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Data suggest an essential role of hepatic Glrx (show GRX1 Antibodies) in regulating SirT1 (show SIRT1 Antibodies), which controls protein glutathione adducts in the pathogenesis of hepatic steatosis.
Grx1 (show GRX1 Antibodies) deficiency leads to eNOS (show NOS3 Antibodies) dysfunction through oxidative modification of S-glutathionylation of eNOS (eNOS (show NOS3 Antibodies)-SSG) and inactivation of NO production, enhancing the endothelial TLR4 (show TLR4 Antibodies) activation, and ultimately exacerbating necrotizing enterocolitis severity.
Study reports a decrease of Grx (show GRX1 Antibodies) expression levels in pancreatic islets of diabetic mice which was accompanied by declining insulin (show INS Antibodies) secretion, increase of reactive oxygen species (ROS (show ROS1 Antibodies)) production level, and cell cycle alterations. These data demonstrate the essential role of the Grx (show GRX1 Antibodies) system for the beta-cell during metabolic stress which may provide a new target for diabetes mellitus type 2 treatment.
Our results indicate that Grx1 (show GRX1 Antibodies) upregulation promotes neuroinflammation and consequent neuronal cell death in vitro, and synergizes with proinflammatory insults to promote DA loss in vivo.
the Glrx1 (show GRX1 Antibodies)-Protein S-glutathionylation axis plays a pivotal role in house dust mite-induced allergic airways disease.
Glrx (show GRX1 Antibodies) ablation stabilizes HIF-1alpha (show HIF1A Antibodies) by increasing GSH adducts on Cys (show DNAJC5 Antibodies)(520) promoting in vivo HIF-1alpha (show HIF1A Antibodies) stabilization, VEGF-A (show VEGFA Antibodies) production, and revascularization in the ischemic muscles.
Prx2 (show PRRX2 Antibodies) glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling. GSH/Grx1 (show GRX1 Antibodies) provide an alternative mechanism to thioredoxin (show TXN Antibodies) and thioredoxin reductase (show PRDX2 Antibodies) for Prx2 (show PRRX2 Antibodies) recycling.
The temporal relationships of Glrx1 (show GRX1 Antibodies) with protein S-glutathionylation, glutathione, and cytokines/chemokines were observed as dynamic changes in lungs with allergic airway inflammation
Glutaredoxin 1 (show GRX1 Antibodies) plays an important role in controlling epithelial cell responsiveness to IL-17A (show IL17A Antibodies)
Up-r (show GRX1 Antibodies)egulated Glrx inhibits VEGF signaling by increa (show FLT1 Antibodies)sed Flt1 causing impaired vascularization.
Overexpression of NOS3 (show NANOS3 Antibodies) increased the levels and activities of proteins of the redoxin systems, Trx1 (show MLL Antibodies), Grx1 (show GRX1 Antibodies), TrxR1 (show TXNRD1 Antibodies) and TxnIP (show TXNIP Antibodies), and the levels of signaling proteins (Akt1 (show AKT1 Antibodies), pAkt1(-)Ser473, MapK (show MAPK1 Antibodies), pMapK, Stat3 (show STAT3 Antibodies), Fas (show FAS Antibodies)).
Reduction potentials of protein disulfides and catalysis of glutathionylation and deglutathionylation by glutaredoxin (show GRX1 Antibodies) enzymes
GRX1 (show GRX1 Antibodies) overexpression constrains oxidative stress and apoptosis in osteoarthritis chondrocytes by regulating CREB (show CREB1 Antibodies)/HO-1 (show HMOX1 Antibodies), providing a novel insight into the molecular mechanism and potential treatment of osteoarthritis.
Glutaredoxin (show GRX1 Antibodies) desensitizes lens to oxidative stress by connecting and integrating specific signaling and transcriptional regulation for antioxidant response.
The results demonstrate that the antiproliferative effect of NO is hampered by Trx1 (show MLL Antibodies) and Grx1 (show GRX1 Antibodies) and support the strategy of weakening the thiolic antioxidant defenses when designing new antitumoral therapies.
Prx2 (show PRDX2 Antibodies) glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling. GSH/Grx1 (show GRX1 Antibodies) provide an alternative mechanism to thioredoxin (show TXN Antibodies) and thioredoxin reductase (show PRDX5 Antibodies) for Prx2 (show PRDX2 Antibodies) recycling.
Glutaredoxin 1 (show GRX1 Antibodies) protects human retinal pigment epithelial cells from oxidative damage by preventing AKT (show AKT1 Antibodies) glutathionylation.
A new function for GRX1 (show GRX1 Antibodies) in neuronal copper homeostasis and in protection from copper-mediated oxidative injury.
This gene encodes a member of the glutaredoxin family. The encoded protein is a cytoplasmic enzyme catalyzing the reversible reduction of glutathione-protein mixed disulfides. This enzyme highly contributes to the antioxidant defense system. It is crucial for several signalling pathways by controlling the S-glutathionylation status of signalling mediators. It is involved in beta-amyloid toxicity and Alzheimer's disease. Multiple alternatively spliced transcript variants encoding the same protein have been identified.
, glutaredoxin (thioltransferase)
, glutaredoxin 1 (thioltransferase)