Dihazi, Hassan

[["dc.bibliographiccitation.firstpage","697"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","PROTEOMICS"],["dc.bibliographiccitation.lastpage","708"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Tolson, J. R."],["dc.contributor.author","Flad, T."],["dc.contributor.author","Gnau, V."],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Hennenlotter, J."],["dc.contributor.author","Beck, A."],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Kuczyk, M."],["dc.contributor.author","Mueller, C. A."],["dc.date.accessioned","2018-11-07T10:41:53Z"],["dc.date.available","2018-11-07T10:41:53Z"],["dc.date.issued","2006"],["dc.description.abstract","The search for novel molecular markers of tumor invasion is vital if strategies are to become more effective in the diagnostic and prognostic management of transitional cell carcinoma of the bladder. Up to 50% of tumors detected at stage 1 (pT1) progress to a higher grade even after endoscopic surgical resection, and there are currently no protein markers of this aggressive, invasive phenotype. We have combined SELDI-TOF-MS, ClinProt magnetic bead enrichment, Nano-LC-ESI-ion trap tandem mass spectrometry and immunohistochemical analysis to the study of 12 invasive bladder cancer tissue biopsies paired with normal bladder tissue samples obtained from the same patients for the definition and identification of proteins up-regulated in the tumors. We report the inflammation-associated calcium binding protein S100A8 (MRP-8, calgranulin A) to be highly expressed in tumor cells in contrast to normal urothelium in 50% of the samples, as well as two unidentified protein markers at 5.75 and 6.89 kDa that were differentially detected in 9/12 and 10/ 12 tumor samples, respectively. These new markers, when fully characterized, may contribute to new target proteins for the prediction of aggressive, invasive bladder tumors."],["dc.identifier.doi","10.1002/pmic.200500033"],["dc.identifier.isi","000235207700031"],["dc.identifier.pmid","16252305"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46646"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1615-9853"],["dc.title","Differential detection of S100A8 in transitional cell carcinoma of the bladder by pair wise tissue proteomic and immunohistochemical analysis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Der Internist"],["dc.bibliographiccitation.volume","57"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Mueller, G."],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T10:15:48Z"],["dc.date.available","2018-11-07T10:15:48Z"],["dc.date.issued","2016"],["dc.format.extent","S56"],["dc.identifier.isi","000375417500108"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40889"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.issn","1432-1289"],["dc.relation.issn","0020-9554"],["dc.title","Calreticulin is a major Regulator of the Calcium Balance in the Kidney, a persistent Down-regulation of their Expression results in chronic Renal Failure"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["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.firstpage","5858"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["dc.contributor.affiliation","Serin, Nazli; \t\t \r\n\t\t Clinic for Nephrology and Rheumatology, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, nazli.serin@med.uni-goettingen.de\t\t \r\n\t\t Department of Hematology and Oncology, University of Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, nazli.serin@med.uni-goettingen.de"],["dc.contributor.affiliation","Dihazi, Gry H.; \t\t \r\n\t\t Institute of Clinical Chemistry/UMG-Laboratories, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, gryhelene.dihazi@med.uni-goettingen.de"],["dc.contributor.affiliation","Tayyeb, Asima; \t\t \r\n\t\t School of Biological Sciences, University of the Punjab, Lahore 54590, Pakistan, asima.sbs@pu.edu.pk"],["dc.contributor.affiliation","Lenz, Christof; \t\t \r\n\t\t Institute of Clinical Chemistry/UMG-Laboratories, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, christof.lenz@med.uni-goettingen.de\t\t \r\n\t\t Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany, christof.lenz@med.uni-goettingen.de"],["dc.contributor.affiliation","Müller, Gerhard A.; \t\t \r\n\t\t Clinic for Nephrology and Rheumatology, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, gmueller@med.uni-goettingen.de"],["dc.contributor.affiliation","Zeisberg, Michael; \t\t \r\n\t\t Clinic for Nephrology and Rheumatology, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, michael.zeisberg@med.uni-goettingen.de"],["dc.contributor.affiliation","Dihazi, Hassan; \t\t \r\n\t\t Clinic for Nephrology and Rheumatology, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, dihazi@med.uni-goettingen.de\t\t \r\n\t\t Center for Biostructural Imaging of Neurodegeneration (BIN), University Medical Center Göttingen, 37075 Göttingen, Germany, dihazi@med.uni-goettingen.de"],["dc.contributor.author","Serin, Nazli"],["dc.contributor.author","Dihazi, Gry H."],["dc.contributor.author","Tayyeb, Asima"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Müller, Gerhard A."],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2021-07-05T15:00:46Z"],["dc.date.available","2021-07-05T15:00:46Z"],["dc.date.issued","2021"],["dc.date.updated","2022-09-06T07:10:18Z"],["dc.description.abstract","Nephrogenesis is driven by complex signaling pathways that control