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dc.contributor.authorKristinsson, Jakob
dc.contributor.authorSnaedal, Jón
dc.contributor.authorTórsdóttir, Gudlaug
dc.contributor.authorJóhannesson, Torkell
dc.date.accessioned2013-08-29T11:13:19Z
dc.date.available2013-08-29T11:13:19Z
dc.date.issued2012
dc.date.submitted2013-08-29
dc.identifier.citationNeuropsychiatr Dis Treat 2012, 8:515-21en_GB
dc.identifier.issn1178-2021
dc.identifier.pmid23144563
dc.identifier.doi10.2147/NDT.S34729
dc.identifier.urihttp://hdl.handle.net/2336/300230
dc.descriptionTo access publisher full text version of this article. Please click on the hyperlink in Additional Links field.en_GB
dc.description.abstractCeruloplasmin (Cp) concentration and oxidative activity in serum are lowered in Parkinson's disease (PD). In most PD patients, iron increases in the substantia nigra in the midbrain. In PD, the low Cp concentration and activity in serum and the high iron amounts in the substantia nigra appears to be correlated. An hereditary background is common in PD and variations in the Cp gene that have been found in PD are associated with high iron levels in the substantia nigra. Variations in Cp synthesis and in the incorporation of copper into the Cp molecule are essential features of PD. In Alzheimer's disease (AD), the Cp activity in serum is lowered but not the concentration, except in the advanced stages of the disease. Generally, iron is not increased in the AD brain. In the AD brain, iron accumulates in neuritic plaques and in neurofibrillary tangles. There is also increased risk of iron-mediated tissue damage, which may possibly be counteracted by Cp. At the same time, the AD brain is short in copper, which presumably results in the deficient activity of many copper enzymes in the brain, in addition to Cp. Lowered Cp activity in serum most likely stems from lessened incorporation of copper in the Cp molecule and similar incorporation defects might also apply to other copper enzymes in AD.
dc.description.sponsorshipScientific Fund of Helga Scientific Fund of Sigurlidi Kristjansson Scientific Fund of the University of Icelanden_GB
dc.language.isoenen
dc.publisherDove Medical Pressen_GB
dc.relation.urlhttp://dx.doi.org/10.2147/NDT.S34729en_GB
dc.relation.urlhttp://www.dovepress.com/ceruloplasmin-and-iron-in-alzheimerrsquos-disease-and-parkinsonrsquos--peer-reviewed-article-NDTen_GB
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3493298/en_GB
dc.rightsArchived with thanks to Neuropsychiatric disease and treatmenten_GB
dc.titleCeruloplasmin and iron in Alzheimer's disease and Parkinson's disease: a synopsis of recent studies.en
dc.typeArticleen
dc.contributor.departmentDepartment of Pharmacology and Toxicology, University of Iceland, Reykjavik, Iceland.en_GB
dc.identifier.journalNeuropsychiatric disease and treatmenten_GB
dc.rights.accessOpen Access - Opinn aðganguren
html.description.abstractCeruloplasmin (Cp) concentration and oxidative activity in serum are lowered in Parkinson's disease (PD). In most PD patients, iron increases in the substantia nigra in the midbrain. In PD, the low Cp concentration and activity in serum and the high iron amounts in the substantia nigra appears to be correlated. An hereditary background is common in PD and variations in the Cp gene that have been found in PD are associated with high iron levels in the substantia nigra. Variations in Cp synthesis and in the incorporation of copper into the Cp molecule are essential features of PD. In Alzheimer's disease (AD), the Cp activity in serum is lowered but not the concentration, except in the advanced stages of the disease. Generally, iron is not increased in the AD brain. In the AD brain, iron accumulates in neuritic plaques and in neurofibrillary tangles. There is also increased risk of iron-mediated tissue damage, which may possibly be counteracted by Cp. At the same time, the AD brain is short in copper, which presumably results in the deficient activity of many copper enzymes in the brain, in addition to Cp. Lowered Cp activity in serum most likely stems from lessened incorporation of copper in the Cp molecule and similar incorporation defects might also apply to other copper enzymes in AD.


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