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PubMed: 23215741

Title
Role of peroxiredoxin-2 in protecting RBCs from hydrogen peroxide-induced oxidative stress.
Journal
Free radical research
Volume
47
Issue
None
Pages
164-71
Date
2013-03-01
Authors
Friedman JS | Mohanty JG | Nagababu E | Rifkind JM

Evidence bc065a5246
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However, metHb levels may increase when there is an increase in Hb autoxidation and the concomitant generation of H2O2 that is not scavenged by antioxidant defense enzymes making it more difficult for metHb-reductase to keep up with the metHb produced.

a(CHEBI:"hydrogen peroxide") positiveCorrelation a(CHEBI:methemoglobin) View Subject | View Object

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a(CHEBI:methemoglobin) positiveCorrelation a(CHEBI:"hydrogen peroxide") View Subject | View Object

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Evidence fa1aa073f6
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As shown in Figure 3, the level of heme degradation is highly correlated with the level of metHb in RBCs (R = 0.6233, p < 0.0177) supporting the hypothesis that the heme degradation product formed in PRDX2 knockout mice is associated with the un-scavenged H2O2 generated during Hb autoxidation.

a(CHEBI:"hydrogen peroxide") positiveCorrelation deg(a(CHEBI:heme)) View Subject | View Object

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deg(a(CHEBI:heme)) positiveCorrelation a(CHEBI:"hydrogen peroxide") View Subject | View Object

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Evidence a492161916
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The appreciable increase in heme degradation for RBCs from PRDX2 knockout mice in the presence of azide indicates that PRDX2 plays a major role in scavenging H2O2 in the absence of catalase, even with GPx present.

a(CHEBI:"hydrogen peroxide") negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation a(CHEBI:"hydrogen peroxide") View Subject | View Object

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Evidence 05d0a0ef6f
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GPx removes both H2O2 and organic hydroperoxides [8,31] whereas PRDX2 removes H2O2 [2], organic hydroperoxides, lipid hydroperoxides, [32,33] peroxynitrite [34] and protein hydroperoxides [35].

a(CHEBI:"hydrogen peroxide") negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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a(CHEBI:"hydrogen peroxide") negativeCorrelation p(PFAM:GSHPx) View Subject | View Object

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a(CHEBI:"lipid hydroperoxide") negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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a(CHEBI:hydroperoxide) negativeCorrelation p(PFAM:GSHPx) View Subject | View Object

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a(CHEBI:hydroperoxide) negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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a(CHEBI:peroxynitrite) negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation a(CHEBI:"hydrogen peroxide") View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation a(CHEBI:hydroperoxide) View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation a(CHEBI:"lipid hydroperoxide") View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation a(CHEBI:peroxynitrite) View Subject | View Object

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p(PFAM:GSHPx) negativeCorrelation a(CHEBI:"hydrogen peroxide") View Subject | View Object

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p(PFAM:GSHPx) negativeCorrelation a(CHEBI:hydroperoxide) View Subject | View Object

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Evidence 411813eca0
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The in vivo effects that we have observed for PRDX2 knockout mice (Figures 1–4) imply that PRDX2 plays an important role in neutralizing the H2O2 generated in vivo (Figure 6).

a(CHEBI:"hydrogen peroxide") negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation a(CHEBI:"hydrogen peroxide") View Subject | View Object

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Evidence 8ec14ef54c
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The finding that GPx has a greater role in the inhibition of heme degradation products than catalase [3] is consistent with the primary role of catalase to react with the high concentrations of H2O2 coming from exogenous sources and for GPx to react with the low levels of H2O2 coming from the endogenous autoxidation of Hb [39].

a(CHEBI:"hydrogen peroxide") negativeCorrelation p(PFAM:GSHPx) View Subject | View Object

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p(PFAM:GSHPx) negativeCorrelation a(CHEBI:"hydrogen peroxide") View Subject | View Object

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Evidence abd61edc29
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These results indicate that heme degradation increases in RBCs of PRDX2 knockout mice in spite of the presence of catalase and GPx.

deg(a(CHEBI:heme)) negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation deg(a(CHEBI:heme)) View Subject | View Object

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Evidence 3bd9278ba0
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The small increase in heme degradation in the absence of SOD1 may, however, be attributed to low levels of heme degradation products produced either by the increased levels of superoxide [17] or perhaps the peroxynitrite that forms due to the rapid reaction of superoxide with any NO present.

