Ramljak, Sanja

[["dc.bibliographiccitation.firstpage","355"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Neurology"],["dc.bibliographiccitation.lastpage","363"],["dc.bibliographiccitation.volume","256"],["dc.contributor.author","Meissner, Bettina"],["dc.contributor.author","Kallenberg, Kai"],["dc.contributor.author","Sanchez-Juan, Pascual"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Krasnianski, Anna"],["dc.contributor.author","Heinemann, U."],["dc.contributor.author","Eigenbrod, Sabina"],["dc.contributor.author","Gelpi, Elena"],["dc.contributor.author","Barsic, B."],["dc.contributor.author","Kretzschmar, Hans A."],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Knauth, Michael"],["dc.contributor.author","Zerr, I."],["dc.date.accessioned","2018-11-07T08:32:16Z"],["dc.date.available","2018-11-07T08:32:16Z"],["dc.date.issued","2009"],["dc.description.abstract","Iatrogenic Creutzfeldt-Jakob disease (iCJD) is mainly associated with dura mater (DM) grafts and administration of human growth hormones (hGH). Data on disease course in DM-CJD are limited. We describe the clinical and diagnostic findings in this patient group with special emphasis on MRI signal alterations. Ten DM-CJD patients were studied for their clinical symptoms and diagnostic findings. The MRIs were evaluated for signal increase of the cortical and subcortical structures. DM-CJD patients had a median incubation time of 18 years and median disease duration of 7 months. The majority of patients were MM homozygous at codon 129 of the prion protein gene (PRNP) and presented with gait ataxia and psychiatric symptoms. No correlation between the graft site and the initial disease course was found. The MRI showed cortical and basal ganglia signal increase each in eight out of ten patients and thalamic hyperintensity in five out of ten cases. Of interest, patients with thalamic signal increase were homozygous for methionine. The MRI findings in DM-CJD largely resemble those seen in sporadic CJD, as the cortex and basal ganglia are mainly affected."],["dc.identifier.doi","10.1007/s00415-009-0026-z"],["dc.identifier.isi","000265732800008"],["dc.identifier.pmid","19159063"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6742"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17302"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Heidelberg"],["dc.relation.issn","0340-5354"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","MRI and clinical syndrome in dura materrelated Creutzfeldt-Jakob disease"],["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","1566"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["dc.contributor.affiliation","Ramljak, Sanja; \t\t \r\n\t\t Digital Diagnostics AG, 55129 Mainz, Germany, sr@digid.com"],["dc.contributor.affiliation","Schmitz, Matthias; \t\t \r\n\t\t Department of Neurology, University Medicine Goettingen and The German Center for Neurodegenerative Diseases (DZNE), 37075 Goettingen, Germany, matthias.schmitz@med.uni-goettingen.de"],["dc.contributor.affiliation","Repond, Cendrine; \t\t \r\n\t\t Département de Physiologie, Université de Lausanne, 1005 Lausanne, Switzerland, Cendrine.Repond@unil.ch"],["dc.contributor.affiliation","Zerr, Inga; \t\t \r\n\t\t Department of Neurology, University Medicine Goettingen and The German Center for Neurodegenerative Diseases (DZNE), 37075 Goettingen, Germany, ingazerr@med.uni-goettingen.de"],["dc.contributor.affiliation","Pellerin, Luc; \t\t \r\n\t\t Département de Physiologie, Université de Lausanne, 1005 Lausanne, Switzerland, luc.pellerin@univ-poitiers.fr\t\t \r\n\t\t Centre de Résonance Magnétique des Systèmes Biologiques, UMR5536 CNRS, LabEx TRAIL-IBIO, Université de Bordeaux, 33760 Bordeaux CEDEX, France, luc.pellerin@univ-poitiers.fr"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Repond, Cendrine"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Pellerin, Luc"],["dc.date.accessioned","2021-06-01T10:48:47Z"],["dc.date.available","2021-06-01T10:48:47Z"],["dc.date.issued","2021"],["dc.date.updated","2022-09-06T18:21:55Z"],["dc.description.abstract","The effect of a cellular prion protein (PrPc) deficiency on neuroenergetics was primarily analyzed via surveying the expression of genes specifically involved in lactate/pyruvate metabolism, such as monocarboxylate transporters (MCT1, MCT2, MCT4). The aim of the present study was to elucidate a potential involvement of PrPc in the regulation of energy metabolism in different brain regions. By using quantitative real-time polymerase chain reaction (qRT-PCR), we observed a marked reduction in MCT1 mRNA expression in the cortex of symptomatic Zürich I Prnp−/− mice, as compared to their wild-type (WT) counterparts. MCT1 downregulation in the cortex was accompanied with significantly decreased expression of the MCT1 functional interplayer, the Na+/K+ ATPase α2 subunit. Conversely, the MCT1 mRNA level was significantly