Blaschke, Sabine

[["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.firstpage","1280"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","PROTEOMICS - CLINICAL APPLICATIONS"],["dc.bibliographiccitation.lastpage","1284"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Baechle, Daniel"],["dc.contributor.author","Sparbier, Katrin"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Blaschke, Sabine"],["dc.contributor.author","Mueller, Gerhard-Anton"],["dc.contributor.author","Kostrzewa, Markus"],["dc.contributor.author","Flad, Thomas"],["dc.date.accessioned","2018-11-07T10:58:23Z"],["dc.date.available","2018-11-07T10:58:23Z"],["dc.date.issued","2007"],["dc.description.abstract","In routine clinical diagnostics, peptide biomarkers are most commonly quantified using immunological techniques but these methods often lack sensitivity and/or specificity. Hence, quantitative mass spectrometry detection is desirable as an alternative diagnostic tool. To date, quantitative mass spectrometry is mostly based on ESI-MS coupled to LC, requiring highly sophisticated instrumentation and knowledge and is time consuming and expensive. In contrast, MALDI-TOF-MS is a very simple, sensitive and rapid method for the detection of peptide biomarkers. However, the infeasibility of absolute quantification has been a tremendous handicap to the use of MS in stable clinical diagnostics. Here, we describe the development of a technical platform based on ClinProt particles and heavy-isotope internal peptide standards for the fast and reliable preparation of samples. This combines the advantages of MALDI-TOF as a read-out system with absolute quantitation of peptide biomarkers. As a proof-of-concept, this platform was successfully employed for the absolute determination of the concentration of the highly abundant serum peptide des-Ala-Fibrinopeptide A in 45 serum samples from healthy donors. Such technology essentially contributes to the development of a stable MALDI-TOF-MS-based clinical assay."],["dc.identifier.doi","10.1002/prca.200700307"],["dc.identifier.isi","000250476600006"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50468"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1862-8346"],["dc.title","Towards stable diagnostic setups in clinical proteomics: Absolute quantitation of peptide biomarkers using MALDI-TOF-MS"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1558"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Nephrology Dialysis Transplantation"],["dc.bibliographiccitation.lastpage","1566"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Markovic-Lipkovski, Jasmina"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Klein, Gerd"],["dc.contributor.author","Flad, Thomas"],["dc.contributor.author","Klatt, Tatjana"],["dc.contributor.author","Blaschke, Sabine"],["dc.contributor.author","Wessels, Johannes Theodor"],["dc.contributor.author","Mueller, Georg Anton"],["dc.date.accessioned","2018-11-07T11:02:05Z"],["dc.date.available","2018-11-07T11:02:05Z"],["dc.date.issued","2007"],["dc.description.abstract","Background. At early stages of kidney development, the neural cell adhesion molecule (NCAM) is highly expressed on cells of the metanephrogenic mesenchyme. During maturation of the fetal kidney, NCAM gradually disappears. So far, it has been widely accepted that NCAM in the adult kidney is only expressed by nerves, and not by other cell types. Methods. NCAM expression was analysed in human adult healthy and diseased kidneys by immunohistochemistry and western blot analysis. NCAM+ renal interstitial cells were further characterized by double immunofluorescent staining using antibodies against neurofilaments, a smooth muscle actin, vimentin, alpha 5 beta 1 integrin, CD68, CD11c, HLA-DR and the potential progenitor cell markers CD34, CD117, CD133, CD24, nestin and cadherin-11. Results. In adult human kidneys, NCAM expression is restricted to rare interstitial cells with dendritic morphology, which are neurofilament-negative and predominantly localized on the corticomedullary junction. They are also negative for fibroblast cell markers, but co-express the haematopoietic stem cell markers CD34 and CD133. The number of NCAM+ interstitial cells increased in the initial phases of interstitial fibrosis. Western blot analysis of renal tissues with incipient interstitial fibrosis tissues showed the expression of the 140 kDa NCAM isoform. Conclusions. These data indicate that a rare subpopulation of NCAM+ interstitial cells could represent renal progenitors, and that NCAM+ interstitial cells can participate in the initial phase of interstitial fibrosis."],["dc.identifier.doi","10.1093/ndt/gfm006"],["dc.identifier.isi","000247474200012"],["dc.identifier.pmid","17337466"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51294"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.publisher.place","Oxford"],["dc.relation.conference","19th European Congress of Pathology"],["dc.relation.eventlocation","Ljubljana, SLOVENIA"],["dc.relation.issn","0931-0509"],["dc.title","Neural cell adhesion molecule expression on renal interstitial cells"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1442"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PROTEOMICS"],["dc.bibliographiccitation.lastpage","1450"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Sparbier, Katrin"],["dc.contributor.author","Wenzel, Thomas"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Blaschke, Sabine"],["dc.contributor.author","Mueller, Gerhard-Anton"],["dc.contributor.author","Deelder, Andre"],["dc.contributor.author","Flad, Thomas"],["dc.contributor.author","Kostrzewa, Markus"],["dc.date.accessioned","2018-11-07T08:32:28Z"],["dc.date.available","2018-11-07T08:32:28Z"],["dc.date.issued","2009"],["dc.description.abstract","The discovery of novel biomarkers by means of advanced detection tools based on proteomic analysis technologies necessitates the development of improved diagnostic methods for application in clinical routine. On the basis of three different application examples, this review presents the limitations of conventional routine diagnostic assays and illustrates the advantages of immunoaffinity enrichment combined with MALDI-TOF MS. Applying this approach increases the specificity of the analysis supporting a better diagnostic recognition, sensitivity, and differentiation of certain diseases. The use of MALDI-TOF MS as detection method facilitates the identification of modified peptides and proteins providing additional information. Further, employing respective internal standard peptides allows for relative and absolute quantitation which is mandatory in the clinical context. Although MALDI-TOF MS is not yet established for clinical routine diagnostics this technology has a high potential for improvement of clinical diagnostics and monitoring therapeutic efficacy."],["dc.description.sponsorship","BMBF [0313684B]"],["dc.identifier.doi","10.1002/pmic.200800616"],["dc.identifier.isi","000264890400004"],["dc.identifier.pmid","19235164"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6185"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17349"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1615-9853"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Immuno-MALDI-TOF MS: New perspectives for clinical applications of mass spectrometry"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]