cell growth and differentiation. The endoplasmic reticulum chaperone calreticulin (Calr) is well known for its function in calcium storage and in the folding of glycoproteins. Its role in kidney development is still not understood. We provide evidence for a pivotal role of Calr in nephrogenesis in this investigation. We show that Calr deficiency results in the disrupted formation of an intact nephrogenic zone and in retardation of nephrogenesis, as evidenced by the disturbance in the formation of comma-shaped and s-shaped bodies. Using proteomics and transcriptomics approaches, we demonstrated that in addition to an alteration in Wnt-signaling key proteins, embryonic kidneys from Calr−/− showed an overall impairment in expression of ribosomal proteins which reveals disturbances in protein synthesis and nephrogenesis. CRISPR/cas9 mediated knockout confirmed that Calr deficiency is associated with a deficiency of several ribosomal proteins and key proteins in ribosome biogenesis. Our data highlights a direct link between Calr expression and the ribosome biogenesis."],["dc.description.abstract","Nephrogenesis is driven by complex signaling pathways that control cell growth and differentiation. The endoplasmic reticulum chaperone calreticulin (Calr) is well known for its function in calcium storage and in the folding of glycoproteins. Its role in kidney development is still not understood. We provide evidence for a pivotal role of Calr in nephrogenesis in this investigation. We show that Calr deficiency results in the disrupted formation of an intact nephrogenic zone and in retardation of nephrogenesis, as evidenced by the disturbance in the formation of comma-shaped and s-shaped bodies. Using proteomics and transcriptomics approaches, we demonstrated that in addition to an alteration in Wnt-signaling key proteins, embryonic kidneys from Calr−/− showed an overall impairment in expression of ribosomal proteins which reveals disturbances in protein synthesis and nephrogenesis. CRISPR/cas9 mediated knockout confirmed that Calr deficiency is associated with a deficiency of several ribosomal proteins and key proteins in ribosome biogenesis. Our data highlights a direct link between Calr expression and the ribosome biogenesis."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3390/ijms22115858"],["dc.identifier.pii","ijms22115858"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87900"],["dc.language.iso","en"],["dc.notes.intern","DOI Import DOI-Import GROB-441"],["dc.relation.eissn","1422-0067"],["dc.relation.orgunit","Klinik für Nephrologie und Rheumatologie"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Calreticulin Deficiency Disturbs Ribosome Biogenesis and Results in Retardation in Embryonic Kidney Development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","45"],["dc.bibliographiccitation.journal","Arthritis Research & Therapy"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Blaschke, Sabine"],["dc.contributor.author","Rinke, Kathinka"],["dc.contributor.author","Maring, Michael"],["dc.contributor.author","Flad, Thomas"],["dc.contributor.author","Patschan, Susann A."],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T09:59:46Z"],["dc.date.available","2018-11-07T09:59:46Z"],["dc.date.issued","2015"],["dc.description.abstract","Introduction: The introduction of tumor necrosis factor-alpha (TNF-alpha) antagonists has substantially improved patient's clinical outcome in rheumatoid arthritis (RA). However, nearly 20% to 40% of RA patients do not respond to anti-TNF-alpha treatment strategies. To identify valid predictors of TNF-alpha antagonist response in RA, serum proteome profiles from responders (R) and non-responders (NR) to etanercept, a soluble recombinant TNF-alpha receptor/IgG Fc fusion protein receptor, were compared in a prospective cohort study. Methods: In this clinical study 50 RA patients with inadequate response to conventional DMARDs were included and treated with etanercept. The primary efficacy endpoint was response according to the European League against Rheumatism (EULAR) improvement criteria. Serum samples collected prior to initiation and after six months of etanercept therapy were cleared of the most abundant major proteins by immunoaffinity chromatography. After separation by two-dimensional differential gel electrophoresis (2D-DIGE) and identification by mass spectrometry (MS) data were validated by Western blot analysis. Results: After six months of etanercept treatment 62% (n = 31) of RA patients achieved response. Haptoglobin-alpha 1 (Hp-alpha 1) and -alpha 2 (Hp-alpha 2) and vitamin D-binding protein (VDBP) were found to be significantly upregulated in responder sera (P <= 0.02) at study entry. In contrast, apolipoprotein C-III (ApoC-III) showed significantly higher levels in non-responders (P = 0.0162). At study end ApoA-II, Hp-alpha 1, Hp-alpha 2 and VDBP were identified to be expressed at significantly higher levels (P < 0.05) in responder sera. Conclusions: By application of clinical proteomics in immunodepleted sera we could identify and validate for the first time Hp-alpha 1, -alpha 2, VDBP and ApoC-III as potential biomarkers for prediction of etanercept drug response in RA."],["dc.description.sponsorship","Pfizer Research