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Review
. 2019 Aug;18(2):983-989.
doi: 10.3892/ol.2019.10458. Epub 2019 Jun 7.

ST6GAL1: A key player in cancer

Rebecca Garnham  1 , Emma Scott  1 , Karen E Livermore  1 , Jennifer Munkley  1
Affiliations
Review

ST6GAL1: A key player in cancer

Rebecca Garnham et al. Oncol Lett. 2019 Aug.

Abstract

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.

Keywords: ST6 β-galactoside α-2,6- sialyltransferase 1; glycans; glycosylation; hallmarks of cancer; sialylation.

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Figures

Figure 1.
Figure 1.
The role of ST6 β-galactoside α-2,6-sialyltransferase 1 in the hallmarks of cancer. Image created using BioRender.
See this image and copyright information in PMC

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