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

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

[["dc.bibliographiccitation.firstpage","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"]]