Initiative"],["dc.identifier.doi","10.1186/s13075-015-0553-1"],["dc.identifier.isi","000352187400001"],["dc.identifier.pmid","25884688"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13467"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37661"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1478-6362"],["dc.relation.issn","1478-6354"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Haptoglobin-alpha 1, -alpha 2, vitamin D-binding protein and apolipoprotein C-III as predictors of etanercept drug response in rheumatoid arthritis"],["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.issue","11"],["dc.bibliographiccitation.journal","Blood"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Wessels, Johannes Theodor"],["dc.contributor.author","Glowacka, M."],["dc.contributor.author","Tepper-Wessels, Kathrin"],["dc.contributor.author","Robrecht, D."],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Mahrt, Jens"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Klein, George J."],["dc.date.accessioned","2018-11-07T10:34:39Z"],["dc.date.available","2018-11-07T10:34:39Z"],["dc.date.issued","2003"],["dc.format.extent","179B"],["dc.identifier.isi","000186537100722"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44924"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Hematology"],["dc.publisher.place","Washington"],["dc.relation.conference","45th Annual Meeting of the American-Society-of-Hematology"],["dc.relation.eventlocation","SAN DIEGO, CALIFORNIA"],["dc.relation.issn","0006-4971"],["dc.title","Members of the membrane linked metalloproteinase family ADAM are expressed on human cord blood CD34(+) haematopoetic progenitor cells."],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","99"],["dc.bibliographiccitation.journal","European Journal of Pharmacology"],["dc.bibliographiccitation.lastpage","110"],["dc.bibliographiccitation.volume","784"],["dc.contributor.author","Trivedi, Rachana"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Mishra, Durga P."],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T10:10:18Z"],["dc.date.available","2018-11-07T10:10:18Z"],["dc.date.issued","2016"],["dc.description.abstract","Clear cell renal cell carcinoma (ccRCC) is the most malignant tumor in the adult kidney. Many factors are responsible for the development and progression of this tumor. Increased reactive oxygen species accumulation and altered redox status have been observed in cancer cells and this biochemical property of cancer cells can be exploited for therapeutic benefits. In earlier work we identified and characterize Protein DJ-1 (PARK7) as an oxidative stress squevenger in renal cells exposed to oxidative stress. To investigate whether the PARK7 or other oxidative stress proteins play a role in the renal cell carcinoma and its sensitivity or resistance to cytostatic drug treatment, differential proteomics analysis was performed with a cell model for clear cell renal carcinoma (Caki-2 and A498). Caki-2 cells were treated with cisplatin and differentially expressed proteins were investigated. The cisplatin treatment resulted in an increase in reactive oxygen species accumulation and ultimately apoptosis of Caki-2 and A498 cells. In parallel, the apoptotic effect was accompanied by a significant downregulation of antioxidant proteins especially PARK7. Knockdown of PARK7 using siRNA and overexpression using plasmid highlights the role of PARK7 as a key player in renal cell carcinoma response to cisplatin induced apoptosis. Over expression of PARK7 resulted in significant decrease in apoptosis, whereas knockdown of the protein was accompanied by an increase in apoptosis in Caki-2 and A498 cells treated with cisplatin. These results highlights for the first time the important role of PARK7 in cisplatin induced apoptosis in clear renal cell carcinoma cells. (C) 2016 Elsevier B.V. All rights reserved."],["dc.description.sponsorship","DAAD [A/12/76098]"],["dc.identifier.doi","10.1016/j.ejphar.2016.04.014"],["dc.identifier.isi","000379653600011"],["dc.identifier.pmid","27112662"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39827"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1879-0712"],["dc.relation.issn","0014-2999"],["dc.title","The antioxidant protein PARK7 plays an important role in cell resistance to Cisplatin-induced apoptosis in case of clear cell renal cell carcinoma"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1445"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Molecular & Cellular Proteomics"],["dc.bibliographiccitation.lastpage","1458"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Asif, Abdul Rahman"],["dc.contributor.author","Agarwal, Nitin K."],["dc.contributor.author","Doncheva, Y."],["dc.contributor.author","Mueller, Gerhard A."],["dc.date.accessioned","2018-11-07T10:55:30Z"],["dc.date.available","2018-11-07T10:55:30Z"],["dc.date.issued","2005"],["dc.description.abstract","Epithelial cells of the thick ascending limb of Henle's loop (TALH cells) play a major role in the urinary concentrating mechanism. They are normally exposed to variable and often very high osmotic stress, which is particularly due to high sodium and chloride reabsorption and very low water permeability of the luminal membrane. It is already established that elevation of the activity of aldose reductase and hence an increase in intracellular sorbitol are indispensable for the osmotic adaptation and stability of the TALH cells. To identify new molecular factors potentially associated with the osmotic stress-resistant phenotype in kidney cells, TALH cells