Journal
RAPID COMMUNICATIONS IN MASS SPECTROMETRY
Volume 31, Issue 10, Pages 825-841Publisher
WILEY
DOI: 10.1002/rcm.7845
Keywords
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Funding
- Australian Research Council [LP110100693]
- Bioplatforms Australia
- Government of South Australia
- ARC CoE in NanoScale BioPhotonics [ARC CE140100003]
- Australian Research Council [LP110100693] Funding Source: Australian Research Council
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RationaleMatrix-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 ResultsOur 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. ConclusionsOur 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. Copyright (c) 2017 John Wiley & Sons, Ltd.
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