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.
Highlights
Glycosylation, an enzymatic process that attaches glycans to proteins or other organic molecules, is essential for multicellular life
A total of 30 patients (25.4%) with both AFP ≤2800 ng/mL and the GLANT14 “TT” genotype exhibited longer median progressive-free survival (PFS) and overall survival (OS) (3.11 vs. 2.11 months, p = 0.014; and 5.75 vs. 3.93 months, p = 0.001, respectively), and nine patients (7.6%) with all four favorable factors exhibited the longest median PFS and OS (10.64 vs. 2.07 months, p = 0.002; and 25.50 vs. 4.50 months, p < 0.001, respectively). These results suggest that a lower AFP level in combination with the GALNT14 “TT” genotype could serve as favorable pre-therapeutic predictors for advanced hepatocellular carcinoma (HCC) patients receiving FMP chemotherapy
In order to identify the subgroups of HCC patients with the best outcomes out of those receiving either chemotherapy, Hepatic Arterial Infusion Chemotherapy (HAIC), or targeted agents, previously identified single nucleotide polymorphism (SNP) predictors (GALNT14-rs9679162, WWOX-rs13338697, and rs6025211) were tested in a real-world cohort of 237 advanced HCC patients (171 receiving systemic FMP chemotherapy followed by various anticancer treatments including sorafenib; 66 receiving HAIC) [24]
Summary
Glycosylation, an enzymatic process that attaches glycans to proteins or other organic molecules, is essential for multicellular life. The members of the N-acetylgalactosaminyltransferase (GALNT) family are enzymes that initiate O-glycosylation by the addition of an N-acetylgalactosamine (GalNAc) to a serine or threonine residue of a mucin-type protein [5] This process plays a pivotal role in the synthesis of Thomsen-nouvelle (Tn) antigens, which are well-characterized tumor-associated molecules [6]. A categorical analysis showed that a subgroup of patients with the “TT” genotype, who had a tumor size
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