raised in the cerebellum of Prnp−/− vs. WT control group, without a substantial change in the Na+/K+ ATPase α2 subunit expression. To validate the observed mRNA findings, we confirmed the observed change in MCT1 mRNA expression level in the cortex at the protein level. MCT4, highly expressed in tissues that rely on glycolysis as an energy source, exhibited a significant reduction in the hippocampus of Prnp−/− vs. WT mice. The present study demonstrates that a lack of PrPc leads to altered MCT1 and MCT4 mRNA/protein expression in different brain regions of Prnp−/− vs. WT mice. Our findings provide evidence that PrPc might affect the monocarboxylate intercellular transport, which needs to be confirmed in further studies."],["dc.description.sponsorship","IDEX"],["dc.identifier.doi","10.3390/ijms22041566"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86055"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1422-0067"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Altered mRNA and Protein Expression of Monocarboxylate Transporter MCT1 in the Cerebral Cortex and Cerebellum of Prion Protein Knockout Mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5370"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Journal of Proteome Research"],["dc.bibliographiccitation.lastpage","5382"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Schumacher, Julia"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Schaffrath, Michael"],["dc.contributor.author","Zischler, Hans"],["dc.contributor.author","Herlyn, Holger"],["dc.date.accessioned","2018-11-07T09:17:03Z"],["dc.date.available","2018-11-07T09:17:03Z"],["dc.date.issued","2013"],["dc.description.abstract","We investigated possible associations between sequence evolution of mammalian sperm proteins and their phosphorylation status in humans. As a reference, spermatozoa from three normozoospermic men were analyzed combining two-dimensional gel electrophoresis, immuno-blotting, and mass spectrometry. We identified 99 sperm proteins (thereof 42 newly described) and determined the phosphorylation status for most of them. Sequence evolution was studied across six mammalian species using nonsynonymous/synonymous rate ratios (dN/dS) and amino acid distances. Site-specific purifying selection was assessed employing average ratios of evolutionary rates at phosphorylated versus nonphosphorylated amino acids (a). According to our data, mammalian sperm proteins do not show statistically significant sequence conservation difference, no matter if the human ortholog is a phosphoprotein with or without tyrosine (Y) phosphorylation. In contrast, overall phosphorylation of human sperm proteins, i.e., phosphorylation at serine (S), threonine (T), and/or Y residues, associates with above-average conservation of sequences. Complementary investigations suggest that numerous protein-protein interactants constrain sequence evolution of sperm phosphoproteins. Although our findings reject a special relevance of Y phosphorylation for sperm functioning, they still indicate that overall phosphorylation substantially contributes to proper functioning of sperm proteins. Hence, phosphorylated sperm proteins might be considered as prime candidates for diagnosis and treatment of reduced male fertility."],["dc.identifier.doi","10.1021/pr400228c"],["dc.identifier.isi","000328231300003"],["dc.identifier.pmid","23919900"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28074"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1535-3907"],["dc.relation.issn","1535-3893"],["dc.title","Evolutionary Conservation of Mammalian Sperm Proteins Associates with Overall, not Tyrosine, Phosphorylation in Human Spermatozoa"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","129"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Protein Expression and Purification"],["dc.bibliographiccitation.lastpage","136"],["dc.bibliographiccitation.volume","70"],["dc.contributor.author","Heinig, Lars"],["dc.contributor.author","Mueller, Daniel A."],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Holznagel, Edgar"],["dc.contributor.author","Stuke, Andreas W."],["dc.date.accessioned","2022-10-06T13:33:22Z"],["dc.date.available","2022-10-06T13:33:22Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1016/j.pep.2009.09.015"],["dc.identifier.pii","S104659280900240X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115615"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.issn","1046-5928"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Inducible expression of chimpanzee prion protein (PrP) in murine PrP knock-out cells"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","292"],["dc.bibliographiccitation.journal","Frontiers in Cellular Neuroscience"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Herlyn, Holger"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T10:04:26Z"],["dc.date.available","2018-11-07T10:04:26Z"],["dc.date.issued","2016"],["dc.description.abstract","The