Visfatin promotes angiogenesis by activation of extracellular signal-regulated kinase 1/2

Kim, Su-Ryun; Bae, Soo-Kyung; Choi, Kyoo Wan; Park, Shi-Young; Jun, Hyung Oh; Lee, Ju-Youn; Jang, Hye-Ock; Yun, Il Dong; Yoon, Kwon‐Ha; Kim, Yung-Jin; Yoo, Mi‐Ae; Kim, Kyu‐Won; Bae, Moon‐Kyoung

doi:10.1016/j.bbrc.2007.03.105

Cited by 135 publications

(111 citation statements)

References 28 publications

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“…Previous studies showed that visfatin promotes the proliferation of vascular smooth muscle cells and endothelium (9,10) and facilitates the synthesis of type I collagen (28,30). There are relatively few studies on visfatin expression in cardiac tissues and the pathological and physiological involvement of visfatin in myocardial fibrosis in DCM remains a disputed issue.…”

Section: Discussionmentioning

confidence: 99%

“…The plasma levels of visfatin are associated with a wide range of diseases, including cardiovascular diseases, endothelial dysfunction, insulin resistance, and the occurrence and progression of diabetes. visfatin also plays a role in vulnerable plaque formation and vascular proliferation and inflammation, by exerting an insulin-like effect (8), facilitating adipocyte differentiation, inhibiting cell apoptosis, and promoting cell maturation and proliferation as a pro-inflammatory factor (9,10). It has been suggested that visfatin is overexpressed in obese patients and in patients with diabetes, causing myocardial fibrosis, causing an increase in extracellular matrix synthesis, or even leading to heart failure (11)(12)(13).…”

Section: Introductionmentioning

confidence: 99%

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High glucose induces Rho/ROCK-dependent visfatin and typeï¿½I procollagen expressionï¿½inï¿½rat primaryï¿½cardiac fibroblasts

et al. 2014

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Abstract. Myocardial fibrosis and excessive proliferation of cardiac fibroblasts (CFs) contribute to diabetic cardiomyopathy (DCM). However, the underlying mechanism is still not completely clear. The aim of this study was to investigate the relationship between high-glucose treatment and the expression of visfatin and type I procollagen in rat CFs, and examine the regulatory effects of high-glucose treatment on the Rho/ROCK signaling pathway. CFs from newborn Sprague Dawley rats were treated with high concentrations of glucose (10, 30 and 50 mmol/l D-glucose), a baseline concentration of glucose (5.5 mmol/l) as a control, and mannitol (5.5 mmol/l D-glucose + 44.5 mmol/l mannitol) as an osmotic control. CFs were also treated with 30 mmol/l D-glucose for 6, 12, 24 and 48 h. The proliferation of CFs was determined by the MTT assay. The mRNA and protein expression of visfatin and type I procollagen were quantified by RT-qPCR and western blot analysis, respectively. Cardiac fibroblast proliferation reached a peak at 30 mmol/l D-glucose, and visfatin and type I procollagen expression were significantly increased upon treatment with high concentrations of glucose (10 and 30 mmol/l) compared to baseline glucose treatment. Treatment with 30 mmol/l D-glucose time-dependently promoted cardiac fibroblast proliferation. The mRNA and protein expression of visfatin and type I procollagen were significantly increased compared to the control at 24 h after 30 mmol/l D-glucose treatment. Y27632, a Rho-associated protein kinase (ROCK) inhibitor, significantly decreased the mRNA and protein levels of visfatin and type I procollagen, induced by 30 mmol/l D-glucose (all P<0.05). In conclusion, a high level of glucose promotes cardiac fibroblast proliferation, and induces visfatin and type I procollagen expression in CFs, at least partially via the Rho/ROCK signaling pathway. These results may be helpful in developing an appropriate therapeutic strategy for DCM.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

High glucose induces Rho/ROCK-dependent visfatin and typeï¿½I procollagen expressionï¿½inï¿½rat primaryï¿½cardiac fibroblasts

et al. 2014

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“…A few previous studies have evaluated the role of visfatin in endothelial cells and have suggested that visfatin may function to improve endothelial cell function and support postnatal angiogenesis (1,8). Although the mechanism(s) of these effects remain unclear, they may involve activation of MAP kinase ERK-dependent pathways, upregulation of vascular endothelial growth factor, and/or stimulation of PI 3-kinase/ Akt pathways.…”

Section: Discussionmentioning

confidence: 99%

“…Recent data have suggested that visfatin may also function analogous to a visceral fat adipocytokine and may alter insulin and glucose signaling, although this remains controversial (5). Evidence is accumulating to suggest that visfatin may serve as a cellular survival factor and may exert beneficial effects on both endothelial (8) and vascular smooth muscle cells (25). Indeed, in vascular smooth muscle cells, visfatin functions as a longevity protein, in part via optimizing Sirt1-mediated p53 degradation, whereas, in endothelial cells, visfatin may stimulate angiogenesis and augment endothelial survival (24).…”

mentioning

confidence: 99%

Visfatin activates eNOS via Akt and MAP kinases and improves endothelial cell function and angiogenesis in vitro and in vivo: translational implications for atherosclerosis

