta of Parkinsonian Brains
Sofic, E., Paulus, W., Jellinger, K. A., Riederer, P. F., & Youdim, M. B. H. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb02017.x · Cited by 523 · see citing works
A Practical Guide to Protein and Peptide Purification for Microsequencing
(1993) · Elsevier eBooks · doi:10.1016/c2009-0-03542-9 · Cited by 502 · see citing works
HOW GLYCOSYL-PHOSPHATIDYLINOSITOL-ANCHORED MEMBRANE PROTEINS ARE MADE
Udenfriend, S., & Kodukula, K. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.003023 · Cited by 481 · see citing works
Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe (LAMMA) study
Good, P. F., Perl, D. P., Bierer, L. M., & Schmeidler, J. (1992) · Annals of Neurology · doi:10.1002/ana.410310310 · Cited by 476 · see citing works
A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans
Yoshida, K., Furihata, K., Takeda, S., Nakamura, A., Yamamoto, K., Morita, H., Hiyamuta, S., Ikeda, S.-I., Shimizu, N., & Yanagisawa, N. (1995) · Nature Genetics · doi:10.1038/ng0395-267 · Cited by 463 · see citing works
Increased levels of lipid hydroperoxides in the parkinsonian substantia nigra: An HPLC and ESR study
Dexter, D. T., Holley, A. E., Flitter, W. D., Slater, T. F., Wells, F. R., Daniel, S. E., Lees, A. J., Jenner, P. G., & MARSDEN, C. D. (1994) · Movement Disorders · doi:10.1002/mds.870090115 · Cited by 407 · see citing works
Regional distribution of iron and iron‐regulatory proteins in the brain in aging and Alzheimer's disease
Connor, J. R., Snyder, B. S., Beard, J. L., Fine, R. E., & Mufson, E. J. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310214 · Cited by 374 · see citing works
The Iron Chelator Desferrioxamine (Desferal) Retards 6‐Hydroxydopamine‐Induced Degeneration of Nigrostriatal Dopamine Neurons
Ben‐Shachar, D., Eshel, G., Finberg, J. P. M., & Youdim, M. B. H. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb11444.x · Cited by 299 · see citing works
Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration
Miyajima, H., Nishimura, Y., Mimguchi, K., Sakamoto, M., Shimizu, T., & Honda, N. (1987) · Neurology · doi:10.1212/wnl.37.5.761 · Cited by 295 · see citing works
The FET3 Gene Product Required for High Affinity Iron Transport in Yeast Is a Cell Surface Ferroxidase
Silva, D. M. D., Askwith, C. C., Eide, D. J., & Kaplan, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.3.1098 · Cited by 246 · see citing works
Hereditary ceruloplasmin deficiency with hemosiderosis: A clinicopathological study of a japanese family
Morita, H., Ikeda, S., Yamamoto, K., Morita, S., Yoshida, K., Nomoto, S., Kato, M., & Yanagisawa, N. (1995) · Annals of Neurology · doi:10.1002/ana.410370515 · Cited by 245 · see citing works
Amyotrophic lateral sclerosis: T2 shortening in motor cortex at MR imaging.
Oba, H., Araki, T., Ohtomo, K., et al. (1993) · Radiology · doi:10.1148/radiology.189.3.8234713 · Cited by 205 · see citing works
Ceruloplasmin gene expression in the murine central nervous system.
Klomp, L. W. J., Farhangrazi, Z. S., Dugan, L. L., & Gitlin, J. D. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118768 · Cited by 194 · see citing works
Molecular mechanisms of iron uptake in eukaryotes
de Silva, D. M., Askwith, C. C., & Kaplan, J. (1996) · Physiological Reviews · doi:10.1152/physrev.1996.76.1.31 · Cited by 182 · see citing works
Characterization of a transferrin-independent uptake system for iron in HeLa cells.
Sturrock, A., Alexander, J. K., Lamb, J., Craven, C., & Kaplan, J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39745-5 · Cited by 178 · see citing works
Inhibition of superoxide and ferritin-dependent lipid peroxidation by ceruloplasmin
Samokyszyn, V. M., Miller, D. M., Reif, D. W., & Aust, S. D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31218-8 · Cited by 166 · see citing works
Characterization of the cross‐reacting determinant (CRD) of the glycosyl‐phosphatidylinositol membrane anchor of Trypanosoma brucei variant surface glycoprotein
ZAMZE, S. E., Ferguson, M. A. J., COLLINS, R., Dwek, R. A., & Rademacher, T. W. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14310.x · Cited by 153 · see citing works
Aluminum, calcium, and iron in the spinal cord of patients with sporadic amyotrophic lateral sclerosis using laser microprobe mass spectroscopy: a preliminary study
Kasarskis, E. J., Tandon, L., Lovell, M. A., & Ehmann, W. D. (1995) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(95)00037-3 · Cited by 145 · see citing works
Primary structure of rat ceruloplasmin and analysis of tissue-specific gene expression during development.
