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Ceruloplasmin, ferroxidase
The protein encoded by this gene is a metalloprotein that binds most of the copper in plasma and is involved in the peroxidation of Fe(II)transferrin to Fe(III) transferrin. Mutations in this gene cause aceruloplasminemia, which results in iron accumulation and tissue damage, and is associated with diabetes and neurologic abnormalities. Two transcript variants, one protein-coding and the other not protein-coding, have been found for this gene. [provided by RefSeq, Feb 2012] (from NCBI)
Top mentioned proteins: CAN, ACID, HAD, Transferrin, V1a
Papers on Ceruloplasmin
Iron metabolism and related genetic diseases: A cleared land, keeping mysteries.
Loréal et al., Rennes, France. In J Hepatol, Feb 2016
Physiologically, the liver synthesizes transferrin, in charge of blood iron transport; ceruloplasmin, acting through its ferroxidase activity; and hepcidin, the master regulator of systemic iron.
Brain iron accumulation affects myelin-related molecular systems implicated in a rare neurogenetic disease family with neuropsychiatric features.
Milward et al., Newcastle, Australia. In Mol Psychiatry, Feb 2016
Apart from the ferroxidase ceruloplasmin, all are involved in myelin homeostasis; 16 other myelin-related genes also showed reduced expression (P<0.05),
First comparative characterization of three distinct ferritin subunits from a teleost: Evidence for immune-responsive mRNA expression and iron depriving activity of seahorse (Hippocampus abdominalis) ferritins.
Lee et al., Cheju, South Korea. In Fish Shellfish Immunol, Jan 2016
Recombinantly expressed HaFer proteins demonstrated detectable in vivo iron sequestrating (ferroxidase) activity, consistent with their putative iron binding capability.
Expression of Iron-Related Proteins at the Neurovascular Unit Supports Reduction and Reoxidation of Iron for Transport Through the Blood-Brain Barrier.
Moos et al., Aalborg, Denmark. In Mol Neurobiol, Jan 2016
The expression of soluble ceruloplasmin by brain endothelial cells, pericytes, and astrocytes that together form the neurovascular unit (NVU) provides the ferroxidase activity necessary to reoxidize ferrous iron once released inside the brain.
Ferroxidase-Mediated Iron Oxide Biomineralization: Novel Pathways to Multifunctional Nanoparticles.
Okuda et al., Leioa, Spain. In Trends Biochem Sci, Jan 2016
The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers.
[Testing the influence of lipid laden and iron-overloading on ceruloplasmin expression in RAW 264.7 cells].
Qiao et al., Nanjing, China. In Zhonghua Yi Xue Za Zhi, Sep 2015
OBJECTIVE: To investigate whether the treatment of oxidized low density lipoprotein (ox-LDL) could reduce ceruloplasmin (Cp) expression and then, influence iron efflux in macrophages.
Insights into molecular mechanisms of disease in neurodegeneration with brain iron accumulation: unifying theories.
Wray et al., London, United Kingdom. In Neuropathol Appl Neurobiol, May 2015
Mutations in 10 genes have been associated with NBIA that include Ceruloplasmin (Cp) and ferritin light chain (FTL), both directly involved in iron homeostasis, as well as Pantothenate Kinase 2 (PANK2), Phospholipase A2 group 6 (PLA2G6), Fatty acid hydroxylase 2 (FA2H), Coenzyme A synthase (COASY), C19orf12, WDR45 and DCAF17 (C2orf37).
Ceruloplasmin and Hypoferremia: Studies in Burn and Non-Burn Trauma Patients.
Atkins et al., Houston, United States. In Antioxidants (basel), 2014
Ceruloplasmin (Cp), an acute phase reactant protein that can convert ferrous iron to its less reactive ferric form facilitating binding to ferritin, has ferroxidase activity that is important to iron handling.
Biochemical, Biomedical and Metabolic Aspects of Imidazole-Containing Dipeptides with the Inherent Complexity to Neurodegenerative Diseases and Various States of Mental Well-Being: A Challenging Correction and Neurotherapeutic Pharmaceutical Biotechnology for Treating Cognitive Deficits, Depression and Intellectual Disabilities.
