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.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","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.firstpage","222"],["dc.bibliographiccitation.journal","Nephrology Dialysis Transplantation"],["dc.bibliographiccitation.lastpage","223"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Mattes, Harry"],["dc.contributor.author","Mueller, Georg Anton"],["dc.date.accessioned","2018-11-07T09:38:47Z"],["dc.date.available","2018-11-07T09:38:47Z"],["dc.date.issued","2006"],["dc.identifier.isi","000239919001307"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33135"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.publisher.place","Oxford"],["dc.relation.conference","43rd ERA-EDTA Congress"],["dc.relation.eventlocation","Glasgow, SCOTLAND"],["dc.relation.issn","0931-0509"],["dc.title","Proteomic analysis of haemo- and peritoneal dialysate fluids: Comparison of proteins dialysed with high, low flux filters and the peritoneal membrane"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1297"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Nephrology Dialysis Transplantation"],["dc.bibliographiccitation.lastpage","1300"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T11:02:56Z"],["dc.date.available","2018-11-07T11:02:56Z"],["dc.date.issued","2007"],["dc.identifier.doi","10.1093/ndt/gfl806"],["dc.identifier.isi","000246124100004"],["dc.identifier.pmid","17299005"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51501"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0931-0509"],["dc.title","Clinical proteomics - on the long way from bench to bedside?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1994"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Proteomics"],["dc.bibliographiccitation.lastpage","2007"],["dc.bibliographiccitation.volume","74"],["dc.contributor.author","Pesic, Ivana"],["dc.contributor.author","Stefanovic, Vladisav"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Cukuranovic, Rade"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Bojanic, Vladmila"],["dc.contributor.author","Koziolek, Michael"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T08:51:48Z"],["dc.date.available","2018-11-07T08:51:48Z"],["dc.date.issued","2011"],["dc.description.abstract","Endemic nephropathy (EN) is defined as a slow progressive renal tubulointestitial disease that mainly occurs in the restricted areas of the Balkan Peninsula. The complexity of the pathogenesis of EN makes its earlier diagnosis very difficult. Urine samples from healthy volunteers from EN regions, EN patients with proteinuria less than 150 mg/L and EN patients with proteinuria more than 150 mg/L, patients with acute kidney injury, patients with diabetic nephropathy and healthy volunteers from Germany were collected. The urinary proteome analyses were performed using 2-D DICE and mass spectrometry. The validation of biomarkers was investigated by two approaches (Western blot (WB) and dot blot) in successively increasing size - and partially overlapping - sample sets. Comparative and statistical analyses of the proteomics data from the different patient groups allowed the identification of six proteins (alpha-l-microglobulin, alpha-2-glycoprotein-1, beta-2-microglobulin, mannose-binding-lectin-2, protection-of-telomeresprotein-1, and superoxide-dismutase [Cu-Zn]), which were able to discriminate EN with low and high proteinuria from the other groups with high significance (p < 0.05). The reliability of the identified proteins as EN marker was underlined with high statistical significance using WB analyses (sensitivity 66.7-98% and specificity 70-100%), whereas the dot blot analyses revealed a decrease in the sensitivity and specificity of these biomarkers. (C) 2011 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.jprot.2011.05.020"],["dc.identifier.isi","000295302800016"],["dc.identifier.pmid","21635978"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22022"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1874-3919"],["dc.title","Identification and validation of six proteins as marker for endemic nephropathy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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"]]