Gawinecka, Joanna

[["dc.bibliographiccitation.firstpage","758"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Journal of neuropathology and experimental neurology"],["dc.bibliographiccitation.lastpage","767"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Wemheuer, Wiebke M."],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.date.accessioned","2015-11-18T10:28:52Z"],["dc.date.accessioned","2021-10-27T13:20:22Z"],["dc.date.available","2015-11-18T10:28:52Z"],["dc.date.available","2021-10-27T13:20:22Z"],["dc.date.issued","2013-08-01"],["dc.description.abstract","In brain biopsies taken from patients with rapidly progressive dementia, the first differential diagnoses to be ruled out are prion diseases. For safe diagnostic processing of tissue and instruments, a rapid, highly sensitive, and specific analysis for prion aggregates is necessary. Here, we examined 16 brain biopsies and brain samples (frontal cortex and cerebellum) from 65 autopsies by Western blot, paraffin-embedded tissue (PET) blot, immunohistochemistry, and the recently described membrane adsorption assay (MAA) for their suitability to detect pathologic prion protein. In our hands, the PET blot method provided the highest sensitivity in prion detection (biopsies, 100%; all autopsy sections, 96.3%), closely followed by the MAA (biopsies, 100%; all autopsy samples, 96%) and Western blot analysis (biopsies, 100%; all autopsy samples, 92%). Conventional immunohistochemistry is the least sensitive method (biopsies, 50%; all autopsy sections, 80%) and also gave 1 false-positive biopsy result. Consequently, our standard diagnostic protocol is to use the MAA as a first step for detecting or excluding a prion disease, followed by the PET blot for the prion deposition pattern, Western blotting for prion typing, and immunohistochemistry for differential diagnoses. With this standard and the availability of unfixed tissue, a diagnosis was possible in all 16 biopsies examined."],["dc.description.sponsorship","VolkswagenStiftung [VWZ2168]; Prionscreen [FP6-2005-SSP-5A]"],["dc.format.extent","19"],["dc.identifier.doi","10.1097/NEN.0b013e31829d2799"],["dc.identifier.isi","000330383600005"],["dc.identifier.pmid","23860029"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12445"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91960"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.issn","1554-6578"],["dc.relation.issn","0022-3069"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.mesh","Alzheimer Disease"],["dc.subject.mesh","Biopsy"],["dc.subject.mesh","Brain"],["dc.subject.mesh","Cell Membrane"],["dc.subject.mesh","Dementia"],["dc.subject.mesh","Female"],["dc.subject.mesh","Filtration"],["dc.subject.mesh","Frontotemporal Lobar Degeneration"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Male"],["dc.subject.mesh","Parkinson Disease"],["dc.subject.mesh","Positron-Emission Tomography"],["dc.subject.mesh","PrPSc Proteins"],["dc.subject.mesh","Prion Diseases"],["dc.subject.mesh","Prions"],["dc.subject.mesh","Sensitivity and Specificity"],["dc.title","Filtration of protein aggregates increases the accuracy for diagnosing prion diseases in brain biopsies."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2566"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","American Journal Of Pathology"],["dc.bibliographiccitation.lastpage","2573"],["dc.bibliographiccitation.volume","175"],["dc.contributor.author","Wemheuer, Wiebke M."],["dc.contributor.author","Benestad, Sylvie L."],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Schulze-Sturm, Ulf"],["dc.contributor.author","Wemheuer, Wilhelm E."],["dc.contributor.author","Hahmann, Uwe"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Schuetz, Ekkehard"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Brenig, Bertram"],["dc.contributor.author","Bratberg, Bjorn"],["dc.contributor.author","Andreoletti, Olivier"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.date.accessioned","2018-11-07T11:21:14Z"],["dc.date.available","2018-11-07T11:21:14Z"],["dc.date.issued","2009"],["dc.description.abstract","Transmissible spongiform encephalopathies such as scrapie in sheep, Creutzfeldt-Jakob disease (CJD) in humans, and bovine sporadic encephalopathy in cattle are characterized by the accumulation of a mis-folded protein: the pathological prion protein. Ever since bovine sporadic encephalopathy was discovered as the likely cause of the new variant of CJD in