Platelet‐induced neutrophil activation: platelet‐expressed fibrinogen induces the oxidative burst in neutrophils by an interaction with CD11C/CD18

Ruf, Andreas; Patscheke, Heinrich

doi:10.1111/j.1365-2141.1995.tb05197.x

Cited by 84 publications

(55 citation statements)

References 28 publications

(18 reference statements)

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“…In specific situations, P-selectin may cooperate with other platelet-signaling factors to alter leukocyte function (75). Indeed, platelet-released fibrinogen can bridge GPIIb/ IIIa on platelets with CD11c/CD18 on neutrophils, an interaction that generates a neutrophil oxidative burst (76). This process requires adhesion via P-selectin, further indicating that P-selectin may act in concert with platelet-signaling factors (75) and with other adhesion molecules (75,77,78) to elicit unique patterns of gene expression at sites of inflammation.…”

Section: Discussionmentioning

confidence: 99%

Activated platelets signal chemokine synthesis by human monocytes.

et al. 1996

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Human blood monocytes adhere rapidly and for prolonged periods to activated platelets that display P-selectin, an adhesion protein that recognizes a specific ligand on leukocytes, P-selectin glycoprotein-1. We previously demonstrated that P-selectin regulates expression and secretion of cytokines by stimulated monocytes when it is presented in a purified, immobilized form or by transfected cells. Here we show that thrombin-activated platelets induce the expression and secretion of monocyte chemotactic protein-1 and IL-8 by monocytes. Enhanced monokine synthesis requires engagement of P-selectin glycoprotein-1 on the leukocyte by P-selectin on the platelet. Secretion of the chemokines is not, however, directly signaled by P-selectin; instead, tether-

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Section: Discussionmentioning

confidence: 99%

Activated platelets signal chemokine synthesis by human monocytes.

et al. 1996

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“…The selectin mediated tethering and rolling mechanisms of neutrophils and platelets are highly shear dependent. Leukocyte  2 -integrins may bind directly to ICAM-2, via fibrinogen bridging indirectly to GpIIb/IIIa (CD41/CD61 or IIb/IIIa) [14] or possibly to GpIb [15]. It is generally considered that an integrin-mediated firm adhesion of neutrophils to endothelial cells or platelets require a prior selectin-dependent interaction.…”

Section: Introductionmentioning

confidence: 99%

Platelets stimulated by IgG-coated surfaces bind and activate neutrophils through a selectin-dependent pathway

2003

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Blood platelets bind rapidly to foreign surfaces and interact with adsorbed proteins and neutrophil granulocytes. We demonstrate by use of luminol-amplified chemiluminescence under stirred and nonstirred conditions that platelets at IgG-coated surfaces amplify the neutrophil extracellular release of reactive oxygen species (ROS). The neutrophil response involved tyrosine phosphorylation, but was only in part induced by neutrophil F c -receptor stimulation. The platelet mediated effects were contact-dependent since the respiratory burst was inhibited when the IgG-stimulated platelets were removed by filtration, but not when they were fixed in paraformaldehyde. Bodipyphallacidin-staining of filamentous actin (F-actin) revealed that an actin-dependent platelet adhesion supported the subsequent adhesion and spreading of neutrophils. The neutrophil ROS-response was lowered when the interaction between platelet P-selectin (CD62P) and neutrophil P-selectin glycoprotein ligand-l (PSGL-1 or CD162) was inhibited. The blocking of L-selectin (CD62L) or blocking of the interaction between platelet glycoprotein (Gp) IIb/IIIa and neutrophil complement receptor 3 (CR3) showed no effect. We conclude that platelet activation on immobilized IgG trigger a contact-dependent "frustrated" phagocytosis by neutrophils, associated with a release of toxic ROS. IgG-stimulated platelets activate neutrophils -Wetterö et al.3

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“…Collagen-adherent platelets are comparatively more procoagulant 15,16 than are fibrinogen-adherent platelets in promoting fibrin formation. Interactions of neutrophils with platelets in aggregometer-mixed cell suspensions 17 have been found to cause neutrophil oxidative burst and arachidonic acid exchange. 18 However, the effects of neutrophil-platelet interactions, which primarily occur during adhesion and heterotypic aggregation, on subsequent fibrin formation have not been previously studied in a system that decouples flow-regulated adhesion events from flow-regulated coagulation biochemistry.…”

