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p(MGI:Prdx2)

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Entity

Name
Prdx2
Namespace
mgi
Namespace Version
20181021
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/f2f993e599694ab5ce989cc39d789a499f75db99/external/mgi-names.belns

Appears in Networks 1

Heme Curation v0.0.1-dev

Mechanistic knowledge surrounding heme

In-Edges 22

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

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. PubMed:23215741

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Cell Ontology (CL)
erythrocyte
Text Location
Results

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

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]. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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). PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

Peroxiredoxin-2 (Prx-2) has emerged as the critical antioxidant protecting RBCs from H2O2 produced endogenously (by Hb autoxidation and subsequent superoxide dismutation) and exogenously (e.g., from activated neutrophils) at low (physiologic) concentrations (11, 32, 38, 40, 43, 45) and, therefore, may limit oxidative injury to other cells/tissues in the vasculature (6, 57). PubMed:25264713

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Introduction

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

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]. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

These results indicate that heme degradation increases in RBCs of PRDX2 knockout mice in spite of the presence of catalase and GPx. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

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

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]. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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. PubMed:23215741

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Cell Ontology (CL)
erythrocyte
Text Location
Results

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

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]. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

a(HM:"nitrite oxidation") positiveCorrelation p(MGI:Prdx2) View Subject | View Object

Figures 4B-D shows that d7 Prx-2 oxidation correlates positively with nitrite oxidation kinetics in the lag phase (i.e. inversely with lag time, positively with lag rates, Figures 4B-C respectively). PubMed:26202471

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Text Location
Results

a(HM:"nitrite oxidation") positiveCorrelation p(MGI:Prdx2) View Subject | View Object

Figure 5E shows that d7 nitrite oxidation propagation rates also positively correlate with the extent of Prx-2 oxidation that occurred during storage (i.e. d35 – d7 Prx-2 oxidation in RBC). PubMed:26202471

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Text Location
Results

a(HM:"stored erythrocytes") positiveCorrelation p(MGI:Prdx2) View Subject | View Object

Figure 2G shows storage also resulted in a significant increase in Prx-2 oxidation. PubMed:26202471

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Text Location
Results

a(HM:"stored erythrocytes") positiveCorrelation p(MGI:Prdx2) View Subject | View Object

The higher the basal (d7) level of Prx-2 oxidation, the higher the level of Prx-2 oxidation in the same RBC after 35 days of storage. PubMed:26202471

Appears in Networks:
Annotations
Text Location
Discussion

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

Figure 4 shows a significant decrease in the elongation index, which is a measure of deformability, for the PRDX2 knockout mice. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

PRDX2 deficiency, thus, causes cells to undergo more oxidative stress during in vitro aging, even in the presence of catalase. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

Peroxiredoxin-2 (Prx-2) has emerged as the critical antioxidant protecting RBCs from H2O2 produced endogenously (by Hb autoxidation and subsequent superoxide dismutation) and exogenously (e.g., from activated neutrophils) at low (physiologic) concentrations (11, 32, 38, 40, 43, 45) and, therefore, may limit oxidative injury to other cells/tissues in the vasculature (6, 57). PubMed:25264713

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Introduction

complex(p(MGI:Prdx1), p(MGI:Prdx2), p(MGI:Prdx3), p(MGI:Prdx4), p(MGI:Prdx5), p(MGI:Prdx6)) hasComponent p(MGI:Prdx2) View Subject | View Object

Appears in Networks:

path(MESH:Hemolysis) negativeCorrelation p(MGI:Prdx2) View Subject | View Object

Finally, slower Prx-2 reduction correlated with increased H2O2 (10 lM)-induced hemolysis of day 35 RBC compared with day 7 RBC (Fig. 1D). PubMed:25264713

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

Out-Edges 26

p(MGI:Prdx2) hasVariant p(MGI:Prdx2, pmod(ADPRib)) View Subject | View Object

Appears in Networks:

p(MGI:Prdx2) hasVariant p(MGI:Prdx2, pmod(Ox)) View Subject | View Object

Appears in Networks:

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

These results indicate that heme degradation increases in RBCs of PRDX2 knockout mice in spite of the presence of catalase and GPx. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

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

Figure 4 shows a significant decrease in the elongation index, which is a measure of deformability, for the PRDX2 knockout mice. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

PRDX2 deficiency, thus, causes cells to undergo more oxidative stress during in vitro aging, even in the presence of catalase. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

Peroxiredoxin-2 (Prx-2) has emerged as the critical antioxidant protecting RBCs from H2O2 produced endogenously (by Hb autoxidation and subsequent superoxide dismutation) and exogenously (e.g., from activated neutrophils) at low (physiologic) concentrations (11, 32, 38, 40, 43, 45) and, therefore, may limit oxidative injury to other cells/tissues in the vasculature (6, 57). PubMed:25264713

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Introduction

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

This is consistent with increased Prx-2 oxidation and a role for this enzyme in protecting RBC membrane constituents from storage-dependent oxidative stress (49, 50). PubMed:25264713

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

The potential significance of this finding is underscored by the fact that Prx-2 is considered the primary antioxidant system to negate H2O2-mediated oxidative damage in the RBC (41). PubMed:25264713

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

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

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]. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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). PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

Peroxiredoxin-2 (Prx-2) has emerged as the critical antioxidant protecting RBCs from H2O2 produced endogenously (by Hb autoxidation and subsequent superoxide dismutation) and exogenously (e.g., from activated neutrophils) at low (physiologic) concentrations (11, 32, 38, 40, 43, 45) and, therefore, may limit oxidative injury to other cells/tissues in the vasculature (6, 57). PubMed:25264713

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Introduction

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

The potential significance of this finding is underscored by the fact that Prx-2 is considered the primary antioxidant system to negate H2O2-mediated oxidative damage in the RBC (41). PubMed:25264713

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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]. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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]. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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]. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

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

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. PubMed:23215741

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Discussion

p(MGI:Prdx2) negativeCorrelation path(MESH:Hemolysis) View Subject | View Object

Finally, slower Prx-2 reduction correlated with increased H2O2 (10 lM)-induced hemolysis of day 35 RBC compared with day 7 RBC (Fig. 1D). PubMed:25264713

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Text Location
Results

p(MGI:Prdx2) positiveCorrelation a(HM:"stored erythrocytes") View Subject | View Object

Figure 2G shows storage also resulted in a significant increase in Prx-2 oxidation. PubMed:26202471

Appears in Networks:
Annotations
Text Location
Results

p(MGI:Prdx2) positiveCorrelation a(HM:"stored erythrocytes") View Subject | View Object

The higher the basal (d7) level of Prx-2 oxidation, the higher the level of Prx-2 oxidation in the same RBC after 35 days of storage. PubMed:26202471

Appears in Networks:
Annotations
Text Location
Discussion

p(MGI:Prdx2) positiveCorrelation a(HM:"nitrite oxidation") View Subject | View Object

Figures 4B-D shows that d7 Prx-2 oxidation correlates positively with nitrite oxidation kinetics in the lag phase (i.e. inversely with lag time, positively with lag rates, Figures 4B-C respectively). PubMed:26202471

Appears in Networks:
Annotations
Text Location
Results

p(MGI:Prdx2) positiveCorrelation a(HM:"nitrite oxidation") View Subject | View Object

Figure 5E shows that d7 nitrite oxidation propagation rates also positively correlate with the extent of Prx-2 oxidation that occurred during storage (i.e. d35 – d7 Prx-2 oxidation in RBC). PubMed:26202471

Appears in Networks:
Annotations
Text Location
Results

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.