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A Systematic Review on the Implications of O-linked Glycan Branching and Truncating Enzymes on Cancer Progression and Metastasis

1
Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68105, USA
2
Fred and Pamela Buffett Cancer Center, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, NE 681980-5900, USA
3
Department of Pathology and Microbiology, UNMC, Omaha, NE 68198-5900, USA
*
Authors to whom correspondence should be addressed.
Equal contribution.
Cells 2020, 9(2), 446; https://doi.org/10.3390/cells9020446
Received: 21 January 2020 / Revised: 10 February 2020 / Accepted: 12 February 2020 / Published: 14 February 2020
Glycosylation is the most commonly occurring post-translational modifications, and is believed to modify over 50% of all proteins. The process of glycan modification is directed by different glycosyltransferases, depending on the cell in which it is expressed. These small carbohydrate molecules consist of multiple glycan families that facilitate cell–cell interactions, protein interactions, and downstream signaling. An alteration of several types of O-glycan core structures have been implicated in multiple cancers, largely due to differential glycosyltransferase expression or activity. Consequently, aberrant O-linked glycosylation has been extensively demonstrated to affect biological function and protein integrity that directly result in cancer growth and progression of several diseases. Herein, we provide a comprehensive review of several initiating enzymes involved in the synthesis of O-linked glycosylation that significantly contribute to a number of different cancers.
Keywords: glycosylation; cancer; metastasis glycosylation; cancer; metastasis
MDPI and ACS Style

Gupta, R.; Leon, F.; Rauth, S.; Batra, S.K.; Ponnusamy, M.P. A Systematic Review on the Implications of O-linked Glycan Branching and Truncating Enzymes on Cancer Progression and Metastasis. Cells 2020, 9, 446.

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