A4GNT
- Known as:
- A4GNT
- Catalog number:
- 000859A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- A4GNT
Related genes to: A4GNT
- Gene:
- A4GNT NIH gene
- Name:
- alpha-1,4-N-acetylglucosaminyltransferase
- Previous symbol:
- -
- Synonyms:
- alpha4GnT
- Chromosome:
- 3q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-12
- Date modifiied:
- 2016-10-05
Related products to: A4GNT
Related articles to: A4GNT
- Gastric mucins contain O-glycans carrying terminal α1,4-linked N-acetylglucosamine (αGlcNAc). A previous study demonstrated that A4gnt-deficient mice lack αGlcNAc, spontaneously develop differentiated-type gastric adenocarcinoma, and exhibit significant up-regulation of Il11 transcripts in gastric mucosa. This study assessed mechanisms by which αGlcNAc deficiency induces tumorigenesis, focusing on the IL-11 receptor α (IL-11Rα)-glycoprotein 130 (gp130)-Janus kinase 2 (JAK2)-STAT3 axis. A4gnt-deficient mice exhibited enhanced phosphorylation of JAK2 and STAT3 in pyloric mucosa compared with wild-type mice, with significant increases in JAK2 phosphorylation at 5 weeks and in STAT3 phosphorylation at 5 and 10 weeks. IL-11Rα and gp130 proteins significantly increased during this period. The thickness of the pyloric gland cell layer was significantly decreased in A4gnt and Il11 doubly deficient (A4gnt;Il11) mice at 10 but not 30 weeks compared with A4gnt-deficient mice, suggesting an IL-11 requirement in the early stage of tumorigenesis. Significant reduction of the proportion of phosphorylated STAT3-positive nuclei in pyloric mucosa of A4gnt;Il11 mice at 10 weeks supports the IL-11-mediated phosphorylated STAT3 involvement in this stage. Analysis of gastric cancer AGS-A cells overexpressing αGlcNAc using a Tet-On system revealed significant reduction of IL-11-induced STAT3 phosphorylation compared with αGlcNAc-negative conditions. Moreover, both IL-11Rα and gp130 from wild-type mice and αGlcNAc-expressing AGS-A cells carried αGlcNAc, suggesting that the presence of αGlcNAc on these proteins interferes with receptor-complex formation. These findings indicate αGlcNAc protects gastric mucosa from inflammation-induced tumorigenesis by regulating IL-11Rα-gp130-JAK2-STAT3 signaling. - Source: PubMed
Publication date: 2026/07/28
Harumiya SatoruDesamero Mark Joseph MMikoshiba ShusukeFujii ChifumiImamura HitomiKomura HitomiMatoba HisanoriOgawa ShuheiKawakubo MasatomoKakuta ShigeruNakayama Jun - Trefoil factor 2 (TFF2) has been shown to reduce inflammation and promote mucosal repair in models of gastric and colonic injury. However, the role of TFF2 in acute respiratory tract infection remains elusive. Here, we demonstrate that TFF2 protects mice against pneumonia in influenza virus infections. studies have revealed that TFF2 does not directly bind to the previously reported potential receptors but recognizes the terminal GlcNAc-α-1,4-Gal disaccharide of cell surface proteins mediated by the glycosyltransferase activity of α1,4-N-acetylglucosaminyltransferase (A4GNT). Functionally, TFF2 organized membranous TFF2-A4GNT-glycan protein complex serves to restrain cellular inflammation pathways by augmenting inhibitory Tyr527 phosphorylation at the C-terminus of Src-family kinases (SFKs), thereby effectively preventing the phosphorylation of stimulatory SFKs Tyr416. Finally, we have conclusively verified that the protective effect of TFF2 relies on the TFF2-A4GNT-glycan axis during influenza virus infection. In the future, TFF2 may offer a potential intervention strategy for acute respiratory inflammatory diseases. - Source: PubMed
Publication date: 2025/08/14
Fu WeihuiFan JunPeng TianyunSun PengYuan SonghuaZhu CuisongDing LongfeiZhang LinxiaZhao ChenZhang ShuyeZhang XiaoyanXu Jianqing - [This corrects the article DOI: 10.3389/fmicb.2025.1541800.]. - Source: PubMed
Publication date: 2025/04/22
Gong DaweiGao YuqiangShi RuiXu XiaonaYu MengchaoZhang ShuminWang LiliDong Quanjiang - Cardiovascular diseases (CVDs) encompass a group of diseases that affect the heart and/or blood vessels, making them the leading cause of global mortality. In our study, we performed proteome-wide Mendelian randomization (MR) and colocalization analyses to identify novel therapeutic protein targets for CVDs and evaluate the potential drug-related protein side effects. We conducted a comprehensive proteome-wide MR study to assess the causal relationship between plasma proteins and the risk of CVDs. Summary-level data for 4907 circulating protein levels were extracted from a large-scale protein quantitative trait loci (pQTL) study involving 35,559 individuals. Additionally, genome-wide association study (GWAS) data for CVDs were extracted from the UK Biobank and the Finnish database. Colocalization analysis was utilized to identify causal variants shared between plasma proteins and CVDs. Finally, we conducted a comprehensive phenome-wide association study (PheWAS) using the R10 version of the Finnish database. This study was aimed at examining the potential drug-related protein side effects in the treatment of CVDs. A total of 2408 phenotypes were included in the analysis, categorized into 44 groups. The research findings indicate the following associations: (1) In coronary artery disease (CAD), the plasma proteins A4GNT, COL6A3, KLC1, CALB2, KPNA2, MSMP, and ADH1B showed a positive causal relationship (-fdr < 0.05). LAYN and GCKR exhibited a negative causal relationship (-fdr < 0.05). (2) In chronic heart failure (CHF), PLG demonstrated a positive causal relationship (-fdr < 0.05), while AZGP1 displayed a negative causal relationship (-fdr < 0.05). (3) In ischemic stroke (IS), ALDH2 exhibited a positive causal relationship (-fdr < 0.05), while PELO showed a negative causal relationship (-fdr < 0.05). (4) In Type 2 diabetes (T2DM), the plasma proteins MCL1, SVEP1, PIP4K2A, RFK, HEXIM2, ALDH2, RAB1A, APOE, ANGPTL4, JAG1, FGFR1, and MLN demonstrated a positive causal relationship (-fdr < 0.05). PTPN9, SNUPN, VAT1, COMT, CCL27, BMP7, and MSMP displayed a negative causal relationship (-fdr < 0.05). Colocalization analysis conclusively identified that AZGP1, ALDH2, APOE, JAG1, MCL1, PTPN9, PIP4K2A, SNUPN, and RAB1A share a single causal variant with CVDs (PPH3 + PPH4 > 0.8). Further phenotype-wide association studies have shown some potential side effects of these nine targets (-fdr < 0.05). This study identifies plasma proteins with significant causal associations with CVDs, providing a more comprehensive understanding of potential therapeutic targets. These findings contribute to our knowledge of the underlying mechanisms and offer insights into potential avenues for treatment. - Source: PubMed
Publication date: 2025/02/21
Fan MaoxiaLi NaHuang LibinChen ChenDong XueyanGao Wulin - Selective antimicrobial effects have been found for α1,4-linked N-acetylglucosamine residues at the terminus of O-glycans attached to a core protein of gastric gland mucin. encodes α1,4-N-acetylglucosaminyl transferase, which is responsible for the biosynthesis of α1,4-linked N-acetylglucosamine. The impact of A4GNT on the establishment and homeostasis of the gastric microbiome remains to be clarified. The aim of this study was to characterize the gastric microbiome in mice deficient for the production of α1,4-linked N-acetylglucosamine. - Source: PubMed
Publication date: 2025/02/12
Gong DaweiGao YuqiangShi RuiXu XiaonaYu MengchaoZhang ShuminWang LiliDong Quanjiang