Translating N‐glycan analytical applications into clinical strategies for ovarian cancer

Autor: Arun V. Everest-Dass, Martin K. Oehler, Mark R. Condina, Gurjeet Kaur, Manuela Klingler-Hoffmann, Matthew T. Briggs, Georgia Arentz, Nicolle H. Packer, Peter Hoffmann
Přispěvatelé: Briggs, Matthew T, Condina, Mark R, Klingler-Hoffmann, Manuela, Arentz, Georgia, Everest-Dass, Arun V, Kaur, Gurjeet, Oehler, Martin K, Packer, Nicolle H, Hoffmann, Peter
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Popis: Protein glycosylation, particularly N‐linked glycosylation, is a complex post‐translational modification (PTM), which plays an important role in protein folding and conformation, regulating protein stability and activity, cell‐cell interaction, and cell signalling pathways. This review focuses on analytical techniques, primarily mass spectrometry‐based techniques, to qualitatively and quantitatively assess N‐glycosylation while successfully characterising compositional, structural and linkage features with high specificity and sensitivity. The analytical techniques explored in this review include liquid chromatography electrospray ionisation tandem mass spectrometry (LC‐ESI‐MS/MS) and matrix‐assisted laser desorption/ionisation time‐of‐flight mass spectrometry (MALDI‐TOF‐MS), which have been used to analyse clinical samples, such as serum, plasma, ascites and tissue. Targeting the aberrant N‐glycosylation patterns observed in MALDI mass spectrometry imaging (MSI) offers a platform to visualise N‐glycans in tissue‐specific regions. Our 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 identified specific N‐glycan differences that improve our understanding of the tumour microenvironment and potentially improve therapeutic strategies for the clinic. Refereed/Peer-reviewed
Databáze: OpenAIRE