B3GALT5

Last update 08 May 2025

Basic Info

Synonyms

b3Gal-T5, B3GalT-V, B3GALT5

+ [9]

Introduction

Catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Can use glycolipid LC3Cer as an efficient acceptor.

100 Clinical Results associated with B3GALT5

100 Translational Medicine associated with B3GALT5

0 Patents (Medical) associated with B3GALT5

Literatures (Medical) associated with B3GALT5

01 Jun 2025·Bioorganic Chemistry

Drug repurposing of 6-AZA-UTP and itraconazole reveals novel B3GALT5 inhibitors for pancreatic cancer

Article

Author: Sehar, Misbah ; Chuang, Po-Kai ; Cheng, Yi-Chi ; Botcha, Lavanya ; Zhang, Sheng-Cheng ; Khan Jadoon, Muhammad Siraj

Pancreatic cancer has a poor prognosis with limited therapeutic options, necessitating novel treatment strategies. While B3GALT5 enzyme overexpression has been reported in pancreatic cancer cases, effective mechanisms to suppress its activity remain unexplored. In this study, we utilized bioinformatics and in silico studies to evaluate the relationship between B3GALT5 enzyme and pancreatic cancer. Through molecular docking analysis, FDA-approved drugs 6-AZA-UTP and itraconazole were identified as potential B3GALT5 enzyme inhibitors. Biological evaluation on MIA PaCa-2 and AsPC-1 pancreatic cancer cell lines demonstrated that both compounds significantly reduced cell viability. Flow cytometry analysis revealed that both drugs effectively suppressed B3GALT5 enzyme activation by decreasing SSEA-3 expression. Furthermore, both compounds exhibited potent anti-tumor effects by inhibiting cell adhesion, colony formation, and migration while inducing apoptosis in pancreatic cancer cells. Notably, both drugs demonstrated favorable ADMET profiles with no carcinogenic or toxic effects. Our investigations revealed that 6-AZA-UTP and itraconazole can effectively suppress B3GALT5 enzyme activity, resulting in tumor suppression and metastasis inhibition. These findings suggest that either 6-AZA-UTP or itraconazole can inhibit B3GALT5 enzyme activity and may serve as promising therapeutic options for pancreatic cancer treatment through drug repurposing strategy.

01 Apr 2025·Nature Chemical Biology

Fucosylation of glycoproteins and glycolipids: opposing roles in cholera intoxication

Article

Author: Konada, Rohit Sai Reddy ; Ghorashi, Atossa C. ; Azadi, Parastoo ; Xing, Chao ; Teneberg, Susann ; Murray, Nathan B ; Boucher, Andrew ; Kohler, Jennifer J. ; Murray, Nathan B. ; Zhang, Xunzhi ; Yrlid, Ulf ; Zalem, Dani ; Kohler, Jennifer J ; Archer-Hartmann, Stephanie A ; Ghorashi, Atossa C ; Taherzadeh Ghahfarrokhi, Mehrnoush ; Archer-Hartmann, Stephanie A.

Cholera toxin (CT) is the etiological agent of cholera. Here we report that multiple classes of fucosylated glycoconjugates function in CT binding and intoxication of intestinal epithelial cells. In Colo205 cells, knockout (KO) of B3GNT5, which encodes an enzyme required for synthesis of lacto and neolacto series glycosphingolipids (GSLs), reduces CT binding but sensitizes cells to intoxication. Overexpressing B3GNT5 to generate more fucosylated GSLs confers protection against intoxication, indicating that fucosylated GSLs act as decoy receptors for CT. KO of B3GALT5 causes increased production of fucosylated O-linked and N-linked glycoproteins and leads to increased CT binding and intoxication. KO of B3GNT5 in B3GALT5-KO cells eliminates production of fucosylated GSLs but increases intoxication, identifying fucosylated glycoproteins as functional receptors for CT. These findings provide insight into the molecular determinants regulating CT sensitivity of host cells.

01 Sep 2024·Journal of Cellular and Molecular Medicine

Highly expressed B3GALT5‐AS1 contributes to gastric cancer progression by recruiting WDR5 to mediate B3GALT5 and regulating β‐catenin/ZEB1 axis

Article

Author: Feng, Wei ; Tang, Yelan ; Zong, Wei ; Jing, Rongrong ; Ju, Shaoqing

AbstractLong non‐coding RNAs (lncRNAs) play an important role in the progression of gastric cancer (GC), but its specific regulatory mechanism remains to be further studied. We previously identified that lncRNA B3GALT5‐AS1 was upregulated in GC serum. Here, we investigated the functions and molecular mechanisms of B3GALT5‐AS1 in GC tumorigenesis. qRT‐PCR was used to detect B3GALT5‐AS1 expression in GC. EdU, CCK‐8, and colony assays were utilized to assess the proliferation ability of B3GAL5‐AS1, and transwell, tube formation assay were used to assess the invasion and metastasis ability. Mechanically, FISH and nuclear plasmolysis PCR identified the subcellular localization of B3GALT5‐AS1. RIP and CHIP assays were used to analyse the regulation of B3GALT5‐AS1 and B3GALT5. We observed that B3GALT5‐AS1 was highly expressed in GC, and silencing B3GALT5‐AS1 could inhibit the proliferation, invasion, and migratory capacities of GC. Additionally, B3GALT5‐AS1 was bound to WDR5 and modulated the expression of B3GALT5 via regulating the ZEB1/β‐catenin pathway. High‐expressed B3AGLT5‐AS1 promoted GC tumorigenesis and regulated B3GALT5 expression via recruiting WDR5. Our study is expected to provide a new idea for clinical diagnosis and treatment.

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B3GALT5

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