cellular prion protein (PrPc) and hypoxia appear to be tightly intertwined. Beneficial effects of PrPc on neuronal survival under hypoxic conditions such as focal cerebral ischemia are strongly supported. Conversely, increasing evidence indicates detrimental effects of increased PrPc expression on cancer progression, another condition accompanied by low oxygen tensions. A switch between anaerobic and aerobic metabolism characterizes both conditions. A cellular process that might unite both is glycolysis. Putative role of PrPc in stimulation of glycolysis in times of need is indeed thought provoking. A significance of astrocytic PrPc expression for neuronal survival under hypoxic conditions and possible association of PrPc with the astrocyte-neuron lactate shuttle is considered. We posit PrPc-induced lactate production via transactivation of lactate dehydrogenase A by hypoxia inducible factor 1 alpha as an important factor for survival of both neurons and tumor cells in hypoxic microenvironment. Concomitantly, we discuss a cross-talk between Wnt/beta-catenin and PI3K/Akt signaling pathways in executing PrPc-induced activation of glycolysis. Finally, we would like to emphasize that we see a great potential in joining expertise from both fields, neuroscience and cancer research in revealing the mechanisms underlying hypoxia-related pathologies. PrPc may prove focal point for future research."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.3389/fncel.2016.00292"],["dc.identifier.isi","000390160200001"],["dc.identifier.pmid","28066187"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14019"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38694"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Frontiers Media Sa"],["dc.relation.issn","1662-5102"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Cellular Prion Protein (PrPc) and Hypoxia: True to Each Other in Good Times and in Bad, in Sickness, and in Health"],["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.artnumber","e2557"],["dc.bibliographiccitation.journal","Cell Death and Disease"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Behrens, Christina"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Asif, Abdul R."],["dc.date.accessioned","2018-11-07T10:29:07Z"],["dc.date.available","2018-11-07T10:29:07Z"],["dc.date.issued","2017"],["dc.description.abstract","Anti-apoptotic properties of physiological and elevated levels of the cellular prion protein (PrPc) under stress conditions are well documented. Yet, detrimental effects of elevated PrPc levels under stress conditions, such as exposure to staurosporine (STS) have also been described. In the present study, we focused on discerning early apoptotic STS-induced proteome and phosphoproteome changes in SH-SY5Y human neuroblastoma cells stably transfected either with an empty or PRNP-containing vector, expressing physiological or supraphysiological levels of PrPc, respectively. PrPc-overexpression per se appears to stress the cells under STS-free conditions as indicated by diminished cell viability of PrPc-overexpressing versus control cells. However, PrPc-overexpression becomes advantageous following exposure to STS. Thus, only a short exposure (2 h) to 1 mu M STS results in lower survival rates and significantly higher caspase-3 activity in control versus PrPc-overexpressing cells. Hence, by exposing both experimental groups to the same apoptotic conditions we were able to induce apoptosis in control, but not in PrPc-overexpressing cells (as assessed by caspase-3 activity), which allowed for filtering out proteins possibly contributing to protection against STS-induced apoptosis in PrPc-overexpressing cells. Among other proteins regulated by different PrPc levels following exposure to STS, those involved in maintenance of cytoskeleton integrity caught our attention. In particular, the finding that elevated PrPc levels significantly reduce profilin-1 (PFN-1) expression. PFN-1 is known to facilitate STS-induced apoptosis. Silencing of PFN-1 expression by siRNA significantly increased viability of PrPc-overexpressing versus control cells, under STS treatment. In addition, PrPc-overexpressing cells depleted of PFN-1 exhibited increased viability versus PrPc-overexpressing cells with preserved PFN-1 expression, both subjected to STS. Concomitant increase in caspase-3 activity was observed in control versus PrPc-overexpressing cells after treatment with siRNA-PFN-1 and STS. We suggest that reduction of PFN-1 expression by elevated levels of PrPc may contribute to protective effects PrPc-overexpressing SH-SY5Y cells confer against STS-induced apoptosis."