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confidence: 99%

Neutrophil Enhancement of Fibrin Deposition Under Flow Through Platelet-Dependent and -Independent Mechanisms

Goel

Diamond

2001

ATVB

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Abstract-We examined the effect of adherent neutrophils on fibrin deposition under laminar flow conditions. Perfusion of recalcified citrated platelet-free plasma (PFP) over neutrophils adherent to fibrinogen-coated glass at a venous wall shear rate of 62.5 s Ϫ1 for 15 minutes resulted in dense deposition of fibrin around each neutrophil, whereas fibrin deposition on glass alone was sparse. Fibrin deposition on neutrophils was markedly reduced by anti-CD18 or anti-CD11b or a higher shear rate (250 s Ϫ1 ). Significantly less fibrin was deposited around adherent fibrinogen-coated beads, indicating that nonspecific "cross-sectional capture" effects were not responsible for the massive fibrin deposition on neutrophils. Direct visualization of fibrin capture by neutrophils and elimination of fibrin deposition at 15 minutes by a factor XIIa inhibitor (50 g/mL corn trypsin inhibitor [CTI]) or elastase/cathepsin G inhibitors (MethoxysuccinylAla-Ala-Pro-Ala-Chloromethyl-Ketone/Z-Gly-Leu-Phe-CMK, 100 mol/L) indicated that neutrophils can capture short fibrin strands flowing in recalcified PFP lacking CTI and can also promote thrombin generation through pathways attenuated by inhibitors of factor XIIa, elastase, and cathepsin G. When neutrophils were allowed to interact with platelets on a fibrinogen surface before perfusion of recalcified CTI-treated PFP, the fibrin deposition was observed to be dramatic compared with that over surfaces coated with platelets alone or neutrophils alone and compared with that formed on platelets adherent to collagen. This neutrophil promotion of platelet-mediated fibrin formation was attenuated by inhibitors of elastase or cathepsin G but not anti-tissue factor antibody. Neutrophils can interact with platelets via released proteases to increase platelet procoagulant activity and fibrin formation in CTI-treated plasma under the low-flow conditions expected in venous thrombosis or inflammation. Key Words: P-selectin Ⅲ CD11b/CD18 Ⅲ thrombin Ⅲ deep vein thrombosis B lood coagulation on the inner wall of blood vessels is the major cause of cardiovascular diseases, such as deep vein thrombosis, myocardial infarction, and stroke. In a Dacron graft model, Palabrica et al 1 showed that neutrophils enhance fibrin deposition through P-selectin-dependent mechanisms. Adherent neutrophils may promote thrombosis via pathways such as deencryption of tissue factor, 2 release of proteases that activate platelets, 3,4 Mac-1 (CD11b/CD18) binding of factor X, 5 and improved capture of flowing platelets via protrusion into the flow stream. 6 The capture of neutrophils by the vessel wall involves neutrophil P-selectin glycoprotein ligand-1 (PSGL-1)-mediated rolling 7 and membrane tethering 8 on P-selectin presented by activated endothelium or spread platelets, 9 followed by ␤ 2 -integrin-mediated firm arrest. 10 The neutrophil ␤ 2 -integrin Mac-1, when upregulated, can bind endothelial intercellular adhesion molecule-1 and an unknown platelet ligand, 11 which may be glycoprotein Ib␣. 12 Adherent neutrophils can a...

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Platelet‐induced neutrophil activation: platelet‐expressed fibrinogen induces the oxidative burst in neutrophils by an interaction with CD11C/CD18

Cited by 84 publications

References 28 publications

Activated platelets signal chemokine synthesis by human monocytes.

Activated platelets signal chemokine synthesis by human monocytes.

Platelets stimulated by IgG-coated surfaces bind and activate neutrophils through a selectin-dependent pathway

Neutrophil Enhancement of Fibrin Deposition Under Flow Through Platelet-Dependent and -Independent Mechanisms

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