Lovren¹,

Pan²,

Shukla³

et al. 2009

American Journal of Physiology-Endocrinology and Metabolism

102

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-Improving endothelial nitric oxide synthase (eNOS) bioactivity and endothelial function is important to limit native, vein graft, and transplant atherosclerosis. Visfatin, a NAD biosynthetic enzyme, regulates the activity of the cellular survival factor, Sirt1. We hypothesized that visfatin may improve eNOS expression, endothelial function, and postnatal angiogenesis. In human umbilical vein (HUVEC) and coronary artery endothelial cells, we evaluated the effects of recombinant human visfatin on eNOS protein and transcript expression and mRNA stability, in the presence and absence of visfatin RNA silencing. We also assessed visfatin-induced protein kinase B (Akt) activation and its association with src-tyrosine kinases, phosphorylation of Ser 1177 within eNOS in the presence and absence of phosphatidylinositol 3-kinase (PI 3-kinase) inhibition with LY-294002, and evaluated the contributory role of extracellular signal-regulated kinase 1/2. Finally, we determined the impact of visfatin on HUVEC migration, proliferation, inflammation-induced permeability, and in vivo angiogenesis. Visfatin (100 ng/ml) upregulated and stabilized eNOS mRNA and increased the production of nitric oxide and cGMP. Visfatin-treated HUVEC demonstrated greater proliferation, migration, and capillary-like tube formation but less tumor necrosis factor-␣-induced permeability; these effects were decreased in visfatin gene-silenced cells. Visfatin increased total Akt and Ser 473 -phosphoAkt expression with concomitant rises in eNOS phosphorylation at Ser 1177 ; these effects were blocked by LY-2940002. Studies with PP2 showed that the nonreceptor tyrosine kinase, src, is an upstream stimulator of the PI 3-kinase-Akt pathway. Visfatin also activated mitogen-activated protein (MAP) kinase through PI 3-kinase, and mitogen/extracellular signal-regulated kinase inhibition attenuated visfatin-elicited Akt and eNOS phosphorylation. Visfatin-filled Matrigel implants showed an elevated number of infiltrating vessels, and visfatin treatment produced significant recovery of limb perfusion following hindlimb ischemia. These results indicate a novel effect of visfatin to stimulate eNOS expression and function in endothelial cells, via a common upstream, src-mediated signaling cascade, which leads to activation of Akt and MAP kinases. Visfatin represents a translational target to limit endothelial dysfunction, native, vein graft and transplant atherosclerosis, and improve postnatal angiogenesis. nitric oxide; mice; endothelium; atherosclerosis; visfatin; protein kinase B; phosphatidylinositol 3-kinase; mitogen-activated protein kinase; endothelial nitric oxide synthase

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“…It has been shown that the inhibition of the Visfatin-induced expression of inflammatory mediators W-J Lee et al p38 mitogen-activated protein kinase abrogated visfatininduced cytokine production in monocytes 12 and visfatin promoted angiogenesis through the activation of the extracellular signal-regulated kinase 1/2 in endothelial cells. 32 Therefore, visfatin-induced NF-kB activation might be partly through the phosphorylation of mitogen-activated protein kinase pathway. A recent study demonstrated that the inhibition of visfatin-induced activation of phosphatidylinositol 3-kinase/Akt and extracellular signal-regulated kinase 1/2 pathways led to a significant decrease in visfatin-induced matrix metalloproteinase and vascular endothelial growth factor production, along with a significant reduction in endothelial proliferation and capillary tube formation.…”

mentioning

confidence: 99%

Visfatin-induced expression of inflammatory mediators in human endothelial cells through the NF-κB pathway

Lee

et al. 2009

Int J Obes

107

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Background: Visfatin is an adipokine that is highly expressed in visceral fat. Plasma levels of visfatin have been reported to be higher in subjects with obesity and/or type 2 diabetes mellitus. However, the role of visfatin in endothelial dysfunction has been largely unexplored. Objectives: We investigated the possible pathogenic role of visfatin in endothelial dysfunction, particularly focusing on its effect on inflammatory mediators. Design: Primary human umbilical vein endothelial cells (HUVECs) pretreated with visfatin (1, 10 and 50 ng ml À1 ) were used to study the relationship between visfatin and endothelium dysfunction. Expressions of adhesion molecules (ICAM-1, VCAM-1 and E-selectin) and cytokines (interleukin (IL)-6 and IL-8) affected by visfatin were investigated by enzyme-linked immunosorbent assay, flow cytometry and real-time PCR. Activity of nuclear factor (NF)-kB was examined by electrophoretic mobility shift assay. Results: At a visfatin concentration of 50 ng ml À1 , significant increases in IL-6, IL-8, ICAM-1, VCAM-1 and E-selectin gene expression along with increased IL-6, IL-8 and sE-selectin protein levels in the conditioned medium were detected. Flow cytometry showed that the addition of visfatin significantly increased ICAM-1 expression and VCAM-1 expression (10 and 50 ng ml À1 , respectively). Electrophoretic mobility shift assay confirmed that visfatin increased the DNA-binding activity of NFkB. In addition, pretreatment with visfatin (10 and 50 ng ml À1 ) increased human monocyte cell line THP-1 adhesion to HUVECs. Conclusions: Our findings suggest that visfatin causes endothelial dysfunction by increasing inflammatory and adhesion molecule expression at least partly through the upregulation of NF-kB activity.

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Visfatin promotes angiogenesis by activation of extracellular signal-regulated kinase 1/2

Cited by 135 publications

References 28 publications

High glucose induces Rho/ROCK-dependent visfatin and typeï¿½I procollagen expressionï¿½inï¿½rat primaryï¿½cardiac fibroblasts

High glucose induces Rho/ROCK-dependent visfatin and typeï¿½I procollagen expressionï¿½inï¿½rat primaryï¿½cardiac fibroblasts

Visfatin activates eNOS via Akt and MAP kinases and improves endothelial cell function and angiogenesis in vitro and in vivo: translational implications for atherosclerosis

Visfatin-induced expression of inflammatory mediators in human endothelial cells through the NF-κB pathway

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