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The Glrx3.BolA is a [2Fe-2S] chaperone complex capable of transferring [2Fe-2S] clusters to apoproteins in human cells.
apo (show C9orf3 ELISA Kits) GRX3 and apo (show C9orf3 ELISA Kits) BOLA2 (show BOLA2 ELISA Kits) form a heterotrimeric complex, composed by two BOLA2 (show BOLA2 ELISA Kits) molecules and one GRX3 molecule
findings provide novel insights into the regulation of Grx3, which is crucial for cell survival against environmental insults
These findings provide an advanced view of the functional role of glutaredoxin-3 in iron metabolism.
These in vitro studies suggest that human GLRX3 is important for cytosolic Fe-S protein (show CDSN ELISA Kits) maturation.
Data indicate that silencing of Grx3 in HeLa cells decreases the activities of several cytosolic Fe/S proteins, including iron-regulatory protein 1, a major component of posttranscriptional iron regulation.
these data raise the possibility that the pro-apoptotic role of PICOT is actively regulated via caspase-3 (show CASP3 ELISA Kits)-mediated cleavage.
the unusual [2Fe-2S]-bridging Grx-BolA interaction is conserved in higher eukaryotes and may play a role in signaling cellular iron status in humans.
investigations into role of Grx3: Grx3-knockdown in HeLa cells leads to significant delay in mitotic exit and a higher percentage of binucleated cells.
analysis of primary breast cancer samples demonstrated that enhanced TXNL2 expression correlated with metastasis to the lung and brain and with decreased overall patient survival
Grx3 is a key regulator of ROS (show ROS1 ELISA Kits) in vivo and is involved in pregnancy-dependent mammary gland development and secretory activation through modulating cellular ROS (show ROS1 ELISA Kits).
Data show that protein kinase C (show PKC ELISA Kits)-interacting cousin of thioredoxin (show TXN ELISA Kits) (PICOT) alleviates myocardial I/R injury by regulating intracellular reactive oxygen species (ROS (show ROS1 ELISA Kits)) and free iron levels, and suggest that PICOT presents a therapeutic strategy for myocardial I/R injury.
investigation of role of Grx3: embryos absent Grx3 were small, morphological defects, early embryonic lethality; mRNA ubiquitously expressed in developing embryos, adult tissues; induced during oxidative stress; necessary for cell cycle progression
These data suggest that AM and PICOT might play cooperatively essential roles in embryogenesis as iron-sulfur cluster proteins.
Demonstrated a differential expression of PICOT in various cell types, with a predominant cytosolic staining of epithelial cells and low or undetectable levels of PICOT in the stroma.
PICOT inhibits cardiac hypertrophy induced by pressure overload; overexpression increased ventricular function and cardiomyocyte contractility measured by ejection fraction & end-systolic pressure of transgenic hearts & peak shortening of cardiomyocytes
PICOT regulated FcepsilonRI (show FCER1A ELISA Kits)-mediated signals in RBL-2H3 cells and acted as a positive regulator on IL-4 (show IL4 ELISA Kits) and TNF-alpha (show TNF ELISA Kits) expression, NFAT (show NFATC1 ELISA Kits) and degranulation and a negative regulator on a JNK (show MAPK8 ELISA Kits) signal pathway.
the precise PICOT protein level significantly affects the process of cardiac hypertrophy and cardiomyocyte contractility.
Data indicate that during embryonic development, depletion of Grx3 severely impairs the maturation of hemoglobin, the major iron-consuming process.
This gene encodes a member of the glutaredoxin family. Glutaredoxins are oxidoreductase enzymes that reduce a variety of substrates using glutathione as a cofactor. The encoded protein binds to and modulates the function of protein kinase C theta. The encoded protein may also inhibit apoptosis and play a role in cellular growth, and the expression of this gene may be a marker for cancer. Pseudogenes of this gene are located on the short arm of chromosomes 6 and 9. Alternatively spliced transcript variants have been observed for this gene.
thioredoxin domain containing 6
, thioredoxin-like 2
, PKC-interacting cousin of thioredoxin
, PKC-theta-interacting protein
, PKCq-interacting protein
, glutaredoxin 4
, thioredoxin-like protein 2
, PKC interacting cousin of thioredoxin