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Hydrophilic Interaction Chromatography Coupled to Ultraviolet Photodissociation Affords Identification, Localization, and Relative Quantitation of Glycans on Intact Glycoproteins

https://doi.org/10.1021/acs.jproteome.4c00600

James, Virginia K; van_der_Zon, Annika_A M; Escobar, Edwin E; Dunham, Sean D; Gargano, Andrea_F G; Brodbelt, Jennifer S (October 2024, Journal of Proteome Research)

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Conformational Characterization of Peptides and Proteins by 193 nm Ultraviolet Photodissociation in the Collision Cell of a Trapped Ion Mobility Spectrometry-Time-of-Flight Mass Spectrometer

https://doi.org/10.1021/acs.analchem.4c02686

Butalewicz, Jamie P; Escobar, Edwin E; Wootton, Christopher A; Theisen, Alina; Park, Melvin A; Seeley, Erin H; Brodbelt, Jennifer S (October 2024, Analytical Chemistry)

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

https://doi.org/10.3390/cancers15041224

Escobar, Edwin E.; Seeley, Erin H.; Serrano-Negrón, Jesús E.; Vocadlo, David J.; Brodbelt, Jennifer S. (February 2023, Cancers)

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.
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Nanohydrophobic Interaction Chromatography Coupled to Ultraviolet Photodissociation Mass Spectrometry for the Analysis of Intact Proteins in Low Charge States

https://doi.org/10.1021/acs.jproteome.2c00450

Blevins, Molly S.; Juetten, Kyle J.; James, Virginia K.; Butalewicz, Jamie P.; Escobar, Edwin E.; Lanzillotti, Michael B.; Sanders, James D.; Fort, Kyle L.; Brodbelt, Jennifer S. (October 2022, Journal of Proteome Research)

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