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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

Kris Gevaert UGent, Jozef Pinxteren, Hans Demol UGent, Koen Hugelier, An Staes UGent, Jozef Van Damme UGent, Lennart Martens UGent and Joël Vandekerckhove UGent (2006) JOURNAL OF PROTEOME RESEARCH. 5(6). p.1415-1428
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
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
journal title
JOURNAL OF PROTEOME RESEARCH
J. Proteome Res.
volume
5
issue
6
pages
1415 - 1428
Web of Science type
Article
Web of Science id
000237973400013
JCR category
BIOCHEMICAL RESEARCH METHODS
JCR impact factor
5.151 (2006)
JCR rank
7/56 (2006)
JCR quartile
1 (2006)
ISSN
1535-3893
DOI
10.1021/pr060026a
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
346273
handle
http://hdl.handle.net/1854/LU-346273
date created
2006-09-20 10:38:00
date last changed
2012-03-02 16:54:03
@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},
}

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.