Ask about this productRelated genes to: B4GALNT1 Blocking Peptide
- Gene:
- B4GALNT1 NIH gene
- Name:
- beta-1,4-N-acetyl-galactosaminyltransferase 1
- Previous symbol:
- GALGT, SPG26
- Synonyms:
- beta1-4GalNAc-T
- Chromosome:
- 12q13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-01-29
- Date modifiied:
- 2016-02-22
Related products to: B4GALNT1 Blocking Peptide
Related articles to: B4GALNT1 Blocking Peptide
- Osteosarcoma (OS) is a malignant primary bone tumor developing from primitive mesenchymal cells. Glycosylation is important in the adhesion, metastasis and transformation of cancer cells. Nevertheless, the investigation of glycosylation-related genes (GRGs) in OS has been infrequently described. - Source: PubMed
Publication date: 2026/03/12
Ding NingLi JinlongShi SongboWang JizuDing YinliangYang Qingshan - Tay-Sachs disease is a severe neurodegenerative disorder caused by mutations in the gene, which encodes the α-subunit of the β-hexosaminidase A (HexA) enzyme. HexA deficiency leads to abnormal GM2 accumulation, eventually causing cell death and neurodegeneration. A double-knockout mouse model lacking both and genes (, ) exhibits neuropathological and clinical features similar to those of the disease, including neuroinflammation. B4Galnt1 (ß-1,4-N-acetyl-galactosaminyltransferase 1) is involved in lipid biosynthesis in mice. We hypothesized that creating a triple knockout model (, ) could prevent excessive GM2 ganglioside accumulation and reduce disease symptoms. Molecular biology and immunohistochemistry analyses showed that GM2 ganglioside accumulation was halted in mice. Preventing GM2 ganglioside accumulation alleviated neuroinflammation and neuronal death, extending lifespan by more than 18 months. Our findings suggest that knocking out to block GM2 ganglioside accumulation may reverse disease symptoms in the mouse model, indicating a promising, safe target for substrate-reduction therapy via siRNA silencing. - Source: PubMed
Publication date: 2026/03/09
Yanbul SelmanCalıskan Tufan UtkuTurali Mustafa CanSeyrantepe Volkan - The cerebrospinal fluid (CSF) proteome offers a direct readout of central nervous system (CNS) biology but its genetic architecture remains incompletely defined. We conducted the largest single-site CSF genome-wide association study (GWAS) to date, analysing 7,092 SomaScan proteins in 1,259 individuals. Using a covariate-adjusted model including proteomic PCs and disease status, we identified 1,971 genome-wide significant pQTLs (954 cis, 971 trans), 1,409 of which replicated in an independent CSF dataset. We discovered 264 previously unreported loci, replicated 511 associations, refined 80 known loci, and 265 proxy-based associations. Using a previously published reproducibility framework, we show that robust discovery concentrates in reliable measurements, underscoring the importance of rigorous quality control. Enrichment analyses revealed immune/complement and extracellular matrix biology. Mendelian randomization prioritised causal proteins: PILRA, TREM2, IL34, CR2, SHARPIN and ERBB1 (Alzheimer's disease); BST1 and GPNMB (Parkinson's disease); STX6 (Creutzfeldt Jacobs disease); and ATXN3 and B4GALNT1 (Amyotrophic lateral sclerosis), providing a scalable framework for orthogonal target validation in neurodegeneration. - Source: PubMed
Publication date: 2026/02/22
Puerta RaquelGarcía-González Pablode Rojas ItziarCapdevila-Bayo MariaOlivé ClàudiaMuñoz-Morales ÁlvaroBayón-Buján PaulaValenzuela AlejandroYang ChengranTimsina JigyashaLiu MenghanChakkarai SathyaseelanSotolongo-Grau OscarCalm BertaMiguel AndreaSolivar AriadnaMontrreal LauraMartínez MartaKhan AsifZhao FeiyangTantinyà NatàliaRosende-Roca MaitéeAlegret MontserratMoreno-Grau SoniaFernández Maria VictoriaMarquié MartaValero SergiCavazos Jose EnriqueSanz PilarMontalban XavierTàrraga LluisSmets BartBoada MercèSeshadri SudhaSargurupremraj MuralidharanCruchaga CarlosCano AmandaCabrera-Socorro AlfredoRuiz Agustín - Glycolipids constitute an important component of the plasma membrane based on both abundance as well as function. Gangliosides, being