Vasko, Radovan

[["dc.bibliographiccitation.firstpage","jcs219014"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","131"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Bibi, Asima"],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Rubel, Diana"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Mueller, Gerhard A."],["dc.date.accessioned","2020-12-10T18:41:52Z"],["dc.date.available","2020-12-10T18:41:52Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1242/jcs.219014"],["dc.identifier.eissn","1477-9137"],["dc.identifier.issn","0021-9533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77711"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation.iserratumof","/handle/2/29071"],["dc.title","Correction: Secretion of ERP57 is important for extracellular matrix accumulation and progression of renal fibrosis, and is an early sign of disease onset (doi:10.1242/jcs.125088)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","erratum_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Arthritis"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Blaschke, Sabine"],["dc.contributor.author","Streich, Jan-Hendrik"],["dc.contributor.author","Müller, Gerhard A."],["dc.contributor.author","Korsten, Peter"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2020-05-04T07:22:22Z"],["dc.date.available","2020-05-04T07:22:22Z"],["dc.date.issued","2016"],["dc.description.abstract","Background: To identify differentially regulated serum proteins, we compared proteome profiles of sera from patients with rheumatoid arthritis (RA) and healthy controls using proteomics. Methods: Sera were collected from 43 patients with RA and 48 healthy volunteers. The samples were cleared of the most abundant major proteins by immunoaffinity chromatography. Serum protein profiles between the two groups were compared by two-dimensional differential gel electrophoresis (2D-DIGE) and differentially regulated proteins were studied using mass spectrometry. Results: We identified 26 differentially expressed serum proteins between patients with RA and healthy controls. A quantitatively significant change of protein levels was defined as at least 1.5-fold upregulation or 0.6-fold downregulation respectively. Using these criteria, patients with RA exhibited significantly higher levels of leucine-rich alpha-2-glycoprotein (p<0.01), apolipoprotein A-IV (p<0.001), clusterin (p<0.001), haptoglobin (p<0.001), Ig alpha-1 chain C region (p<0.05), retinol-binding protein 4 (p<0.001), serum amyloid A (p<0.01) and alpha-1-antichymotrypsin (p<0.01). The levels of serotransferrin were significantly decreased in RA patients (p<0.01). Conclusion: We identified eight proteins with significantly increased and one protein with significantly decreased serum levels in RA patients compared to healthy controls. Several of these proteins may be implicated in the pathogenesis of RA and may have potential in diagnostics and activity assessment of RA."],["dc.identifier.doi","10.4172/2167-7921.1000201"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/64544"],["dc.language.iso","en"],["dc.relation.issn","2167-7921"],["dc.title","Comparative Serum Proteomic Analysis of Differentially Regulated Proteins in Patients with Rheumatoid Arthritis and Healthy Volunteers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","50"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Journal of Pharmacology"],["dc.bibliographiccitation.lastpage","57"],["dc.bibliographiccitation.volume","670"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","von Jaschke, Ann-Kristin"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T08:49:50Z"],["dc.date.available","2018-11-07T08:49:50Z"],["dc.date.issued","2011"],["dc.description.abstract","Renal cell carcinoma (RCC) is the most common renal neoplasm in adults. Considering that chemoresistance is a typical feature of RCC, every effort should be made in order to identify mechanisms of drug resistance. We used two-dimensional gel electrophoresis and mass spectrometry to study changes in protein expression levels that occur in primary resistant LN78 RCC cells when treated with therapeutic concentrations of cisplatin. Expression differences of selected proteins were confirmed by immunoblot. Up-regulation of heat-shock proteins can block apoptosis indirectly by altered protein folding and by direct interaction with apoptosis regulatory proteins. Cyclophilin A and stratifin can modify cell cycle control and enable tumor cells to escape and further proliferate despite DNA damage caused by cisplatin. Increased activity of glycolytic enzymes reflect metabolic adaptations to increased energy requirements as well as converting to alternative energy sources because of cisplatin-induced disturbed mitochondrial oxidation. Changes in cytoskeletal proteins may change the handling of cisplatin by altering transport and increasing cellular efflux of the drug. Repression of vimentin and disturbance of antioxidative mechanisms may represent vulnerable points in tumor cellular defense against cisplatin. The involvement of these proteins in cisplatin resistance and their potential as therapeutic targets requires further evaluation. (C) 2011 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.ejphar.2011.08.030"],["dc.identifier.isi","000296550500008"],["dc.identifier.pmid","21924258"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21550"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0014-2999"],["dc.title","Impact of cisplatin administration on protein expression levels in renal cell carcinoma: A proteomic analysis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","304"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Proteomics"],["dc.bibliographiccitation.lastpage","318"],["dc.bibliographiccitation.volume","74"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Mueller, Claudia"],["dc.contributor.author","Lahrichi, Loubna"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Bibi, Asima"],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Mueller, Georg Anton"],["dc.date.accessioned","2018-11-07T08:58:57Z"],["dc.date.available","2018-11-07T08:58:57Z"],["dc.date.issued","2011"],["dc.description.abstract","Renal fibroblasts are thought to play a major role in the development of renal fibrosis (RF). The mechanisms leading to this renal alteration remain poorly understood. We performed differential proteomic analyses with two established fibroblast cell lines with RF phenotype to identify new molecular pathways associated with RF. Differential 