scholarly journals Shear Rate Dependence of Platelet Adhesion to Collagenous Surfaces in Willebrand Factor-Depleted Blood

1977 ◽  
Author(s):  
H. R. Baumgartner ◽  
Th. B. Tschopp ◽  
D. Meyer
Keyword(s):  
Shear Rate ◽  
Human Blood ◽  
Platelet Adhesion ◽  
Platelet Rich Plasma ◽  
Shear Rates ◽  
Small Vessels ◽  
Perfusion Chamber ◽  
Function Defect ◽  
Induced Aggregation ◽  
Willebrand Factor

A platelet function defect similar to that in von Willebrand’s disease, was produced by adding to human blood an antibody raised in rabbits against human factor Vlll/Willebrand factor. The effect of this antibody (F VIII Ab) on platelet adhesion was tested in an annular perfusion chamber. Only a small adhesion defect was observed at a shear rate corresponding to that in large arteries (830 s-1) . Since bleeding usually occurs from small vessels, platelet adhesion to collagenous surfaces was investigated at higher shear rates corresponding to those in small vessels. The surfaces were exposed to human blood (l5mM citrate) at 1, 2 and 4x103 s-1 shear rate for 6, and 3 min, respectively. Different exposure times were chosen in order to obtain in control perfusions 50 – 70 % coverage of subendothelium with platelets at each shear rate. Platelet adhesion and adhesion-induced aggregation were measured morphometrically. As compared to control, F VIII Ab inhibited adhesion to subendothelium by 15±6, 32±21, 40±10 and 90±2 % (mean ± SE) at 0.83, 1, 2 and 4x103 s-1 shear rate, respectively. The corresponding inhibition by F VIII Ab observed on the fibrillar collagen of α-chymotrypsin-digested subendothelium was 62±11, 75±20, 99±1 and 100 %. In platelet rich plasma, F VIII Ab abolished Ristocetin-, inhibited collagen- and had no effect on ADP-induced aggregation.Thus the defect in platelet adhesion to collagenous surfaces observed in Willebrand factor-depleted blood is minimal at low (venous) and maximal at high (small vessel) shear rates.

scholarly journals Platelet von Willebrand factor: evidence for its involvement in platelet adhesion to collagen

Blood ◽  
1987 ◽  
Vol 70 (4) ◽  
pp. 1214-1217
Author(s):  
E Fressinaud ◽  
D Baruch ◽  
C Rothschild ◽  
HR Baumgartner ◽  
D Meyer
Keyword(s):  
Shear Rate ◽  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
Von Willebrand Disease ◽  
High Shear ◽  
Shear Rates ◽  
High Shear Rates ◽  
Von Willebrand ◽  
Willebrand Factor

Although it is well established that plasma von Willebrand Factor (vWF) is essential to platelet adhesion to subendothelium at high shear rates, the role of platelet vWF is less clear. We studied the respective role of both plasma and platelet vWF in mediating platelet adhesion to fibrillar collagen in a parallel-plate perfusion chamber. Reconstituted blood containing RBCs, various mixtures of labeled washed platelets and plasma from controls or five patients with severe von Willebrand disease (vWD), was perfused through the chamber for five minutes at a shear rate of 1,600 s-1. Platelet-collagen interactions were estimated by counting the radioactivity in deposited platelets and by quantitative morphometry. When the perfusate consisted of normal platelets suspended in normal plasma, platelet deposition on the collagen was 24.7 +/- 3.6 X 10(6)/cm2 (mean +/- SEM, n = 6). Significantly less deposition (16 +/- 2.3) was observed when vWD platelets were substituted for normal platelets. In mixtures containing vWD plasma, significantly greater deposition (9 +/- 2.2) was obtained with normal than with vWD platelets (1 +/- 0.4) demonstrating a role for platelet vWF in mediating the deposition of platelets on collagen. Morphometric analysis confirmed these data. Our findings indicate that platelet, as well as plasma, vWF mediates platelet-collagen interactions at a high shear rate.

scholarly journals Prostacyclin (prostaglandin I2, PGI2) inhibits platelet adhesion and thrombus formation on subendothelium

