Disease relevance of PRDX3

• The cloning and overexpression in Escherichia coli of recombinant wild type SP-22 and its three cysteine mutants (C47S, C66S, and C168S) are reported [1].
• By a homology search in the NBRF-PIR data base, SP-22 was found to be 91% homologous to murine erythroleukemia cell MER-5 protein, which may have an important role in the induction of differentiation [2].
• Aspirin-induced cytoprotection from hydrogen peroxide toxicity was mimicked by exogenous iron-free apoferritin but not iron-loaded ferritin, demonstrating the antioxidant function of newly synthesized ferritin under these conditions [3].
• A series of antioxidant agents did not prevent the elevation in heme oxygenase activity by hypoxia; however, the precursor of glutathione synthesis and thiol donor, N-acetylcysteine, completely abolished HO-1 induction [4].
• The induction of SP-22 protein by oxidative stress in vivo was demonstrated in an experimental model of myocardial infarction in rat heart [5].

Psychiatry related information on PRDX3

• The singlet oxygen-mediated damage to SOD and catalase may result in the perturbation of cellular antioxidant defense mechanisms and subsequently lead to a pro-oxidant condition [6].

High impact information on PRDX3

• Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST [7].
• Elevated levels of antioxidant enzymes and apoptosis were inhibited by the nitric oxide synthase inhibitor, S-isopropylisothiourea, and the peroxynitrite scavenger, selenomethionine [8].
• However treatment using the antioxidant N-acetylcysteine had no effect on either IkappaB levels or NFkappaB activation, indicating that the parasite subverts the normal IkappaB regulatory pathway downstream of the requirement for reactive oxygen intermediates [9].
• Thus, endothelium exposure to estrogens appears to induce a receptor-mediated antioxidant effect that enhances the biological activity of endothelium-derived NO [10].
• Aspirin increases ferritin synthesis in endothelial cells: a novel antioxidant pathway [3].

Chemical compound and disease context of PRDX3

• Differences in antioxidant enzyme activities observed between BREC and BRP, cultured with high concentrations of glucose or AGE, might help to explain their different behavior during the pathogenesis of diabetic retinopathy, i.e., early pericyte drop-out and late endothelial cell proliferation [11].
• The effects of the dietary antioxidant N-acetylcysteine (NAC) on alcoholic liver damage were examined in a total enteral nutrition (TEN) model of ethanol toxicity in which liver pathology occurs in the absence of endotoxemia [12].
• Our previous in vivo study demonstrated that methylprednisolone (MP) activates glomerular antioxidant enzymes and attenuates glomerular oxidant injuries, including those in experimental nephrosis [13].
• CONCLUSIONS: The combined data suggest that oxidative injury to RPE cells and photoreceptors may be caused by elevated levels of zinc in diseases such as age-related macular degeneration (AMD) and that metipranolol may act as an efficacious antioxidant to blunt this process [14].
• Thus, the alterations of retinal glutamate, oxidative stress and NO appear to be inter-related in diabetes, and antioxidant therapy may be a suitable approach to determine the roles of these abnormalities in the development of diabetic retinopathy [15].

Biological context of PRDX3

• We determined the amino acid sequence of SP-22, which is composed of 195 amino acids [2].
• We have isolated cDNA clones coding SP-22, an antioxidant protein in mitochondria, from a bovine adrenal medulla cDNA library constructed with (lambda)gt11 [16].
• Because of its rapid reduction and negligible oxidation, MitoQ10 is a more effective antioxidant against lipid peroxidation, peroxynitrite and superoxide [17].
• BAEC with an increased level of SP-22 protein caused by pretreatment with mild oxidative stress became tolerant to subsequent intense oxidative stress [5].
• This strain-induced PYK2 and Src phosphorylation was inhibited by pretreating ECs with an antioxidant N-acetylcysteine [18].

