TXNL2 Antibody
- Known as:
- TXNL2 Antibody
- Catalog number:
- XW-8000
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- TXNL2 Antibody
Related genes to: TXNL2 Antibody
- Gene:
- GLRX3 NIH gene
- Name:
- glutaredoxin 3
- Previous symbol:
- TXNL2
- Synonyms:
- PICOT, bA500G10.4, GRX3, GLRX4, GRX4
- Chromosome:
- 10q26.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-27
- Date modifiied:
- 2016-10-05
Related products to: TXNL2 Antibody
Related articles to: TXNL2 Antibody
- Chronic neuropathic pain disproportionately affects older individuals, particularly in the context of persistent oxaliplatin-induced peripheral neuropathy (OIPN); however, the molecular mechanisms sustaining this ageing-biased chronicity remain elusive. In this study, we integrated age-stratified murine models and a multicentre longitudinal cohort of patients receiving oxaliplatin-based chemotherapy for colorectal cancer to investigate a glia-to-neuron redox circuit in the dorsal root ganglion. Using single-nucleus RNA sequencing and redox proteomics, we identified selective upregulation of the deglutathionylase glutaredoxin-3 (GLRX3) in satellite glial cells in aged mice during the chronic phase of OIPN. This upregulation leads to a pronounced loss of protein S-glutathionylation (PSSG) within the dorsal root ganglion, a pattern absent in young mice and during acute stages. Mechanistically, GLRX3, via its catalytic Cys148 residue, catalyses the deglutathionylation of high-mobility group box 1 (HMGB1) at the Cys106 site. This modification converts HMGB1 into a potent agonist for the toll-like receptor 4 (TLR4)-myeloid differentiation factor 2 (MD2) complex, triggering neuronal nuclear factor-κB signalling and the subsequent upregulation of transient receptor potential ankyrin 1 and vanilloid 2 channels in PACAP-positive (C1 subtype) peptidergic nociceptors, thereby sustaining long-term mechanical and cold hypersensitivity. Satellite glial cell-targeted knockdown of GLRX3 restored HMGB1 glutathionylation and reversed the pain phenotype specifically in aged mice. In the clinical cohort, advanced age was significantly associated with a higher incidence of chronic neuropathy. Longitudinal serum analysis revealed that systemic levels of PSSG and glutathionylated HMGB1 declined progressively and correlated inversely with pain duration, particularly among older individuals. Furthermore, oral γ-glutamylcysteine or pharmacologic TLR4 blockade (TAK-242) effectively alleviated refractory hypersensitivity in aged models. These findings define the satellite glial GLRX3-HMGB1-TLR4 redox axis as a critical driver of age-biased neuropathic pain. Circulating PSSG represents a novel age-stratified clinical biomarker, and targeting this redox-sensitive pathway offers a promising therapeutic strategy for geriatric and chemotherapy-related neuropathies. - Source: PubMed
Publication date: 2026/04/20
Yang YangZhao BingLiu XinyuWei GuoliHu YueChen JiaoWang YuanzheHuo JiegeCao Peng - Human cytosolic monothiol glutaredoxin-3 (GLRX3) plays a central role in the maturation of cytosolic [4Fe-4S] proteins by acting as a [2Fe2S] cluster donor to early components of the cytosolic iron-sulfur assembly (CIA) machinery, including the P-loop NTPase nucleotide-binding protein 1 (NUBP1). While previous studies have established that dimeric, cluster-bridged GLRX3 transfers its [2Fe-2S] clusters to NUBP1 promoting the formation of the [4Fe4S] cluster, the determinants within GLRX3 that enable this transfer remain unclear. Here, we analyze the specific contribution of each GLRX3 domain-glutaredoxin A (GrxA), glutaredoxin B (GrxB), and thioredoxin-like (Trx)-to the transfer of [2Fe-2S] clusters to NUBP1. We show in vitro that a cooperative mechanism between the two cluster-binding domains, GrxA and GrxB, is essential for the formation of a functional dimeric GLRX3 complex capable of efficient cluster transfer and for the assembly of the [4Fe4S] cluster on NUBP1. In contrast, the Trx domain appears dispensable for this activity in these experimental conditions. These findings may provide new insights into the features underlying GLRX3 function in cytosolic [4Fe-4S] cluster biogenesis and highlight the domain-specific contributions to its role as a [2Fe2S] cluster chaperone. - Source: PubMed
