In Situ Imaging of O-Linked β-N-Acetylglucosamine Using On-Tissue Hydrolysis and MALDI Mass Spectrometry

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Abstract
Post-translational O-glycosylation of proteins via the addition of N-acetylglucosamine (O-GlcNAc) is a regulator of many aspects of cellular physiology. Processes driven by perturbed dynamics of O-GlcNAcylation modification have been implicated in cancer development. Variability in O-GlcNAcylation is emerging as a metabolic biomarker of many cancers. Here, we evaluate the use of MALDI-mass spectrometry imaging (MSI) to visualize the location of O-GlcNAcylated proteins in tissue sections by mapping GlcNAc that has been released by the enzymatic hydrolysis of glycoproteins using an O-GlcNAc hydrolase. We use this strategy to monitor O-GlcNAc within hepatic VX2 tumor tissue. We show that increased O-GlcNAc is found within both viable tumor and tumor margin regions, implicating GlcNAc in tumor progression.
Funding Information
  • National Science Foundation (CHE-2203602, CPRIT RP190617, F-1155, PJT-148732, PJT-156202)
  • Cancer Prevention and Research Institute of Texas (CHE-2203602, CPRIT RP190617, F-1155, PJT-148732, PJT-156202)
  • Welch Foundation (CHE-2203602, CPRIT RP190617, F-1155, PJT-148732, PJT-156202)
  • Canadian Institutes of Health Research (CHE-2203602, CPRIT RP190617, F-1155, PJT-148732, PJT-156202)

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