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

(2006) JOURNAL OF PROTEOME RESEARCH. 5(6). p.1415-1428
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Abstract
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.
Keywords
STEM-CELLS, diagonal chromatography, INTEGRATED DATABASE, IN-VITRO, PROTEINS, IDENTIFICATION, ELECTROPHORESIS, ABUNDANCE, SAMPLE PREPARATION METHOD, GAS-PHASE CHEMISTRY, TANDEM MASS-SPECTROMETRY, multidimensional chromatography, gel-free proteomics, COFRADIC

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Chicago
Gevaert, Kris, Jozef Pinxteren, Hans Demol, Koen Hugelier, An Staes, Jozef Van Damme, Lennart Martens, and Joël Vandekerckhove. 2006. “Four Stage Liquid Chromatographic Selection of Methionyl Peptides for Peptide-centric Proteome Analysis: The Proteome of Human Multipotent Adult Progenitor Cells.” Journal of Proteome Research 5 (6): 1415–1428.
APA
Gevaert, K., Pinxteren, J., Demol, H., Hugelier, K., Staes, A., Van Damme, J., Martens, L., et al. (2006). Four stage liquid chromatographic selection of methionyl peptides for peptide-centric proteome analysis: the proteome of human multipotent adult progenitor cells. JOURNAL OF PROTEOME RESEARCH, 5(6), 1415–1428.
Vancouver
1.
Gevaert K, Pinxteren J, Demol H, Hugelier K, Staes A, Van Damme J, et al. Four stage liquid chromatographic selection of methionyl peptides for peptide-centric proteome analysis: the proteome of human multipotent adult progenitor cells. JOURNAL OF PROTEOME RESEARCH. 2006;5(6):1415–28.
MLA
Gevaert, Kris, Jozef Pinxteren, Hans Demol, et al. “Four Stage Liquid Chromatographic Selection of Methionyl Peptides for Peptide-centric Proteome Analysis: The Proteome of Human Multipotent Adult Progenitor Cells.” JOURNAL OF PROTEOME RESEARCH 5.6 (2006): 1415–1428. Print.
@article{346273,
  abstract     = {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.},
  author       = {Gevaert, Kris and Pinxteren, Jozef and Demol, Hans and Hugelier, Koen and Staes, An and Van Damme, Jozef and Martens, Lennart and Vandekerckhove, Jo{\"e}l},
  issn         = {1535-3893},
  journal      = {JOURNAL OF PROTEOME RESEARCH},
  keyword      = {STEM-CELLS,diagonal chromatography,INTEGRATED DATABASE,IN-VITRO,PROTEINS,IDENTIFICATION,ELECTROPHORESIS,ABUNDANCE,SAMPLE PREPARATION METHOD,GAS-PHASE CHEMISTRY,TANDEM MASS-SPECTROMETRY,multidimensional chromatography,gel-free proteomics,COFRADIC},
  language     = {eng},
  number       = {6},
  pages        = {1415--1428},
  title        = {Four stage liquid chromatographic selection of methionyl peptides for peptide-centric proteome analysis: the proteome of human multipotent adult progenitor cells},
  url          = {http://dx.doi.org/10.1021/pr060026a},
  volume       = {5},
  year         = {2006},
}

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