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","1640"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Neuroscience"],["dc.bibliographiccitation.lastpage","1650"],["dc.bibliographiccitation.volume","169"],["dc.contributor.author","Weiss, Elisabeth"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Asif, Abdul Rahman"],["dc.contributor.author","Ciesielczyk, Barbara"],["dc.contributor.author","Schmitz, M."],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Behrens, C."],["dc.contributor.author","Zerr, I."],["dc.date.accessioned","2018-11-07T08:39:11Z"],["dc.date.available","2018-11-07T08:39:11Z"],["dc.date.issued","2010"],["dc.description.abstract","The definite physiological role of the cellular prion protein (PrPc) remains elusive. There is ample in vitro and in vivo evidence suggesting a neuroprotective role for PrPc. On the other hand, several in vitro and in vivo studies demonstrated detrimental effects of PrPc overexpression through activation of a p53 pathway. Recently, we reported that transient overexpression of PrPc in human embryonic kidney 293 cells elicits proteome expression changes which point to deregulation of proteins involved in energy metabolism and cellular homeostasis. Here we report proteome expression changes following stable PrPc overexpression in human neuronal SH-SY5Y cells. In total 18 proteins that are involved in diverse biological processes were identified as differentially regulated. The majority of these proteins is involved in cell signaling, cytoskeletal organization and protein folding. Annexin V exhibited a several fold up-regulation following stable PrPc overexpression in SH-SY5Y cells. This finding has been reproduced in alternative, mouse N2a and human SK-N-LO neuroblastoma cell lines transiently overexpressing PrPc. Annexin V plays an important role in maintenance of calcium homeostasis which when disturbed can activate a p53-dependent cell death. Although we did not detect changes in p53 expression between PrPc overexpressing SH-SY5Y and control cells, deregulation of several proteins including annexin V, polyglutamine tract-binding protein-1, spermine synthase and transgelin 2 indicates disrupted cellular equilibrium. We conclude that stable PrPc overexpression in SH-SY5Y cells is sufficient to perturb cellular balance but insufficient to affect p53 expression. (C) 2010 IBRO. Published by Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.neuroscience.2010.06.013"],["dc.identifier.isi","000281050600016"],["dc.identifier.pmid","20547212"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18932"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.relation.issn","0306-4522"],["dc.title","CELLULAR PRION PROTEIN OVEREXPRESSION DISTURBS CELLULAR HOMEOSTASIS IN SH-SY5Y NEUROBLASTOMA CELLS BUT DOES NOT ALTER p53 EXPRESSION: A PROTEOMIC STUDY"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","51"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Alzheimer s Disease"],["dc.bibliographiccitation.lastpage","61"],["dc.bibliographiccitation.volume","37"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Nowak, Martin"],["dc.contributor.author","Carimalo, Julie"],["dc.contributor.author","Cardone, Franco"],["dc.contributor.author","Asif, Abdul R."],["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","2018-11-07T09:29:44Z"],["dc.date.available","2018-11-07T09:29:44Z"],["dc.date.issued","2013"],["dc.description.abstract","Sporadic Creutzfeldt-Jakob disease (sCJD) is characterized by wide clinical and pathological variability, which is mainly influenced by the conformation of the misfolded prion protein (PrPSc) and by methionine and valine polymorphism at codon 129 of the gene encoding PrP. This heterogeneity likely implies differences in the molecular cascades that lead to the development of certain disease phenotypes. Here, we investigated synaptic proteome patterns in two most common sCJD subtypes(MM1and VV2) using 2D DIGE and mass spectrometry. We found that 23 distinct proteins were differentially expressed in at least one sCJD subtype when compared to age-matched controls. The majority of these proteins displayed significant subtype-specific alterations, with only up-regulated glial fibrillary acidic protein and down-regulated spectrin alpha chain in both sCJD subtypes. Differentially expressed proteins found in this study are mainly involved in synaptic structure and activity, mitochondrial function, or calcium metabolism. Moreover, several of them have been already linked to the pathophysiological processes occurring in Alzheimer's disease."],["dc.description.sponsorship","European Commission [PRIORITY KBBE-2007-2-4-06]; EU [01ED1201A]"],["dc.identifier.doi","10.3233/JAD-130455"],["dc.identifier.isi","000323487300007"],["dc.identifier.pmid","23780662"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31114"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Ios Press"],["dc.relation.issn","1387-2877"],["dc.title","Subtype-Specific Synaptic Proteome Alterations in Sporadic Creutzfeldt-Jakob Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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"]]

[["dc.bibliographiccitation.firstpage","5646"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Proteome Research"],["dc.bibliographiccitation.lastpage","5657"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Dieks, Jana"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Carimalo, Julie"],["dc.contributor.author","Heinemann, Uta"],["dc.contributor.author","Streich, Jan-Hendrik"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T08:37:40Z"],["dc.date.available","2018-11-07T08:37:40Z"],["dc.date.issued","2010"],["dc.description.abstract","Cerebrospinal fluid (CSF) contains a dynamic and complex mixture of proteins, which can reflect a physiological and pathological state of the central nervous system. In our present study, we show CSF protein patterns from patients with the two most frequent subtypes of sporadic Creutzfeldt-Jakob disease (sCJD) defined by the codon 129 genotype (MM, MV, and VV) and the protease-resistant form of prion protein (type 1 and type 2). The densitometric analysis of 2D gels showed up-regulation of 27 and down-regulation of 3 proteins in the MM-sCJD as well as the up-regulation of 24 proteins in the VV-sCJD as compared to nondemented control. Almost 40% of sCJD specific regulated proteins in CSF are involved in glucose metabolism, regardless of the codon 129 polymorphism. The increase in CSF levels of lactate dehydrogenase (LDH), glucose-6-phosphate isomerase (G6PI), and fructosebisphosphate aldolase A (ALDOA) were validated on a larger group of sCJD patients including three possible codon 129 polymorphism carriers and three control groups consisting of nondemented, neurological cases as well as patients suffering from Alzheimer's disease or vascular dementia. Subsequently, the abundance of these glycolytic enzymes in the brain as well as their cellular localization were determined. This study demonstrates for the first time the implication of G6PI in prion-induced pathology as well as its cellular translocalization in sCJD. The identification of sCJD-regulated proteins in CSF of living symptomatic patients in our study can broaden our knowledge about pathological processes occurring in sCJD, as they are still not fully understood."],["dc.description.sponsorship","European Commission [SP5A-CT-2007-044438]"],["dc.identifier.doi","10.1021/pr1004604"],["dc.identifier.isi","000283810500014"],["dc.identifier.pmid","20866111"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18590"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1535-3893"],["dc.title","Codon 129 Polymorphism Specific Cerebrospinal Fluid Proteome Pattern in Sporadic Creutzfeldt-Jakob Disease and the Implication of Glycolytic Enzymes in Prion-Induced Pathology"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]