Carboni, Eleonora

[["dc.bibliographiccitation.artnumber","jnc.15461"],["dc.bibliographiccitation.firstpage","554"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","573"],["dc.bibliographiccitation.volume","159"],["dc.contributor.affiliation","Dauer née Joppe, Karina; 1Department of Neurology University Medical Center Goettingen Goettingen Germany"],["dc.contributor.affiliation","Caldi Gomes, Lucas; 1Department of Neurology University Medical Center Goettingen Goettingen Germany"],["dc.contributor.affiliation","Zhang, Shuyu; 3Department of Neurology School of Medicine University Hospital rechts der IsarTechnical University of Munich Munich Germany"],["dc.contributor.affiliation","Parvaz, Mojan; 3Department of Neurology School of Medicine University Hospital rechts der IsarTechnical University of Munich Munich Germany"],["dc.contributor.affiliation","Carboni, Eleonora; 1Department of Neurology University Medical Center Goettingen Goettingen Germany"],["dc.contributor.affiliation","Roser, Anna‐Elisa; 1Department of Neurology University Medical Center Goettingen Goettingen Germany"],["dc.contributor.affiliation","El DeBakey, Hazem; 4Department of Neurology University Hospital of Wuerzburg Wuerzburg Germany"],["dc.contributor.affiliation","Bähr, Mathias; 1Department of Neurology University Medical Center Goettingen Goettingen Germany"],["dc.contributor.affiliation","Vogel‐Mikuš, Katarina; 6Biotechnical faculty University of Ljubljana Ljubljana Slovenia"],["dc.contributor.affiliation","Wang Ip, Chi; 4Department of Neurology University Hospital of Wuerzburg Wuerzburg Germany"],["dc.contributor.affiliation","Becker, Stefan; 8Department of NMR Based Structural BiologyMax Planck Institute for Biophysical Chemistry Goettingen Germany"],["dc.contributor.affiliation","Zweckstetter, Markus; 1Department of Neurology University Medical Center Goettingen Goettingen Germany"],["dc.contributor.author","Tatenhorst, Lars"],["dc.contributor.author","Caldi Gomes, Lucas"],["dc.contributor.author","Zhang, Shuyu"],["dc.contributor.author","Parvaz, Mojan"],["dc.contributor.author","Carboni, Eleonora"],["dc.contributor.author","Roser, Anna‐Elisa"],["dc.contributor.author","El DeBakey, Hazem"],["dc.contributor.author","Bähr, Mathias"],["dc.contributor.author","Lingor, Paul"],["dc.contributor.author","Dauer née Joppe, Karina"],["dc.contributor.author","Vogel‐Mikuš, Katarina"],["dc.contributor.author","Wang Ip, Chi"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2021-07-05T14:57:43Z"],["dc.date.available","2021-07-05T14:57:43Z"],["dc.date.issued","2021"],["dc.date.updated","2022-03-21T09:42:08Z"],["dc.description.abstract","Abstract Regional iron accumulation and α‐synuclein (α‐syn) spreading pathology within the central nervous system are common pathological findings in Parkinson's disease (PD). Whereas iron is known to bind to α‐syn, facilitating its aggregation and regulating α‐syn expression, it remains unclear if and how iron also modulates α‐syn spreading. To elucidate the influence of iron on the propagation of α‐syn pathology, we investigated α‐syn spreading after stereotactic injection of α‐syn preformed fibrils (PFFs) into the striatum of mouse brains after neonatal brain iron enrichment. C57Bl/6J mouse pups received oral gavage with 60, 120, or 240 mg/kg carbonyl iron or vehicle between postnatal days 10 and 17. At 12 weeks of age, intrastriatal injections of 5‐µg PFFs were performed to induce seeding of α‐syn aggregates. At 90 days post‐injection, PFFs‐injected mice displayed long‐term memory deficits, without affection of motor behavior. Interestingly, quantification of α‐syn phosphorylated at S129 showed reduced α‐syn pathology and attenuated spreading to connectome‐specific brain regions after brain iron enrichment. Furthermore, PFFs injection caused intrastriatal microglia accumulation, which was alleviated by iron in a dose‐dependent way. In primary cortical neurons in a microfluidic chamber model in vitro, iron application did not alter trans‐synaptic α‐syn propagation, possibly indicating an involvement of non‐neuronal cells in this process. Our study suggests that α‐syn PFFs may induce cognitive deficits in mice independent of iron. However, a redistribution of α‐syn aggregate pathology and reduction of striatal microglia accumulation in the mouse brain may be mediated via iron‐induced alterations of the brain connectome. image"],["dc.description.abstract","Brain iron accumulation and α‐synuclein (α‐syn) spreading pathology are common pathological findings in Parkinson's disease. To elucidate the influence of iron on α‐syn propagation, we investigated α‐syn spreading after stereotactic injection of α‐syn preformed fibrils (PFFs) into the striatum of C57Bl/6 mice after neonatal brain iron enrichment. 