Blood ◽  
1979 ◽  
Vol 53 (2) ◽  
pp. 244-250 ◽  
Author(s):  
HJ Weiss ◽  
VT Turitto
Keyword(s):  
Blood Vessels ◽  
Human Blood ◽  
Platelet Adhesion ◽  
Platelet Rich Plasma ◽  
Thrombus Formation ◽  
Rabbit Aorta ◽  
Prostaglandin I2 ◽  
Shear Rates ◽  
Platelet Spreading ◽  
Aggregation Of Platelets

Abstract Prostaglandin I2 (prostacyclin, PGI2), a substance synthesized in the wall of blood vessels, has been previously shown to inhibit the aggregation of platelets in stirred platelet-rich plasma. We used a method in which segments of deendothelialized rabbit aorta are perfused at arterial shear rates with human blood and found that both platelet adhesion and thrombus formation on subendothelium was inhibited in blood containing 10 nM PGI2. PGI2 appears to reduce adhesion by inhibiting platelet spreading. These findings suggest that PGI2 could regulate the deposition of platelets on vascular surfaces.

scholarly journals Glycoprotein Ib, von Willebrand factor, and glycoprotein IIb:IIIa are all involved in platelet adhesion to fibrin in flowing whole blood

Blood ◽  
1990 ◽  
Vol 76 (2) ◽  
pp. 345-353 ◽  
Author(s):  
RR Hantgan ◽  
G Hindriks ◽  
RG Taylor ◽  
JJ Sixma ◽  
PG de Groot
Keyword(s):  
Platelet Aggregation ◽  
Shear Rate ◽  
Von Willebrand Factor ◽  
Whole Blood ◽  
Platelet Adhesion ◽  
Thrombus Formation ◽  
Shear Rates ◽  
Wall Shear ◽  
Von Willebrand ◽  
Willebrand Factor

We have investigated the molecular basis of thrombus formation by measuring the extent of platelet deposition from flowing whole blood onto fibrin-coated glass coverslips under well-defined shear conditions in a rectangular perfusion chamber. Platelets readily and specifically adhered to fibrin-coated coverslips in 5 minute perfusion experiments done at either low (300 s-1) or high (1,300 s-1) wall shear rates. Scanning electron microscopic examination of fibrin-coated coverslips after perfusions showed surface coverage by a monolayer of adherent, partly spread platelets. Platelet adhesion to fibrin was effectively inhibited by a monoclonal antibody (MoAb) specific for glycoprotein (GP) IIb:IIIa. The dose-response curve for inhibition of adhesion by anti-GPIIb:IIIa at both shear rates paralleled that for inhibition of platelet aggregation. Platelet aggregation and adhesion to fibrin were also blocked by low concentrations of prostacyclin. In contrast, anti- GPIb reduced adhesion by 40% at 300 s-1 and by 70% at 1,300 s-1. A similar pattern of shear rate-dependent, incomplete inhibition resulted with a MoAb specific for the GPIb-recognition region of von Willebrand factor (vWF). Platelets from an individual with severe von Willebrand's disease, whose plasma and platelets contained essentially no vWF, exhibited defective adhesion to fibrin, especially at the higher shear rate. Addition of purified vWF restored adhesion to normal values. These results are consistent with a two-site model for platelet adhesion to fibrin, in which the GPIIb:IIIa complex is the primary receptor, with GPIb:vWF providing a secondary adhesion pathway that is especially important at high wall shear rates.

scholarly journals Prostacyclin (prostaglandin I2, PGI2) inhibits platelet adhesion and thrombus formation on subendothelium

Blood ◽  
1979 ◽  
Vol 53 (2) ◽  
pp. 244-250 ◽  
Author(s):  
HJ Weiss ◽  
VT Turitto
Keyword(s):  
Blood Vessels ◽  
Human Blood ◽  
Platelet Adhesion ◽  
Platelet Rich Plasma ◽  
Thrombus Formation ◽  
Rabbit Aorta ◽  
Prostaglandin I2 ◽  
Shear Rates ◽  
Platelet Spreading ◽  
Aggregation Of Platelets

Prostaglandin I2 (prostacyclin, PGI2), a substance synthesized in the wall of blood vessels, has been previously shown to inhibit the aggregation of platelets in stirred platelet-rich plasma. We used a method in which segments of deendothelialized rabbit aorta are perfused at arterial shear rates with human blood and found that both platelet adhesion and thrombus formation on subendothelium was inhibited in blood containing 10 nM PGI2. PGI2 appears to reduce adhesion by inhibiting platelet spreading. These findings suggest that PGI2 could regulate the deposition of platelets on vascular surfaces.

