SORD Rabbit antibody Ab Aff - Purified
- Known as:
- SORD Rabbit (anti-) Antibody Aff - Purified
- Catalog number:
- GTX114791
- Product Quantity:
- 0.1 ml
- Category:
- -
- Supplier:
- ACR
- Gene target:
- SORD Rabbit antibody Aff - Purified
Related genes to: SORD Rabbit antibody Ab Aff - Purified
- Gene:
- SORD NIH gene
- Name:
- sorbitol dehydrogenase
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 15q21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-10-05
Related products to: SORD Rabbit antibody Ab Aff - Purified
Related articles to: SORD Rabbit antibody Ab Aff - Purified
- The carcinogenic relevance of environmental contaminant bisphenol A (BPA) to colorectal cancer (CRC) has gained growing attention, yet the molecular networks potentially linking BPA exposure to CRC remain incompletely characterized. This study integrated network toxicology and machine learning to predict candidate molecular targets and putative signaling networks associated with BPA-correlated colorectal carcinogenesis. The study's methodology involved an initial differential expression screening across several CRC transcriptomic datasets to establish a disease-specific gene signature. Subsequently, a multi-tiered computational strategy was employed: network toxicology was used to map potential BPA-protein interactions, machine learning algorithms were applied to distill a minimal set of high-impact targets, and molecular docking simulations provided atomic-level validation of the proposed binding events. We identified 53 overlapping genes between predicted BPA-interacting proteins and CRC-related transcripts. Machine learning screening further filtered a 12-gene panel with favorable predictive performance for CRC status, including MET, SORD, DPEP1, KIT, RIPK2, SET, HSP90AB1, DBF4, MMP1, MMP12, ANPEP, and GLA. Molecular docking simulations predicted stable binding interactions between BPA and the protein products encoded by these 12 genes. This study delineates a specific gene network potentially targeted by BPA to promote CRC pathogenesis. The machine learning-derived 12-gene signature, interpreted as CRC-associated genes overlapping with predicted BPA targets and supported by in silico molecular docking, offers valuable insights into the molecular basis of BPA-associated colorectal carcinogenesis and presents candidate targets for subsequent experimental validation. - Source: PubMed
Publication date: 2026/08/16
Li XiaoxuanMai GenningXiao YuexiZhao RuijunHuang XiyueLi JunxiXiao YuchenDeng ZhujunLi MiaoXiong Wenjun - Biallelic pathogenic variants in SORD (Sorbitoldehydrongenase gene), encoding sorbitol dehydrogenase, are a common cause of autosomal recessive axonal Charcot-Marie-Tooth disease type 2 (CMT2). Recent evidence suggests direct involvement of skeletal muscle in addition to peripheral nerve degeneration. We investigated muscle biopsies from 4 genetically confirmed CMT-SORD patients using an integrative approach. Histological evaluation revealed features of chronic denervation with grouped fiber atrophy, fiber-type grouping and central nuclei, ie, non-specific neurogenic muscle atrophy. Ultrastructural studies demonstrated mitochondrial abnormalities and expansion of the sarcoplasmic reticulum (SR). Proteomic profiling identified 220 significantly dysregulated proteins in CMT-SORD muscle, including alterations in mitochondrial complex I components, redox enzymes, and metabolic regulators distinct from changes observed in other rare recessive CMTs. Quantitative PCR validated increased levels of NNMT, POSTN, TACO1, as well as complement and immunomodulatory factors, suggesting mitochondrial stress, compensatory metabolic activation and tissue remodeling. Despite mitochondrial vulnerability, serum studies indicated that GDF-15 and FGF-21 did not appear to be suitable biomarkers for CMT-SORD. These findings demonstrate that SORD deficiency induces molecular and structural changes in skeletal muscle that extend beyond denervation, implicating impaired sorbitol metabolism, oxidative stress, and mitochondrial dysfunction as intrinsic myopathic features of SORD-related CMT2. They indicate the need for therapeutic strategies targeting both neuronal and muscular compartments. - Source: PubMed
