Disease relevance of Prdx5

• Azelaic acid as a competitive inhibitor of thioredoxin reductase in human melanoma cells [1].
• Randomly selected hearts from Prdx6(-/-) mice and wild-type mice were subjected to 30 min of global ischemia followed by 120 min of reperfusion at normothermia [2].
• The hearts from the Prdx6(-/-) mice were more susceptible to ischemic reperfusion injury as evidenced by reduced recovery of left ventricular function, increased myocardial infarct size, and higher amount of apoptotic cardiomyocytes compared with wild-type mouse hearts [2].
• Since significant amounts of catalase and GSHPx are present in the heart contributing toward the attenuation of H(2)O(2) and hydroperoxides formed during ischemia-reperfusion injury and thereby providing cardioprotection, we asked whether Prdx6 also has any role in this process [2].
• A novel strain, Origami(DE3), of Escherichia coli with mutations in the glutathione and thioredoxin reductase genes yielded 60% more soluble PvMSP-1 p42 than the conventional E. coli BL21(DE3) strain [3].

High impact information on Prdx5

• Defective metabolism of pyridoxal 5'-phosphate (PLP), characterized by elevated serum PLP levels, results in reduced levels of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) in the brain [4].
• We used an IL-17 ELISPOT assay to track the neuroantigen-specific IL-17-producing T cells at single-cell resolution in various organs of SJL mice undergoing PLP 139-151-induced EAE [5].
• Pmp20 homologs containing the putative peroxisome targeting signal type 1 have also been identified in mammals and lower eukaryotes [6].
• A structural comparison revealed that a core fragment of ACS in fold type I is superimposable over tryptophan synthase beta subunit in fold type II and mouse ornithine decarboxylase in fold type III, thus suggesting a divergent evolution of PLP-dependent enzymes [7].
• Mice were injected with peroxisomal membrane, and hybridoma lines were isolated that produced antibody against PMP 20, PMP 47, and dihydroxyacetone synthase [8].

Chemical compound and disease context of Prdx5

• RESULTS: Bacterial lung inflammation did not change expression of PRXV in murine epithelia but produced massive influx of leukocytes highly expressing PRXV [9].

Biological context of Prdx5

• We have cloned two cDNA isoforms as well as genomic sequences of the mouse Prx V gene and characterized their molecular genetic features [10].
• Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis [11].
• These Prdx6(-/-) hearts were also subjected to a higher amount of oxidative stress as evidenced by the presence of higher amount of malondialdehyde [2].
• These regions were not, however, sufficient to mediate up-regulation by the known Prdx6 inducers in our system [12].
• Together, these data support multiple pathways of Prdx6 regulation and reveal important promoter regions that mediate its transcriptional regulation [12].

Anatomical context of Prdx5

• Two isoforms of the mouse Prx V cDNA were identified from liver and testis [10].
• Azelaic acid has been shown to inhibit thioredoxin reductase (TR) at the surface of guinea pig and human skin, on cultures of human keratinocytes, melanocytes, melanoma cells, murine melanoma cells (Cloudman S91), and on purified enzymes from Escherichia coli, rat liver, and human melanoma [1].
• Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells [13].
• Contribution of Thioredoxin Reductase to T-Cell Mitogenesis and NF-kB DNA-Binding Promoted by Selenite [14].
• Investigating transcriptional regulation of Prdx6 in mouse liver cells [12].

Associations of Prdx5 with chemical compounds

• In this study, we investigated the biochemical and physiological functions of recombinant CbPmp20 protein in methanol-induced peroxisomes of C. boidinii using the PMP20-deleted strain of C. boidinii (pmp20Delta strain) [6].
• Fluorescence spectroscopy has been used to show that azelaic acid does not interfere with electron transfer from NADPH to FAD on TR [1].
• A comparative study of TR inhibition by C6, C9, C10 and C12 saturated dicarboxylic acids was also determined on guinea pig skin in vivo [1].
• Both human and mouse Grx2 showed glutathione (GSH)-dependent and thioredoxin reductase (TR)-dependent peroxidase activity [13].
• Cyclophosphamide as a potent inhibitor of tumor thioredoxin reductase in vivo [15].

Other interactions of Prdx5

• We found that Prdx6 expression is down-regulated upon serum deprivation and subsequently induced in a time-dependent manner in response to KGF, TNF-alpha, dexamethasone, and H(2)O(2) [12].
• We further investigated the role of BM-derived cells in restoration of expression of peroxiredoxin V (PRXV), one of the major proteins of antioxidant defense, specifically expressed in the bronchial epithelium [16].

Analytical, diagnostic and therapeutic context of Prdx5

• Molecular cloning and characterization of the mouse peroxiredoxin V gene [10].
• These SCID mouse-SJL mouse hematopoietic cell chimeras developed passive EAE following adoptive transfer of PLP S139-151-specific SJL T lymphocyte line cells, but were resistant to active EAE induced by primary immunization with PLP S139-151 [17].
• In primary airway cell culture (cow), alveolar epithelial cells A549, or co-culture of A549 with murine macrophages RAW264.7, exposure to live bacteria increased expression of PRXV, which required serum [9].
• METHODS: Studies in anesthetized rats and mice; PRXV expression determined by Western blot analyses and immunohistochemistry; PRXV m-RNA expression determined by Taq-Man RT-PCR [9].

References