Translating N-Glycan Analytical Applications Into Clinical Strategies for Ovarian Cancer

Proteomics Clin Appl. 2019 May;13(3):e1800099. doi: 10.1002/prca.201800099. Epub 2018 Nov 9.

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.

Keywords: FFPE; MALDI; N-glycan; mass spectrometry imaging; ovarian cancer; tissue.

Publication types

  • Review

MeSH terms

  • Chemistry Techniques, Analytical*
  • Female
  • Humans
  • Mass Spectrometry
  • Ovarian Neoplasms / metabolism*
  • Polysaccharides / metabolism*

Substances

  • Polysaccharides