Fluid Dynamical Considerations of Platelet-Vessel Wall Interaction

1979 ◽  
Author(s):  
V.T. Turitto
Keyword(s):  
Shear Rate ◽  
Platelet Adhesion ◽  
Relative Magnitude ◽  
Physical Factors ◽  
Shear Rates ◽  
Adhesion Rate ◽  
Flowing Blood ◽  
Wall Interaction ◽  
Von Willebrand ◽  
Willebrand Factor

Platelet adhesion to subendothelium is dependent on two distinct processes: (1) diffusive transport (T) of platelets to the surface and (2) platelet-subendothelial reactivity (R). The relative magnitude of T to R will determine which factors control the adhesion rate. Physical factors, specifically, wall shear rate (γ) and platelet diffusivity (D) influence T, whereas chemical alterations modify R. An increase in the magnitude of γ or D or a decrease in R tends toward R controlled adhesion. An increase in low rate or decrease in vessel dimensions increases γ, whereas D increases with both red cell concentration (up to 40 %) and γ.In flowing blood at shear rates comparable to those found in veins or large arteries (< 650 see-1), T determines platelet adhesion. Moderate alterations in R, such as produced by the addition to blood of 45 mM citrate, 10-100 nM prostacyclin or in von Willebrand factor depleted blood, have little effect on platelet adhesion values under these flow conditions. However, as shear rate is increased to values comparable to those in the microcirculation {1300-2600 sec-1), the same blood samples show values of platelet adhesion which are reduced compared to controls, and the reduction increases with shear rate Thus, measurements of R should be determined under controlled shear conditions which are high enough to be outside the range of predominantly transport controlled adhesion.

scholarly journals Glycoprotein Ib, von Willebrand factor, and glycoprotein IIb:IIIa are all involved in platelet adhesion to fibrin in flowing whole blood

Blood ◽  
1990 ◽  
Vol 76 (2) ◽  
pp. 345-353 ◽  
Author(s):  
RR Hantgan ◽  
G Hindriks ◽  
RG Taylor ◽  
JJ Sixma ◽  
PG de Groot
Keyword(s):  
Platelet Aggregation ◽  
Shear Rate ◽  
Von Willebrand Factor ◽  
Whole Blood ◽  
Platelet Adhesion ◽  
Thrombus Formation ◽  
Shear Rates ◽  
Wall Shear ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract We have investigated the molecular basis of thrombus formation by measuring the extent of platelet deposition from flowing whole blood onto fibrin-coated glass coverslips under well-defined shear conditions in a rectangular perfusion chamber. Platelets readily and specifically adhered to fibrin-coated coverslips in 5 minute perfusion experiments done at either low (300 s-1) or high (1,300 s-1) wall shear rates. Scanning electron microscopic examination of fibrin-coated coverslips after perfusions showed surface coverage by a monolayer of adherent, partly spread platelets. Platelet adhesion to fibrin was effectively inhibited by a monoclonal antibody (MoAb) specific for glycoprotein (GP) IIb:IIIa. The dose-response curve for inhibition of adhesion by anti-GPIIb:IIIa at both shear rates paralleled that for inhibition of platelet aggregation. Platelet aggregation and adhesion to fibrin were also blocked by low concentrations of prostacyclin. In contrast, anti- GPIb reduced adhesion by 40% at 300 s-1 and by 70% at 1,300 s-1. A similar pattern of shear rate-dependent, incomplete inhibition resulted with a MoAb specific for the GPIb-recognition region of von Willebrand factor (vWF). Platelets from an individual with severe von Willebrand's disease, whose plasma and platelets contained essentially no vWF, exhibited defective adhesion to fibrin, especially at the higher shear rate. Addition of purified vWF restored adhesion to normal values. These results are consistent with a two-site model for platelet adhesion to fibrin, in which the GPIIb:IIIa complex is the primary receptor, with GPIb:vWF providing a secondary adhesion pathway that is especially important at high wall shear rates.