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1038/cddis.2016.384"],["dc.identifier.isi","000393679000006"],["dc.identifier.pmid","28102851"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14209"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43571"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-4889"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Cellular prion protein mediates early apoptotic proteome alternation and phospho-modification in human neuroblastoma cells"],["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","1203"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","ELECTROPHORESIS"],["dc.bibliographiccitation.lastpage","1214"],["dc.bibliographiccitation.volume","43"],["dc.contributor.affiliation","Kwiatkowski, Marcel; 1\r\nDepartment of Biochemistry and Center for Molecular Biosciences Innsbruck\r\nUniversity of Innsbruck\r\nInnsbruck Austria"],["dc.contributor.affiliation","Hotze, Madlen; 1\r\nDepartment of Biochemistry and Center for Molecular Biosciences Innsbruck\r\nUniversity of Innsbruck\r\nInnsbruck Austria"],["dc.contributor.affiliation","Schumacher, Julia; 2\r\nAbbott GmbH\r\nCore Diagnostics\r\nWiesbaden Germany"],["dc.contributor.affiliation","Asif, Abdul R.; 3\r\nDepartment of Clinical Chemistry/UMG‐Laboratories\r\nUniversity Medical Center\r\nGöttingen Germany"],["dc.contributor.affiliation","Pittol, Jose Miguel Ramos; 1\r\nDepartment of Biochemistry and Center for Molecular Biosciences Innsbruck\r\nUniversity of Innsbruck\r\nInnsbruck Austria"],["dc.contributor.affiliation","Brenig, Bertram; 4\r\nDepartment of Molecular Biology of Livestock\r\nInstitute of Veterinary Medicine\r\nUniversity of Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Ramljak, Sanja; 5\r\nDigital Diagnostics AG\r\nMainz Germany"],["dc.contributor.affiliation","Zischler, Hans; 6\r\nInstitute of Organismic and Molecular Evolution, Anthropology\r\nUniversity of Mainz\r\nMainz Germany"],["dc.contributor.author","Kwiatkowski, Marcel"],["dc.contributor.author","Hotze, Madlen"],["dc.contributor.author","Schumacher, Julia"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Pittol, Jose Miguel Ramos"],["dc.contributor.author","Brenig, Bertram"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Zischler, Hans"],["dc.contributor.author","Herlyn, Holger"],["dc.date.accessioned","2022-04-01T10:01:29Z"],["dc.date.available","2022-04-01T10:01:29Z"],["dc.date.issued","2022"],["dc.date.updated","2022-06-14T22:04:26Z"],["dc.description.abstract","Abstract Multiple spotting due to protein speciation might increase a protein's chance of being captured in a random selection of 2‐DE spots. We tested this expectation in new (PXD015649) and previously published 2‐DE/MS data of porcine and human tissues. For comparison, we included bottom‐up proteomics studies (BU‐LC/MS) of corresponding biological materials. Analyses of altogether ten datasets proposed that amino acid modification fosters multispotting in 2‐DE. Thus, the number of 2‐DE spots containing a particular protein more tightly associated with a peptide diversity measure accounting for amino acid modification than with an alternative one disregarding it. Furthermore, every 11th amino acid was a post‐translational modification candidate site in 2‐DE/MS proteins, whereas in BU‐LC/MS proteins this was merely the case in every 21st amino acid. Alternative splicing might contribute to multispotting, since genes encoding 2‐DE/MS proteins were found to have on average about 0.3 more transcript variants than their counterparts from BU‐LC/MS studies. Correspondingly, resolution completeness as estimated from the representation of transcript variant‐rich genes was higher in 2‐DE/MS than BU‐LC/MS datasets. These findings suggest that the ability to resolve proteomes down to protein species can lead to enrichment of multispotting proteins in 2‐DE/MS. Low sensitivity of stains and MS instruments appears to enhance this effect."],["dc.description.sponsorship","University of Mainz"],["dc.identifier.doi","10.1002/elps.202000393"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/105675"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.eissn","1522-2683"],["dc.relation.issn","0173-0835"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes."],["dc.rights.uri","http://onlinelibrary.wiley.com/termsAndConditions#vor"],["dc.title","Protein speciation is likely to increase the chance of proteins to be determined in 2‐DE/MS"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","463"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","HYBRIDOMA"],["dc.bibliographiccitation.lastpage","472"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Mueller, Daniel A."],["dc.contributor.author","Heinig, Lars"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Krueger, Astrid"],["dc.contributor.author","Schulte, Reiner"],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Stuke, Andreas W."],["dc.date.accessioned","2018-11-07T08:36:15Z"],["dc.date.available","2018-11-07T08:36:15Z"],["dc.date.issued","2010"],["dc.description.abstract","Because of their high antigen