In Situ Imaging of O-Linked β-N-Acetylglucosamine Using On-Tissue Hydrolysis and MALDI Mass Spectrometry
- Resource Type
- article
- Authors
- Edwin E. Escobar; Erin H. Seeley; Jesús E. Serrano-Negrón; David J. Vocadlo; Jennifer S. Brodbelt
- Source
- Cancers, Vol 15, Iss 4, p 1224 (2023)
- Subject
- mass spectrometry imaging
MALDI
ultraviolet photodissociation
O-glycosylation
in situ digestion
biomarkers
Neoplasms. Tumors. Oncology. Including cancer and carcinogens
RC254-282
- Language
- English
- ISSN
- 2072-6694
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.