90 days post‐injection, PFFs injected mice displayed memory deficits, reduced α‐syn pathology and spreading to connectome‐specific regions after brain iron enrichment. Our study suggests that α‐syn PFFs may induce cognitive deficits in mice independent of iron. However, a redistribution of α‐syn pathology may be mediated via iron‐induced alterations of the brain connectome. image"],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship","MPI"],["dc.identifier.doi","10.1111/jnc.15461"],["dc.identifier.pmid","34176164"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87716"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/315"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-441"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1471-4159"],["dc.relation.issn","0022-3042"],["dc.relation.workinggroup","RG Bähr (Neurobiological Research Laboratory)"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made."],["dc.title","Brain iron enrichment attenuates α‐synuclein spreading after injection of preformed fibrils"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","309"],["dc.bibliographiccitation.issue","2-3"],["dc.bibliographiccitation.journal","NeuroMolecular Medicine"],["dc.bibliographiccitation.lastpage","321"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Carboni, Eleonora"],["dc.contributor.author","Tatenhorst, Lars"],["dc.contributor.author","Tönges, Lars"],["dc.contributor.author","Barski, Elisabeth"],["dc.contributor.author","Dambeck, Vivian"],["dc.contributor.author","Bähr, Mathias"],["dc.contributor.author","Lingor, Paul"],["dc.date.accessioned","2018-04-23T11:49:32Z"],["dc.date.available","2018-04-23T11:49:32Z"],["dc.date.issued","2017"],["dc.description.abstract","Parkinson’s disease (PD) is the most common neurodegenerative movement disorder, and its causes remain unknown. A major hallmark of the disease is the increasing presence of aggregated alpha-synuclein (aSyn). Furthermore, there is a solid consensus on iron (Fe) accumulation in several regions of PD brains during disease progression. In our study, we focused on the interaction of Fe and aggregating aSyn in vivo in a transgenic mouse model overexpressing human aSyn bearing the A53T mutation (prnp.aSyn.A53T). We utilized a neonatal iron-feeding model to exacerbate the motor phenotype of the transgenic mouse model. Beginning from day 100, mice were treated with deferiprone (DFP), a ferric chelator that is able to cross the blood–brain barrier and is currently used in clinics as treatment for hemosiderosis. Our paradigm resulted in an impairment of the learning abilities in the rotarod task and the novel object recognition test. DFP treatment significantly improved the performance in both tasks. Although this was not accompanied by alterations in aSyn aggregation, our results support DFP as possible therapeutic option in PD."],["dc.identifier.doi","10.1007/s12017-017-8447-9"],["dc.identifier.gro","3142070"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13724"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","1535-1084"],["dc.title","Deferiprone Rescues Behavioral Deficits Induced by Mild Iron Exposure in a Mouse Model of Alpha-Synuclein Aggregation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1769"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","ACS Chemical Neuroscience"],["dc.bibliographiccitation.lastpage","1779"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Dučić, Tanja"],["dc.contributor.author","Carboni, Eleonora"],["dc.contributor.author","Lai, Barry"],["dc.contributor.author","Chen, Si"],["dc.contributor.author","Michalke, Bernhard"],["dc.contributor.author","Lazaro, Diana F."],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Bähr, Mathias"],["dc.contributor.author","Barski, Elisabeth"],["dc.contributor.author","Lingor, Paul"],["dc.date.accessioned","2017-09-07T11:43:30Z"],["dc.date.available","2017-09-07T11:43:30Z"],["dc.date.issued","2015"],["dc.description.abstract","Manganese (Mn) may foster aggregation of alpha-synuclein (alpha Syn) contributing to the pathogenesis of PD. Here, we examined the influence of aSyn overexpression on distribution and oxidation states of Mn in frozen-hydrated primary midbrain neurons (PMNs) by synchrotron-based Xray fluorescence (XRF) and X-ray absorption near edge structure spectroscopy (XANES). Overexpression of aSyn increased intracellular Mn levels, whereas levels of Ca, Zn, K, P, and S were significantly decreased. Mn oxidation states were not altered. A strong correlation between Cu-/Mn-levels as well as Fe-/Mn-levels was observed in alpha Syn-overexpressing cells. Subcellular resolution revealed a punctate or filament-like perinuclear and neuritic distribution of Mn, which resembled the expression of DMT1 and MnSOD. While overexpression of aSyn did not significantly alter the expression patterns of the most-expressed Mn transport proteins (DMT1, VGCC, Fpn1), it attenuated the Mn release from Mn-treated neurons. Thus, these data suggest that aSyn may act as an intracellular Mn store. In total, neurotoxicity in PD could be mediated via regulation of transition metal levels and the metal-binding capacity of aSyn, which could represent a promising therapeutic target for this neurodegenerative disorder."],["dc.identifier.doi","10.1021/acschemneuro.5b00093"],["dc.identifier.gro","3141816"],["dc.identifier.isi","000363435300012"],["dc.identifier.pmid","26284970"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1390"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1948-7193"],["dc.title","Alpha-Synuclein Regulates Neuronal Levels of Manganese and Calcium"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]