Publication date: 2026/08/19
Kölbel HeikeHentschel AndreasPreuße CorinnaTiet MayDohrn Maike FMuhmann Davidvan den Ameele JelleChen LeiSchara-Schmidt UlrikeWeis JoachimHorvath RitaMensch AlexanderRoos Andreas - The upregulation of cyclooxygenase-2 (COX-2) and the subsequent production of prostaglandin E (PGE) in synovial tissue are hallmarks of autoimmune arthritis, including rheumatoid arthritis (RA). While glucosamine (GlcN) derivatives modulate RA symptoms, their specific anti-inflammatory mechanisms in synovial fibroblasts (SFBs) are poorly understood. In this study, we evaluated the anti-inflammatory efficacy of various GlcN derivatives: glucosamine hydrochloride (GlcN-HCl), glucosamine sulfate (GlcN-S), glucosaminate (GlcNA), and N-acetylglucosamine (GlcNAc). GlcN-HCl and GlcN-S inhibited IL-1β-induced PGE release and the expression of COX-2 at both protein and mRNA levels, whereas GlcNA and GlcNAc exhibited no such inhibitory activity. Structure-activity relationship analysis using GlcN-HCl epimers revealed that whereas the C-4 epimer, galactosamine hydrochloride (GalN-HCl), retained potent anti-inflammatory effects, the C-2 epimer, mannosamine hydrochloride (ManN-HCl), showed significantly diminished bioactivity, highlighting the critical role of the C-2 stereochemical configuration in modulating inflammatory responses. Mechanistically, we demonstrated that GlcN-HCl-mediated COX-2 suppression occurs via epigenetic silencing rather than mRNA destabilization. GlcN-HCl treatment significantly reduced the enrichment of active chromatin marks, H3K27ac and H3K4me3, at the COX-2 promoter, whereas mRNA stability remained unaffected. Given that metabolic dysregulation is intrinsically linked to inflammatory pathogenesis, we characterized the metabolic profile of GlcN-HCl-treated SFBs. We found that GlcN-HCl triggers metabolic reprogramming of the polyol pathway by modulating the expression of AKR1B1 and sorbitol dehydrogenase (SORD), resulting in elevated intracellular sorbitol levels. Pharmacological inhibition of AKR1B1 effectively abrogated the anti-inflammatory effects of GlcN-HCl, indicating that polyol pathway activation is essential for its efficacy. We confirmed the evolutionary conservation of these findings in human SFBs, demonstrating the translational relevance of the GlcN-HCl-mediated metabolic and epigenetic axis. Our findings demonstrate that GlcN-HCl induces metabolic reprogramming of the polyol pathway in synovial fibroblasts, facilitating the epigenetic silencing of inflammatory mediators. This metabolic-epigenetic axis suggests a mechanistic rationale for pharmacological metabolic intervention in RA, shifting the therapeutic paradigm toward targeted reprogramming of synovial fibroblast metabolism. - Source: PubMed
Publication date: 2026/07/01
Okada JunichiNakano ReiKitanaka NanakoKitanaka TakuNamba ShinichiNakano MasumiNaruke AtsutoNunomura JunichiSuwabe YokoKonno TadayoshiTohi TomokoKuno SatoruKimura TaroUechi MasamiNakayama TomohiroYamazaki JunSugiya Hiroshi - The plasmid-borne gene poses a significant threat to global health by conferring resistance to colistin, a critical last-resort antibiotic. While its spread is well documented, the adaptations enabling its concurrent antibiotic resistance and clinical pathogenicity remain unknown. The metabolism of bacterial pathogens has evolved to support virulence in nutrient-limiting host environments. Here, we show that sorbose metabolism promotes the fitness and virulence of positive (MCRPEC), but does not affect its resistance to colistin or polymyxin B. Notably, the virulence contribution is also observed in an -negative background. Genetic disruption of sorbose catabolism (Δ) attenuated MCRPEC virulence and fitness both and . Integrated transcriptomic and metabolomic analyses suggest that this attenuation is associated with impaired expression of two major virulence determinants. First, defective sorbose metabolism limits the supply of monosaccharide precursors required for LPS biosynthesis, leading to reduced LPS content. Second, metabolic disruption decreases intracellular cAMP levels, which downregulates expression via a