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Review
. 2020 Feb 21;21(4):1491.
doi: 10.3390/ijms21041491.

GALNT14: An Emerging Marker Capable of Predicting Therapeutic Outcomes in Multiple Cancers

Affiliations
Review

GALNT14: An Emerging Marker Capable of Predicting Therapeutic Outcomes in Multiple Cancers

Wey-Ran Lin et al. Int J Mol Sci. .

Abstract

Members of the polypeptide N-acetylgalactosaminyltransferase (GALNT) family function as the initiating enzymes that catalyze mucin-type O-glycosylation of proteins, and their dysregulated expression can alter cancer cell behaviors such as de novo occurrence, proliferation, migration, metastasis, and drug resistance. Recent studies have demonstrated that one of the family's members, GALNT14, is aberrantly expressed in multiple cancers and involved in a variety of biological functions. Moreover, the single nucleotide polymorphisms (SNPs) of GALNT14-rs9679162 have been shown to predict therapeutic outcomes in patients with hepatocellular carcinoma as well as several other different types of gastrointestinal cancer. This review summarizes the structural features of GANLT14, its functional roles, and the predictive values of GALNT14 genotypes and enzyme levels in multiple cancers receiving distinct anticancer therapies.

Keywords: biomarker; cancer; polypeptide N-acetylgalactosaminyltransferase; single nucleotide polymorphism.

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Conflict of interest statement

The authors declare no conflict of interest. The funders had no role in the writing of the manuscript, or in the decision to publish the results.

Figures

Figure 1
Figure 1
The structure of the GALNT14 gene, including the location of rs9679162 (A), and the common functional domains of GALNT proteins (B). The GALNT14 gene is located on chromosome 2 and includes at least 17 exons. rs9679162 is located between exons 3 and 4 (A). The members of the GALNT family possess several common functional domains (B). The N-terminal cytoplasmic domain contains 4 to 22 amino acids. The transmembrane domain contains 15 to 25 amino acids. The catalytic region contains more than 450 amino acids, which can be divided into three parts: a glycosyltransferase 1 motif, a Gal/GalNAc-T motif, and a ricin like motif.

References

    1. Moremen K.W., Tiemeyer M., Nairn A.V. Vertebrate protein glycosylation: Diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 2012;13:448–462. doi: 10.1038/nrm3383. - DOI - PMC - PubMed
    1. Tarp M.A., Clausen H. Mucin-type o-glycosylation and its potential use in drug and vaccine development. Biochim. Biophys. Acta. 2008;1780:546–563. doi: 10.1016/j.bbagen.2007.09.010. - DOI - PubMed
    1. Tian E., Ten Hagen K.G. Recent insights into the biological roles of mucin-type o-glycosylation. Glycoconj. J. 2009;26:325–334. doi: 10.1007/s10719-008-9162-4. - DOI - PMC - PubMed
    1. Tran D.T., Ten Hagen K.G. Mucin-type o-glycosylation during development. J. Biol. Chem. 2013;288:6921–6929. doi: 10.1074/jbc.R112.418558. - DOI - PMC - PubMed
    1. Bennett E.P., Mandel U., Clausen H., Gerken T.A., Fritz T.A., Tabak L.A. Control of mucin-type o-glycosylation: A classification of the polypeptide galnac-transferase gene family. Glycobiology. 2012;22:736–756. doi: 10.1093/glycob/cwr182. - DOI - PMC - PubMed

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