B3GALNT2
- Known as:
- B3GALNT2
- Catalog number:
- 002343A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- B3GALNT2
Related genes to: B3GALNT2
- Gene:
- B3GALNT2 NIH gene
- Name:
- beta-1,3-N-acetylgalactosaminyltransferase 2
- Previous symbol:
- -
- Synonyms:
- MGC39558
- Chromosome:
- 1q42.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-02-10
- Date modifiied:
- 2014-11-19
Related products to: B3GALNT2
Related articles to: B3GALNT2
- The aim of this study was to gain insight into the molecular spectrum of anophthalmia and microphthalmia (A/M) in the Egyptian population. - Source: PubMed
Publication date: 2026/01/20
Elmakkawy GehadNabil AmiraNabil KarimAmin Asmaa KenawyMaskill DavidAli ManirSchorderet DanielBayoumi NaderShakankiri NihalAbdalla Ebtesam - Transcriptome analysis can improve the diagnostic yield for neurodevelopmental disorders. We applied RNA-seq using urine-derived cells (UDCs) to a family with two affected brothers with a muscular dystrophy-dystroglycanopathy and dilated cardiomyopathy. Exome sequencing identified a maternally inherited heterozygous B3GALNT2 splice-site variant (NM_152490.5:c.261-2A>G) but no second pathogenic allele. UDCs RNA-seq with OUTRIDER detected markedly decreased expression of B3GALNT2 in the proband and a milder decrease in the father, suggesting a paternally inherited non-coding variant. Genome sequencing revealed a 357-bp heterozygous deletion encompassing the B3GALNT2 promoter and transcription start site, which segregated with the phenotype. RNA-seq supported aberrant splicing from the splice-site allele and reduction of transcripts from the deletion allele. These findings provide proof of concept that UDCs RNA-seq-guided outlier-expression analysis can identify non-coding second hits and support genetic diagnosis, and they suggest that cardiac surveillance may be warranted in B3GALNT2-related disorder as they age. - Source: PubMed
Publication date: 2026/03/24
Takagi ToruMiyamoto SachikoShimizu KenjiTanaka YasuhikoMatsubayashi TomokoMasunaga YoheiSaitsu Hirotomo - This study aimed to investigate the clinical application of genetic testing in the prenatal diagnosis of fetal agenesis of the corpus callosum (ACC). - Source: PubMed
Zeng Li-NaZhang YanLin LiHuang Jie-XiangLin Li-HuaChen Bin-BinDong XianWang Jing-JingYing Qin - Background mutations cause α-dystroglycanopathy (α-DGP), a rare condition characterized by muscular dystrophy, brain malformations, and developmental delay. However, its pathogenic mechanisms remain poorly understood. To date, limited cases have been reported, and the pathogenic mechanisms remain incompletely understood.MethodsClinical and genetic data from 3 newly diagnosed Chinese patients and 28 patients previously diagnosed with -related α-DGP were analyzed. Using patient-derived fibroblasts, α-dystroglycan (α-DG) glycosylation and laminin-binding capacity were assessed by immunoblotting, laminin overlay and immunofluorescence. mRNA and protein levels were quantified by real-time PCR and immunoblotting. Enzymatic activity was measured using purified recombinant proteins. Differentially expressed genes were identified via an mRNA microarray.ResultsAll three patients carried compound heterozygous variants involving one truncating and one missense mutation. Two novel mutations (c.657_658insTT and c.1384T > C) were identified. Functional studies confirmed that the missense mutations (Y436C and C462R) impaired enzymatic activity to 40-50% of wild-type levels, while splice variants caused frameshifts and likely complete loss of protein. Despite partial residual activity, all patients showed severely reduced α-DG glycosylation and loss of laminin binding, consistent with a functional threshold effect. Transcriptomic analysis revealed upregulation of in two patients.ConclusionsThis study expands the mutational spectrum of -related α-DGP and provides mechanistic insight into the pathogenicity of novel variants. Our findings support a functional threshold model for B3GALNT2 activity in α-DG glycosylation and suggest CHST10 as a potential transcriptional responder to glycosylation defects. These results deepen the understanding of -related dystroglycanopathies and may inform future diagnostic and therapeutic strategies. - Source: PubMed
Publication date: 2025/07/15
Fu XiaonaWang HuiChai WenjiaChen XiaoyuSong DanyuWang WeiZhong JingweiLiu ZhimeiTong XiaoXiong HuiRen XiaotunGui Jingang - Dystroglycan (DG) binds to extracellular matrix via its O-glycans, which are sequentially modified in a specific order by DG-specific enzymes: POMGNT2, B3GalNT2, and POMK in the endoplasmic reticulum (ER), followed by FKTN, FKRP, TMEM5, B4GAT1 and LARGE1 in the Golgi apparatus. However, there have been no comprehensive and systematic studies on the major localization of these enzymes. Here, we expressed fluorescent fusion proteins of DG-specific modifying enzymes under the control of short CMV promoter and observed their primary localization using the latest microscopy along with localization markers: mEGFP-KDEL for the ER, GM130 and GRASP55 for the cis-/medial-Golgi, and TGN46 and GCC1 for the trans-Golgi network. As a result, POMGNT2 and B3GalNT2 were localized to the ER as expected, but POMK was localized predominantly to the cis-/medial-Golgi showing co-localization with GRASP55. FKTN, FKRP and TMEM5 were partially co-localized with both cis-/medial- and trans-Golgi network markers. Though B4GAT1 did not co-localize with GM130 or TGN46, it co-localized with GCC1 another trans-Golgi network marker, indicating Golgi subcompartmentalization. LARGE1, the final glycosyltransferase involved in the modification of DG's O-glycan, was localized in the cis-/medial-Golgi, but did not overlap with trans-Golgi network markers. An EndoH sensitivity assay demonstrated that DG-specific enzymes interacting with DG were localized in the early secretory pathway. Our results reveal that POMK and B4GAT1 function at locations distinct from their major localization and support the conclusion that the modification of matriglycan on DG is completed at the cis-/medial-Golgi. - Source: PubMed
Aso ShinyaLowe MartinMori KazutoshiNinagawa Satoshi