Ask about this productRelated genes to: CHST2 antibody
- Gene:
- CHST2 NIH gene
- Name:
- carbohydrate sulfotransferase 2
- Previous symbol:
- -
- Synonyms:
- C6ST
- Chromosome:
- 3q24
- Locus Type:
- gene with protein product
- Date approved:
- 1999-04-09
- Date modifiied:
- 2018-05-14
Related products to: CHST2 antibody
Related articles to: CHST2 antibody
- Esophageal cancer (ESCA) ranks among the most lethal malignancies worldwide, with late-stage diagnosis, poor prognosis, and limited treatment options contributing to its high mortality. MicroRNAs (miRNAs), short non-coding RNAs with gene-silencing functions, have emerged as crucial regulators in cancer biology and hold promise as diagnostic and therapeutic tools. This study investigates miRNA-mRNA interactions in ESCA using a comprehensive in silico approach to uncover potential regulatory nodes that may underlie tumor progression. Fourteen overexpressed genes in both esophageal squamous cell carcinoma (ESCC) and esophageal adenocarcinoma (EAC) were selected. TargetScanHuman and miRDB were used to detect miRNAs with high-confidence 8mer seed matches (score ≥90). The majority of genes exhibited multi-miRNA targeting with clustered or overlapping seed regions, indicative of cooperative or redundant repression mechanisms. Several miRNAs demonstrated highly stable interactions, with favorable MFE and ΔG values, reinforcing their silencing potential. GC/GC3 enrichment further supported duplex stability. GO analysis revealed that the target genes are predominantly involved in transcriptional regulation, apoptosis inhibition, immune response modulation, and cell signaling-pathways central to cancer pathogenesis. TCGA-based validation showed that only a subset of predicted interactions is functionally relevant, with hsa-miR-30d-5p exhibiting a significant inverse correlation with CHST2. These findings highlight the importance of integrating predictive and expression data to identify biologically meaningful miRNA-mRNA interactions in esophageal cancer. - Source: PubMed
Publication date: 2026/04/26
Choudhury Sabnam NasrinMazumder Tarikul HudaSaikia SahidulUddin Arif - Sulfated -glycans are widely distributed and play key roles in a wide range of physiological and disease processes, yet their synthesis remains challenging due to difficulties in regioselective sulfation. Here, we systematically characterized two human GlcNAc-6--sulfotransferases, CHST2 and CHST6, revealing their strong preference towards -glycans (including -GalNAc and -mannosyl glycans) over -glycans and poly-LacNAc chains. Both enzymes favored β1-6 branched GlcNAc residues, with CHST6 showing higher activity and broader substrate tolerance than CHST2. Guided by these insights, we established a modular enzymatic assembly platform for efficient synthesis of 32 well-defined sulfated -GalNAc, -mannosyl glycans, and -glycopeptides. This streamlined strategy enables versatile access to sulfated -glycans and provides a general route for constructing other classes of sulfated glycans. - Source: PubMed
Publication date: 2026/04/13
Fan ShuquanHan JinghuaShen TangliangShabahang MohammadHosseinDu ZhenmingPan JunBai GuitaoBao ShuminIttuveetil AvinashLi Lei - Exosomes and lactylation modification have been increasingly recognized as key regulators of diseases, yet their integrative role in periodontitis remains unclear. No diagnostic model based on exosome-related lactylation genes (ERLGs) has been previously established for periodontitis. This study aimed to explore ERLGs as potential diagnostic biomarkers for periodontitis. - Source: PubMed
Publication date: 2025/12/30
Liang XueyiFu RunxiChen Xiaochuan - Typhi assembles and secretes two forms of typhoid toxin by using two receptor-binding subunits, PltB and PltC. Unlike PltB typhoid toxin, little is known about the tropism and functional consequences of PltC typhoid toxin. Here, we report that PltC typhoid toxin has hepatobiliary tropism through the binding of PltC subunit to sulfated glycans on liver sinusoidal endothelial cells and gallbladder epithelial cells. Critical bacterial and mammalian cell factors involved are PltC R109 residue and carbohydrate sulfotransferases CHST2/4. One notable effect associated with the hepatobiliary tropism of PltC typhoid toxin is a reduction in bile acids, consequently promoting Typhi pathogenicity in infected mice. Similarly, bile acids serve as anti- Typhi infectivity agents at the cellular level, as bile acids inhibit invasion of mammalian cells. These findings highlight a distinct mechanism used by a bacterial exotoxin promoting the pathogenicity of the cognate bacteria and offer insights into the development of antivirulence agents against PltC typhoid toxin and/or Typhi. - Source: PubMed
Publication date: 2025/06/06
Kim Hwa YoungLee Gi YoungThompson Andrew JMcBride RyanFu Dah-JiunPaulson James CSong Jeongmin - Carbohydrate sulfation plays a pivotal role in modulating the strength of Siglec-glycan interactions. Recently, new aspects of Siglec binding to sulfated cell surface carbohydrates have been discovered, but the class of glycan presenting these sulfated Siglec ligands has not been fully elucidated. In this study, the contribution of different classes of glycans to and Siglec ligands was investigated within cells expressing the carbohydrate sulfotransferase 1 (CHST1) or CHST2. For some Siglecs, the glycan class mediating binding was clear, such as -glycans for Siglec-7 and -glycans for Siglec-2 and Siglec-9. Both -glycans and mucin-type -glycans contributed to ligands for Siglec-3, -5, -8, and -15. However, significant levels of Siglec-3 and -8 ligands remained in CHST1-expressing cells lacking complex -glycans and mucin-type -glycans. A combination of genetic, pharmacological, and enzymatic treatment strategies ruled out heparan sulfates and glycoRNA as contributors, although Siglec-8 did exhibit some binding to glycolipids. Genetic disruption of -mannose glycans within CHST1-expressing cells had a small but significant impact on Siglec-3 and -8 binding, demonstrating that this class of glycans can present sulfated Siglec ligands. We also investigated the ability of sulfated ligands to mask Siglec-3 and Siglec-7. For Siglec-7, ligands were again found to be mucin-type -glycans. While -glycans were the major sulfated ligands for Siglec-3, disruption of complex mucin-type -glycans had the largest impact on Siglec-3 masking. Overall, this study enhances our knowledge of the types of sulfated glycans that can serve as Siglec ligands. - Source: PubMed
Publication date: 2025/01/21
Jung JaesooSchmidt Edward NChang Hua-ChienJame-Chenarboo ZeinabEnterina Jhon RMcCord Kelli AGray Taylor EKageler LaurenSt Laurent Chris DWang ChaoFlynn Ryan AWu PengKhoo Kay-HooiMacauley Matthew S