Long Pentraxin PTX3 Upregulates Tissue Factor Expression in Human Endothelial Cells

Napoleone, E.; Santo, Angelomaria Di; Bastone, Antonio; Peri, Giuseppe; Mantovani, Alberto; Gaetano, Giovanni de; Donati, Maria Benedetta; Lorenzet, Roberto

doi:10.1161/01.atv.0000012282.39306.64

Cited by 146 publications

(107 citation statements)

References 36 publications

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“…PTX3 specifically enhances LPS-elicited tissue factor activity in vitro, possibly promoting activation of the coagulation cascade in the presence of microbial moieties (49,50). The effect is specific for bacterial endotoxin, since PTX3 does not influence the action of primary proinflammatory cytokines, such as TNF-a and IL-1b.…”

Section: Discussionmentioning

confidence: 99%

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Early and Transient Release of Leukocyte Pentraxin 3 during Acute Myocardial Infarction

Maugeri

Rovere‐Querini

Slavich

et al. 2011

The Journal of Immunology

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Pentraxin 3 (PTX3) plays cardioprotective and anti-atherogenic roles in murine models. PTX3 blood levels raise during early acute myocardial infarction (AMI). Neutrophils from healthy subjects physiologically contain PTX3 in secondary (also called specific) granules. In this study, we report that circulating neutrophils release preformed PTX3 in the early phase of AMI (within 6 h from the onset of clinical symptoms). Depletion of intracellular PTX3 correlates with increased plasma levels and with platelet–neutrophil heterotypic aggregates. Neutrophil PTX3 returns to normal values 48 h after the onset of symptoms; concentration does not vary in matched healthy controls or in patients with chronic stable angina. In vitro, recognition of activated P-selectin+ platelets causes the formation of neutrophil–platelet heteroaggregates and the release of neutrophil PTX3. Purified or membrane-bound P-selectin triggers PTX3 release from resting neutrophils. Released PTX3 binds to activated platelets in vitro. Moreover, PTX3 binds to a substantial fraction of platelets from patients in the circulating blood. PTX3-bound activated platelets have a reduced ability to 1) form heterotypic aggregates with neutrophils and monocytes; 2) activate neutrophils, as evaluated assessing the upregulation of leukocyte β2 integrins; 3) aggregate with other platelets; and 4) bind to fibrinogen. Our results suggest that neutrophils early release prestored PTX3 in patients undergoing AMI. PTX3 binds to activated circulating platelets and dampens their proinflammatory and prothrombotic action, thus possibly contributing to its cardioprotective effects.

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Section: Discussionmentioning

confidence: 99%

“…These results hint at a possible involvement of PTX3 in thrombotic events associated to sepsis. PTX3 per se does not influence tissue factor expression and activity in monocytes and endothelial cells (49,50), making it unlikely that this is the case in sterile vascular injuries, such as those occurring in acute coronary syndromes.…”

Section: Discussionmentioning

confidence: 99%

Early and Transient Release of Leukocyte Pentraxin 3 during Acute Myocardial Infarction

Maugeri

Rovere‐Querini

Slavich

et al. 2011

The Journal of Immunology

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“…Some reports have revealed that, in humans, PTX3 is produced in areas of atherosclerosis and may contribute to the pathogenesis of atherosclerosis 16,33,34) . It has been shown that endothelial cells, macrophages and smooth muscle cells involved in atherosclerosis produce PTX3 16,35) ; therefore, levels of PTX3 may directly indicate the status of vascular inflammation. It has been reported that circulating PTX3 concentrations were higher in patients with heart failure and that these concentrations varied depending on the severity of CVD 13,17,36,37) ; however, it has not yet been confirmed if the levels of circulating PTX3 in obese subjects are higher than in nonobese subjects.…”

Section: Discussionmentioning

confidence: 99%

Is Pentraxin 3 Involved in Obesity-Induced Decrease in Arterial Distensibility?

