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AIMS Medical Science

2016, Volume 3, Issue 4: 386-416. doi: 10.3934/medsci.2016.4.386
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Review

Genomic-Glycosylation Aberrations in Tumor Initiation, Progression and Management

  • 1.
    Department of Systems Biology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA;
  • 2.
    Sheikh Khalifa Bin Zayed Al Nahyan Institute for Personalized Cancer Therapy, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.
  • Received: 11 October 2016 Accepted: 19 December 2016 Published: 22 December 2016

  • Post-translation modifications of proteins alter their functional activity and thus are key contributors of tumor initiation and progression. Glycosylation, one of the most common post-translational modifications of proteins, has been associated with tumorigenesis for decades. However, due to complexity in analysis of the functional effects of glycosylation, definitive information on the role of altered glycosylation in cancer is lacking. Importantly, imputing changes in glycosylation in proteins from analysis of DNA mutations has not been attempted globally. It is thus critical to elucidate the role of glycosylation in tumor pathophysiology as well as potential roles of altered glycosylation as cancer biomarkers and therapeutic targets. In this review, we summarize the evidence that glycosylation regulates functions of a set of frequently mutated oncogenes and tumor suppressors. Moreover, we explore the potential that protein sequence changes engendered by genomic mutations broadly alter glycosylation and thus promote tumor initiation and progression.

    Citation: Carman K.M. Ip, Jun Yin, Patrick K.S. Ng, Shiaw-Yih Lin, Gordon B. Mills. Genomic-Glycosylation Aberrations in Tumor Initiation, Progression and Management[J]. AIMS Medical Science, 2016, 3(4): 386-416. doi: 10.3934/medsci.2016.4.386

    Related Papers:

  • Post-translation modifications of proteins alter their functional activity and thus are key contributors of tumor initiation and progression. Glycosylation, one of the most common post-translational modifications of proteins, has been associated with tumorigenesis for decades. However, due to complexity in analysis of the functional effects of glycosylation, definitive information on the role of altered glycosylation in cancer is lacking. Importantly, imputing changes in glycosylation in proteins from analysis of DNA mutations has not been attempted globally. It is thus critical to elucidate the role of glycosylation in tumor pathophysiology as well as potential roles of altered glycosylation as cancer biomarkers and therapeutic targets. In this review, we summarize the evidence that glycosylation regulates functions of a set of frequently mutated oncogenes and tumor suppressors. Moreover, we explore the potential that protein sequence changes engendered by genomic mutations broadly alter glycosylation and thus promote tumor initiation and progression.


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