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Grx2 and Trx1 (show MLL Proteins) 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 (show TXN2 Proteins)/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 (show HOMER1 Proteins) ISU, supports a direct link for glutaredoxin 2 and glutathione involvement in ISU promoted Fe-S cluster biosynthesis.
Both thioredoxin 2 (show TXN2 Proteins) and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys (show DNAJC5 Proteins) peroxiredoxin Prx3 (show PRDX3 Proteins).
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 (show GRX1 Proteins) and Grx2 were present in placenta extracts and in cell lysates prepared from tumor cell lines; however, the levels of Grx1 (show GRX1 Proteins) were at least 20 times higher than those of Grx2; Grx2 was not detected in plasma from healthy blood donors
Lung cells can synthesize Grx2 mRNA and protein.
characterization of Grx2 as an iron-sulfur center-containing member of the thioredoxin (show TXN Proteins) fold protein family
Increasing Grx2a activity in macrophage mitochondria disrupts mitochondrial respiration and ATP production, but without affecting the proatherogenic potential of macrophages from LDL receptor (show LDLR Proteins) 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 (show TNFSF11 Proteins)-induced osteoclastogenesis via p38 (show CRK Proteins) 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 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 (show PRDX3 Proteins), and Prx6 (show PRDX6 Proteins) were highly expressed in proximal tubule cells
Data indicate that glutaredoxin 2 plays a central role in the response of mitochondria to both redox signals and oxidative stress by facilitating the interplay between the mitochondrial glutathione pool and protein thiols.
Glutaredoxin-2 expression increased in a murine model of high-fat diet-induced atherogenesis.
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