specificity and metabolic stability, genetically engineered human monoclonal antibodies are on the way to becoming one of the most promising medical diagnostics and therapeutics. In order to establish an in vitro system capable of producing such biosimilar antibodies, we used human constant chain sequences to design the novel human antibody expressing vector cassette pMAB-ABX. A bidirectional tetracycline (tet)-controllable promotor was used for harmonized expression of immunoglobulin type G (IgG) heavy and light chains. As an example we used anti-prion protein (anti-PrP) IgGs. Therefore, the variable heavy (V(H)) and light chain (V(L)) sequences of anti-PrP antibodies, previously generated in our laboratory by DNA immunization of prion protein knock-out mice, were isolated from murine hybridoma cell lines and inserted into pMAB-ABX vector. After transfection of Chinese hamster ovary (CHO) cells, a number of stable antibody producing cell clones were selected. One cell line (pMAB-ABX-13F10/3B5) stably expressing the recombinant humanized antibody (rechuAb) 13F10/3B5 was selected for detailed characterization by Western blot, immunofluorescence, and flow cytometric analyses. The full-length recombinant humanized IgG antibody showed a high level of expression in the cytoplasm. In conclusion, the new cell system described here is a suitable tool to produce functional intact full-length humanized IgG antibodies."],["dc.description.sponsorship","DPZ; Ersatzmethoden zum Tierversuch; German BMBF [FKZ 0315279A]"],["dc.identifier.doi","10.1089/hyb.2010.0041"],["dc.identifier.isi","000285145300001"],["dc.identifier.pmid","21087094"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18267"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Mary Ann Liebert Inc"],["dc.relation.issn","1554-0014"],["dc.title","Conditional Expression of Full-Length Humanized Anti-Prion Protein Antibodies in Chinese Hamster Ovary Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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","2681"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Proteome Research"],["dc.bibliographiccitation.lastpage","2695"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Armstrong, Victor William"],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Groschup, Martin H."],["dc.contributor.author","Buschman, Anne"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Bodemer, Walter"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T11:13:39Z"],["dc.date.available","2018-11-07T11:13:39Z"],["dc.date.issued","2008"],["dc.description.abstract","The physiological role of the cellular prion protein (PrPc) is still not fully understood. Current evidence strongly suggests that PrPc overexpression in different cell lines sensitizes cells to apoptotic stimuli through a p53 dependent pathway. On the other hand, an expression of PrPc in PrPc-deficient cells undergoing apoptosis exhibited repeatedly antiapoptotic effects. Therefore, the presence/absence and/ or the level of PrPc expression seem to be critical for the fluctuation between PrPc's pro- and antiapoptotic properties. The present study examined whether an overexpression of PrPc itself, without addition of any apoptotic agent, can lead to proteome changes that might account for the higher responsiveness to apoptotic stimuli. Beyond this, we examined whether the sole introduction of PrPc into PrPc-deficient cells could be sufficient to up-regulate antiapoptotic proteins capable of mitigating apoptosis. For this purpose, we used two cell lines, one expressing [human embryonic kidney (HEK) 293 cells] and the other lacking (mouse neuronal PrPc-deficient cells) endogenous PrPc. Protein profiling following transient PrPc overexpression in HEK 293 cells revealed a major PrPc involvement in regulation of proteins participating in energy metabolism and cellular homeostasis, whereas transient introduction of PrPc into mouse neuronal PrPc-deficient cells resulted mainly in the regulation of proteins involved in protection against oxidative stress and apoptosis. In addition, we report for the first time that PrPc overexpression influenced the regulation of several proteins known to have contributory roles in the pathogenesis of Alzheimer disease (AD). Revealing the correlation between presence/absence and/or different levels of PrPc expression with the regulation of certain cellular proteins might further contribute to our understanding of the complex role of PrPc in cell physiology."],["dc.identifier.doi","10.1021/pr7007187"],["dc.identifier.isi","000257449500009"],["dc.identifier.pmid","18537284"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53946"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1535-3893"],["dc.title","Physiological role of the cellular prion protein (PrPc): Protein profiling study in two cell culture systems"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]