Poster Presentation HUPO 2019 - 18th Human Proteome Organization World Congress

Monitoring of N-linked Glycans in Endometrial Cancer (#726)

Parul Mittal 1 , Manuela Klingler-Hoffmann 2 , Matthew Briggs 2 , Martin Oehler 3 , Peter Hoffmann 2
  1. Adelaide Proteomics Centre, School of Biological Sciences, University of Adelaide, Adealaide, SA, Australia
  2. University of South Australia, Mawson Lakes, SA, Australia
  3. Department of Gynaecological Oncology, Royal Adelaide Hospital, Adelaide, SA, Australia

Protein glycosylation is a posttranslational modification, which can result in functional changes of the glycoproteins and can play a key role in cancer progression and treatment. Here, we have analysed formalin fixed paraffin embedded (FFPE) endometrial cancer and adjacent tissues to explore tissue specific N-linked glycan abundance using glycan matrix assisted laser desorption ionisation mass spectrometry imaging (MALDI MSI). We have used single sections and tissue microarrays (TMA) in our analysis. Identification of discriminative m/z values was achieved using porous graphitized carbon liquid chromatography (PGC-LC) and collision induced electrospray negative mode MS fragmentation analysis (ESI-MS/MS). High mannose glycan structures were predominately detected in the tumour regions, while complex bi- and tri-antennary structures were observed in the normal/adjacent regions, indicating a biological role for these modifications.  In summary, tumour and normal regions were clearly distinguished based on their N-glycan distributions.