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ST6GAL1-mediated aberrant sialylation promotes prostate cancer progression

Scott, Emma, Goode, Emily Archer, Garnham, Rebecca, Hodgson, Kirtsy, Orozco-Moreno, Margarita, Turner, Helen, Livermore, Karen, Kyla, Nangkana Putri, Fiona, Frame M, Bermudez, Abel, Marques, Fernando Jose Garcia, McClurg, Urszula L, Wilson, Laura, Thomas, Huw, Buskin, Adriana, Hepburn, Anastasia, Duxfield, Adam, Bastian, Kayla, Pye, Hayley, Arredondo, Hector M, Hysenaj, Gerald, Heavey, Susan, Stopka-Farooqui, Urszula, Haider, Aiman, Freeman, Alex, Singh, Saurabh, Johnston, Edward W, Punwani, Shonit, Knight, Bridget, McCullagh, Paul, McGrath, John, Crundwell, Malcolm, Harries, Lorna, Heer, Rakesh, Maitland, Norman J, Whitaker, Hayley, Pitteri, Sharon, Troyer, Dean A, Wang, Ning, Elliott, David J, Drake, Richard R and Munkley, Jennifer (2023) ST6GAL1-mediated aberrant sialylation promotes prostate cancer progression. Journal of Pathology, 261 (1). pp. 71-84. ISSN 1096-9896

Item Type: Article


Aberrant glycosylation is a universal feature of cancer cells, and cancer-associated glycans have been detected in virtually every cancer type. A common change in tumour cell glycosylation is an increase in α2,6 sialylation of N-glycans, a modification driven by the sialyltransferase ST6GAL1. ST6GAL1 is overexpressed in numerous cancer types, and sialylated glycans are fundamental for tumour growth, metastasis, immune evasion, and drug resistance, but the role of ST6GAL1 in prostate cancer is poorly understood. Here, we analyse matched cancer and normal tissue samples from 200 patients and verify that ST6GAL1 is upregulated in prostate cancer tissue. Using MALDI imaging mass spectrometry (MALDI-IMS), we identify larger branched α2,6 sialylated N-glycans that show specificity to prostate tumour tissue. We also monitored ST6GAL1 in plasma samples from >400 patients and reveal ST6GAL1 levels are significantly increased in the blood of men with prostate cancer. Using both in vitro and in vivo studies, we demonstrate that ST6GAL1 promotes prostate tumour growth and invasion. Our findings show ST6GAL1 introduces α2,6 sialylated N-glycans on prostate cancer cells and raise the possibility that prostate cancer cells can secrete active ST6GAL1 enzyme capable of remodelling glycans on the surface of other cells. Furthermore, we find α2,6 sialylated N-glycans expressed by prostate cancer cells can be targeted using the sialyltransferase inhibitor P-3FAX-Neu5Ac. Our study identifies an important role for ST6GAL1 and α2,6 sialylated N-glycans in prostate cancer progression and highlights the opportunity to inhibit abnormal sialylation for the development of new prostate cancer therapeutics.

The Journal of Pathology - 2023 - Scott - ST6GAL1‐mediated aberrant sialylation promotes prostate cancer progression.pdf
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Uncontrolled Keywords: ST6GAL1; prostate cancer; glycosylation; sialylation; sialic acid; N-glycans
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Depositing User: Rebecca Garnham


Item ID: 17648
Identification Number:
ISSN: 1096-9896
Official URL:

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Catalogue record

Date Deposited: 28 Jun 2024 13:23
Last Modified: 28 Jun 2024 13:30


Author: Emma Scott
Author: Emily Archer Goode
Author: Rebecca Garnham
Author: Kirtsy Hodgson
Author: Margarita Orozco-Moreno
Author: Helen Turner
Author: Karen Livermore
Author: Nangkana Putri Kyla
Author: Frame M Fiona
Author: Abel Bermudez
Author: Fernando Jose Garcia Marques
Author: Urszula L McClurg
Author: Laura Wilson
Author: Huw Thomas
Author: Adriana Buskin
Author: Anastasia Hepburn
Author: Adam Duxfield
Author: Kayla Bastian
Author: Hayley Pye
Author: Hector M Arredondo
Author: Gerald Hysenaj
Author: Susan Heavey
Author: Urszula Stopka-Farooqui
Author: Aiman Haider
Author: Alex Freeman
Author: Saurabh Singh
Author: Edward W Johnston
Author: Shonit Punwani
Author: Bridget Knight
Author: Paul McCullagh
Author: John McGrath
Author: Malcolm Crundwell
Author: Lorna Harries
Author: Rakesh Heer
Author: Norman J Maitland
Author: Hayley Whitaker
Author: Sharon Pitteri
Author: Dean A Troyer
Author: Ning Wang
Author: David J Elliott
Author: Richard R Drake
Author: Jennifer Munkley

University Divisions

Faculty of Health Sciences and Wellbeing > School of Medicine


Sciences > Health Sciences

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