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Human Glutaredoxin 1 Protein expressed in Escherichia coli (E. coli) - ABIN2181166
Yang, Jao, Nanduri, Starke, Mieyal, Qin: Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. in Biochemistry 1999
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These results indicate that PEP1GLRX1 attenuates neuronal cell death resulting from oxidative stress in vitro and in vivo. Therefore, PEP1GLRX1 may exhibit a beneficial role in the treatment of neuronal disorders, including ischemic injury.
Data suggest an essential role of hepatic Glrx in regulating SirT1, which controls protein glutathione adducts in the pathogenesis of hepatic steatosis.
Grx1 deficiency leads to eNOS dysfunction through oxidative modification of S-glutathionylation of eNOS (eNOS-SSG) and inactivation of NO production, enhancing the endothelial TLR4 activation, and ultimately exacerbating necrotizing enterocolitis severity.
Study reports a decrease of Grx expression levels in pancreatic islets of diabetic mice which was accompanied by declining insulin secretion, increase of reactive oxygen species (ROS) production level, and cell cycle alterations. These data demonstrate the essential role of the Grx 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 upregulation promotes neuroinflammation and consequent neuronal cell death in vitro, and synergizes with proinflammatory insults to promote DA loss in vivo.
the Glrx1-Protein S-glutathionylation axis plays a pivotal role in house dust mite-induced allergic airways disease.
Glrx ablation stabilizes HIF-1alpha by increasing GSH adducts on Cys(520) promoting in vivo HIF-1alpha stabilization, VEGF-A production, and revascularization in the ischemic muscles.
Prx2 glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling. GSH/Grx1 provide an alternative mechanism to thioredoxin and thioredoxin reductase for Prx2 recycling.
The temporal relationships of Glrx1 with protein S-glutathionylation, glutathione, and cytokines/chemokines were observed as dynamic changes in lungs with allergic airway inflammation
Glutaredoxin 1 plays an important role in controlling epithelial cell responsiveness to IL-17A
Up-regulated Glrx inhibits VEGF signaling by increased Flt1 causing impaired vascularization.
S-glutathionylation of Fas in lung epithelium enhances epithelial apoptosis and clearance of P. aeruginosa. Glutaredoxin-1 impairs bacterial clearance and increases severity of pneumonia in association with deglutathionylation of Fas.
These data suggest that the overexpression of GRX1 could protect cardiomyocytes against NO-induced apoptosis, likely through the inhibition of the oxidative modification and the nuclear translocation of GAPDH.
we provide evidence that Grx1 has an important role in regulating cigarette smoke-induced lung inflammation which seems to diverge from its effects on total PSSG.
Data show that glutaredoxin acts as a reductant for methionine sulfoxide reductases A and B (MsrA and MsrB) with or without resolving cysteine.
results are the first to demonstrate that Grx-1 induces angiogenesis and diminishes ventricular remodeling apparently through neovascularization mediated by Akt, VEGF, Ang-1 and NF-kappaB as well as Bcl-2 and survivin-mediated anti-apoptotic pathway
This result signifies that the presence of the gene allows a 1.3 times longer in vivo exposure to UVR, at equivalent irradiance, than the absence of the gene before early-onset.
These results showed that cigarette smoke can modulate glutaredoxin 1, not only at the expression level, but can also directly modify glutaredoxin 1 itself, decreasing its activity.
gene activation is positively regulated by NF-kappaB
Grx1 regulates the production of inflammatory mediators through control of S-glutathionylation-sensitive signaling pathways.
Glutaredoxin-1 silencing induces cell senescence via p53/p21/p16 signaling axis.
Overexpression of NOS3 increased the levels and activities of proteins of the redoxin systems, Trx1, Grx1, TrxR1 and TxnIP, and the levels of signaling proteins (Akt1, pAkt1(-)Ser473, MapK, pMapK, Stat3, Fas).
Based on the roGFP2-hGrx1 signals, glutathione-dependent redox potentials of -267mV and -328mV, respectively, were obtained. Employing these novel tools, initial studies on the effects of redox-active agents and clinically employed antimalarial drugs were carried out on both organelles.
Reduction potentials of protein disulfides and catalysis of glutathionylation and deglutathionylation by glutaredoxin enzymes
GRX1 overexpression constrains oxidative stress and apoptosis in osteoarthritis chondrocytes by regulating CREB/HO-1, providing a novel insight into the molecular mechanism and potential treatment of osteoarthritis.
Glutaredoxin 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 and Grx1 and support the strategy of weakening the thiolic antioxidant defenses when designing new antitumoral therapies.
Glutaredoxin 1 protects human retinal pigment epithelial cells from oxidative damage by preventing AKT glutathionylation.
A new function for GRX1 in neuronal copper homeostasis and in protection from copper-mediated oxidative injury.
Human Grx1 can catalyse reduction of Atox1 by glutathione but only in the presence of Cu(I).
Levels of GLRX in the cerebrospinal fluid increase significantly in the early stages of Alzheimer's disease.
Glrx overexpression increased soluble VEGF receptor 1 (sFlt) in endothelial cells via NF-kappaB-dependent Wnt5a production.
Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system.
sputum glutaredoxin-1 may have a role in asthma, while protein S may have a role in better lung function
Studies show that the glutaredoxin system with glutathione plays a backup role to keep oxidized thioredoxin 1 (Trx1) reduced in cells with loss of thioredoxin reductase 1 (TrxR1) activity.
Results indicate that the activation of eNOS/NO system is regulated by Grx 1 and coupled with inhibition of JNK and NF-kappaB signaling pathway which could alleviate the oxidative stress/apoptosis in coronary arteries endothelial cells induced by HG.
Long molecular dynamics simulations and electrostatic calculations were used to analyze the structure, dynamics and electrostatics of reduced pGrx and some of its mutants.
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 1 (thioltransferase)
, glutaredoxin Grx1
, glutaredoxin (grx-1)
, glutaredoxin (thioltransferase)
, hypothetical protein
, thiol disulfide oxidoreductase
, glutaredoxin-1 (Grx1)
, glutaredoxin L homeolog