Cover Image

Identification of MALDI imaging proteolytic peptides using LC-MS/MS-based biomarker discovery data: a proof of concept

Show other versions (1)

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 alternati...

Full description

Saved in:
Bibliographic Details
Main Authors: Longuespée, Rémi (Author) , Kazdal, Daniel (Author) , Zgorzelski, Christiane (Author) , Kriegsmann, Katharina (Author) , Schirmacher, Peter (Author) , Fresnais, Margaux (Author) , Kriegsmann, Mark (Author)
Format: Article (Journal)
Language:English
Published: 2019
In: Proteomics. Clinical applications
Year: 2018, Volume: 13, Issue: 1
ISSN:1862-8354
DOI:10.1002/prca.201800158
Online Access:Verlag, Volltext: https://doi.org/10.1002/prca.201800158
Verlag: https://onlinelibrary.wiley.com/doi/abs/10.1002/prca.201800158
Get full text
Author Notes: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
Description
Summary: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.
Item Description:Published online: December 19, 2018
Gesehen am 30.10.2019
Physical Description:Online Resource
ISSN:1862-8354
DOI:10.1002/prca.201800158

Similar Items