Fleming, R. E., & Gitlin, J. D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39171-9 · Cited by 138 · see citing works
Antioxidant properties of caeruloplasmin towards iron‐ and copper‐dependent oxygen radical formation
Gutteridge, J. M. C. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)81111-9 · Cited by 137 · see citing works
Hereditary caeruloplasmin deficiency, dementia and diabetes mellitus
LOGAN, J. I., HARVEYSON, K. B., WISDOM, G. B., HUGHES, A. E., & ARCHBOLD, G. P. R. (1994) · QJM · doi:10.1093/oxfordjournals.qjmed.a068881 · Cited by 130 · see citing works
Synthesis and localization of plasma proteins in the developing human brain
Møllgård, K., Dzięgielewska, K. M., Saunders, N. R., Zakut, H. V., & Soreq, H. (1988) · Developmental Biology · doi:10.1016/0012-1606(88)90283-7 · Cited by 124 · see citing works
Iron Metabolism in Eukaryotes—Mars and Venus at It Again
Kaplan, J., & O’Halloran, T. V. (1996) · Science · doi:10.1126/science.271.5255.1510 · Cited by 124 · see citing works
Rat ceruloplasmin. Molecular cloning and gene expression in liver, choroid plexus, yolk sac, placenta, and testis.
Aldred, A. R., Grimes, A., Schreiber, G., et al. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61588-1 · Cited by 122 · see citing works
Characterization of a Nonsense Mutation in the Ceruloplasmin Gene Resulting in Diabetes and Neurodegenerative Disease
Takahashi, Y., Miyajima, H., Shirabe, S., Nagataki, S., Suenaga, A., & Gitlin, J. D. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.1.81 · Cited by 118 · see citing works
Hereditary ceruloplasmin deficiency with hemosiderosis
Okamoto, N., Wada, S., Oga, T., Kawabata, Y., Baba, Y., Habu, D., Takeda, Z., & Wada, Y. (1996) · Human Genetics · doi:10.1007/bf02346185 · Cited by 112 · see citing works
Coincident expression and distribution of melanotransferrin and transferrin receptor in human brain capillary endothelium
Rothenberger, S., Food, M. R., Gabathuler, R., Kennard, M. L., Yamada, T., Yasuhara, O., McGeer, P. L., & Jefferies, W. A. (1996) · Brain Research · doi:10.1016/0006-8993(96)88505-2 · Cited by 105 · see citing works
Transferrin receptors in rat central nervous system
Giometto, B., Bozza, F., Argentiero, V., Gallo, P., Pagni, S., Piccinno, M. G., & Tavolato, B. F. (1990) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(90)90183-n · Cited by 101 · see citing works
Ceruloplasmin levels in the human superior temporal gyrus in aging and Alzheimer's disease
Connor, J. R., Tucker, P., Johnson, M. J., & Snyder, B. S. (1993) · Neuroscience Letters · doi:10.1016/0304-3940(93)90805-u · Cited by 95 · see citing works
Ferritin and ceruloplasmin in oxidative damage: review and recent findings
de Silva, D. M., & Aust, S. D. (1993) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y93-107 · Cited by 78 · see citing works
Developmental patterns of gene expression of secreted proteins in brain and choroid plexus
Thomas, T., Schreiber, G., & Jaworowski, A. (1989) · Developmental Biology · doi:10.1016/0012-1606(89)90076-6 · Cited by 77 · see citing works
Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: the important primary role for iron-binding and iron-oxidising proteins
Gutteridge, J. M. C., & Quinlan, G. J. (1993) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(93)90129-v · Cited by 74 · see citing works
Determinants of Ion Specificity on EF-hands Sites
da Silva, A. C. R., Kendrick‐Jones, J., & Reinach, F. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.12.6773 · Cited by 73 · see citing works
Increased plasma lipid peroxidation in patients with aceruloplasminemia
Miyajima, H., Takahashi, Y., Serizawa, M., Kaneko, E., & Gitlin, J. D. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02178-7 · Cited by 70 · see citing works
Human ceruloplasmin. Tissue-specific expression of transcripts produced by alternative splicing.
