Ask about this productRelated genes to: ST3GAL3 antibody
- Gene:
- ST3GAL3 NIH gene
- Name:
- ST3 beta-galactoside alpha-2,3-sialyltransferase 3
- Previous symbol:
- SIAT6, MRT12
- Synonyms:
- -
- Chromosome:
- 1p34.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-09-20
- Date modifiied:
- 2018-08-06
Related products to: ST3GAL3 antibody
Related articles to: ST3GAL3 antibody
- Human milk oligosaccharides (HMOs) are complex sugars present in human milk. These sugars possess prebiotic, immunomodulatory, and antagonistic properties towards pathogens and therefore are important for the health and well-being of newborn babies. The backbone of an HMO contains either Type I LacNAc (Gal-β-1,3-GlcNAc) or Type II LacNAc (Gal-β-1,4-GlcNAc). Fucosylation and sialylation of these disaccharides lead to different varieties of glycan epitopes, that may convey different biological functions. Previously, we described one-pot labeling strategy for detecting HMOs with azido-fucose using the combination of neuraminidase and fucosyltransferase. However, the method does not allow us to distinguish these two basic types of glycans. Here we describe a complementary method for HMO detection involving the incorporation of N3-Neu5Ac using the combination of a fucosidase and ST3Gal3 or ST6Gal1. While ST3Gal3 recognizes both types of disaccharides, ST6Gal1 specifically recognizes Type II LacNAc, therefore allowing these two types of disaccharides to be distinguished. Both enzymes achieved visible labeling of LNnO, a linear octasaccharide, at a minimal concentration of 10 nM, but ST3Gal3 showed at least 2-fold higher activity than ST6Gal1. ST3Gal3 therefore is more active and has broader specificity than the commonly used ST6Gal1 for attaching N3-Neu5Ac to target glycans. The methods were further illustrated on assigning isomeric specific HMOs (e.g. LNT vs. LNnT) and identifying fucosylated HMOs (e.g. LNFP I vs. LNDFH III) in fractionated human milk whey samples based on labeling sensitivity to enzyme treatment and gel mobility of the labeled bands together with data obtained from MALDI mass spectrometry. - Source: PubMed
Wu Zhengliang LNauman Todd ABowman Michael JSkory Christopher D - This study investigates the genetic diversity, population structure, and adaptive differentiation of Yunnan native cattle (YNC) using whole-genome SNP data from 457 individuals, representing eight cattle populations and two closely related bovine species (Zhongdian yak and Dulong gayal). Genetic diversity analyses revealed a distinct latitudinal gradient from north to south, with the highest diversity observed in the northern Diqing (DQC) and Zhaotong (ZTC) populations. The observed population structure was largely consistent with geographic distribution, identifying distinct ancestral components and complex admixture patterns. Genome-wide selective sweep scans revealed several key candidate genes underlying local adaptation. Notably, and were associated with cold tolerance in northern populations, and and were implicated in heat stress adaptation in southern populations. Genome-wide balancing selection analyses further detected significant loci, such as and , where divergent haplotype frequencies reflected differential selective pressures on milk-related traits between northern and southern populations. Additionally, we detected signals of historical introgression from Zhongdian yak into DQC cattle, highlighting the introgressed gene as a potential candidate associated with high-altitude thermogenesis. Collectively, these results provide a comprehensive genomic framework for the management and conservation of indigenous bovine genetic resources in Southwest China. - Source: PubMed
Publication date: 2026/04/03
