GALNT2

Last update 08 May 2025

Basic Info

Synonyms

GalNAc-T2, GALNT2, Polypeptide GalNAc transferase 2

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Introduction

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. Involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism (PubMed:27508872, PubMed:32293671).

100 Clinical Results associated with GALNT2

100 Translational Medicine associated with GALNT2

0 Patents (Medical) associated with GALNT2

175

Literatures (Medical) associated with GALNT2

01 Jul 2025·Protein Expression and Purification

High soluble expression and characterization of human GalNAc transferase T2 and T11 in Escherichia coli

Article

Author: Shi, Wenjing ; Wang, Linhan ; Wang, Shengjun ; Tang, Wenzhu ; Mao, Weian ; Zhang, Hongmei ; Rong, Yongheng ; Kong, Yun ; Wang, Yankang

The efficient expression of soluble glycosyltransferases from mammalian sources in Escherichia coli (E. coli) remains a significant challenge, often resulting in misfolding and the formation of inclusion bodies. In this study, we investigated strategies to enhance the solubility and catalytic activity of human GalNAc-T2 and GalNAc-T11, two O-glycosyltransferases involved in O-glycosylation of glycoproteins. We found that fusion with maltose-binding protein (MBP) and cellulase catalytic domain (Cel-CD), which led to majority of the fusion proteins being soluble, could increase the solubility of the recombinant proteins. Enzyme activity assays revealed that the fusion glycosyltransferase exhibited significantly higher catalytic efficiency than non-fused enzymes. In addition, the influence of GalNAc-T11 lectin domain on substrate specificity was also determined. The presence of lectin domain had no influence on the recognition of specific substrate and the specific activity of GalNAc-T11. This work offers an efficient approach for the large-scale production of human glycosyltransferases with enhanced bioactivity, highlighting its potential for glycosylation engineering of glycoprotein drugs.

01 Apr 2024·Heliyon

Identification and validation of a glycosyltransferase gene signature as a novel prognostic model for lung adenocarcinoma

Article

Author: Zhang, Kun ; Chen, Mingwei ; Zhou, Jiejun ; Li, Anqi ; Li, Meng ; Yang, Tian ; Peng, Xiaojing

BackgroundThe role of glycosyltransferase (GT) genes in lung adenocarcinoma (LUAD) needs further elucidation. Thus, our study aims to identify the prognostic gene signature of LUAD and explore its molecular functions.MethodsWe initially extracted GT gene sets from the database, and obtained mRNA expression levels and clinical data from The Cancer Genome Atlas (TCGA) database. For constructing a prognostic model for GT genes, we utilized univariate, least absolute shrinkage and selection operator (LASSO), and multivariate Cox regression analyses. Using the model, patients were categorized into high- and low-risk groups. Additionally, we evaluated differences in tumor immune infiltration between these groups and identified potential therapeutic drugs. Finally, we experimentally validated the expression levels of these crucial prognostic genes.ResultsWe developed a risk score comprising nine GT genes (C1GALT1, FUT1, GALNT2, PLOD2, POMK, PYGB, ST3GAL6, UGT2B11, UGT3A1). Patients were then categorized into low- and high-risk groups based on this score. The low-risk group showed superior overall survival (OS) compared to the high-risk group. There were significantly distinct tumor immune microenvironment statuses observed between the two groups. We identified potential therapeutic drugs, including the MEK inhibitor (PD-184352). Finally, we verified the expression of these nine GT genes through immunohistochemistry (IHC) staining and quantitative real-time PCR (qPCR).ConclusionWe identified a distinct LUAD GT gene signature, and these differentially expressed mRNAs could serve as valuable prognostic biomarkers and therapeutic targets. Furthermore, we experimentally validated their expression levels and identified potential therapeutic agents.

01 Jan 2024·Journal of Biological Chemistry

Position-specific N- and O-glycosylation of the reactive center loop impacts neutrophil elastase–mediated proteolysis of corticosteroid-binding globulin

Article

Author: Sumer-Bayraktar, Zeynep ; Thaysen-Andersen, Morten ; Woods, Robert J ; Kawahara, Rebeca ; Abrahams, Jodie L ; Chernykh, Anastasia ; Payne, Richard J ; Ugonotti, Julian ; Corcilius, Leo ; Grant, Oliver C ; Kambanis, Lucas

Corticosteroid-binding globulin (CBG) delivers anti-inflammatory cortisol to inflamed tissues through proteolysis of an exposed reactive center loop (RCL) by neutrophil elastase (NE). We previously demonstrated that RCL-localized Asn347-linked N-glycans impact NE proteolysis, but a comprehensive structure-function characterization of the RCL glycosylation is still required to better understand CBG glycobiology. Herein, we first performed RCL-centric glycoprofiling of serum-derived CBG to elucidate the Asn347-glycans and then used molecular dynamics simulations to study their impact on NE proteolysis. Importantly, we also identified O-glycosylation (di/sialyl T) across four RCL sites (Thr338/Thr342/Thr345/Ser350) of serum CBG close to the NE-targeted Val344-Thr345 cleavage site. A restricted N- and O-glycan co-occurrence pattern on the RCL involving exclusively Asn347 and Thr338 glycosylation was experimentally observed and supported in silico by modeling of a CBG-GalNAc-transferase (GalNAc-T) complex with various RCL glycans. GalNAc-T2 and GalNAc-T3 abundantly expressed by liver and gall bladder, respectively, showed in vitro a capacity to transfer GalNAc (Tn) to multiple RCL sites suggesting their involvement in RCL O-glycosylation. Recombinant CBG was then used to determine roles of RCL O-glycosylation through longitudinal NE-centric proteolysis experiments, which demonstrated that both sialoglycans (disialyl T) and asialoglycans (T) decorating Thr345 inhibit NE proteolysis. Synthetic RCL O-glycopeptides expanded on these findings by showing that Thr345-Tn and Thr342-Tn confer strong and moderate protection against NE cleavage, respectively. Molecular dynamics substantiated that short Thr345-linked O-glycans abrogate NE interactions. In conclusion, we report on biologically relevant CBG RCL glycosylation events, which improve our understanding of mechanisms governing cortisol delivery to inflamed tissues.

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GALNT2

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