Dihazi, Hassan

[["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.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","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","1277"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular BioSystems"],["dc.bibliographiccitation.lastpage","1288"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Bibi, Asima"],["dc.contributor.author","Phuc Van Nguye, Phuc Van Nguye"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T09:01:42Z"],["dc.date.available","2018-11-07T09:01:42Z"],["dc.date.issued","2011"],["dc.description.abstract","Renal fibrosis is a process that is characterized by declining excretory renal function. The molecular mechanisms of fibrosis are not fully understood. Oxidative stress pathways were reported to be involved in renal tissue deterioration and fibrosis progression. In order to identify new molecular targets associated with oxidative stress and renal fibrosis, differential proteomics analysis was performed with established renal cell lines (TK173 and HK-2). The cells were treated with oxidative stress triggering factor H(2)O(2) and the proteome alterations were investigated. Two dimensional protein maps were generated and differentially expressed proteins were processed and identified using mass spectrometry analysis combined with data base search. Interestingly the increase of ROS in the renal cell lines upon H(2)O(2) treatment was accompanied by alteration of a large number of proteins, which could be classified in three categories: the first category grouped the proteins that have been described to be involved in fibrogenesis (e.g. ACTA2, VIN, VIM, DES, KRT, COL1A1, COL4A1), the second category, which was more interesting involved proteins of the oxidative stress pathway (PRDX1, PRDX2, PRDX6, SOD, PARK7, HYOU1), which were highly up-regulated under oxidative stress, and the third category represented proteins, which are involved in different other metabolic pathways. Among the oxidative stress proteins the up-regulation of PARK7 was accompanied by a shift in the pI as a result of oxidation. Knockdown of PARK7 using siRNA led to significant reduction in renal cell viability under oxidative stress. Under H(2)O(2) treatment the PARK7 knockdown cells showed up to 80% decrease in cell viability and an increase in apoptosis compared to the controls. These results highlight for the first time the important role of PARK7 in oxidative stress resistance in renal cells."],["dc.identifier.doi","10.1039/c0mb00116c"],["dc.identifier.isi","000288329300036"],["dc.identifier.pmid","21308111"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8349"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24498"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc Chemistry"],["dc.relation.issn","1742-206X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Proteomics analysis identifies PARK7 as an important player for renal cell resistance and survival under oxidative stress"],["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","10"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Proteome Science"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Dihazi, Gry H."],["dc.contributor.author","Mueller, Gerhard A."],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Wessels, Johannes T."],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2019-07-09T11:45:30Z"],["dc.date.available","2019-07-09T11:45:30Z"],["dc.date.issued","2018"],["dc.description.abstract","Upon publication of the original article [1], Marwa Eltoweissy noticed that her affiliation: “3. Department of Zoology, Faculty of Science, Alexandria University, Alexandria, Egypt” was missing. This affiliation has now been added in this correction article."],["dc.identifier.doi","10.1186/s12953-018-0138-4"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15230"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59243"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.iserratumof","/handle/2/37930"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Correction to: Proteomic characterization of adrenal gland embryonic development reveals early initiation of steroid metabolism and reduction of the retinoic acid pathway"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","erratum_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","World Journal of Stem Cells"],["dc.bibliographiccitation.lastpage","25"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Dihazi, Gry H."],["dc.contributor.author","Bibi, Asima"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Nolte, Jessica"],["dc.contributor.author","Mueller, Gerhard A."],["dc.contributor.author","Engel, Wolfgang"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2019-07-09T11:40:20Z"],["dc.date.available","2019-07-09T11:40:20Z"],["dc.date.issued","2013-01-26"],["dc.description.abstract","AIM: To investigate the proteome changes of stem cells due to ciclopirox olamine (CPX) treatment compared to control and retinoic acid treated cells. METHODS: Stem cells (SCs) are cells, which have the ability to continuously divide and differentiate into various other kinds of cells. Murine embryonic stem cells (ESCs) and multipotent adult germline stem cells (maGSCs) were treated with CPX, which has been shown to have an antiproliferative effect on stem cells, and compared to stem cells treated with retinoic acid (RA), which is known to have a differentiating effect on stem cells. Classical proteomic techniques like 2-D gel electrophoresis and differential in-gel electrophoresis (DIGE) were used to generate 2D protein maps from stem cells treated with RA or CPX as well as from non-treated stem cells. The resulting 2D gels were scanned and the digitalized images were collated with the help of Delta 2D software. The differentially expressed proteins were analyzed by a MALDI-TOF-TOF mass spectrometer, and the identified proteins were investigated and categorized using bioinformatics. RESULTS: Treatment of stem cells with CPX, a synthetic antifungal clinically used to treat superficial mycoses, resulted in an antiproliferative effect in vitro, without impairment of pluripotency. To understand the mechanisms induced by CPX treatments which results in arrest of cell cycle without any marked effect on pluripotency, a comparative proteomics study was conducted. The obtained data revealed that the CPX impact on cell proliferation was accompanied with a significant alteration in stem cell proteome. By peptide mass fingerprinting and tandem mass spectrometry combined with searches of protein sequence databases, a set of 316 proteins was identified, corresponding to a library of 125 non-redundant proteins. With proteomic analysis of ESCs and maGSCs treated with CPX and RA, we could identify more than 90 single proteins, which were differently expressed in both cell lines. We could highlight, that CPX treatment of stem cells, with subsequent proliferation inhibition, resulted in an alteration of the expression of 56 proteins compared to non-treated cells, and 54 proteins compared to RA treated