| Timetable |
| Download Conference Program |
| Download All Abstracts |
| Zoom Access |
| Corporate Program |
Poster Presentations
Day 1, June 22（Sun.）
Room P (Maesato East, Foyer, Ocean Wing)
- 1P-PM-19
Glycoproteomic Characterization of Colorectal Cancer FFPE Tissue Sections.
(Yokohama City Univ.)
oManato Oishi, Daisuke Takakura, Nana Kawasaki
Changes in glycosyltransferase expression in cancer can cause changes in N-glycosylation, and differential analysis of N-glycosylation between tumor and nontumor regions has the potential to reveal new therapeutic targets and diagnostic markers.
The use of formalin-fixed paraffin-embedded (FFPE) tissue sections allow for targeted analysis of tumor regions, however, glycoproteomics revealed only a few cancer-associated glycoproteins in FFPE tissue sections due to the difficulties in extracting glycopeptides from trace amounts of FFPE tissue sections. In this study, we created an efficient glycoproteomic approach using FFPE tissue sections with cellulose-based solid-phase extraction (C-SPE).
Glycoproteins were enriched from tumor and nontumor regions of FFPE tissue sections from the same CRC patient with C-SPE. Differential analysis using LC/MS/MS revealed that 648 glycoforms from 90 different glycoproteins were altered in tumor regions. Particularly, fucosylated and high mannose-type glycans were elevated in carcinoembryonic antigen-related cell adhesion molecule 5, and high mannose-type glycans were elevated at Asn103/261 in lysosomal-associated membrane protein 1, which is consistent with prior research using frozen tissue. However, this study discovered changes in the glycan modifications of myeloperoxidase, azurocidin, mucin 2, and tenascin. These findings suggest that this method is reliable and useful for glycoproteomics in FFPE tissue sections.