a class of structurally diverse and functionally varied glycolipids, can act both as a receptor as well as a ligand and therefore are established as a crucial player in several normal cellular processes. In certain diseases, and in particular cancer, select gangliosides are over-expressed often leading to disease manifestation. GM2-synthase, the enzyme responsible for the formation of a pro-tumorigenic ganglioside, GM2, is well reported to be over-expressed across various cancer tissues and cell lines. This over-expression of GM2-synthase has been linked with increased migration, invasion, and epithelial to mesenchymal transition (1) as well as induction of a local and systemic host immune suppression in cancer. Despite only a handful of studies demonstrating an epigenetic regulation underlying the transcriptional regulation of the GM2-synthase (B4GalNT1) gene, the detailed mechanism still remains unclear. Here we identified the total proteome associated with the GM2-synthase promoter through a two-step CRISPR-dCas9 based proteome profiling approach by categorizing all the identified proteins leading to a detailed elucidation of the molecular drivers behind GM2-synthase transcription. While the previous study identified an acetylation-dependent de-repression of the transcription factor SP1 causing GM2-synthase activation, the underlying molecular mechanism driving its activation wasn't clear. This study demonstrated that the histone acetyl transferase p300, acts as a pivotal factor which on one hand causes acetylation-mediated degradation of SP1, and on the other hand activates SMAD2/4 to have a direct positive impact on GM2-synthase gene transcription. We identified p300 to have an activator role in GM2-synthase gene transcription through knock out, knock down, and over-expression experiments. Furthermore, SP1 degradation, SMAD activation, and their DNA binding patterns show the reciprocal role of p300 on SP1 and SMAD complexes. Altogether we have identified SMAD2/4 as an activator complex, p300 as a positive regulator, and uncovered a critical p300-SMAD-SP1 regulatory axis in GM2-synthase transcriptional regulation. - Source: PubMed
Banerjee SounakBanerjee AvisekRay SubhaRay AishwaryaPaul DebaratiDastidar Shubhra GhoshWillard BelindaBiswas Kaushik - Sphingolipid metabolism is an important component of various biological processes, particularly in cancer pathology. This metabolic pathway significantly influences the behavior of cancer cells by regulating growth, apoptosis, and survival. Although modulating sphingolipid metabolism has attracted attention as a novel therapeutic strategy, its complexity and specific mechanisms remain incompletely understood. In the current study, transcriptomic profiling was employed to compare the expression of sphingolipid metabolism-related genes between normal solid tissues and lung adenocarcinoma tissues. Additionally, Gene Ontology, Kyoto Encyclopedia of Genes and Genomes enrichment, and protein-protein interaction (PPI) analyses were performed to investigate the functional relevance of these genes. Twelve sphingolipid metabolism-related genes formed a highly interconnected core, suggesting their potential central role within the regulatory network. Four genes were found to be significantly correlated with overall survival. Notably, B4GALNT1 upregulation and CERS4 downregulation correlated with advanced tumor stage and metastasis. They also showed prognostic significance in Cox regression analyses, and these findings were consistently validated in an independent cohort. In vitro, within lung adenocarcinoma cell lines, B4GALNT1 knockdown and CERS4 overexpression suppressed cell proliferation, migration, and epithelial-to-mesenchymal transition, supporting their roles in lung adenocarcinoma progression. These findings highlight B4GALNT1 and CERS4 as potential prognostic biomarkers and therapeutic targets in lung adenocarcinoma, warranting further clinical investigation. - Source: PubMed
Publication date: 2026/02/10
Jeon JieunKang JunhoPark Jae-HyungLee Jae-HoKim Dong EunPark Woo-JaeKim Shin