Ask about this productRelated genes to: CHST1 antibody
- Gene:
- CHST1 NIH gene
- Name:
- carbohydrate sulfotransferase 1
- Previous symbol:
- -
- Synonyms:
- C6ST, KSGal6ST
- Chromosome:
- 11p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-02
- Date modifiied:
- 2016-02-24
Related products to: CHST1 antibody
Related articles to: CHST1 antibody
- Sulfate is a vital nutrient for healthy brain development. More than 90 sulfate-related genes are highly conserved across mammalian species, with 16 of these genes being clinically reportable for adverse brain conditions. To determine the potential involvement of additional sulfate-related genes in human neuropathology, this study curated the spatial and temporal expression patterns of all known sulfate biology genes in the human fetal brain from 8 to 37 post conception weeks (pcw) using data from the BrainSpan database and performed network analysis to cluster sulfate-related genes with genes involved in neurodevelopmental processes. A total of 64 sulfate-related genes were abundantly or moderately expressed in 11 brain regions throughout gestation. Steady state expression was observed for some of these genes from 8 to 37 pcw, including genes that encode sulfotransferases (, ), sulfatases (, , , ), sulfatase modifying enzyme (), key enzymes in amino acid metabolism (, ), sulfate transporter (), as well as genes involved in neurodevelopmental processes (, , , , , ). Between 21-24 weeks, there were numerous clusters of sulfate biology genes with neurodevelopmental genes involved in neuronal migration ( and synaptogenesis (, , , ). At 8-13 and 17-21 pcw, fifteen sulfate genes (, , , , , , , , , , , , , , ) were expressed in the hippocampus and clustered with genes involved in neurogenesis, differentiation and synaptogenesis (, , ). Overall, this study identified 48 sulfate-related genes with moderate/abundant expression in the fetal brain that are coexpressed with genes for neurodevelopmental processes but are not considered in clinical settings. These findings provide information for future studies into the physiological roles of sulfate-related genes that are expressed in the fetal brain. - Source: PubMed
Publication date: 2026/05/08
Vijayakumar PrasidheeSummers Kim MDawson Paul A - : Autism Spectrum Disorder (ASD) is a complex neurodevelopmental condition marked by heterogeneous behavioral symptoms and systemic comorbidities, including immune and gastrointestinal dysfunctions. Emerging studies suggest that glycosylation-a fundamental post-translational modification regulating cellular communication and immune responses-may play a role in ASD pathophysiology, yet its contribution remains underexplored. : In this study, we developed an integrative transcriptomic and network analysis framework to investigate glycosylation-related gene expression changes and their functional associations in ASD. Using publicly available datasets from bulk and single-cell RNA sequencing of brain and blood tissues, we focused on four prior-knowledge gene subsets: glycogenes, extracellular matrix glycoproteins, immune response genes, and autism risk genes. : Differential expression and pathway enrichment analyses revealed consistent dysregulation of glycosylation pathways, including mucin-type -glycan biosynthesis, glycosaminoglycan metabolism, GPI-anchor formation, and sialylation, across ASD tissues. These transcriptional changes were functionally linked to altered immune signaling (e.g., IL-17, Toll-like receptor, and complement pathways) and synaptic development pathways, forming a distinct glyco-immune axis. Network analysis identified key glycogenes such as , , , and as central molecular nodes, interacting with immune and neuronal regulators. Linkage disequilibrium analysis further revealed ASD-associated SNPs influencing the expression of these glycogenes in both blood and brain tissues. : Together, these findings support a model in which disrupted glycosylation contributes to ASD pathophysiology by mediating immune dysregulation and altered neuronal connectivity. This study offers a systems-level framework to understand the molecular complexity of ASD and highlights glycogenes as potential biomarkers and targets for future therapeutic exploration. - Source: PubMed
Publication date: 2026/04/19
Oommen Anup MammenMorel MarieCunningham StephenSeoighe CathalJoshi Lokesh - Gastric cancer (GC) is among the most frequently diagnosed malignancies worldwide. Identifying novel therapeutic targets is of great significance. - Source: PubMed
Qin XufuHan YuWang ZetaoZhou XiaohuiShi Lijun - 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 - O-Mannose (Man) glycans are branched specifically in the brain by a dedicated glycosyltransferase, N-acetylglucosaminyltransferase IX (GnT-IX, also known as MGAT5B). Such branching of O-Man glycans was reported to be involved in diseases, including demyelination and glioma, but the enzymatic mechanisms by which O-Man glycan is specifically recognized by GnT-IX and how branched O-Man glycans are subsequently elongated by other enzymes in the brain have remained unclear. To shed light on these issues, we here first compared the structural model of GnT-IX complexed with its O-Man substrate with the crystal structure of the homologous N-glycan branching enzyme GnT-V (also known as MGAT5). Several residues in GnT-IX were predicted to be critical to recognition of the O-Man substrate, and an enzyme assay revealed that R304 in GnT-IX is crucial for the specificity toward O-Man glycans. We further investigated the role of O-Man branching for subsequent elongation in the brain and found that the level of keratan sulfate (KS) in O-Man glycans was significantly reduced in GnT-IX-knockout (KO) mouse brain, suggesting that O-Man branching promotes KS biosynthesis. Mechanistically, our enzymatic assays of the KS biosynthetic enzymes demonstrated that B4GALT1, B4GALT4, and CHST1 exhibited significantly higher activity toward branched O-Man glycans than toward their linear counterparts. These results imply that branching of O-Man glycans by GnT-IX provides the scaffold for efficient subsequent glycan elongation. Our findings deepen our understanding of the complex biosynthetic pathway of O-Man glycans in the brain. - Source: PubMed
Publication date: 2026/01/07
Itoh TomoyaTanaka Hide-NoriPareek MohitNagae MasamichiManya HiroshiIdo AkemiMishra Sushil KKizuka Yasuhiko