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ST6GAL1: A key player in cancer (Review)

Lookup NU author(s): Rebecca Garnham, Dr Emma Scott, Karen Livermore, Dr Jennifer Munkley



This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (CC BY-NC-ND).


Aberrant glycosylation is a universal feature of cancer cells and there is now overwhelming evidence that glycans can modulate pathways intrinsic to tumour cell biology. Glycans are important in all of the cancer hallmarks and there is a renewed interest in the glycomic profiling of tumours to improve early diagnosis, determine patient prognosis and identify targets for therapeutic intervention. One of the most widely occurring cancer associated changes in glycosylation is abnormal sialylation which is often accompanied by changes in sialyltransferase activity. Several sialyltransferases are implicated in cancer, but in recent years ST6 β‑galactoside α‑2,6‑sialyltransferase 1 (ST6GAL1) has become increasingly dominant in the literature. ST6GAL1 catalyses the addition of α2,6‑linked sialic acids to terminal N‑glycans and can modify glycoproteins and/or glycolipids. ST6GAL1 is upregulated in numerous types of cancer (including pancreatic, prostate, breast and ovarian cancer) and can promote growth, survival and metastasis. The present review discusses ST6GAL in relation to the hallmarks of cancer, and highlights its key role in multiple mechanisms intrinsic to tumour cell biology.

Publication metadata

Author(s): Garnham R, Scott E, Livermore KE, Munkley J

Publication type: Review

Publication status: Published

Journal: Oncology Letters

Year: 2019

Volume: 18

Issue: 2

Pages: 983-989

Print publication date: 01/08/2019

Online publication date: 07/06/2019

Acceptance date: 04/06/2019

ISSN (print): 1792-1074

ISSN (electronic): 1792-1082


DOI: 10.3892/ol.2019.10458


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