N-Glycan matrix-assisted laser desorption/ionization mass spectrometry imaging protocol for formalin-fixed paraffin-embedded tissues

Matthew T. Briggs, Yin Ying Ho, Gurjeet Kaur, Martin K. Oehler, Arun V. Everest-Dass, Nicolle H. Packer, Peter Hoffmann*

*Corresponding author for this work

    Research output: Contribution to journalArticle

    13 Citations (Scopus)

    Abstract

    Rationale: Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) of the proteome of a tissue has been an established technique for the past decade. In the last few years, MALDI-MSI of the N-glycome has emerged as a novel MALDI-MSI technique. To assess the accuracy and clinical significance of the N-linked glycan spatial distribution, we have developed a method that utilises MALDI-MSI followed by liquid chromatography coupled to tandem mass spectrometry (LC/MS/MS) in order to assign glycan structures to the differentiating MALDI-MSI glycan masses released from the tissue glycoproteins.

    Methods and Results: Our workflow presents a comprehensive list of instructions on how to (i) apply MALDI-MSI to spatially map the N-glycome across formalin-fixed paraffin-embedded (FFPE) clinical samples, (ii) structurally characterise N-glycans extracted from consecutive FFPE tissue sections by LC/MS/MS, and (iii) match relevant N-glycan masses from MALDI-MSI with confirmed N-glycan structures determined by LC/MS/MS.

    Conclusions: Our protocol provides groups that are new to this technique with instructions how to establish N-glycan MALDI-MSI in their laboratory. Furthermore, the method assigns N-glycan structural detail to the masses obtained in the MALDI-MS image.

    Original languageEnglish
    Pages (from-to)825-841
    Number of pages17
    JournalRapid Communications in Mass Spectrometry
    Volume31
    Issue number10
    DOIs
    Publication statusPublished - 30 May 2017

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