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Anal Chem. 2016 Aug 2;88(15):7745-53. doi: 10.1021/acs.analchem.6b01739. Epub 2016 Jul 14.

Multimodal Mass Spectrometry Imaging of N-Glycans and Proteins from the Same Tissue Section.

Author information

1
Center for Proteomics and Metabolomics, Leiden University Medical Center , Leiden, The Netherlands.
2
Department of Pathology, Leiden University Medical Center , Leiden, The Netherlands.
3
Department of Surgery, Leiden University Medical Center , Leiden, The Netherlands.
4
Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina , Charleston, South Carolina 29425, United States.
5
Department of Microbiology and Immunology, College of Medicine, Drexel University , Philadelphia, Pennsylvania 19129, United States.
6
Fondazione Pisana per la Scienza ONLUS , Pisa, Italy.

Abstract

On-tissue digestion matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) can be used to record spatially correlated molecular information from formalin-fixed, paraffin-embedded (FFPE) tissue sections. In this work, we present the in situ multimodal analysis of N-linked glycans and proteins from the same FFPE tissue section. The robustness and applicability of the method are demonstrated for several tumors, including epithelial and mesenchymal tumor types. Major analytical aspects, such as lateral diffusion of the analyte molecules and differences in measurement sensitivity due to the additional sample preparation methods, have been investigated for both N-glycans and proteolytic peptides. By combining the MSI approach with extract analysis, we were also able to assess which mass spectral peaks generated by MALDI-MSI could be assigned to unique N-glycan and peptide identities.

PMID:
27373711
DOI:
10.1021/acs.analchem.6b01739
[Indexed for MEDLINE]

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