Babizhayev, Moscow, Russia. In Curr Pharm Biotechnol, 2013
Carnosine serves as a physiological buffering agent and a metal ion (e.g., zinc and copper) chelator, endowed with ferroxidase type activity; possess anti-aging functions, and free-radical scavenging activity, is capable of delaying senescence and extending the life-span of cultured human fibroblasts; is able to kill transformed cells and protect cells against aldehydes and amyloid peptide fragment.
Molecular mediators governing iron-copper interactions.
Collins et al., Gainesville, United States. In Annu Rev Nutr, 2013
Copper accumulation and/or redistribution within enterocytes may influence iron transport, and high hepatic copper may enhance biosynthesis of a circulating ferroxidase, which potentiates iron release from stores.
Solution and solid state NMR approaches to draw iron pathways in the ferritin nanocage.
Turano et al., Sesto Fiorentino, Italy. In Acc Chem Res, 2013
Through this approach, we could identify ferric dimers at the ferroxidase site and on their pathway towards the nanocage.
Immunoreactive hephaestin and ferroxidase activity are present in the cytosolic fraction of rat enterocytes.
Collins et al., Gainesville, United States. In Biometals, 2012
FOX activity was present in rat cytosol, and was partly inhibited by anti-Heph antibody.
Increased copper levels in in vitro and in vivo models of Niemann-Pick C disease.
Zanlungo et al., Santiago, Chile. In Biometals, 2012
Data found an increase in ceruloplasmin levels in the plasma of Npc1 -/- mice compared to Npc1 +/+ mice, and this increase was statistically significant (*p < 0.05).
Ferroxidase hephaestin's cell-autonomous role in the retinal pigment epithelium.
Dunaief et al., Philadelphia, United States. In Am J Pathol, 2012
Cp and Heph are necessary for iron export from the retina but are not essential for iron import into the retina.
[The investigation of alpha1-antitripsin, orozomukoid and ceruloplasmin in peripheral blood and oral fluid. Paradontitis is one of more risk factors of cardiovascular diseases].
Zubarev et al., In Patol Fiziol Eksp Ter, 2012
change of the maintenance of three acute phase proteins: ceruloplasmin, alpha1-antitripsin and orosomucoid in an oral fluid and blood plasma at paradontitis and myocardial infarction
Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export.
Bush et al., Melbourne, Australia. In Nat Med, 2012
Amyloid precursor protein (APP) ferroxidase activity couples with surface ferroportin to export iron, but its activity is inhibited in Alzheimer's disease, thereby causing neuronal iron accumulation.
Ceruloplasmin deficiency results in an anxiety phenotype involving deficits in hippocampal iron, serotonin, and BDNF.
Mattson et al., Baltimore, United States. In J Neurochem, 2012
levels of 5HT and norepinephrine and the expression of BDNF and its receptor trkB, are significantly reduced in the hippocampus of ceruloplasmin knockout mice
The role of ubiquitination in hepcidin-independent and hepcidin-dependent degradation of ferroportin.
Kaplan et al., Salt Lake City, United States. In Cell Metab, 2011
Nedd4-2 is also required for internalization of Fpn in the absence of ferroxidase activity as well as for the entry of hepcidin-induced Fpn into the multivesicular body.
Iron-export ferroxidase activity of β-amyloid precursor protein is inhibited by zinc in Alzheimer's disease.
Bush et al., Melbourne, Australia. In Cell, 2010
We found that the AD β-amyloid protein precursor (APP) possesses ferroxidase activity mediated by a conserved H-ferritin-like active site, which is inhibited specifically by Zn(2+).
Ferritin is used for iron storage in bloom-forming marine pennate diatoms.
Armbrust et al., Seattle, United States. In Nature, 2009
The crystal structure and functional assays of recombinant ferritin derived from Pseudo-nitzschia multiseries reveal a maxi-ferritin that exhibits ferroxidase activity and binds iron.
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