cells. Bioinformatics analysis of the regulated proteins demonstrated their involvement in various biological processes. To our interest, a number of proteins have potential roles in the regulation of cell proliferation either directly or indirectly. Furthermore the classification of the altered polypeptides according to their main known/postulated functions revealed that the majority of these proteins are involved in molecular functions like nucleotide binding and metal ion binding, and biological processes like nucleotide biosynthetic processes, gene expression, embryonic development, regulation of transcription, cell cycle processes, RNA and mRNA processing. Proteins, which are involved in nucleotide biosynthetic process and proteolysis, were downregulated in CPX treated cells compared to control, as well as in RA treated cells, which may explain the cell cycle arrest. Moreover, proteins which were involved in cell death, positive regulation of biosynthetic process, response to organic substance, glycolysis, anti-apoptosis, and phosphorylation were downregulated in RA treated cells compared to control and CPX treated cells. CONCLUSION: The CPX treatment of SCs results in downregulation of nucleotide binding proteins and leads to cell cycle stop without impairment of pluripotency."],["dc.identifier.doi","10.4252/wjsc.v5.i1.9"],["dc.identifier.fs","603239"],["dc.identifier.pmid","23362436"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10937"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58149"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1948-0210"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Impact of the antiproliferative agent ciclopirox olamine treatment on stem cells proteome."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","6"],["dc.bibliographiccitation.journal","Proteome Science"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Wessels, Johannes Theodor"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T10:01:01Z"],["dc.date.available","2018-11-07T10:01:01Z"],["dc.date.issued","2015"],["dc.description.abstract","Background: Adrenal glands are essential endocrine organs composed of two embryological distinct tissues. Morphological changes during their development are well described, but less understood with regard to their molecular mechanisms. To identify proteins and pathways, which drive the initial steps of the specification of the endocrine function of the adrenal gland, rat's adrenal glands were isolated at different embryonic days (E): E14, E16, E18, E19 and postnatal day 1 (P1). Results: The alteration of the proteome during the stages E16, E19 and P1 was investigated by combining two dimensional gel electrophoresis and mass spectrometric analysis. Out of 594 excised protein spots, 464 spots were identified, resulting in 203 non-redundant proteins. The ontogenic classification of the identified proteins according to their molecular function resulted in 10 different categories, whereas the classification of their biological processes resulted in 19 different groups. This gives an insight into the complex mechanisms underlying adrenal gland development. Interestingly, the expression of retinoic acid pathway proteins was decreased during the development of the adrenal gland, suggesting that this pathway is only important at early stages. On the other hand, key proteins of the cholesterol synthesis increased their expression significantly at E19 revealing the initiation of the endocrine specialization of the adrenal glands. Conclusions: This study presents the first comprehensive wide proteome analysis of three different stages of embryonic adrenal gland development. The identified proteins, which were expressed in early stages of development, will shed light on the molecular mechanisms underlying embryonic development of the adrenal gland."],["dc.identifier.doi","10.1186/s12953-015-0063-8"],["dc.identifier.isi","000349921600001"],["dc.identifier.pmid","25694770"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11740"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37930"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.haserratum","/handle/2/59243"],["dc.relation.issn","1477-5956"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Proteomic characterization of adrenal gland embryonic development reveals early initiation of steroid metabolism and reduction of the retinoic acid pathway"],["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","5497"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Journal of Proteome Research"],["dc.bibliographiccitation.lastpage","5510"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Nolte, Jessica"],["dc.contributor.author","Meyer, Sandra"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Engel, Wolfgang"],["dc.date.accessioned","2018-11-07T11:21:36Z"],["dc.date.available","2018-11-07T11:21:36Z"],["dc.date.issued","2009"],["dc.description.abstract","Spermatogonial stem cells isolated from the adult mouse testis acquire under certain culture conditions pluripotency and become so-called multipotent adult germline stem cells (maGSCs). They can be differentiated into somatic cells of the three germ layers. We investigated a subset of the maGSCs and ESCs proteomes using cell lines derived from two different mouse strains, narrow range immobilized pH gradients to favor the detection of less abundant proteins, and DIGE to ensure confident comparison between the two cell types. 2-D reference maps of maGSCs and ESCs in the p/ ranges 3-6 and 5-8 were created, and protein entities were further processed for protein identification. By peptide mass fingerprinting and tandem mass spectrometry combined with searches of protein sequence databases, a set of 409 proteins was identified, corresponding to a library of 166 nonredundant stem cell-associated proteins. The identified proteins were classified according to their main known/postulated functions using bioinformatics. Furthermore, we used DIGE to highlight the ESC-like nature of maGSCs on the proteome scale. We concluded that the proteome of maGSCs is highly similar to that of ESCs as we could identify only a small subset of 18 proteins to be differentially expressed between the two cell types. Moreover, comparative analysis of the cell line proteomes from two different mouse strains showed that the interindividual differences in maGSCs proteomes are minimal. With our study, we created for the first time a proteomic map for maGSCs and compared it to the ESCs proteome from the same mouse. We confirmed on the proteome level the ESC-like nature of maGSCs."],["dc.description.sponsorship","Deutsche Forschungsgesellschaft [SPP 1356]"],["dc.identifier.doi","10.1021/pr900565b"],["dc.identifier.isi","000272339100009"],["dc.identifier.pmid","19810753"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55810"],["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","Multipotent Adult Germline Stem Cells and Embryonic Stem Cells: Comparative Proteomic Approach"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]