Miyaki

Maeda

Yoshizawa

et al. 2010

JAT

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Aim: Obesity is a strong risk factor for cardiovascular morbidity and mortality. In addition, decreased central arterial distensibility is recognized as an independent risk factor for cardiovascular disease (CVD). Obese subjects exhibit low arterial distensibillity; however, the mechanism responsible for the decrease in arterial distensibility in obese subjects has not yet been elucidated. Pentraxin 3 (PTX3), a recently identified member of the pentraxin family of proteins, is produced in areas of atherosclerosis. A recent study has revealed that the PTX3 level may indicate the vascular inflammatory status. The aim of this study was to investigate plasma PTX3 concentrations and arterial distensibility in obese subjects. ) participated in this study. We measured arterial compliance (using simultaneous B-mode ultrasound and arterial applanation tonometry of the common carotid artery); -stiffness index, an index of arterial compliance adjusted for distending pressure; and plasma PTX3 concentrations. Results: Arterial compliance was significantly lower and the -stiffness index was significantly higher in obese men than in non-obese men. Plasma PTX3 concentration was markedly higher in obese than non-obese men. Conclusions: Obese men have lower arterial distensibility and higher circulating PTX3 levels than non-obese men; therefore, higher PTX3 levels and decreased arterial distensibility coexist in obese men. The high PTX3 concentrations in obese men may be involved in the mechanism underlying the obesity-induced decrease in arterial distensibility. J Atheroscler Thromb, 2010; 17:278-284.

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“…Clinical significance of these different types of human endothelial cells in response to CRP remains to be determined. In addition, CRP also increases tissue factor, cytokines, and another important thrombotic factor secreted from peripheral monocytes [24] and endothelial cells [25]. In our previous studies, we have demonstrated that CRP decreased the expression of thrombomodulin, endothelial protein C receptor, VEGF receptors and neuropilins in human endothelial cells [26,27].…”

Section: Discussionmentioning

confidence: 99%

C-reactive protein increases plasminogen activator inhibitor-1 expression in human endothelial cells

Chen

Nan

Lin

et al. 2008

Thrombosis Research

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C-reactive protein (CRP) is an inflammatory marker which predicts cardiovascular disease. However, it is not fully understood whether CRP has direct effects on endothelial functions and gene expression. The purpose of current study was to determine the effects and molecular mechanisms of CRP on the expression of plasminogen activator inhibitor-1 (PAI-1) in human endothelial cells. Human coronary artery endothelial cells (HCAEC) were treated with CRP at clinically relevant concentrations for different durations. PAI-1 mRNA, protein and enzyme activities were studied. The effects of CRP on MAPK p38 phosphorylation was also studied by Bio-Plex luminex immunoassay. In addition, other types of human endothelial cells isolated from umbilical vein, skin, and lung microvessels were tested. CRP significantly increased PAI-1 mRNA levels in a time-and concentration-dependent manner. The protein level and enzyme activity of PAI-1 in the supernatant of CRP-treated HCAEC cultures were significantly increased. Anti-CD32 antibody effectively blocked CRP-induced PAI-1 mRNA expression. In addition, CRP significantly increased CD32 mRNA levels and enhanced phosphorylation of MAPK p38. Furthermore, antioxidant curcumin dramatically inhibited CRP-induced PAI-1 mRNA expression. The effect of CRP on PAI-1 expression was also confirmed in other types of human endothelial cells. In conclusion, CRP significantly increased the expression of PAI-1 in HCAEC and other human endothelial cells. CRP also increased its receptor CD32 expression which may further enhance its action. CRP-induced PAI-1 expression may be mediated by oxidative stress and p38 signal pathway as antioxidant effectively blocks the effect of CRP on HCAEC.

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Long Pentraxin PTX3 Upregulates Tissue Factor Expression in Human Endothelial Cells

Cited by 146 publications

References 36 publications

Early and Transient Release of Leukocyte Pentraxin 3 during Acute Myocardial Infarction

Early and Transient Release of Leukocyte Pentraxin 3 during Acute Myocardial Infarction

Is Pentraxin 3 Involved in Obesity-Induced Decrease in Arterial Distensibility?

C-reactive protein increases plasminogen activator inhibitor-1 expression in human endothelial cells

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