humans, parallels between human and animal transmissible spongiform encephalopathies must be viewed under the aspect of a disease risk for humans. In our study we have compared prion characteristics of different forms of sheep scrapie with those of different phenotypes of sporadic CJD. The disease characteristics of sporadic CJD depend considerably on the prion type 1 or 2. Our results show that there are obvious parallels between sporadic CJD type 1 and the so-called atypical/Nor98 scrapie. These parelleles apply to the deposition form of pathological prion protein in the brain, detected by the paraffm-embedded-tissue blot and the prion aggregate stability with regard to denaturation by the chaotropic salt guanidine hydrochloride. The same applies to sporadic CJD type 2 and classical scrapie. The observed parallels between types of sporadic CJD and types of sheep scrapie demonstrate that distinct groups of prion disease exist in different species. This should be taken into consideration when discussing interspecies transmission. (Am J Pathol 2009, 175:2566-2573 DOI: 10.2353/ajpath.2009.090623"],["dc.description.sponsorship","VolkswagenStiftung [ZN 1294, ZN2168]"],["dc.identifier.doi","10.2353/ajpath.2009.090623"],["dc.identifier.isi","000272600600031"],["dc.identifier.pmid","19850886"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10435"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55724"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","1525-2191"],["dc.relation.issn","0002-9440"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Similarities between Forms of Sheep Scrapie and Creutzfeldt-Jakob Disease Are Encoded by Distinct Prion Types"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3610"],["dc.bibliographiccitation.issue","23-24"],["dc.bibliographiccitation.journal","PROTEOMICS"],["dc.bibliographiccitation.lastpage","3620"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Cardone, Franco"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","De Pascalis, Angela"],["dc.contributor.author","Wemheuer, Wiebke M."],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Pocchiari, Maurizio"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:02:39Z"],["dc.date.available","2018-11-07T09:02:39Z"],["dc.date.issued","2012"],["dc.description.abstract","Sporadic CreutzfeldtJakob disease (sCJD) is characterized by wide clinical and pathological variability, which is mainly influenced by the conformation of the misfolded prion protein, and by the methionine and valine polymorphism at codon 129 of the prion protein gene. This heterogeneity likely implies differences in the molecular cascade that leads to the development of certain disease phenotypes. In this study, we investigated the proteome of the frontal cortex of patients with the two most common sCJD subtypes (MM1 and VV2) using 2D-DIGE and MS. Analysis of 2D maps revealed that 46 proteins are differentially expressed in the sCJD. Common differential expression was detected for seven proteins, four showed opposite direction of differential expression, and the remaining ones displayed subtype-specific alteration. The highest number of differentially expressed proteins was associated with signal transduction and neuronal activity. Moreover, functional groups of proteins involved in cell cycle and death, as well as in structure and motility included subtype-specific expressed proteins exclusively. The expression of Rab GDP dissociation inhibitor alpha, which regulates Rab3a-mediated neurotransmitter release, was affected in both sCJD subtypes that were analyzed. Therefore, we also investigated as to whether Rab3a recycling is altered. Indeed, we found an accumulation of the membrane-associated form, thus the active one, which suggests that dysfunction of the Rab3a-mediated exocytosis might be implicated in sCJD pathology."],["dc.description.sponsorship","European Commission [222887, NeuroPrion FOOD-CT-2004-506579]"],["dc.identifier.doi","10.1002/pmic.201200201"],["dc.identifier.isi","000312650100016"],["dc.identifier.pmid","23070823"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9494"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24734"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1615-9853"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Sporadic Creutzfeldt-Jakob disease subtype-specific alterations of the brain proteome: Impact on Rab3a recycling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]