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anti-Human Glutaredoxin 2 Anticorps:
anti-Rat (Rattus) Glutaredoxin 2 Anticorps:
anti-Mouse (Murine) Glutaredoxin 2 Anticorps:
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GRX2 is important in the control of cardiac mitochondrial structure and function, and protects against human cardiac pathologies.
Study shows that Grx2 detoxifies *NO in mature oligodendrocytes and oligodendroglial precursor cellsvia the formation of dinitrosyl-iron-complexes, inhibiting the formation of harmful peroxynitrite and reducing subsequent oligodendroglial damage. Findings link inorganic biochemistry to neuroinflammation and identify glutaredoxin 2 as a protective factor against neuroinflammation-mediated myelin damage.
Grx2 and Trx1 (Montrer MLL Anticorps) contribute significantly to neuronal integrity and could be clinically relevant in neuronal damage following perinatal asphyxia and other neuronal disorders.
The Grx2 system could help to keep Trx2 (Montrer TXN2 Anticorps)/1 reduced during an oxidative stress, thereby contributing to the anti-apoptotic signaling.
Grx2 thiol redox regulation is essential for vertebrate embryonic development
Exchange of [2Fe-2S] centers between glutaredoxin 2 and the cluster scaffold protein (Montrer HOMER1 Anticorps) ISU, supports a direct link for glutaredoxin 2 and glutathione involvement in ISU promoted Fe-S cluster biosynthesis.
Both thioredoxin 2 (Montrer TXN2 Anticorps) and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys (Montrer DNAJC5 Anticorps) peroxiredoxin Prx3 (Montrer PRDX3 Anticorps).
Studies indicate that the mechanism of Grx2 protection against H(2)O(2)-induced apoptosis is likely associated with its ability to preserve complex I.
results suggest an important role for glutaredoxin 2 in protection and recovery from oxidative stress
Grx1 (Montrer GRX1 Anticorps) and Grx2 were present in placenta extracts and in cell lysates prepared from tumor cell lines; however, the levels of Grx1 (Montrer GRX1 Anticorps) were at least 20 times higher than those of Grx2; Grx2 was not detected in plasma from healthy blood donors
Grx2 absence impairs mitochondrial fusion, ultrastructure and energetics in primary cardiomyocytes and cardiac tissue.
pre-incubation of permeabilized liver mitochondria from mouse depleted of GSH showed an approximately ~3.5-fold increase in Ogdh (Montrer alphaKGDHC Anticorps)-mediated O2(-)/H2O2 production that was matched by a significant decrease in NADH formation which could be reversed by Grx2. Taken together, our results demonstrate GSH and GSSG modulate ROS (Montrer ROS1 Anticorps) production by Ogdh (Montrer alphaKGDHC Anticorps) through S-glutathionylation of different subunits
Increasing Grx2a activity in macrophage mitochondria disrupts mitochondrial respiration and ATP production, but without affecting the proatherogenic potential of macrophages from LDL receptor (Montrer LDLR Anticorps) knockout mice.
Grx2 gene deletion altered the function of lens structural proteins through S-glutathionylation and also caused severe disturbance in mitochondrial function.
The results suggest that Glrx2b enhances RANKL (Montrer TNFSF11 Anticorps)-induced osteoclastogenesis via p38 (Montrer CRK Anticorps) activation.
Data indicate that glutaredoxin-2 (Grx2) plays a vital role in modulating mitochondrial metabolism in cardiac muscle, and Grx2 deficiency leads to pathology.
Grx2 deactivates UCP3 (Montrer UCP3 Anticorps) by glutathionylation.
Grx2 has a function that protects cells against H(2)O(2)-induced injury via its peroxidase and dethiolase activities; particularly, Grx2 prevents complex I inactivation and preserves mitochondrial function.
Immunohistochemical analysis revealed segment-specific alterations induced by the ischemic insult. Grx2, Prx3 (Montrer PRDX3 Anticorps), and Prx6 (Montrer PRDX6 Anticorps) were highly expressed in proximal tubule cells
The protein encoded by this gene is a member of the glutaredoxin family of proteins, which maintain cellular thiol homeostasis. These proteins are thiol-disulfide oxidoreductases that use a glutathione-binding site and one or two active cysteines in their active site. This gene undergoes alternative splicing to produce multiple isoforms, one of which is ubiquitously expressed and localizes to mitochondria, where it functions in mitochondrial redox homeostasis and is important for the protection against and recovery from oxidative stress. Other isoforms, which have more restrictive expression patterns, show cytosolic and nuclear localization, and are thought to function in cellular differentiation and transformation, possibly with a role in tumor progression.
glutaredoxin 2 (Grx2)
, glutaredoxin Grx2
, glutaredoxin (grx-2)
, bA101E13.1 (GRX2 glutaredoxin (thioltransferase) 2)
, glutaredoxin 2 (thioltransferase)
, glutaredoxin-2, mitochondrial