Step-by-step analysis of adhesion of human platelets to a collagen-coated surface defect in initial attachment and spreading of platelets in Von Willebrand's disease

Leytin, Valery; Gorbunova, N. A.; Misselwitz, Frank; Novikov, I. D.; Podrez, Eugene A.; Plyusch, O. P.; Likhachova, E. A.; Repin, V. S.; Smirnov, V.N.

doi:10.1016/0049-3848(84)90105-1

Cited by 19 publications

(5 citation statements)

References 17 publications

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“…Platelets on the TSM sensor surface were fixed for SEM imaging with 2.5% glutaraldehyde solution and rinsed with 0.15 M NaCl solution at pH 7.4. 25 This was followed by rinsing with ethanol for several minutes before air drying. TSM sensors were coated with gold using a Polaron 11HD SEM coating system giving a thickness of 30 nm.…”

Section: Instrumentationmentioning

confidence: 99%

Blood platelet adhesion to protein studied by on-line acoustic wave sensor

Čavić

Freedman

Morel

et al. 2001

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The attachment of blood platelets to the surface of bare and protein-coated thickness-shear mode acoustic wave devices operating in a flow-through configuration has been studied. Platelets in washed from bind to the gold electrodes of such sensors, but the resulting frequency shifts are far less than predicted by the conventional mass-based model of device operation. Adherence to albumin and various types of collagen can be produced by on-line introduction of protein or by a pre-coating strategy. Differences in attachment of platelets to collagen types I and IV and the Horm variety can be detected. Platelets attached to collagen yield an interesting delayed, but reversible signal on exposure to a flowing medium of low pH. Scanning electron microscopy of sensor surfaces at various time points in this experiment reveals that originally intact platelets are eventually destroyed by the high acidity of the medium. The reversible frequency is attributed to the presence of removable platelet granular components at the sensor-liquid interface.

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Section: Instrumentationmentioning

confidence: 99%

Blood platelet adhesion to protein studied by on-line acoustic wave sensor

Čavić

Freedman

Morel

et al. 2001

Analyst

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“…The role for FVIII-VWF as a spreading factor on subendothelium at high shear rates was recently disputed by Turitto et al (56), who implicated a role for FVIII-VWF in the initial contact phase. Studies with collagen-coated slides recently implicated FVIII-VWF in both initial attachment and spreading (57).…”

Section: 7±13 (3)mentioning

confidence: 99%

Role of factor VIII-von Willebrand factor and fibronectin in the interaction of platelets in flowing blood with monomeric and fibrillar human collagen types I and III.

Houdijk¹,

Sakariassen²,

Nievelstein³

et al. 1985

J. Clin. Invest.

231

106

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Platelet adhesion to monomeric collagen types I and III, which were purified from human umbilical arteries, was studied in a perfusion chamber under well defined flow conditions. For this purpose, glass coverslips were coated with 20-30 'sg/cm2 of collagen types I and III by spraying a solution of these collagens with a retouching air brush. Platelet deposition increased with the time of perfusion. Adhesion to both collagen types was similar in the first 3 min, but increased platelet deposition occurred on collagen type III after 3 min due to thrombus formation. Adhesion at a shear rate of 800 s-' was strongly impaired with plasma of a patient with von Willebrand's disease or with fibronectin-free plasma. Addition of purified fibronectin to fibronectin-free plasma restored adhesion to the level obtained with normal plasma. Platelet deposition in normal plasma increased with increasing shear rates. Platelet deposition in VWD-plasma was normal at 490 s-', but there was no increase at higher shear rates. Platelet deposition in fibronectin-free plasma was diminished at all shear rates studied from 490 to 1,300 sO.Perfusion with a human albumin solution (HAS) to which purified Factor VIII-von Willebrand factor complex (FVIII-VWF) and fibronectin had been added gave similar platelet deposition as with normal plasma. Preincubation of collagen with FVIII-VWF and perfusion with HAS containing fibronectin, or, conversely, preincubation with fibronectin and perfusion with HAS containing FVIII-VWF, also resulted in adhesion similar to that observed in normal plasma. Similar adhesion was also observed after preincubation with both FVIII-VWF and fibronectin and subsequent perfusion with HAS alone. Sequential preincubations with first FVIII-VWF and then fibronectin, or with first fibronectin and then FVIII-VWF followed by perfusion with HAS, also gave a similar adhesion as observed with normal plasma.These data indicate that platelet adhesion to monomeric collagen types I and III is dependent on both FVIII-VWF and fibronectin. FVIII-VWF is only required at relatively high shear rates; fibronectin also at relatively low shear rates. Their Part of this work was presented at the IXth International Congress on Thrombosis and Haemostasis, Stockholm, Sweden, 1983, and has been published in abstract form in Thromb. Haemostasis, 50:1276.Address correspondence to Dr. Houdijk.Receivedfor publication 14 November 1983 and in revisedform 14 September 1984.complementary role in platelet adhesion suggests separate binding sites for FVIII-VWF and fibronectin on collagen.Platelet deposition on preformed fibrils of collagen types I and III was also studied. Initial adhesion expressed as percentage surface coverage was similar to that found with monomeric collagen, but thrombus formation was much enhanced.Adhesion on fibrillar collagen at 800 s-5 was impaired in VWD-plasma and fibronectin-free plasma, and was restored by addition of purified fibronectin to fibronectin-free plasma.When perfusions were performed with HAS, only addition of ...

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“…27 Whether the primary defect was in platelet spreading or in primary platelet contact remained a matter of debate, 28,29 but recent data indicate that vWF may support both. 30 The effect of vWF on platelet adhesion was only observed at high shear rates, but it has now become evident that vWF contributes to adhesion also at low shear rates, but it is of much less importance, because other adhesive proteins, such as fibronectin, may take over. 31 At high shear rates, the adhesive forces provided by these proteins are no longer sufficient and vWF is required for platelet adhesion.…”

Section: Function Of Vwf In Platelet Adhesionmentioning

confidence: 99%