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results suggest JNK/FOXO mediated dPrxV (Peroxiredoxin 5) expression plays a critical role in Drosophila melanogaster gut during bacterial infection in protecting the host gut epithelial cells from oxidative damage
flies underexpressing peroxiredoxin 3 and peroxiredoxin 5 showed an 80% reduction in lifespan and a massive induction of apoptosis in the muscle and digestive system tissues
Overexpressiion of Prx5 were more susceptible to bacterial infection in Drosophila melanogaster .
the antioxidant and anti-apoptotic activities of dPrx5 play a critical role in development and aging of the fly
Single-molecule experiments demonstrate that PRDX5 specifically binds to TLR4. PRDX5 binding induces a cellular mechanoresponse.
High PRX5 expression is associated with gastric cancer.
Results found that Prx5 was increased in the cellular model of Alzheimer's disease (AD) and, identify a role for Prx5 as an upregulator of Cdk5 activation via reactive oxygen species-mediated Ca2+-mediated calpain activation.
The PRX5 can be used as a predictive biomarker and serves as a putative therapeutic target for the development of clinical treatments for human CRC.
peroxisomal PRDX5 protects oligodendrocytes against peroxisomal and mitochondrial oxidative stress.
show here how the ligand-observed saturation transfer difference (STD) experiment and the PRDX5 protein-observed 15N-HSQC experiment, two popular NMR screening experiments, can be used to compare the binding modes of analogous fragments
PRX5 is either consumed or its production is impaired in severe stroke
This study demonistrated that overexpression of mitochondrial PRDX5 protects SH-SY5Y cells against the ROS/RNS-dependent neuronal death induced by MPP+.
The promoter region critical for Prx5 gene regulation to which the novel negative transcription regulator, GATA1 binds in human breast cancer cell lines.
basal expression of the human PRDX5 gene is regulated by GABP
analysis of fragment molecules that bind the human peroxiredoxin 5 active site
Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism
the expression of peroxiredoxin 5 is upregulated in osteoarthritis
multiple subcellular targeting of peroxiredoxin 5 in mammalian cells can be implicated in antioxidant protective mechanisms under nonpathological conditions
Transfection of PRXVI protects immortalized human WI-38 and murine NIH3T3 fibroblasts against cytotoxic doses of tert-butylhydroperoxide and H2O2
new crystal form of human peroxiredoxin 5 is described at 2.0 A resolution; under initial reducing conditions, one chain remains oxidized and forms an homodimer with a symmetry-related one through intermolecular disulfide bonds between Cys47 and Cys151
plays a protective role in human tendon cells against oxidative stress by reducing apoptosis and maintaining collagen synthesis
Human peroxiredoxin 5 is also a peroxynitrite reductase.
nuclear PrxV associates with coilin-containing bodies suggesting possible interaction of this protein with transcription complexes
The level of expression is directly correlated with the functional status of epithelial cells, being higher in multinodular goiters, and even more pronounced in hyperthyroid tissues, such as Graves' disease.
glutamate-stimulated activation of ROS may provoke the induction of Prx V, which has an antioxidative function in glutamate-stimulated HT22 cell apoptosis, and PrxV may serve a role in neural apoptosis.
PRX1 and PRX5 were upregulated in osteoblasts in the proximal tibial metaphysis of ovariectomized mice. Interestingly, PRX1 and PRX5 showed different distribution patterns, with PRX1 mainly accumulated in cell nuclei and PRX5 in the cytoplasm.
These data provided a plausible mechanism linking maternal vitamin D deficiency with altered postnatal lung function.
The ventral signal observed from E12.5 on colocalized with motor neuron markers Isl1/2 and FoxP1 and The strong ventral signal colocalizing wtth Isl1/2 was observed in all rostrocaudal segments of the spinal cord.
results suggest that PrdxV is a key mediator contributing to the regulation of LPS/TLR4-induced immune responses
IMS-PRDX5 expression also attenuates the increase in cytosolic [Ca(2+)] in PASMCs during hypoxia.
The SirT1 regulates the expression of several antioxidant genes in bovine aortic endothelial cells, including Mn superoxide dismutase, catalase, peroxiredoxins 3 and 5, thioredoxin 2, thioredoxin reductase 2, and uncoupling protein 2.
Prx V plays a key role in the microglial activation process through modulation of the balance between ROS/NO generation and the corresponding JNK cascade activation.
PRDX5 has a role in neuroprotection
Prx5 levels also appear to be highly dependent on c-Myc, and chromatin immunoprecipitation experiments showed differential occupancy of c-Myc and Prx1 complexes at E-box elements in the prx5 gene proximal promoter
These results suggest that the antioxidant and antiapoptotic activities of PRDX5 play important roles in the in vitro development of bovine SCNT embryos.
Bovine cauda sperm PRDX5 acts as an antioxidant enzyme in the epididymal environment.
This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in different tissues under normal conditions and during inflammatory processes. This protein interacts with peroxisome receptor 1. The crystal structure of this protein in its reduced form has been resolved to 1.5 angstrom resolution. This gene uses alternate in-frame translation initiation sites to generate mitochondrial or peroxisomal/cytoplasmic forms. Three transcript variants encoding distinct isoforms have been identified for this gene.
, peroxiredoxin 5
, Alu co-repressor 1
, TPx type VI
, antioxidant enzyme B166
, liver tissue 2D-page spot 71B
, peroxiredoxin V
, peroxisomal antioxidant enzyme
, thioredoxin peroxidase PMP20
, thioredoxin reductase
, liver tissue 2D-page spot 2D-0014IV
, peroxiredoxin 6
, peroxisomal membrane protein 20