Involvement of vascular peroxidase 1 in angiotensin II-induced vascular smooth muscle cell proliferation

Shi, Ruizheng; Hu, Chong; Yuan, Qiong; Yang, Tianlun; Peng, Jun; Li, Yuan‐Jian; Bai, Yongping; Cao, Zehong; Cheng, Guangjie; Zhang, Guogang

doi:10.1093/cvr/cvr042

Cited by 70 publications

(41 citation statements)

References 30 publications

(35 reference statements)

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“…In addition, MPO is only expressed in neutrophils and monocytes under inflammatory response and VPO1 is highly expressed in cells of the cardiovascular system,10 therefore, it may be more significant to explore the role of VPO1 in AAA development. Our previous studies demonstrated that VPO1/HOCl pathway‐mediated oxidative stress contributed to hypoxia‐induced pulmonary vascular remodeling, angiotensin II‐induced VSMC proliferation and myocardial ischemia‐reperfusion injury 8, 11, 19. In this study, we find that VPO1 and 3‐Cl‐tyr (a product of HOCl reacting with tyrosine residues) are significantly increased in human aneurysm tissues compared with healthy aortic tissues.…”

Section: Discussionsupporting

confidence: 50%

“…Activation of the ERK and p38MAPK pathways triggered by growth factors such as platelet‐derived growth factor, epidermal growth factor, and basic fibroblast growth factor have been shown to be associated with VSMC phenotypic switch and subsequent AAA formation 34. As reactive oxygen species are a representative MAPK‐activating factor, especially the ERK pathway, they are necessary for cell proliferation and migration 7, 8. We hypothesize that VSMC phenotypic switch regulated by VPO1 may be due to HOCl‐induced ERK1/2 activation.…”

Section: Discussionmentioning

confidence: 99%

“…Vascular peroxidase 1 (VPO1), a member of the heme‐containing peroxidase family, is highly expressed in the cardiovascular tissues, especially VSMCs 7, 8. In the presence of chloride, VPO1 catalyzes the formation of hypochlorous acid (HOCl) from H 2 O 2 and enhances oxidative stress 9, 10.…”

Section: Introductionmentioning

confidence: 99%

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VPO1 Modulates Vascular Smooth Muscle Cell Phenotypic Switch by Activating Extracellular Signal‐regulated Kinase 1/2 (ERK 1/2) in Abdominal Aortic Aneurysms

Peng

Zhang

Liu

et al. 2018

JAHA

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BackgroundHydrogen peroxide (H2O2) is a critical molecular signal in the development of abdominal aortic aneurysm (AAA) formation. Vascular peroxidase 1 (VPO1) catalyzes the production of hypochlorous acid (HOCl) from H2O2 and significantly enhances oxidative stress. The switch from a contractile phenotype to a synthetic one in vascular smooth muscle cells (VSMCs) is driven by reactive oxygen species and is recognized as an early and important event in AAA formation. This study aims to determine if VPO1 plays a critical role in the development of AAA by regulating VSMC phenotypic switch.Methods and Results VPO1 is upregulated in human and elastase‐induced mouse aneurysmal tissues compared with healthy control tissues. Additionally, KLF4, a nuclear transcriptional factor, is upregulated in aneurysmatic tissues along with a concomitant downregulation of differentiated smooth muscle cell markers and an increase of synthetic phenotypic markers, indicating VSMC phenotypic switch in these diseased tissues. In cultured VSMCs from rat abdominal aorta, H2O2 treatment significantly increases VPO1 expression and HOCl levels as well as VSMC phenotypic switch. In support of these findings, depletion of VPO1 significantly attenuates the effects of H2O2 and HOCl treatment. Furthermore, HOCl treatment promotes VSMC phenotypic switch and ERK1/2 phosphorylation. Pretreatment with U0126 (a specific inhibitor of ERK1/2) significantly attenuates HOCl‐induced VSMC phenotypic switch.ConclusionsOur results demonstrate that VPO1 modulates VSMC phenotypic switch through the H2O2/VPO1/HOCl/ERK1/2 signaling pathway and plays a key role in the development of AAA. Our findings also implicate VPO1 as a novel signaling node that mediates VSMC phenotypic switch and plays a key role in the development of AAA.Clinical Trial Registration URL: http://www.chictr.org.cn. Unique identifier: ChiCTR1800016922.

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Section: Discussionsupporting

confidence: 50%

Section: Discussionmentioning

confidence: 99%

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VPO1 Modulates Vascular Smooth Muscle Cell Phenotypic Switch by Activating Extracellular Signal‐regulated Kinase 1/2 (ERK 1/2) in Abdominal Aortic Aneurysms

Peng

Zhang

Liu

et al. 2018

JAHA

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“…Similar to MPO, VPO is able to catalyze H 2 O 2 (a weak oxidant) and chloride anion to form HOCl (a strong oxidant). In vitro, VPO1 is found to utilize H 2 O 2 generated from co-expressed NOX enzymes to catalyze peroxidative reactions [7,30]. We hypothesize that VPO1 is activated to catalyze the generation of HOCl with the increase of NOX-derived H 2 O 2 production during IR, which in turn promotes the oxidative injury.…”

Section: Discussionmentioning

confidence: 95%

A novel pathway of NADPH oxidase/vascular peroxidase 1 in mediating oxidative injury following ischemia–reperfusion

