Identification of MALDI imaging proteolytic peptides using LC-MS/MS-based biomarker discovery data

• Verfasst von: Longuespée, Rémi [VerfasserIn]
• Verfasst von: Kazdal, Daniel [VerfasserIn]
• Verfasst von: Zgorzelski, Christiane [VerfasserIn]
• Verfasst von: Kriegsmann, Katharina [VerfasserIn]
• Verfasst von: Schirmacher, Peter [VerfasserIn]
• Verfasst von: Fresnais, Margaux [VerfasserIn]
• Verfasst von: Kriegsmann, Mark [VerfasserIn]
• Titel: Identification of MALDI imaging proteolytic peptides using LC-MS/MS-based biomarker discovery data
• Titelzusatz: a proof of concept
• Verf.angabe: Rémi Longuespée, Alice Ly, Rita Casadonte, Kristina Schwamborn, Daniel Kazdal, Christiane Zgorzelski, Christine Bollwein, Katharina Kriegsmann, Wilko Weichert, Jörg Kriegsmann, Peter Schirmacher, Margaux Fresnais, Cristiano Oliveira, and Mark Kriegsmann
• Jahr: 2019
• Jahr des Originals: 2018
• Fussnoten: Published online: December 19, 2018 ; Gesehen am 30.10.2019
• Titel Quelle: Enthalten in: Proteomics / Clinical applications
• Ort Quelle: Weinheim : Wiley VCH, 2007
• Jahr Quelle: 2019
• Band/Heft Quelle: 13(2019,1) Artikel-Nummer 1800158, 5 Seiten
• ISSN Quelle: 1862-8354
• DOI: doi:10.1002/prca.201800158
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: identification
• Sach-SW: liquid chromatography tandem mass spectrometry
• Sach-SW: matrix-assisted laser desorption/ionization imaging
• Sach-SW: microproteomics
• K10plus-PPN: 1679746588

Abstract

Purpose Identification of proteolytic peptides from matrix-assisted laser desorption/ionization (MALDI) imaging remains a challenge. The low fragmentation yields obtained using in situ post source decay impairs identification. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) is an alternative to in situ MS/MS, but leads to multiple identification candidates for a given mass. The authors propose to use LC-MS/MS-based biomarker discovery results to reliably identify proteolytic peptides from MALDI imaging. Experimental design The authors defined m/z values of interest for high grade squamous intraepithelial lesion (HSIL) by MALDI imaging. In parallel the authors used data from a biomarker discovery study to correlate m/z from MALDI imaging with masses of peptides identified by LC-MS/MS in HSIL. The authors neglected candidates that were not significantly more abundant in HSIL according to the biomarker discovery investigation. Results The authors assigned identifications to three m/z of interest. The number of possible identifiers for MALDI imaging m/z peaks using LC-MS/MS-based biomarker discovery studies was reduced by about tenfold compared using a single LC-MS/MS experiment. One peptide identification candidate was validated by immunohistochemistry. Conclusion and clinical relevance This concept combines LC-MS/MS-based quantitative proteomics with MALDI imaging and allows reliable peptide identification. Public datasets from LC-MS/MS biomarker discovery experiments will be useful to identify MALDI imaging m/z peaks.