Retinol binding protein 4 induces mitochondrial dysfunction and vascular oxidative damage

Wang, Jingjing; Chen, Hongen; Liu, Yan; Sun, Ruifang; Xia, Min

doi:10.1016/j.atherosclerosis.2015.03.036

Cited by 42 publications

(35 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Serum RBP4 increasing has been connected to cardiovascular system disease. Researchers (Wang et al, 2015 ) found a mechanism by which RBP4 causes the oxidative stress of blood vessels and promotes the pathogenesis of atherosclerosis. In another study, RBP4 therapy enhanced superoxide production in the dose-dependent way in the human aortic endothelial cells (HAECs) (Blaner, 1989 ; Newcomer and Ong, 2000 ; Wang et al, 2015 ).…”

Section: Mitochondria Induce Oxidative Stress In Atherosclerosismentioning

confidence: 99%

“…Researchers (Wang et al, 2015 ) found a mechanism by which RBP4 causes the oxidative stress of blood vessels and promotes the pathogenesis of atherosclerosis. In another study, RBP4 therapy enhanced superoxide production in the dose-dependent way in the human aortic endothelial cells (HAECs) (Blaner, 1989 ; Newcomer and Ong, 2000 ; Wang et al, 2015 ). Exposed to RBP4 also expedited mitochondrial function disorder, as-ascertained by lessened mitochondrial contents and completeness as well as membrane potential (Wang et al, 2014a ).…”

Section: Mitochondria Induce Oxidative Stress In Atherosclerosismentioning

confidence: 99%

“…Exposed to RBP4 also expedited mitochondrial function disorder, as-ascertained by lessened mitochondrial contents and completeness as well as membrane potential (Wang et al, 2014a ). The RBP4 stimulation restrained protein kinase B signaling in the HAECs (Wang et al, 2015 ). The RBP4-Tg mice also showed serious vascular oxidative injure as well as mitochondrial function disorder in aorta, compared with widespread-type C57BL/6J mice (Blaner, 1989 ; Newcomer and Ong, 2000 ; Wang et al, 2015 ).…”

Section: Mitochondria Induce Oxidative Stress In Atherosclerosismentioning

confidence: 99%

See 2 more Smart Citations

Oxidative Stress-Mediated Atherosclerosis: Mechanisms and Therapies

et al. 2017

View full text Add to dashboard Cite

Atherogenesis, the formation of atherosclerotic plaques, is a complex process that involves several mechanisms, including endothelial dysfunction, neovascularization, vascular proliferation, apoptosis, matrix degradation, inflammation, and thrombosis. The pathogenesis and progression of atherosclerosis are explained differently by different scholars. One of the most common theories is the destruction of well-balanced homeostatic mechanisms, which incurs the oxidative stress. And oxidative stress is widely regarded as the redox status realized when an imbalance exists between antioxidant capability and activity species including reactive oxygen (ROS), nitrogen (RNS) and halogen species, non-radical as well as free radical species. This occurrence results in cell injury due to direct oxidation of cellular protein, lipid, and DNA or via cell death signaling pathways responsible for accelerating atherogenesis. This paper discusses inflammation, mitochondria, autophagy, apoptosis, and epigenetics as they induce oxidative stress in atherosclerosis, as well as various treatments for antioxidative stress that may prevent atherosclerosis.

show abstract

Section: Mitochondria Induce Oxidative Stress In Atherosclerosismentioning

confidence: 99%

Section: Mitochondria Induce Oxidative Stress In Atherosclerosismentioning

confidence: 99%

Section: Mitochondria Induce Oxidative Stress In Atherosclerosismentioning

confidence: 99%

See 1 more Smart Citation

Oxidative Stress-Mediated Atherosclerosis: Mechanisms and Therapies

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Additionally, phosphorylation of Akt at Ser473 via a PI3K-dependent pathway served a crucial role in regulating mitochondrial oxidative stress-mediated tissue injury (16,17). As described by Wang et al (18), impaired PI3K/Akt signaling may be associated with retinol binding protein 4 (RBP4)-induced imbalance of the fusion and fission cycles in mitochondria.…”

Section: Introductionmentioning

confidence: 96%

Phosphatidylinositol 3‑kinase‑mediated HO‑1/CO represses Fis1 levels and alleviates lipopolysaccharide‑induced oxidative injury in alveolar macrophages

