Linking mass spectrometric imaging and traditional peptidomics: a validation in the obese mouse model
- Author
- Laurens Minerva, Kurt Boonen, Gerben Menschaert (UGent) , Bart Landuyt, Geert Baggerman and Lut Arckens
- 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
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-2033379
- MLA
- Minerva, Laurens, et al. “Linking Mass Spectrometric Imaging and Traditional Peptidomics: A Validation in the Obese Mouse Model.” ANALYTICAL CHEMISTRY, vol. 83, no. 20, 2011, pp. 7682–91, doi:10.1021/ac200888j.
- 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. https://doi.org/10.1021/ac200888j
- 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): 7682–91. https://doi.org/10.1021/ac200888j.
- 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. doi:10.1021/ac200888j.
- 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}},
}
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