2-DE combined with mass spectrometry analysis revealed the alteration of more than 30 proteins in fibrotic kidney fibroblasts (TK188) compared to normal kidney fibroblast. (TK173). Among these proteins, markers of the endoplasmic reticulum (ER) stress- and the unfolded protein response (UPR) pathway (GRP78, GRP94, ERP57, ERP72, and CALR) and the oxidative stress pathway proteins (PRDX1, PRDX2, PRDX6, HSP70, HYOU1) were highly up-regulated in fibrotic cells. Activation of these stress pathways through long time exposition of TK173, to high NaCl or glucose concentrations resulted in TK188 like phenotype. Parallel to an increase in reactive oxygen species, the stressed cells showed significant alteration of fibrosis markers, ER-stress and oxidative stress proteins. Similar effects of osmotic stress could be also observed on renal proximal tubule cells. Our data suggest an important role of the ER-stress proteins in fibrosis and highlights the pro-fibrotic effect of osmotic stress through activation of oxidative stress and ER-stress pathways. (C) 2010 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.jprot.2010.11.007"],["dc.identifier.isi","000287061200004"],["dc.identifier.pmid","21118732"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23770"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1874-3919"],["dc.title","Proteomics characterization of cell model with renal fibrosis phenotype: Osmotic stress as fibrosis triggering factor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","513"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","CLINICAL AND EXPERIMENTAL RHEUMATOLOGY"],["dc.bibliographiccitation.lastpage","520"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Streich, J.-H."],["dc.contributor.author","Blaschke, S."],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Mai, Burkhard"],["dc.contributor.author","Kostrzewa, Markus"],["dc.contributor.author","Sparbier, Katrin"],["dc.contributor.author","Korsten, Peter"],["dc.contributor.author","Bohr, Stefan"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T10:14:47Z"],["dc.date.available","2018-11-07T10:14:47Z"],["dc.date.issued","2016"],["dc.description.abstract","Objective To study the protein expression differences between primary fibroblasts explanted from synovial membranes of patients with rheumatoid arthritis (RA) and osteoarthritis (OA). Methods Fibroblast cultures were obtained from 10 patients with RA and 5 patients with OA. After two-dimensional gel electrophoresis, proteins were excised and identified using peptide mass fingerprint. Expression of selected proteins was subsequently examined by immunoblot. Furthermore, we examined the cellular lysates for the presence of citrullinated proteins. Results The study was designed to compare expression changes of the common proteins detected in all studied fibroblast cultures (i.e. detected in all patients samples). We totally identified 191 shared proteins between RA and OA fibroblasts. A significant difference was defined as at least 2-fold upregulation or 0.6-fold downregulation of protein expression. The most obvious alteration observed in RA was the appearance of several vimentin fragments not present in OA. We did not detect citrullinated proteins in lysates from RA fibroblasts. This corroborates the current assumption that fibroblasts are not able to citrullinate proteins by themselves and that invading macrophages play a central role in this process. Conclusion We demonstrated that fibroblasts from patients with RA, despite being grown under identical conditions, preserve a particular feature and generate vimentin fragments not present in fibroblasts from OA. Elevated levels of different vimentin fragments have been recently reported in several rheumatic conditions. Further studies are needed to elucidate the pathogenic mechanisms induced by vimentin fragments in RA."],["dc.identifier.isi","000376977900019"],["dc.identifier.pmid","27049516"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40684"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1593-098X"],["dc.relation.issn","0392-856X"],["dc.title","Vimentin fragments are potential markers of rheumatoid synovial fibroblasts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3649"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","3663"],["dc.bibliographiccitation.volume","126"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Bibi, Asima"],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Rubel, Diana"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Mueller, Georg Anton"],["dc.date.accessioned","2018-11-07T09:21:15Z"],["dc.date.available","2018-11-07T09:21:15Z"],["dc.date.issued","2013"],["dc.description.abstract","Renal fibrosis is characterized by excessive accumulation of extracellular matrix (ECM), which compromises organ function by replacing normal organ tissue. The molecular mechanisms leading to renal fibrosis are not fully understood. Here we demonstrated that TGF beta 1, AGT or PDGF stimulation of renal cells resulted in endoplasmic reticulum (ER) stress followed by activation of the protective unfolded protein response pathway and a high secretory level of protein disulfide isomerase ERP57 (also known as PDIA3). The TGF beta 1-induced impairment of ER function could be reversed by treatment with BMP7, suggesting a specific involvement in renal fibrosis. A clear correlation between the degree of fibrosis, ER stress and the level of ERP57 could be seen in fibrosis animal models and in biopsies of renal fibrosis patients. Protein interaction studies revealed that secreted ERP57 exhibits a strong interaction with ECM proteins. Knockdown of ERP57 or antibody-targeted inhibition of the secreted form significantly impaired the secretion and accumulation of ECM. Moreover, ERP57 was excreted in the early stages of chronic kidney disease, and its level in urine correlated with the degree of renal fibrosis, suggesting that the secretion of ERP57 represents one of the first signs of renal fibrosis onset and progression."],["dc.identifier.doi","10.1242/jcs.125088"],["dc.identifier.isi","000323204400015"],["dc.identifier.pmid","23781031"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29071"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.haserratum","/handle/2/77711"],["dc.relation.issn","0021-9533"],["dc.title","Secretion of ERP57 is important for extracellular matrix accumulation and progression of renal fibrosis, and is an early sign of disease onset"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]