Linking Mass Spectrometric Imaging and Traditional Peptidomics: A Validation in the Obese Mouse Model
| Autor: | Laurens Minerva, Gerben Menschaert, Bart Landuyt, Kurt Boonen, Geert Baggerman, Lut Arckens |
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| Rok vydání: | 2011 |
| Předmět: |
Proteomics
Difference gel electrophoresis Molecular Sequence Data Analytical chemistry Mice Obese Peptide Tandem mass spectrometry Mass spectrometry imaging Fourier transform ion cyclotron resonance Analytical Chemistry Mice Peptide mass fingerprinting Animals Cluster Analysis Amino Acid Sequence Pancreas Chromatography High Pressure Liquid chemistry.chemical_classification Chromatography Fourier Analysis Chemistry Mass spectrometric Disease Models Animal Tissue sections Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Peptides |
| Zdroj: | Analytical chemistry |
| ISSN: | 1520-6882 0003-2700 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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