deg(a(CHEBI:heme)) positiveCorrelation a(CHEBI:peroxynitrite) View Subject | View Object

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a(CHEBI:peroxynitrite) positiveCorrelation deg(a(CHEBI:heme)) View Subject | View Object

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Evidence 6e06e48d84
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The role of PRDX2 in inhibiting impaired deformability can be attributed to both a reduction in ROS as well as a direct reaction of PRDX2 with protein hydroperoxides [52], which will inhibit the damage to cytoskeletal proteins required for impaired deformability.

a(CHEBI:hydroperoxide) negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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a(CHEBI:hydroperoxide) negativeCorrelation bp(MESH:"Erythrocyte Deformability") View Subject | View Object

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a(MESH:"Reactive Oxygen Species") negativeCorrelation bp(MESH:"Erythrocyte Deformability") View Subject | View Object

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a(MESH:"Reactive Oxygen Species") negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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bp(MESH:"Erythrocyte Deformability") positiveCorrelation p(MGI:Prdx2) View Subject | View Object

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bp(MESH:"Erythrocyte Deformability") negativeCorrelation a(MESH:"Reactive Oxygen Species") View Subject | View Object

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bp(MESH:"Erythrocyte Deformability") negativeCorrelation a(CHEBI:hydroperoxide) View Subject | View Object

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p(MGI:Prdx2) positiveCorrelation bp(MESH:"Erythrocyte Deformability") View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation a(CHEBI:hydroperoxide) View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation a(MESH:"Reactive Oxygen Species") View Subject | View Object

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Evidence 0aeeef7c50
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As shown in Figure 2, the mean metHb levels were also significantly increased in PRDX2 knockout mice, but not in SOD1 knockout mice compared with control mice.

a(CHEBI:methemoglobin) negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation a(CHEBI:methemoglobin) View Subject | View Object

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Evidence e5111f966e
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It has been shown that RBC oxidative stress that damages the membrane reduces the deformability and flexibility of cells.

bp(MESH:"Erythrocyte Deformability") negativeCorrelation bp(MESH:"Oxidative Stress") View Subject | View Object

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bp(MESH:"Oxidative Stress") negativeCorrelation bp(MESH:"Erythrocyte Deformability") View Subject | View Object

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Evidence 86fac7834f
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Figure 4 shows a significant decrease in the elongation index, which is a measure of deformability, for the PRDX2 knockout mice.

bp(MESH:"Erythrocyte Deformability") positiveCorrelation p(MGI:Prdx2) View Subject | View Object

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p(MGI:Prdx2) positiveCorrelation bp(MESH:"Erythrocyte Deformability") View Subject | View Object

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Evidence d92ec52c69
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While it is clear that PRDX2 plays an important role in protecting RBCs from oxidative stress, the relative importance of PRDX2 in scavenging H2O2 in RBC has not been fully elucidated.

bp(MESH:"Oxidative Stress") negativeCorrelation p(HGNC:PRDX2) View Subject | View Object

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p(HGNC:PRDX2) negativeCorrelation bp(MESH:"Oxidative Stress") View Subject | View Object

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Evidence 4045725a95
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PRDX2 deficiency, thus, causes cells to undergo more oxidative stress during in vitro aging, even in the presence of catalase.

bp(MESH:"Oxidative Stress") negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation bp(MESH:"Oxidative Stress") View Subject | View Object

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Evidence 227b8aca42
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PRDX2, which is able to react with low levels of H2O2 even at reduced glutathione levels, may therefore play a role in limiting the increased formation of heme degradation products in older cells.

bp(MESH:"Oxidative Stress") negativeCorrelation p(MGI:Prdx2) View Subject | View Object

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p(MGI:Prdx2) negativeCorrelation bp(MESH:"Oxidative Stress") View Subject | View Object

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Evidence f1a4cfdd1a
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These results are consistent with our earlier observations that the presence of SOD1 does not significantly inhibit or accelerate the formation of heme degradation products during in vitro autoxidation of oxyHb [18]..

p(MGI:Sod1) causesNoChange deg(a(CHEBI:heme)) View Subject | View Object

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Evidence 5e2818f1b5
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No significant change in the elongation index was found for the SOD1 knockout mice.

p(MGI:Sod1) causesNoChange bp(MESH:"Erythrocyte Deformability") View Subject | View Object

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