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.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","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"]]

[["dc.bibliographiccitation.firstpage","155"],["dc.bibliographiccitation.journal","Experimental Neurology"],["dc.bibliographiccitation.lastpage","167"],["dc.bibliographiccitation.volume","271"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Schenkel, Sara"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Carimalo, Julie"],["dc.contributor.author","Doeppner, Thorsten R."],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Weise, Jens"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:52:13Z"],["dc.date.available","2018-11-07T09:52:13Z"],["dc.date.issued","2015"],["dc.description.abstract","Although a physiological function of the cellular prion protein (PrPc) is still not fully clarified, a PrPc-mediated neuroprotection against hypoxic/ischemic insult is intriguing. After ischemic stroke prion protein knockout mice (Prnp(0/0)) display significantly greater lesions as compared to wild-type (WT) mice. Earlier reports suggested an interaction between the glycolytic enzyme lactate dehydrogenase (LDH) and PrPc. Since hypoxic environment enhances LDH expression levels and compels neurons to rely on lactate as an additional oxidative substrate for energy metabolism, we examined possible differences in LDH protein expression in WT and Prnp(0/0) knockout models under normoxic/hypoxic conditions in vitro and in vivo, as well as in a HEK293 cell line. While no differences are observed under normoxic conditions, LDH expression is markedly increased after 60-min and 90-min of hypoxia in WT vs. Prnp(0/0) primary cortical neurons with concurrent less hypoxia-induced damage in the former group. Likewise, cerebral ischemia significantly increases LDH levels in WT vs. Prnp(0/0) mice with accompanying smaller lesions in the WT group. HEK293 cells overexpressing PrPc show significantly higher LDH expression/activity following 90-min of hypoxia as compared to control cells. Moreover, a cytoplasmic co-localization of LDH and PrPc was recorded under both normoxic and hypoxic conditions. Interestingly, an expression of monocarboxylate transporter 1, responsible for cellular lactate uptake, increases with PrPc-overexpression under normoxic conditions. Our data suggest LDH as a direct PrPc interactor with possible physiological relevance under low oxygen conditions. (C) 2015 Published by Elsevier Inc."],["dc.identifier.doi","10.1016/j.expneurol.2015.04.025"],["dc.identifier.isi","000362627200017"],["dc.identifier.pmid","26024859"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36070"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1090-2430"],["dc.relation.issn","0014-4886"],["dc.title","Cellular prion protein directly interacts with and enhances lactate dehydrogenase expression under hypoxic conditions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]