Trends in oligomannosylation and α1,2-mannosidase expression in human cancers
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Sayantani Chatterjee1, Julian Ugonotti1, Ling Y. Lee1, Arun Everest-Dass2, Rebeca Kawahara1,* and Morten Thaysen-Andersen1,3,*
1 Department of Molecular Sciences, Macquarie University, Sydney, Australia
2 Institute for Glycomics, Griffith University, Gold Coast, Australia
3 Biomolecular Discovery Research Centre (BDRC), Macquarie University, Sydney, Australia
* Joint senior authors
Keywords: oligomannose; α1,2-mannosidase; cancer; glycomics; mass spectrometry
Received: May 12, 2021 Accepted: August 18, 2021 Published: October 12, 2021
Aberrant protein glycosylation is a prominent cancer feature. While many tumour-associated glycoepitopes have been reported, advances in glycoanalytics continue to uncover new associations between glycosylation and cancer. Guided by a comprehensive literature survey suggesting that oligomannosylation (Man5–9 GlcNAc2) is a widespread and often regulated glycosignature in human cancers, we here revisit a valuable compilation of nearly 500 porous graphitized carbon LC-MS/MS N-glycomics datasets acquired across 11 human cancer types to systematically test for oligomannose-cancer associations. Firstly, the quantitative glycomics data obtained across 34 cancerous cell lines demonstrated that oligomannosylation is a pan-cancer feature spanning in a wide abundance range. In keeping with literature, our quantitative glycomics data of tumour and matching control tissues and new MALDI-MS imaging data of tissue microarrays showed a strong cancer-associated elevation of oligomannosylation in both basal cell (p = 1.78 × 10–12) and squamous cell (p = 1.23 × 10–11) skin cancer and colorectal cancer (p = 8.0 × 10–4). The glycomics data also indicated that some cancer types including gastric and liver cancer exhibit unchanged or reduced oligomannose levels, observations also supported by literature and MALDI-MS imaging data. Finally, expression data from public cancer repositories indicated that several α1,2-mannosidases are regulated in tumour tissues suggesting that these glycan-processing enzymes may contribute to the cancer-associated modulation of oligomannosylation. This omics-centric study has compiled robust glycomics and enzyme expression data revealing interesting molecular trends that open avenues to better understand the role of oligomannosylation in human cancers.
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