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

Rohitesh Gupta, Frank Leon, Sanchita Rauth, Surinder K. Batra, Moorthy P. Ponnusamy

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

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.

Original languageEnglish (US)
JournalCells
Volume9
Issue number2
DOIs
StatePublished - Feb 14 2020

Keywords

  • cancer
  • glycosylation
  • metastasis

ASJC Scopus subject areas

  • Medicine(all)

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