Platelet von Willebrand factor: evidence for its involvement in platelet adhesion to collagen

Blood ◽  
1987 ◽  
Vol 70 (4) ◽  
pp. 1214-1217 ◽  
Author(s):  
E Fressinaud ◽  
D Baruch ◽  
C Rothschild ◽  
HR Baumgartner ◽  
D Meyer
Keyword(s):  
Shear Rate ◽  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
Von Willebrand Disease ◽  
High Shear ◽  
Shear Rates ◽  
High Shear Rates ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Although it is well established that plasma von Willebrand Factor (vWF) is essential to platelet adhesion to subendothelium at high shear rates, the role of platelet vWF is less clear. We studied the respective role of both plasma and platelet vWF in mediating platelet adhesion to fibrillar collagen in a parallel-plate perfusion chamber. Reconstituted blood containing RBCs, various mixtures of labeled washed platelets and plasma from controls or five patients with severe von Willebrand disease (vWD), was perfused through the chamber for five minutes at a shear rate of 1,600 s-1. Platelet-collagen interactions were estimated by counting the radioactivity in deposited platelets and by quantitative morphometry. When the perfusate consisted of normal platelets suspended in normal plasma, platelet deposition on the collagen was 24.7 +/- 3.6 X 10(6)/cm2 (mean +/- SEM, n = 6). Significantly less deposition (16 +/- 2.3) was observed when vWD platelets were substituted for normal platelets. In mixtures containing vWD plasma, significantly greater deposition (9 +/- 2.2) was obtained with normal than with vWD platelets (1 +/- 0.4) demonstrating a role for platelet vWF in mediating the deposition of platelets on collagen. Morphometric analysis confirmed these data. Our findings indicate that platelet, as well as plasma, vWF mediates platelet-collagen interactions at a high shear rate.

scholarly journals Platelet Adhesion to Collagen Type I, Collagen Type IV, von Willebrand Factor, Fibronectin, Laminin and Fibrinogen: Rapid Kinetics under Shear

1999 ◽  
Vol 81 (01) ◽  
pp. 118-123 ◽  
Author(s):  
Carl Simon ◽  
Adrian Gear ◽  
Renata Polanowska-Grabowska
Keyword(s):  
Shear Rate ◽  
Platelet Adhesion ◽  
Collagen Type ◽  
Lag Phase ◽  
Type I ◽  
Flow Conditions ◽  
Shear Rates ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Kinetics Of

SummaryExtracellular matrix proteins in the blood vessel wall fulfill an essential role in haemostasis by promoting platelet adhesion at the site of vessel injury. We have combined a continuous-flow system with affinity chromatography to study platelet adhesion under conditions mimicking arterial flow and have examined the adhesion kinetics of unstimulated platelets to collagens type I and IV, von Willebrand factor (vWf), fibronectin, laminin and to fibrinogen. In the absence of red cells, in ACD-prepared plasma adhesion to collagens type I and IV or vWf was rapid, efficient (>50% in <1 s ) and independent of shear rates from 650 to 3400 s-1with kinetics following an inverse exponential decay curve. We introduced a simple mathematical model in which this type of kinetics arises, and which may be more generally applicable to various adhesion processes under flow conditions. The model is characterized by the rate of platelet deposition on the adhesive surface being proportional to the number of platelets in the flow. Adhesion to fibronectin was independent of shear rate, but revealed a lag phase of ~1.5 s before significant adhesion began. Laminin and fibrinogen supported efficient adhesion at low shear rates (650-1000 s-1), but a lag phase of ~1.5 s was seen at high shear rates (1700-3400 s-1). Control proteins (albumin and gelatin) supported minimal adhesion. Nonspecific adhesion to poly-l-lysine differed from that to other substrate proteins in that the kinetics were linear. In conclusion, human platelets adhered specifically, rapidly (within seconds) and efficiently to several proteins under flow conditions and the kinetics of adhesion depended on the protein serving as substrate as well as on shear rate.

scholarly journals Platelet adhesion to laminin: role of Ca2+ and Mg2+ ions, shear rate, and platelet membrane glycoproteins

