Atanassov, Ilian

[["dc.bibliographiccitation.firstpage","4"],["dc.bibliographiccitation.journal","Annals of Anatomy"],["dc.bibliographiccitation.lastpage","10"],["dc.bibliographiccitation.volume","212"],["dc.contributor.author","Batschkus, Sarah"],["dc.contributor.author","Atanassov, Ilian"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Meyer-Marcotty, Philipp"],["dc.contributor.author","Cingöz, Gökhan"],["dc.contributor.author","Kirschneck, Christian"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Miosge, Nicolai"],["dc.date.accessioned","2018-10-10T09:10:52Z"],["dc.date.available","2018-10-10T09:10:52Z"],["dc.date.issued","2017-07"],["dc.description.abstract","Tissue engineering offers promising perspectives in the therapy of osteoarthritis. In the context of cell-based therapy, chondrogenic progenitor cells (CPCs) may be used to regenerate defects in cartilage tissue. An in-depth characterization of the secretome of CPCs is a prerequisite to this approach. In this study, a method was developed for the qualitative and quantitative analysis of the secretome of undifferentiated and differentiated CPCs. Secreted proteins from cells grown in two-dimensional as well as three-dimensional alginate cultures were extracted and analyzed by liquid chromatography/tandem mass spectrometry (LC-MS/MS). Quantitation was achieved by internal standardization using stable isotope-labeled amino acids in cell culture (SILAC). Qualitative analysis of CPC secretomes revealed ECM-components, signal proteins and growth factors most of which were also found in healthy cartilage. A quantitative comparison revealed significantly upregulated proteins with regenerative potential during differentiation, while proteins involved in catabolic metabolism were significantly downregulated. The development of methods for qualitative and quantitative analysis of the secretome of CPCs by mass spectrometry provides a foundation for the investigation of progenitor or stem cells from other sources."],["dc.fs.pkfprnr","68163"],["dc.identifier.doi","10.1016/j.aanat.2017.03.003"],["dc.identifier.fs","626873"],["dc.identifier.pmid","28365382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15929"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1618-0402"],["dc.title","Mapping the secretome of human chondrogenic progenitor cells with mass spectrometry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2947"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","PROTEOMICS"],["dc.bibliographiccitation.lastpage","2955"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Atanassov, Ilian"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2018-11-07T09:19:26Z"],["dc.date.available","2018-11-07T09:19:26Z"],["dc.date.issued","2013"],["dc.description.abstract","The in-depth analysis of complex proteome samples requires fractionation of the sample into subsamples prior to LC-MS/MS in shotgun proteomics experiments. We have established a 3D workflow for shotgun proteomics that relies on protein separation by 1D PAGE, gel fractionation, trypsin digestion, and peptide separation by in-gel IEF, prior to RP-HPLC-MS/MS. Our results show that applying peptide IEF can significantly increase the number of proteins identified from PAGE subfractionation. This method delivers deeper proteome coverage and provides a large degree of flexibility in experimentally approaching highly complex mixtures by still relying on protein separation according to molecular weight in the first dimension."],["dc.description.sponsorship","Max Planck Society"],["dc.identifier.doi","10.1002/pmic.201300035"],["dc.identifier.isi","000325489000005"],["dc.identifier.pmid","23943586"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28633"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1615-9861"],["dc.relation.issn","1615-9853"],["dc.title","Increased proteome coverage by combining PAGE and peptide isoelectric focusing: Comparative study of gel-based separation approaches"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]