Liu YiduanDao WenbinXu WenkunFan XinyangYang RuifeiMiao Yongwang - Lysosomal dysfunction is central to Parkinson's disease pathogenesis, with as the strongest established genetic risk factor. Numerous other genes involved in lysosomal sphingolipid, glycosphingolipid and ceramide metabolism have been proposed as contributors to Parkinson's disease, underscoring the need for comprehensive genetic analyses across these pathways. We analysed rare variants (minor allele frequency < 0.01) across 36 lysosomal genes (excluding ) in 8,267 individuals with Parkinson's disease and 68,208 controls, including a subset of 793 early-onset Parkinson's disease (≤50 years) cases. Targeted sequencing was performed in four cohorts at McGill University (3,456 Parkinson's disease patients and 2,664 controls) and results were combined with whole-genome sequencing data from the UK Biobank (2,848 cases, 62,451 controls), and from the Accelerating Medicines Partnership - Parkinson's Disease (1,963 cases, 3,093 controls). We analysed the association of rare variants in these genes with Parkinson's disease using Sequence Kernel Association Test-Optimal (SKAT-O) across variant classes (all rare variants, nonsynonymous, loss-of-function and predicted damaging variants with a Combined Annotation Dependent Depletion (CADD) score >20), with meta-analysis across cohorts. We additionally performed per-domain analyses for variants in gene segments encoding functional domains. False discovery rate correction was applied. Meta-analysis identified a significant association between rare variants in and Parkinson's disease (Pfdr=0.04). Several additional lysosomal genes showed nominal associations (P<0.05), including and . Domain-based analyses identified a strong enrichment of nonsynonymous variants within the beta-acetyl-hexosaminidase-like domain of HEXA (P = 8.0 × 10), although this signal did not survive correction for multiple testing (Pfdr=0.154). In early-onset Parkinson's disease, domain-based analyses revealed significant associations in (Pfdr=7.3×10) and (Pfdr=0.03). Together, these results provide genetic evidence that rare variants across multiple lysosomal pathways, particularly those related to sialylation, ganglioside metabolism, ceramide biology, and lysosomal proteolysis, may contribute to Parkinson's disease susceptibility beyond , highlighting biologically coherent pathways for future replication and functional investigation. - Source: PubMed
Publication date: 2026/02/18
Senkevich KonstantinParlar Sitki CemChantereault CloeLiu LangYu EricRudakou UladzislauAhmad JamilRuskey Jennifer AAsayesh FarnazSpiegelman DanWaters CherylMonchi OuryDauvilliers YvesDupré NicolasGreenbaum LiorHassin-Baer SharonMiliukhina IrinaTimofeeva AllaEmelyanov AntonPchelina SofyaAlcalay Roy NGan-Or Ziv - : Pathogenic ST3GAL3 variants cause neurological and cognitive impairment, defining a distinct congenital disorder of glycosylation (ST3GAL3-CDG). Nonetheless, limited enzyme characterization exists due to the lack of a non-radiochemical assay. : Here, we developed an LC-MS/MS-based method using the artificial substrate para-nitrophenyl-lacto-N-biose (LNB-pNP; Galβ1,3GlcNAcβ1-O-C6H4NO2) to measure ST3GAL3 activity in vitro. : A peak corresponding to sialyl-LNB-NP was detected in reactions with homogenate from HEK-293T cells transfected with pCDNA3 ST3GAL3 plasmid, but was virtually absent in mock-transfected cells. A substrate dependence curve provided an apparent Km value for the substrate (0.40 mM) and closely matched values from prior radiochemical methods. No activity was detected with homogenates from cells expressing pathogenic ST3GAL3 variants, except p.A13D, which is known to retain about 10% of residual activity. Compared to ST3GAL4 and ST3GAL6, ST3GAL3 showed markedly higher specificity toward LNB-NP, lactotetraosylceramide (Lc4) and asialo-GM1, which are rather specific substrates. Instead, neo-lactotetraosylceramide (neoLc4) was processed by all three ST3GALs. : These findings suggest that ST3GAL4 or ST3GAL6 cannot compensate for ST3GAL3 loss in the biosynthesis of gangliosides sialyl-Lc4 and GM1b, but may do so for sialyl-neoLc4. This non-radiochemical assay enables screening and diagnostic evaluation of novel ST3GAL3 variants potentially associated with ST3GAL3-CDG. - Source: PubMed
Publication date: 2026/02/12
Penati SaraDei Cas MicheleMontavoci LindaCaretti AnnaTrinchera Marco - Vesicular stomatitis virus (VSV) is a model rhabdovirus whose infectivity is determined primarily by its envelope glycoprotein (VSV-G). The low-density lipoprotein receptor (LDLR), a cell-surface glycoprotein, has been identified as the major receptor for VSV-G binding. However, the role of host sialylation in VSV-G-dependent entry remains poorly understood. - Source: PubMed
Publication date: 2026/02/22
Isaji TomoyaQi FengChien Yu-ChunOyama YoshiyukiFukuda TomohikoKhoo Kay-HooiGu Jianguo