Translating N-Glycan Analytical Applications into Clinical Strategies for Ovarian Cancer
Date
2019
Authors
Briggs, M.T.
Condina, M.R.
Klingler-Hoffmann, M.
Arentz, G.
Everest-Dass, A.V.
Kaur, G.
Oehler, M.K.
Packer, N.H.
Hoffmann, P.
Editors
Advisors
Journal Title
Journal ISSN
Volume Title
Type:
Journal article
Citation
Proteomics - Clinical Applications, 2019; 13(3):1-5
Statement of Responsibility
Conference Name
Abstract
Protein glycosylation, particularly N-linked glycosylation, is a complex posttranslational modification (PTM), which plays an important role in protein folding and conformation, regulating protein stability and activity, cell-cell interaction, and cell signaling pathways. This review focuses on analytical techniques, primarily MS-based techniques, to qualitatively and quantitatively assess N-glycosylation while successfully characterizing compositional, structural, and linkage features with high specificity and sensitivity. The analytical techniques explored in this review include LC-ESI-MS/MS and MALDI time-of-flight MS (MALDI-TOF-MS), which have been used to analyze clinical samples, such as serum, plasma, ascites, and tissue. Targeting the aberrant N-glycosylation patterns observed in MALDI-MS imaging (MSI) offers a platform to visualize N-glycans in tissue-specific regions. The studies on the intra-patient (i.e., a comparison of tissue-specific regions from the same patient) and inter-patient (i.e., a comparison of tissue-specific regions between different patients) variation of early- and late-stage ovarian cancer (OC) patients identify specific N-glycan differences that improve understanding of the tumor microenvironment and potentially improve therapeutic strategies for the clinic.
School/Discipline
Dissertation Note
Provenance
Description
Access Status
Rights
Copyright 2018 Wiley
Access Condition Notes: Accepted manuscript available after 1 January 2020