cAMP-dependent signaling pathway, thereby compromising bacterial adhesion. Notably, although deletion enhances biofilm formation, this increase is insufficient to rescue the virulence defect. Restoration of the sorbose metabolic pathway partially rescues MCRPEC pathogenicity. These findings suggest that sorbose metabolism contributes to MCRPEC pathogenicity by supporting LPS synthesis and regulating expression via cAMP signaling. This study indicates a metabolic link between sorbose utilization and MCRPEC pathogenicity, raising the possibility that sorbose, a common food additive, could facilitate MCRPEC pathogenicity.IMPORTANCEThe spread of colistin-resistant () limits treatment options for life-threatening infections. This study shows that sorbose metabolism, which utilizes a common dietary sugar, contributes to the fitness and virulence of such resistant bacteria without affecting their colistin resistance. Using -positive , we find that this metabolic pathway supports lipopolysaccharide synthesis and, via a cAMP-dependent mechanism, promotes bacterial adhesion. Disabling sorbose catabolism attenuates the pathogen in animal models. These findings suggest a previously unrecognized link between a specific carbohydrate metabolism and pathogenesis in drug-resistant , raising the possibility that dietary components may influence infection outcomes. - Source: PubMed
Publication date: 2026/06/15
Deng XueShen CongChen LingjuanSun DandanQiu TianZhao ZihanLi TongZhang GuiliWu JiWang JuanTian Guo-BaoXu LingqingYan BinZhong Lan-Lan - The objective of this study was to investigate the effects of trehalose and different doses of melatonin and lipid mixtures on the quality parameters of post-thaw bull sperm during cryopreservation. The ejaculates of three mature bulls were pooled and divided into ten equal aliquots. These aliquots were diluted with a Tris-based extender, which was supplemented with either 5% glycerol (G5) or 3% glycerol combined with 60 mM trehalose (G3T), alongside different doses of melatonin and lipid mixtures. Ten experimental groups were established as follows: G5, G5+0.25 mM melatonin (G5M0.25), G5+0.75 mM melatonin (G5M0.75), G5+ 1.25 μl/ml lipid mixtures (G5L1.25), G5+3.75 μl/ml lipid mixtures (G5L3.75), G3T, G3T+0.25 mM melatonin (G3TM0.25), G3T+0.75 mM melatonin (G3TM0.75), G3T+1.25 μl/ml lipid mixtures (G3TL1.25), and G3T+3.75 μl/ml lipid mixtures (G3TL3.75). No significant interaction was detected between any of the groups containing the G5 and G3T extenders, and all groups were found to be similar for sperm motility and flow cytometry analysis results (p > 0.05). The G5M0.25 and G5L1.25 groups had a higher recovery of post-thaw motility compared to the other groups containing 5% glycerol (p = 0.0004). In terms of motility rates, groups G3TM0.25 and G3TL1.25 displayed a higher level of protection compared to the other groups, and this protection was significantly greater than that determined in groups G3TM0.75 and G3TL3.75 (p = 0.001). The expression of the GFPT1, PFKP, FBF2, HK1, and ALDH2 genes was found to be significantly increased in the G5 and G3T groups containing both doses of lipid mixtures (L1.25 and L3.75) compared to the groups without additives (G5 and G3T) (p < 0.001-0.0001). However, the expression of the SORD gene was found to be increased only in the G3TL1.25 and G3TL3.75 groups compared to group G3T (p < 0.01-0.001). GFPT1 and FBF2 gene expressions were significantly increased in the G5M0.75 group compared to group G5 (p < 0.05). The G3T groups containing both doses of melatonin were found to display increased GFPT1 (p < 0.01) and PFKP (p < 0.05-0.01) expression levels compared to group G3T. It was determined that the addition of lipid mixtures at both doses to both G5 and G3T resulted in a significant transcriptional increase in all of the genes studied (except for SORD gene expression in the G5L1.25 and G5L3.75 groups), compared to the lipid mixtures-free groups (p < 0.05-0.001). Based on the evaluation of all results, G3T can be used as a substitute for G5 to reduce glycerol toxicity. - Source: PubMed
Publication date: 2026/06/10
Ağır VahitBucak Mustafa NumanGarip MustafaSarı Muhammet Eminİnanç Muhammed Enes