Publication date: 2025/10/10
Cuccaro RosannaMasini MartinaMalanho Silva JoséCamponeschi FrancescaBanci Lucia - Persistent organic pollutants (POPs) including polychlorinated biphenyls (PCBs), polybrominated diphenyl ethers (PBDEs), and organochloride pesticides (OCPs) affect biodiversity by bioaccumulating through food webs, impacting marine organisms like endangered sea turtles. This study represents the first evaluation of these contaminants in sea turtles nesting in São Tomé and Príncipe. The main goal was to evaluate PCBs, PBDEs and OCPs levels in sea turtles' blood and investigate their potential effects on erythrocytic nuclear abnormalities (ENAs) and oxidative stress and reproduction-related gene expression. The relative mean abundance for contaminants was ΣPCBs > ΣOCPs > ΣPBDEs. Contaminants such as PCB-28, PCB-138, PCB-153, PCB-180 and p,p'-DDE were associated with ENAs, suggesting potential genetic instability and cellular disruption. PCB-126, PBDE-100, and o,p'-DDD correlated with antioxidant and detoxification genes (glrx3, gst, txnip, txnrd2, and gclc), suggesting oxidative stress responses. The reproduction-related gene est17 was correlated with α- and β-HCH, potentially affecting ovary development. Correlations between ace2 and various PCBs, PBDEs, and o,p'-DDD suggest disruptions in follicular development and egg transport. Embryo development genes (hoxA1 and tuba1) were associated with PBDE-154, PBDE-100 and o,p'-DDD, suggesting possible embryonic alterations. These findings highlight the impacts of POPs on nesting female green turtles in São Tomé, threatening this endangered population. - Source: PubMed
Publication date: 2025/09/03
Morão Inês F CMuñoz-Arnanz JuanSimões TiagoBartalini AliceVieira SaraFerreira-Airaud BetâniaCaliani IlariaDi Noi AgataCasini SilviaFossi Maria CristinaJiménez BegoñaLemos Marco F LNovais Sara C - Glutaredoxin 3 (Grx3) is a multidomain protein (Trx-GrxA-GrxB) with a Trx-like domain and two Grx domains containing a CGFS motif for binding Fe2S2 clusters. To study the function of these domains, HeLa cells with GLRX3 knockout were generated via CRISPR/Cas. The knockout activated iron-regulatory protein 1, indicating iron starvation due to impaired iron metabolism. Transfection with constructs encoding wild-type or individual domains showed that only the Trx-GrxA construct could rescue the phenotype, matching the effect of full-length Grx3. The specific role of the second Grx domain in human Grx3, absent in simpler eukaryotes such as yeast, remains unclear. While the individual domains are insufficient to rescue the knockout of full-length Grx3, the Trx-GrxA module is functionally critical. Impact statement Glutaredoxin 3 (Grx3) contains a Trx-like domain and two Grx domains. The importance of the domains in higher eukaryotes has not previously been addressed in physiological or cellular contexts. Here, we report GLRX3 knockout results in activation of iron regulatory protein 1, and a Trx-GrxA construct could rescue the phenotype. - Source: PubMed
Publication date: 2025/05/21
Jordt Laura MagdalenaGellert ManuelaZelms FinjaBekeschus SanderLillig Christopher Horst - Hepatocellular carcinoma (HCC) is a common malignancy worldwide, and its development is closely related to abnormalities in iron metabolism. This study aims to systematically analyze changes in iron metabolism in the tumor microenvironment of HCC using single-cell sequencing technology, and investigate the potential mechanisms by which iron metabolism regulation affects the survival of liver cancer patients. - Source: PubMed
Publication date: 2024/11/25
Li YangChen YuanZhang YangFang YunshengWu LingZhao YingWang DanqiongQiao Xiaoyuan