Four stage liquid chromatographic selection of methionyl peptides for peptide-centric proteome analysis: The proteome of human multipotent adult progenitor cells

被引:23
作者
Gevaert, K [1 ]
Pinxteren, J [1 ]
Demol, H [1 ]
Hugelier, K [1 ]
Staes, A [1 ]
Van Damme, J [1 ]
Martens, L [1 ]
Vandekerckhove, J [1 ]
机构
[1] Univ Ghent, Fac Med & Hlth Sci, Dept Biochem & Med Prot Res, B-9000 Ghent, Belgium
关键词
diagonal chromatography; gel-free proteomics; COFRADIC; multidimensional chromatography;
D O I
10.1021/pr060026a
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Serial application of strong cation-exchange and diagonal reversed-phase chromatography selecting methionyl peptides by stepwise shifting them from their reduced to their sulfoxide and sulfone forms generates a four-stage fractionation system, allowing high coverage analysis of complex proteome digests by LC-MALDI-MS/MS. Application to the proteome of a human multipotent adult progenitor cell line (MAPC) identified 2151 proteins with high confidence as on average four MS/MS-spectra were linked to each protein. Our dataset contains several novel, potential marker proteins that may be evaluated as affinity-anchors for isolating different adult stem cells in further studies. Furthermore, at least 2 tyrosine kinases that were previously linked to the self-renewal potential of stem cells were identified, validating the stemness of the analyzed cells. We also present data hinting at possible involvement of the ubiquitin/proteasome machinery in steering proliferation and/or differentiation of MAPC. Finally, following comparison of the MAPC proteome with proteomes of four human differentiated cell lines reveals differential usage of chromosomal information: compared to differentiated cells, MAPC do not appear to hold any preference for expressing genes located on specific chromosomes.
引用
收藏
页码:1415 / 1428
页数:14
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