Blood ◽  
1992 ◽  
Vol 79 (4) ◽  
pp. 928-935 ◽  
Author(s):  
G Hindriks ◽  
MJ Ijsseldijk ◽  
A Sonnenberg ◽  
JJ Sixma ◽  
PG de Groot
Keyword(s):  
Shear Rate ◽  
Platelet Adhesion ◽  
Divalent Cations ◽  
Platelet Membrane ◽  
Flow Conditions ◽  
Membrane Glycoproteins ◽  
Shear Rates ◽  
The Matrix ◽  
Von Willebrand ◽  
Willebrand Factor

The adhesion of platelets to purified laminin under flow conditions was investigated. Adhesion to laminin was strongly dependent on the presence of divalent cations. In the absence of cations platelet adhesion (8% coverage in 5 minutes) was maximal at a shear rate of 100/s and no adhesion could be detected at shear rates above 800/s. In the presence of 0.8 mmol/L Mg2+ and 2 mmol/L Ca2+ platelet adhesion reached its maximum (30% coverage) around 800/s. At 1,800/s platelets still adhered to purified laminin (coverage of 6%). Antibodies against the E8 domain of laminin and antibodies against the alpha 6 and beta 1 chains of platelet membrane glycoprotein very late activation antigen-6 (VLA-6), completely inhibited adhesion. No inhibition was found with antibodies against glycoprotein IIb:IIIa, against the alpha 2 chain of VLA-2, and against the alpha 5 chain of VLA-5. Fibronectin and von Willebrand factor were not involved in laminin-dependent adhesion. Anti- VLA-6 partly inhibited platelet adhesion to the extracellular matrix of endothelial cells at shear rates below 800/s. Preincubation of the matrices with antilaminin E8 antibodies did not influence the adhesion. These results show that purified laminin supports platelet adhesion and that the presence of VLA-6 is important for platelet adhesion under flow conditions. The protein in the matrix with which VLA-6 interacts is currently unknown.

Aurin Tricarboxylic Acid Inhibits Platelet Adhesion to Collagen by Binding to the 509-695 Disulphide Loop of von Willebrand Factor and Competing with Glycoprotein Ib

1992 ◽  
Vol 68 (06) ◽  
pp. 707-713 ◽  
Author(s):  
J P Girma ◽  
E Fressinaud ◽  
O Christophe ◽  
C Rouault ◽  
B Obert ◽  
...  
Keyword(s):  
Shear Rate ◽  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
Tricarboxylic Acid ◽  
Dependent Manner ◽  
Binding Studies ◽  
Human Collagen ◽  
Von Willebrand ◽  
Induced Aggregation ◽  
Willebrand Factor

SummaryAurin tricarboxylic acid (ATA) is known to inhibit ristocetin-induced platelet agglutination but not arachidonic acid-, epinephrine- or ADP-induced aggregation. Its capacity to abolish human von Willebrand factor (vWF)-platelet interactions was further investigated by measurement of platelet adhesion to collagen, platelet agglutination tests and binding studies. In flowing blood using parallel-plate perfusion chambers and human collagen, ATA inhibited platelet adhesion to completion in a dose-dependent manner only at the highest shear rate tested (2,600 s–1). It was without effect at 100 and 650 s–1. ATA completely abolished vWF-dependent platelet agglutination induced by ristocetin, botrocetin and asialo-vWF, respectively. 125I-vWF binding to ristocetin- and botrocetin-treated platelets, to heparin and to sulfatides as well as 125I-botrocetin binding to vWF was competitively inhibited by ATA. By contrast, binding of 125I-vWF to collagen was not affected. To further localize the domain of vWF interacting with ATA, experiments of inhibition of binding of selected 125I-monoclonal antibodies (MoAbs) to immobilized vWF by ATA were performed. Our data led to the conclusion that: 1) the interaction of ATA with vWF involves sequences of the A1 disulphide loop of vWF (residues 509–695) and close epitopes which interact with GPIb and 2) the inhibition of platelet adhesion by ATA occurs only at a high shear rate where vWF is known to play a key role. Thus ATA, which blocks the vWF/GPIb pathway by interfering with vWF and not with platelets, is a potential tool in preventing the early stages of thrombosis.

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