Translating N-Glycan analytical applications into clinical strategies for ovarian cancer

Matthew T. Briggs, Mark R. Condina, Manuela Klingler-Hoffmann, Georgia Arentz, Arun V. Everest-Dass, Gurjeet Kaur, Martin K. Oehler, Nicolle H. Packer, Peter Hoffmann*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


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.

Original languageEnglish
Article number1800099
Number of pages15
JournalProteomics - Clinical Applications
Issue number3
Early online date27 Oct 2018
Publication statusPublished - May 2019


  • N-glycan
  • mass spectrometry imaging
  • ovarian cancer
  • FFPE
  • tissue


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