Yang, F., Friedrichs, W. E., Cupples, R. L., Bonifacio, M., Sanford, J. A., Horton, W. A., & Bowman, B. H. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)87015-6 · Cited by 67 · see citing works
The nosology of Hallervorden-Spatz disease
HALLIDAY, W. C. (1995) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(95)00212-k · Cited by 64 · see citing works
Free radical formation in autopsy samples of Alzheimer and control cortex
Zhou, Y., Richardson, J. S., Mombourquette, M. J., & Weil, J. A. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(94)11787-j · Cited by 47 · see citing works
Fine Structure of the Human Ceruloplasmin Gene
Daimon, M., Yamatani, K., Igarashi, M., Fukase, N., Kawanami, T., Kato, T., Tominaga, M., & Sasaki, H. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.1437 · Cited by 44 · see citing works
Multiple isoforms of guinea pig decay-accelerating factor (DAF) generated by alternative splicing
Nonaka, M. I., Miwa, T., Okada, N., et al. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.155.6.3037 · Cited by 40 · see citing works
Transferrin receptor expression in myelin deficient (md)rats
Roskams, A. J., & Connor, J. R. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310304 · Cited by 39 · see citing works
Familial dementia due to a frameshift mutation in the caeruloplasmin gene
Harris, Z. L., Migas, M. C., Hughes, A., Logan, J. I., & Gitlin, J. D. (1996) · QJM · doi:10.1093/qjmed/89.5.355 · Cited by 39 · see citing works
Pumping iron in the '90s
Jefferies, W. A., Gabathuler, R., Rothenberger, S., Food, M. R., & Kennard, M. L. (1996) · Trends in Cell Biology · doi:10.1016/0962-8924(96)10019-2 · Cited by 29 · see citing works
The Role of an Astrocyte Surface Molecule in Neuronal Migration in the Developing Rat Cerebellum
Mittal, B., & David, S. (1994) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1994.1007 · Cited by 15 · see citing works
Self-citation
The Ceruloplasmin and Transferrin System in Cerebrospinal Fluid of Acute Leukemia Patients
Principe, D. D., Menichelli, A., & Colistra, C. (1989) · Acta Paediatrica · doi:10.1111/j.1651-2227.1989.tb11083.x · Cited by 12 · see citing works
A Monoclonal Antibody That Recognizes an Adhesion Molecule Expressed by Certain Cells of Neuroectodermal and Mesenchymal Origin
Mittal, B., & David, S. (1994) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1994.1006 · Cited by 12 · see citing works
Self-citation
[Expression of ceruloplasmin gene in mammalian organs from the data of hybridization analysis with complementary DNA probes].
Шварцман, А. Л., Voronina, O., Gaĭtskhoki, V. S., et al. (1990) · PubMed · Cited by 5 · see citing works
Characterization of the Murine PIG-A Promoter Region High Constitutive PIG-A Gene Expression in Brain
Yu, J. L., & Medof, M. E. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2492 · Cited by 1 · see citing works

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Fauré, J., Lachenal, G., Court, M., Hirrlinger, J., Chatellard-Causse, C., Blot, B., Grange, J., Schoehn, G., Goldberg, Y., Boyer, V., et al. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.12.003 · Cited by 896 · see citing works
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Harris, Z. L., Durley, A. P., Man, T. K., & Gitlin, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10812 · Cited by 568 · see citing works
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Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526 · see citing works
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Patel, B. N., Dunn, R. J., Jeong, S. Y., Zhu, Q., Julien, J.-P., & David, S. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06578.2002 · Cited by 379 · see citing works
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Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377 · see citing works
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De Domenico, I., Ward, D. M., di Patti, M. C. B., Jeong, S. Y., David, S., Musci, G., & Kaplan, J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601735 · Cited by 350 · see citing works
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Hahn, P., Qian, Y., Dentchev, T., Chen, L., Beard, J., Harris, Z. L., & Dunaief, J. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405146101 · Cited by 264 · see citing works
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He, X., Hahn, P., Iacovelli, J., Wong, R., King, C., Bhisitkul, R., Massaro-Giordano, M., & Dunaief, J. L. (2007) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2007.07.004 · Cited by 260 · see citing works
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Thompson, K. J., Shoham, S., & Connor, J. R. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00510-x · Cited by 235 · see citing works
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Dringen, R., Bishop, G. M., Koeppe, M., Dang, T. N., & Robinson, S. R. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9375-0 · Cited by 209 · see citing works
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Patel, B. N., Dunn, R. J., & David, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4305 · Cited by 202 · see citing works
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Authors: Patel, B. N., & David, S.
Affiliations: Montreal General Hospital (CA)
Corresponding author: David, Samuel
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1997-08
Volume: 272
Issue: 32
Pages: 20185-20190
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.272.32.20185
OpenAlex: W2036545911
Cited by: 327
References: 61
Citations by year: 2026: 4 · 2025: 6 · 2024: 5 · 2023: 7 · 2022: 11 · 2021: 13 · 2020: 9 · 2019: 12 · 2018: 15 · 2017: 8 · 2016: 8 · 2015: 10 · 2014: 16 · 2013: 11 · 2012: 11
FWCI: 6.84
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8469 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
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: ceruloplasmin, glycosylphosphatidylinositol anchor, astrocytes, central nervous system, ferroxidase activity, ferrous iron oxidation, copper-binding proteins, aceruloplasminemia, neurodegenerative diseases, blood-brain barrier, free radicals
MeSH terms: Animals, Antibodies, Monoclonal, Astrocytes, Cells, Cultured, Ceruloplasmin, Immunoenzyme Techniques, Peptide Mapping, Tumor Cells, Cultured, Glycosylphosphatidylinositols, Rats

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A Novel Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin Is Expressed by Mammalian Astrocytes

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