Advanced search
1 file | 963.26 KB Add to list

Linking mass spectrometric imaging and traditional peptidomics: a validation in the obese mouse model

(2011) ANALYTICAL CHEMISTRY. 83(20). p.7682-7691
Author
Organization
Abstract
MALDI mass spectrometry imaging (MSI) is a promising technique in the field of molecular (immuno)histology but is confronted with the problematic large-scale identification of peptides from thin tissue sections. In this study we present a workflow that significantly increased the number of identified peptides in a given MALDI-MSI data set and we evaluated its power concerning relative peptide quantifications. Fourier transform mass spectrometry (FTMS) profiling on matrix-coated thin tissue sections allowed us to align spectra of different MS sources, matching identical peaks in the process, thus linking MSI data to tandem mass spectrometry (MS/MS) on one hand and semiquantitative liquid chromatography (LC)/MS data on the other. Bonanza clustering was applied in order to group MS/MS spectra of structurally related peptides, making it possible to infer the identity of MSI-detected compounds based on identified members within the same cluster, effectively increasing the number of identifications in a single MSI data set. Out of 136 detected peptides with MALDI-MSI, we were able to identify 46 peptides. For 31 of these, a LC/quadrupole time-of-flight (QTOF) counterpart was detected, and we observed similar obese (ob/ob) to wild-type (wt) peak intensity ratios for 18 peptides. This workflow significantly increased the number of identifications of peptide masses detected with MALDI-MSI and evaluated the power of this imaging method for relative quantification of peptide levels between experimental conditions.
Keywords
DIFFERENCE GEL-ELECTROPHORESIS, EXPRESSION DIFFERENCES, GENETICALLY-OBESE, OB/OB MICE, IDENTIFICATION, NEUROPEPTIDES, PANCREAS, DISCOVERY, PEPTIDES, SOFTWARE

Downloads

  • (...).pdf
    • full text
    • |
    • UGent only
    • |
    • PDF
    • |
    • 963.26 KB

Citation

Please use this url to cite or link to this publication:

MLA
Minerva, Laurens, Kurt Boonen, Gerben Menschaert, et al. “Linking Mass Spectrometric Imaging and Traditional Peptidomics: a Validation in the Obese Mouse Model.” ANALYTICAL CHEMISTRY 83.20 (2011): 7682–7691. Print.
APA
Minerva, L., Boonen, K., Menschaert, G., Landuyt, B., Baggerman, G., & Arckens, L. (2011). Linking mass spectrometric imaging and traditional peptidomics: a validation in the obese mouse model. ANALYTICAL CHEMISTRY, 83(20), 7682–7691.
Chicago author-date
Minerva, Laurens, Kurt Boonen, Gerben Menschaert, Bart Landuyt, Geert Baggerman, and Lut Arckens. 2011. “Linking Mass Spectrometric Imaging and Traditional Peptidomics: a Validation in the Obese Mouse Model.” Analytical Chemistry 83 (20): 7682–7691.
Chicago author-date (all authors)
Minerva, Laurens, Kurt Boonen, Gerben Menschaert, Bart Landuyt, Geert Baggerman, and Lut Arckens. 2011. “Linking Mass Spectrometric Imaging and Traditional Peptidomics: a Validation in the Obese Mouse Model.” Analytical Chemistry 83 (20): 7682–7691.
Vancouver
1.
Minerva L, Boonen K, Menschaert G, Landuyt B, Baggerman G, Arckens L. Linking mass spectrometric imaging and traditional peptidomics: a validation in the obese mouse model. ANALYTICAL CHEMISTRY. 2011;83(20):7682–91.
IEEE
[1]
L. Minerva, K. Boonen, G. Menschaert, B. Landuyt, G. Baggerman, and L. Arckens, “Linking mass spectrometric imaging and traditional peptidomics: a validation in the obese mouse model,” ANALYTICAL CHEMISTRY, vol. 83, no. 20, pp. 7682–7691, 2011.
@article{2033379,
  abstract     = {MALDI mass spectrometry imaging (MSI) is a promising technique in the field of molecular (immuno)histology but is confronted with the problematic large-scale identification of peptides from thin tissue sections. In this study we present a workflow that significantly increased the number of identified peptides in a given MALDI-MSI data set and we evaluated its power concerning relative peptide quantifications. Fourier transform mass spectrometry (FTMS) profiling on matrix-coated thin tissue sections allowed us to align spectra of different MS sources, matching identical peaks in the process, thus linking MSI data to tandem mass spectrometry (MS/MS) on one hand and semiquantitative liquid chromatography (LC)/MS data on the other. Bonanza clustering was applied in order to group MS/MS spectra of structurally related peptides, making it possible to infer the identity of MSI-detected compounds based on identified members within the same cluster, effectively increasing the number of identifications in a single MSI data set. Out of 136 detected peptides with MALDI-MSI, we were able to identify 46 peptides. For 31 of these, a LC/quadrupole time-of-flight (QTOF) counterpart was detected, and we observed similar obese (ob/ob) to wild-type (wt) peak intensity ratios for 18 peptides. This workflow significantly increased the number of identifications of peptide masses detected with MALDI-MSI and evaluated the power of this imaging method for relative quantification of peptide levels between experimental conditions.},
  author       = {Minerva, Laurens and Boonen, Kurt and Menschaert, Gerben and Landuyt, Bart and Baggerman, Geert and Arckens, Lut},
  issn         = {0003-2700},
  journal      = {ANALYTICAL CHEMISTRY},
  keywords     = {DIFFERENCE GEL-ELECTROPHORESIS,EXPRESSION DIFFERENCES,GENETICALLY-OBESE,OB/OB MICE,IDENTIFICATION,NEUROPEPTIDES,PANCREAS,DISCOVERY,PEPTIDES,SOFTWARE},
  language     = {eng},
  number       = {20},
  pages        = {7682--7691},
  title        = {Linking mass spectrometric imaging and traditional peptidomics: a validation in the obese mouse model},
  url          = {http://dx.doi.org/10.1021/ac200888j},
  volume       = {83},
  year         = {2011},
}

Altmetric
View in Altmetric
Web of Science
Times cited: