Human Endothelial nitric oxide synthase 3(eNOS-3)ELISA Kit
- Known as:
- Human Endothelial nitric oxide synthase 3(eNOS-3)Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- 27021
- Product Quantity:
- 1000pg/ml-15.6pg/ml <5pg/ml
- Category:
- -
- Supplier:
- TEFL
- Gene target:
- Human Endothelial nitric oxide synthase 3(eNOS-3)ELISA Kit
Related genes to: Human Endothelial nitric oxide synthase 3(eNOS-3)ELISA Kit
- Gene:
- C1GALT1 NIH gene
- Name:
- core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Previous symbol:
- -
- Synonyms:
- C1GALT, T-synthase
- Chromosome:
- 7p22.1-p21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-26
- Date modifiied:
- 2018-02-13
Related products to: Human Endothelial nitric oxide synthase 3(eNOS-3)ELISA Kit
Related articles to: Human Endothelial nitric oxide synthase 3(eNOS-3)ELISA Kit
- The GARP complex is an evolutionarily conserved protein complex proposed to tether endosome-derived vesicles at the trans-Golgi network. While complete depletion of the GARP leads to severe trafficking and glycosylation defects, the primary defects linked to GARP dysfunction remain unclear. In this study, we utilized the mAID degron strategy to achieve rapid degradation of VPS54 in human cells, acutely disrupting GARP function. This resulted in the partial mislocalization and degradation of a subset of Golgi-resident proteins, including TGN46, ATP7A, TMEM87A, CPD, C1GALT1 and GS15. Enzyme recycling defects led to O-glycosylation abnormalities. Additionally, while fibronectin and cathepsin D secretion were altered, mannose-6-phosphate receptors were largely unaffected. Partial displacement of COPI, AP1 and GGA coats caused a significant accumulation of vesicle-like structures and large vacuoles. Electron microscopy detection of GARP-dependent vesicles and identifying specific cargo proteins provide direct experimental evidence of GARP's role as a vesicular tether. We conclude that the primary defects of GARP dysfunction involve vesicular coat mislocalization, accumulation of GARP-dependent vesicles, degradation and mislocalization of specific Golgi proteins and O-glycosylation defects. - Source: PubMed
Khakurel AmritaPokrovskaya IrinaAragon-Ramirez Walter SLupashin Vladimir V - Mucin type O-glycan core elongation is typically performed by the C1GALT1, B3GNT6, and ST6GalNAc-I/-II O-glycosyltransferases. These enzymes target the Tn antigen (GalNAc-O-Thr/Ser) dictating the fate of O-glycan elongation, playing important roles in health and disease. Changes in transferase expression and glycan structure are commonly associated with diseases such as cancer, Tn-syndrome, and ulcerative colitis. Despite their significance, their substrate specificities and their biological roles remain elusive. Here, we examine the roles of flanking glycopeptide substrate charge using a library of differently charged glycopeptides and a small library of PSGL-1 Thr57 based charged glycopeptides. We found that C1GALT1 was most influenced by flanking charge preferring negatively charged substrates, while B3GNT6 and ST6GalNAc-II were less influenced, showing unique N- and C-terminal charge preferences. Interestingly, ST6GalNAc-I was not influenced by flanking charge. These charge specificities were further maintained against the charged PSGL-1 glycopeptides, although ST6GalNAc-I showed an increased preference towards a remote N-terminal positive charge. The observed charge preferences were to a large part driven by substrate interactions with the electrostatic surface of the transferase. We propose that negative flanking charge may assist C1GALT1 in targeting key glycosites such as in PSGL-1 and podoplanin. Our findings are consistent with a Golgi hierarchy, where the cis-Golgi localized GalNAc-Ts and C1GALT1 determine the site and thus fate of glycosylation, while the trans-Golgi less-specific ST6GalNAc-I provides a final capping function. This characterization of substrate charge preference furthers our understanding of how these enzymes select their substrates and may contribute to our understanding of their biological roles. - Source: PubMed
Publication date: 2025/03/10
Ballard Collin JSmutny Matthew RChau Lam DWong Collin KAharoni Haley MLee Hana KChapla Digantkumar GHurtado-Guerrero RamonMoremen Kelley WGerken Thomas A - Ewing sarcoma (ES) is an aggressive bone cancer driven by the oncogenic fusion-protein EWSR1::FLI1, which is not present in normal cells and is therefore an attractive therapeutic target. However, as a transcription factor, EWSR1::FLI1 is considered undruggable. Factors that promote EWSR1::FLI1 expression, and thus whose inhibition would reduce EWSR1::FLI1 protein levels and function, are potential drug targets. Here, using genome-scale CRISPR/Cas9 knockout screening, we identify C1GALT1, a galactosyltransferase required for the biosynthesis of many O-glycoproteins, as a factor that promotes EWSR1::FLI1 expression. We show that C1GALT1 acts by O-glycosylating the pivotal Hedgehog (Hh) signaling component Smoothened (SMO), thereby stabilizing SMO and stimulating the Hh pathway, which we find directly activates EWSR1::FLI1 transcription. Itraconazole, an FDA-approved anti-fungal agent that is known to inhibit C1GALT1, reduces EWSR1::FLI1 levels in ES cell lines and suppresses growth of ES xenografts in mice. Our study reveals a therapeutically targetable mechanism that promotes EWSR1::FLI1 expression and ES tumor growth. - Source: PubMed
Publication date: 2025/02/02
Banday ShahidMishra Alok KRashid RomanaYe TianyiAli AmjadLi JunhuiYustein Jason TKelliher Michelle AZhu Lihua JulieDeibler Sara KMalonia Sunil KGreen Michael R - Osteosarcoma is an aggressive bone malignancy with a high propensity for drug resistance and metastasis, leading to poor clinical outcomes. This study investigates the role of core 1 β1,3-galactosyltransferase 1 (C1GALT1) in osteosarcoma, focusing on its implications in chemoresistance. Our findings reveal that high expression of C1GALT1 is associated with advanced stages, adverse overall survival, and increased recurrence rates. Elevated levels of C1GALT1 were observed in doxorubicin-selected osteosarcoma cells, where its suppression significantly promoted doxorubicin-induced apoptosis and reduced drug efflux. Pharmacological inhibition of C1GALT1 using itraconazole replicated these effects, suggesting a potential therapeutic strategy to overcome chemoresistance. Additionally, we identified the involvement of the ATP-binding cassette (ABC) transporter ABCC1 in the drug-resistance phenotype mediated by C1GALT1. C1GALT1-mediated O-glycan changes were found to influence the cell-surface targeting and lysosomal degradation of ABCC1, thereby modulating its efflux capacity. In vitro and in vivo studies confirmed that C1GALT1 impacts ABCC1 expression and function, further supporting its role in osteosarcoma chemoresistance. These results highlight the clinical relevance of C1GALT1 as a biomarker for prognosis and a potential therapeutic target for osteosarcoma. © 2025 The Author(s). The Journal of Pathology published by John Wiley & Sons Ltd on behalf of The Pathological Society of Great Britain and Ireland. - Source: PubMed
Publication date: 2025/01/22
Liu Chun-WeiHuang Jing-HuiChang Hsiu-HaoChen Chia-HuaTsai Yi-HuanChen Wei-LiLin Jung-AnChang Hsiu-LingChen Cheng-ChangLin Mei-ChunHuang Min-ChuanLin Neng-Yu - Goats typically have double coats, with the outermost coarse hairs providing protection against mechanical and radiation damage. While much attention has been paid to cashmere due to its status as a high-end textile material, there is limited information available on coarse hair. This study aimed to identify genomic variants, such as single nucleotide polymorphisms (SNPs) and insertion/deletions (indels), associated with coarse hair diameter using a genome-wide association study (GWAS). Coarse hairs and blood samples were collected from 263 adult female goats. The diameter of coarse hairs was measured using an inverted microscope, and whole genome sequencing was conducted on the blood samples. After reads mapping, variants calling, and quality control, totals of 11 322 006 SNPs and 863 734 indels were included for SNP-GWAS and indel-GWAS analyses. Eight significant SNPs (p < 8.98e-8) and three significant indels (p < 1.16e-6) were identified. Among those, one SNP was located on Chromosome 4 and near the genes COL28A1 and C1GALT1. Seven significant SNPs were found in the region chr10_96664101-96670958, with the genes CDO1 and TMED7 located upstream and downstream, respectively. Haplotype analysis revealed that the diverse haplotypes of these seven SNPs presented varying values for coarse hair diameter. Notably, the only consistently significant insertion (chr10_96665085, GTA>G) was also located within the region chr10_96664101-96670958, further highlighting the importance of this genomic region in influencing coarse hair diameter. These significant variants and genomic regions provide valuable insights for investigating the genetic mechanisms underlying the variation in fiber diameter. - Source: PubMed
Zhang JipanFang JiabeiZhang SiyuanXu JieleZhao Yongju