Ask about this productRelated genes to: ST3GAL2 antibody
- Gene:
- ST3GAL2 NIH gene
- Name:
- ST3 beta-galactoside alpha-2,3-sialyltransferase 2
- Previous symbol:
- SIAT4B
- Synonyms:
- ST3GALII, ST3GalA.2
- Chromosome:
- 16q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-09-12
- Date modifiied:
- 2016-10-05
Related products to: ST3GAL2 antibody
Related articles to: ST3GAL2 antibody
- Coronary heart disease (CHD) and ischemic stroke (IS) frequently co-occur; however, their shared molecular drivers remain poorly understood, limiting the development of dual-indication therapies. This study aims to characterize the bidirectional genetic relationship between CHD and IS and to prioritize shared candidate proteins as potential therapeutic targets or biomarkers. - Source: PubMed
Publication date: 2026/04/16
Chen MiaoLiu ZongniLou Inmaculada XuWan HaitongZhou Huifen - Circulating proteins represent promising candidates for understanding breast cancer (BC) etiology. This study employed a two-sample Mendelian randomization framework to investigate the potential causal relationships between genetically predicted levels of circulating proteins and BC risk. By integrating large-scale protein quantitative trait loci (pQTL) data from two major cohorts (DeCODE and UK Biobank) with BC genetic association data from three independent sources (FinnGen, BCAC), the analysis identified four proteins-intestinal alkaline phosphatase (ALPI), coiled-coil domain containing 134 (CCDC134), cadherin 1 (CDH1), and ST3 beta-galactoside alpha-2,3-sialyltransferase 2 (ST3GAL2)-with levels associated with a significantly reduced risk of BC. Colocalization analysis further supported a shared causal variant for ALPI. These proteins exhibited distinct associations with BC molecular subtypes. The findings highlight specific circulating proteins as potential mediators of BC risk. This work suggests avenues for exploring the biological mechanisms of BC and may inform future strategies for risk assessment. - Source: PubMed
Publication date: 2026/03/07
Chen HanghangLiu QiZhao HuiduoCheng Xufeng - Osteonecrosis of the femoral head (ONFH) is one of the most common and devastating articular cartilage diseases worldwide. The role of glycosylation in cartilage degeneration of ONFH is not yet fully understood. - Source: PubMed
Publication date: 2025/11/25
Lu XueliangWang XuXiong MingyueWang PengboZhu YingkangWang XiangyuLiu XiaYu HanjieLiu Ruiyu - Aberrant sialylation has been associated with many types of tumors, characterized by aggressiveness and undifferentiated state. However, not exhaustive investigations have been performed on the sialylation status in glioblastoma multiforme (GBM), the most common primary and lethal malignant brain tumor in humans. Hence, in this study we performed a comprehensive characterization of the sialylation status in GBM evaluating specific sialyltransferases and various types of sialic acids (Sias) in different GBM cell lines. First, through in silico analysis we showed that the sialyltransferases , and are significantly up-regulated in GBM tissues and related to lower patient survival. Then, we evaluated the expression levels of these sialyltransferases and their related Sias and observed a high variability among the different GBM cell lines. In addition, using the pan-sialyltransferase inhibitor 3-Fax, we highlighted the role of sialylation in some of the main oncogenic properties of GBM. Indeed, a significant reduction in mobility and migration capacity along with increased adhesiveness of GBM cells was observed upon sialyltransferases inhibition. Our findings showed that aberrant expression of different Sias types is crucial for cell migration and adhesion ability of GBM cells, suggesting that Sias might represent biomarkers for GBM and be useful to design innovative therapeutic strategies. - Source: PubMed
Publication date: 2025/11/03
Gargano DeborahCalvitto MariangelaNiro AntonellaPepe GiuseppeMartella NoemiTani AlessiaRosa PaoloMaglione VittorioMusci GiovanniCutone AntimoDi Bartolomeo SabrinaSgambati Eleonora - Aberrant glycosylation is a hallmark of cancer biology, and altered glycosylation influences multiple facets of melanoma progression. To identify glycosyltransferases, glycans, and glycoproteins essential for melanoma maintenance, we conducted an in vivo growth screen with a pooled short hairpin RNA library of glycosyltransferases, lectin microarray profiling of benign nevus and melanoma samples, and mass spectrometry-based glycoproteomics. We found that α-2,3-sialyltransferases ST3GAL1 and ST3GAL2 and corresponding α-2,3-linked sialosides are up-regulated in melanoma compared to nevi and are essential for melanoma growth. Glycoproteomics revealed that glycoprotein targets of ST3GAL1 and ST3GAL2 are enriched in transmembrane proteins involved in growth signaling, including the amino acid transporter SLC3A2/CD98hc. CD98hc suppression mimicked the effect of ST3GAL1 and ST3GAL2 silencing, inhibiting melanoma cell proliferation. We found that both CD98hc protein stability and its prosurvival effect on melanoma are dependent upon α-2,3-sialylation mediated by ST3GAL1 and ST3GAL2. Our studies reveal α-2,3-sialosides functionally contributing to melanoma maintenance, supporting ST3GAL1 and ST3GAL2 as therapeutic targets in melanoma. - Source: PubMed
Publication date: 2025/07/04
Agrawal PraveenChen Shuhuide Pablos AnaVadlamudi YellamandayyaVand-Rajabpour FatemehJame-Chenarboo FaezehKar SwarnaliYanke Amanda FloresBerico Pietrode Vega Eleazar Miera SaenzDarvishian FarbodOsman ImanLujambio AmaiaMahal Lara KHernando Eva