Zhang

Liu

et al. 2012

Basic Res Cardiol

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Vascular peroxidase 1 (VPO1) can utilize reactive oxygen species (ROS) generated from NADPH oxidase (NOX) to catalyze peroxidative reactions. This study was performed to identify a novel pathway of NOX/VPO1 in mediating the oxidative injury following myocardial ischemia reperfusion (IR). In a rat model of myocardial IR, the infarct size, serum creatine kinase (CK) activity, apoptosis, NOX activity, NOX2 and VPO1 expression were measured. In a cell (rat heart-derived H9c2 cells) model of hypoxia/reoxygenation (HR), the apoptosis, NOX activity, NOX2 and VPO1 expression, and H(2)O(2) and HOCl levels were examined. In vivo, IR caused 54.8 ± 1.7 % infarct size in myocardium accompanied by elevated activities of CK, caspase-3 and NOX, up-regulated VPO1 expression and high numbers of myocardial apoptotic cells; these effects were attenuated by pretreatment with the inhibitor of NOX. In vitro, inhibition of NOX or silencing of NOX2 or VPO1 expression significantly suppressed HR-induced cellular apoptosis concomitantly with decreased HOCl production. Inhibition of NOX or silencing of NOX2 led to a decrease in H(2)O(2) production accompanied by a decrease in VPO1 expression and HOCl production. However, silencing of VPO1 expression did not affect NOX2 expression and H(2)O(2) production. H(2)O(2)-induced VPO1 expression was partially reversed by JNK or p38 MAPK inhibitor. Our results demonstrate a novel pathway of NOX2/VPO1 in myocardium, where VPO1 coordinates with NOX2 and amplifies the role of NOX-derived ROS in oxidative injury following IR.

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“…VPO-1 is a novel family member of peroxidases identified in cardiovascular system in 2008 [39]. VPO-1 is highly expressed in cardiomyocytes, endothelial cells and vascular smooth muscle cells [40,41,42], and thereby referred to vascular peroxidase (VPO). It is a glycosylated heme-peroxidase that is actively secreted into circulating plasma by vascular endothelial cells [39].…”

Section: Discussionmentioning

confidence: 99%

Activation of a7 Nicotinic Acetylcholine Receptor Protects Against Oxidant Stress Damage Through Reducing Vascular Peroxidase-1 in a JNK Signaling-Dependent Manner in Endothelial Cells

Zhao

Xin

et al. 2014

Cell Physiol Biochem

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Aim: Alpha7 nicotinic acetylcholine receptor (α7nAChR), a subtype of nAChR regulating neurotransmission in central nervous system, is an essential regulator of cholinergic anti-inflammatory pathway in periphery. The present study was to determine the effects of activation of α7nAChR on oxidant stress-induced injury in endothelial cells. Methods: Cultured human umbilical vein endothelial cells were treated with H₂O₂ (400 µM) or H₂O₂ plus PNU-282987 (10 µM). Cell viability and membrane integrity were measured. Annexin V + PI assay, immunoblotting of bcl-2, bax and cleaved capase-3, and immunofluorescence of apoptosis inducing factor (AIF) were performed to evaluate apoptosis. Protein expression of vascular peroxidase-1 (VPO-1) and phosphor-JNK were measured by immunoblotting. Results: Activation of α7nAChR by a selective agonist PNU-282987 prevented H₂O₂-indced decrease of cell viability and increase of lactate dehydrogenase release. Activation of α7nAChR markedly reduced cell apoptosis and intracellular oxidative stress level. Moreover, activation of α7nAChR reduced H₂O₂-induced VPO-1 protein upregulation and JNK1/2 phosphorylation. The inhibitory effect of α7nAChR activation on VPO-1 was blocked by JNK inhibitor SP600125. In addition, pretreatment of α7nAChR antagonist methyllycaconitine blocked the cytoprotective effect of PNU-282987. Conclusion: These results provide the first evidence that activation of α7nAChR protects against oxidant stress-induced damage by suppressing VPO-1 in a JNK signaling pathway-dependent manner in endothelial cells.

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Involvement of vascular peroxidase 1 in angiotensin II-induced vascular smooth muscle cell proliferation

Abstract: VPO1 is a novel regulator of vascular smooth muscle cell proliferation via NADPH oxidase-H(2)O(2)-VPO1-hypochlorous acid-ERK1/2 pathways, which may contribute to vascular remodelling in hypertension.

Cited by 70 publications

References 30 publications

VPO1 Modulates Vascular Smooth Muscle Cell Phenotypic Switch by Activating Extracellular Signal‐regulated Kinase 1/2 (ERK 1/2) in Abdominal Aortic Aneurysms

VPO1 Modulates Vascular Smooth Muscle Cell Phenotypic Switch by Activating Extracellular Signal‐regulated Kinase 1/2 (ERK 1/2) in Abdominal Aortic Aneurysms

A novel pathway of NADPH oxidase/vascular peroxidase 1 in mediating oxidative injury following ischemia–reperfusion

Activation of a7 Nicotinic Acetylcholine Receptor Protects Against Oxidant Stress Damage Through Reducing Vascular Peroxidase-1 in a JNK Signaling-Dependent Manner in Endothelial Cells

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