Anatomical context of PRDX3

• We have purified SP-22, a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex [2].
• The cDNA sequence encoding bovine SP-22, a new defence system against reactive oxygen species in mitochondria [16].
• Antioxidant enzyme activities were very different in cultured cells than in parent glomeruli [19].
• Effect of cell substrate on antioxidant enzyme activities in cultured renal glomerular epithelium [19].
• The antioxidant enzyme extracellular superoxide dismutase (EC-SOD) is mainly found in the extracellular matrix of tissues [20].

Associations of PRDX3 with chemical compounds

• Antioxidant effects of calcium channel blockers against free radical injury in endothelial cells. Correlation of protection with preservation of glutathione levels [21].
• Ascorbate is a potent antioxidant against peroxynitrite-induced oxidation reactions. Evidence that ascorbate acts by re-reducing substrate radicals produced by peroxynitrite [22].
• The augmented activity of UV-irradiated phosphatidylserine was not affected by the coexistence of an antioxidant, vitamin E or BHT [23].
• Intracellular scavengers of H(2)O(2), cell-permeable iron chelators, anti-TfR receptor antibody, or mitochondria-targeted antioxidant greatly abrogated C(2)-cer- and/or l-NAME-induced oxidative damage, iron signaling, and apoptosis [24].
• With an excess of (*)NO, the PN actions are blocked, which may explain the antioxidant properties of (*)NO and the mechanism of cellular S-nitrosations [25].

Regulatory relationships of PRDX3

• Natural bovine lactoferrin inhibited oxidation in buffered corn oil emulsions and lecithin liposome systems at pH 6.6 and 50 degrees C. The antioxidant activity increased with lactoferrin concentration in both phosphate- and Tris-buffered emulsions, but not in both buffered liposome systems [26].
• The correlation between the levels of some antioxidant enzymes and compounds with progesterone levels indicates that antioxidative mechanisms are activated to cope with steroidogenesis dependent oxyradical formation in the bovine corpus luteum [27].
• We studied whether antioxidant-surfactant liposomes increase cellular antioxidant activity in alveolar type II cells and whether this effect is influenced by the presence of surfactant protein A (SP-A) [28].

Other interactions of PRDX3

• PRDX2, PRDX3, and PRDX6 were not expressed around the 9- to 16-cell stage [29].
• Se-sufficient BAECs up-regulated HO-1 expression following stimulation with the pro-oxidant, 15-HPETE (15-hydroperoxyeicosatetraenoic acid), and levels of this antioxidant inversely correlated with EC apoptosis [30].
• In conclusion, the balance between intracellular growth factors (bFGF and TGF-beta1) and the activity of antioxidant enzyme CAT may participate in the regulation of the transition from myoblast proliferation to differentiation [31].
• An elevated level of homocysteine in vivo and in cell culture systems results in a decrease in the activity of cellular glutathione peroxidase (GPx1), an intracellular antioxidant enzyme that reduces hydrogen peroxide and lipid peroxides [32].
• The oxidant triggered protease activity and the Ca2+ATPase activity were found to be prevented by the antioxidant vitamin E, and also by the Ca2+ dependent matrix metalloprotease inhibitors: EGTA and TIMP-2 [33].

Analytical, diagnostic and therapeutic context of PRDX3

• The concentration of SP-22 in adrenocortical mitochondrial fractions was 16 +/- 3 micrograms/mg proteins (mean +/- SD, n = 6) as determined by radioimmunoassay using specific anti-SP-22 antibody [2].
• This new type of modified hemoglobin oxygen carrier with antioxidant activity may reduce the potential toxicity of hemoglobin-based substitutes in certain applications, especially during reperfusion of ischemic tissues [34].
• Here we investigate the inactivation of catalase and superoxide dismutase, both powerful antioxidant enzymes, by sugars of different glycating abilities, and the loss of antigenicity that was monitored by the loss of activity after immunoprecipitation with monospecific antibodies [35].
• The kinetics of several processes involving the potential antioxidant role of urate in physiological systems have been investigated by pulse radiolysis [36].
• Oocytes cultured in IVM medium supplemented with both cytochalasin B (a protein synthesis inhibitor) and 2-mercaptoethanol (an antioxidant) showed less damage to microtubules, but not to mitochondria after cryopreservation [37].

References