Shi

Zhang

et al. 2018

Exp Ther Med

View full text Add to dashboard Cite

Abstract. Sepsis-related acute respiratory distress syndrome is characterized by marked oxidative stress and mitochondrial dysfunction lacking of specific therapy. Heme oxygenase (HO)-1 followed by endogenous carbon monoxide (CO) exerted a cytoprotective effect against multi-organ damage during sepsis. Additionally, the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (Akt) pathway, which serves as an upstream regulator of HO-1, was associated with inflammation and oxidative stress. Therefore, the purpose of the present study was to investigate whether the PI3K/Akt pathway was involved in the effects of HO-1/CO on the expression of mitochondrial fission 1 protein (Fis1). In the present study, CO releasing molecule-2 (CORM2), as the exogenous source of CO, plus LY294002, as a specific PI3K inhibitor, were pre-incubated in lipopolysaccharide (LPS)-simulated rat NR8383 alveolar macrophages. The results demonstrated that CORM2 improved cell viability, inhibited tumor necrosis factor-α levels, malondialdehyde contents, while elevating interleukin-10 levels and superoxide dismutase activities. In addition, pretreatment with CORM2 suppressed the fragmentation of mitochondria, upregulated the expressions of phosphorylated-Akt and HO-1 but downregulated the levels of Fis1 mRNA and protein in LPS-exposed cells. However, pretreatment with LY294002 significantly inhibited the phosphorylation of Akt, decreased HO-1 levels, aggravated mitochondrial fragmentation, increased Fis1 mRNA and protein levels, and reversed the above protective effects of CORM2. Collectively, the results of the present study indicated that the PI3K/Akt pathway mediated the cytoprotective effects of HO-1/CO on the transcription and translational levels of Fis1, and alleviated LPS-induced oxidative injury in alveolar macrophages.

show abstract

“…Our interest was prompted by in vitro studies demonstrating the stabilizing effect of RBP4 on native TTR [21,23] and the limited information about RBP4 in ATTR cardiac diseases, despite extensive studies of the protein in other pathologies [6,[24][25][26] particularly cardiomyopathy [8,27,28]. This report documents our 1) RBP4 histological and serological findings in ATTRm and ATTRwt; 2) assessment of baseline serological, clinical, and echocardiographic data of patients in each group; and 3) analysis of RBP4 as an indicator of ATTR amyloid disease type.…”

Section: Introductionmentioning

confidence: 99%

Retinol-binding protein 4 in transthyretin-associated forms of cardiac amyloidosis: differences in the pathobiologies of mutant (ATTRm) and wild-type (ATTRwt) diseases

Koch¹,

Chiswick²,

Cui³

et al. 2017

Clin Diagn Pathol

View full text Add to dashboard Cite

The role of retinol-binding protein 4 (RBP4), a natural binding partner of plasma circulating transthyretin (TTR), in TTR-associated cardiomyopathies is unknown. RBP4 is a small (21 kDa) protein that normally functions as a transporter for all-trans retinol (Vitamin A) and travels in the bloodstream as a ternary complex bound to TTR. Previous in vitro studies have demonstrated that RBP4 stabilizes native (tetrameric) TTR and prevents its disassembly into monomers, the key step in TTR amyloid fibril formation. Though increased serum concentrations of RBP4 have been reported in non-amyloidotic cardiomyopathies, there is little information about circulating levels in the inherited (ATTRm) and acquired (ATTRwt) forms of TTR-associated cardiac amyloid disease. Our study objectives were to investigate TTR amyloid-infiltrated cardiac tissue for the presence of RBP4 and to compare serum levels of the protein in ATTRm, ATTRwt and controls. We hypothesized that there would be histological and serological differences in RBP4 between ATTR patient and control samples. In the present study, we demonstrate that RBP4 is highly abundant in ATTRm cardiac tissue surrounding amyloid-infiltrated regions and, to a lesser extent, in ATTRwt specimens. Serum levels of RBP4 are significantly lower in ATTRm compared to ATTRwt (p < 0.0001) and healthy controls (p < 0.0011), with significant correlation between circulating RBP4 concentration and cardiac troponin-I (c-TnI) in our ATTRwt cohort. These data suggest, for the first time, that the pathobiologies of ATTRm and ATTRwt are dissimilar, and provide support for RBP4 as a serum biomarker of amyloid cardiomyopathy in ATTRm.

show abstract

Retinol binding protein 4 induces mitochondrial dysfunction and vascular oxidative damage

Cited by 42 publications

References 48 publications

Oxidative Stress-Mediated Atherosclerosis: Mechanisms and Therapies

Oxidative Stress-Mediated Atherosclerosis: Mechanisms and Therapies

Phosphatidylinositol 3‑kinase‑mediated HO‑1/CO represses Fis1 levels and alleviates lipopolysaccharide‑induced oxidative injury in alveolar macrophages

Retinol-binding protein 4 in transthyretin-associated forms of cardiac amyloidosis: differences in the pathobiologies of mutant (ATTRm) and wild-type (ATTRwt) diseases

Contact Info

Product

Resources

About