exhibiting low or high levels of resistance to osmotic stress were characterized using proteomic tools. Two-dimensional gel analysis showed a total number of 40 proteins that were differentially expressed in TALH cells under osmotic stress. Twenty-five proteins were overexpressed, whereas 15 proteins showed a down-regulation. Besides the sorbitol pathway enzyme aldose reductase, whose expression was 15 times increased, many other metabolic enzymes like glutathione S-transferase, malate dehydrogenase, lactate dehydrogenase, alpha enolase, glyceraldehyde-3-phosphate dehydrogenase, and triose-phosphate isomerase were up-regulated. Among the cytoskeleton proteins and cytoskeleton-associated proteins vimentin, cytokeratin, tropomyosin 4, and annexins I, II, and V were up-regulated, whereas tubulin and tropomyosins 1, 2, and 3 were downregulated. The heat shock proteins alpha-crystallin chain B, HSP70, and HSP90 were found to be overexpressed. In contrast to the results in oxidative stress the endoplasmic reticulum stress proteins like glucose-regulated proteins (GRP78, GRP94, and GRP96), calreticulin, and protein-disulfide isomerase were down-regulated under hypertonic stress."],["dc.identifier.doi","10.1074/mcp.M400184-MCP200"],["dc.identifier.isi","000232207900003"],["dc.identifier.pmid","15975915"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49797"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1535-9484"],["dc.relation.issn","1535-9476"],["dc.title","Proteomic analysis of cellular response to osmotic stress in thick ascending limb of Henle's loop (TALH) cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2674"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Nephrology Dialysis Transplantation"],["dc.bibliographiccitation.lastpage","2683"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Pesic, Ivana"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Hoffmann, Moritz"],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Koziolek, Michael"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T08:53:45Z"],["dc.date.available","2018-11-07T08:53:45Z"],["dc.date.issued","2011"],["dc.description.abstract","Background. The effect of clearance of so-called middle- and high-molecular weight proteins on clinical outcome of patients treated by peritoneal dialysis is still a matter of debate. In our present study, we investigated the impact of short-time alteration of the glucose concentration and the osmolarity of the peritoneal dialysis solution (PDS) on protein removal. Methods. Peritoneal dialysis liquids (PDL) were collected from 19 well-characterized continuous ambulatory peritoneal dialysis (CAPD) patients treated with two types of PDS: Baxter (n = 10) and Fresenius (n = 9). The patients were treated with two different glucose concentration of each PDS in 4-h cycles. The depletion of the six interfering high-abundant proteins from the PDL samples was performed with the Multiple Affinity Removal LC Column-Human 6. The resulting protein fractions were analysed by 2D gel electrophoresis, differential in gel electrophoresis, mass spectrometry and 2D western blot. Results. Proteomics investigation of the PDL fractions after depletion allowed the identification of 198 polypeptides of 424 excised spots. These polypeptides equates to 48 non-redundant proteins. Comparative analyses of 2D gel electrophoresis protein pattern revealed a clear correlation between protein removal and PDS glucose concentration and osmolarity. An increase for 4 h in the PDS osmolarity (with 43-51 mosmol/L) resulted qualitatively in 18-23% more protein removal in PDL. Moreover, 2D western blot analyses of the protein glycation pattern showed that the short-time increase in PDS glucose concentration (45-50 mM) resulted in significant alteration of the advanced glycosylation end products (AGEs) pattern. Conclusions. The data presented in this study demonstrate a clear correlation between the short-time changes in glucose concentration and osmolarity of the PDS, and the augmentation of the protein removal and the appearance of AGEs during CAPD."],["dc.identifier.doi","10.1093/ndt/gfq793"],["dc.identifier.isi","000293336500041"],["dc.identifier.pmid","21285129"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22498"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0931-0509"],["dc.title","Short-time increase of glucose concentration in PDS results in extensive removal and high glycation level of vital proteins during continuous ambulatory peritoneal dialysis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","578"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Der Internist"],["dc.bibliographiccitation.lastpage","586"],["dc.bibliographiccitation.volume","60"],["dc.contributor.author","Wallbach, M."],["dc.contributor.author","Tampe, B."],["dc.contributor.author","Dihazi, H."],["dc.contributor.author","Koziolek, M. J."],["dc.date.accessioned","2020-12-10T14:08:25Z"],["dc.date.available","2020-12-10T14:08:25Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/s00108-019-0602-y"],["dc.identifier.eissn","1432-1289"],["dc.identifier.issn","0020-9554"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70458"],["dc.language.iso","de"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Akute Nierenschädigung: von Kreatinin zu KIM‑1?"],["dc.title.alternative","Acute kidney injury: from creatinine to KIM‑1?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]