Fibrinogen adsorption and platelet adhesion to polymeric materials

1991 ◽  
Vol 19 (2) ◽  
pp. 231-232
Author(s):  
Joseph A. Chinn ◽  
Thomas A. Horbett
Keyword(s):  
Platelet Adhesion ◽  
Polymeric Materials ◽  
Fibrinogen Adsorption

Baboon Fibrinogen Adsorption and Platelet Adhesion to Polymeric Materials

1991 ◽  
Vol 65 (05) ◽  
pp. 608-617 ◽  
Author(s):  
Joseph A Chinn ◽  
Thomas A Horbett ◽  
Buddy D Ratner
Keyword(s):  
Platelet Adhesion ◽  
Coagulation Factor ◽  
Polymeric Materials ◽  
Platelet Suspension ◽  
Perfusion Chamber ◽  
Static Conditions ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Fibrinogen Adsorption

SummaryThe role of fibrinogen in mediating platelet adhesion to polymers exposed to blood plasma was studied by comparison of the effect of plasma dilution on fibrinogen adsorption and platelet adhesion, and by the use of coagulation factor deficient plasmas. Polyetherurethane substrates were first preadsorbed with dilute plasma, then contacted with washed platelets suspended in a modified, apyrase containing Tyrode’s buffer. Platelet adhesion was studied under static conditions in Multiwell dishes, and also under shearing conditions using a parallel plate perfusion chamber. Fibrinogen adsorption and platelet adhesion were measured using 125I radiolabeled baboon fibrinogen and min radiolabeled baboon platelets, respectively. Surfaces were characterized by electron spectroscopy for chemical analysis (ESCA).When fibrinogen adsorption to Biomer was measured after 2 h contact with a series of dilute plasma solutions under static conditions, a peak in adsorption was observed from 0.26% plasma, i.e., adsorption was greater from 0.26% plasma than from either more or less dilute plasma. A peak in subsequent platelet adhesion to the plasma preadsorbed surfaces, measured after 2 h static incubation with washed platelets, was also observed but occurred on Biomer preadsorbed with 1.0% plasma.When fibrinogen adsorption was measured after 5 min contact under shearing conditions, the fibrinogen adsorption peak occurred on surfaces that had been exposed to 1.0% plasma. A peak in platelet adhesion to these preadsorbed surfaces, measured after 5 min contact with the platelet suspensions under shearing conditions, was observed on Biomer preadsorbed with 0.1% plasma. Shifts between the positions of the peaks in protein adsorption and platelet adhesion occurred on other polymers tested as well.Platelet adhesion was almost completely inhibited when baboon and human plasmas lacking fibrinogen (i. e., serum, heat defibrinogenated plasma, and congenitally afibrinogénémie plasma) were used. Platelet adhesion was restored to near normal when exogenous fibrinogen was added to fibrinogen deficient plasmas. Adhesion was also inhibited completely when a monoclonal antibody directed against the glycoprotein IIb/IIIa complex was added to the platelet suspension. Platelet adhesion to surfaces preadsorbed to von Willebrand factor deficient plasma was the same as to surfaces preadsorbed with normal plasma.While it appears that surface bound fibrinogen does mediate the initial attachment of platelets to Biomer, the observation that the fibrinogen adsorption and platelet adhesion maxima do not coincide exactly also suggests that the degree of subsequent platelet adhesion is dictated not only by the amount of surface bound fibrinogen but also by its conformation.

scholarly journals Does the conformation of adsorbed fibrinogen dictate platelet interactions with artificial surfaces?

Blood ◽  
1986 ◽  
Vol 68 (2) ◽  
pp. 355-362 ◽  
Author(s):  
JN Lindon ◽  
G McManama ◽  
L Kushner ◽  
EW Merrill ◽  
EW Salzman
Keyword(s):  
Platelet Adhesion ◽  
Surface Coverage ◽  
Platelet Reactivity ◽  
Polymer Surfaces ◽  
Side Chain ◽  
Alkyl Side Chain ◽  
Fibrinogen Binding ◽  
Artificial Surfaces ◽  
Antibody Preparations ◽  
Fibrinogen Adsorption

Abstract Platelet activation by polymer surfaces is thought to require preliminary adsorption of fibrinogen and perhaps changes in fibrinogen conformation. We measured fibrinogen adsorption by a series of polymers by two methods, using either 125I-labeled fibrinogen or 125I-labeled antifibrinogen antibodies, and correlated the results with platelet reactivity (retention and secretion) in columns of beads coated with the polymers. For polyalkyl methacrylates with 1 to 4 carbon side chains, platelet reactivity varied directly with increasing length of the alkyl side chain and with the quantity of bound fibrinogen recognizable by antifibrinogen antibody but not with the total quantity of fibrinogen adsorbed. The same pattern of results was seen with five antibody preparations, including affinity-purified Fab fragments against the D or E domain of fibrinogen. Tests of platelet retention and fibrinogen binding to four polyalkyl acrylates and to three unrelated polymers (polystyrene, polymethyl methacrylate, and a polyether polyurethane) indicated that platelet retention correlated positively with both total fibrinogen binding and with the amount of antibody-recognizable fibrinogen bound. Drugs that block platelet aggregation, but not adhesion, did not alter the hierarchy of platelet retention to the polyalkyl methacrylates. These data suggest that, contrary to previous views, platelet adhesion to artificial surfaces increases with increasing surface coverage of adsorbed fibrinogen if the bound fibrinogen maintains a conformation such that its functional domains remain recognizable by antibody probes.

Surface Modification with Poly(sulfobetaine methacrylate-co-acrylic acid) To Reduce Fibrinogen Adsorption, Platelet Adhesion, and Plasma Coagulation

2011 ◽  
Vol 12 (12) ◽  
pp. 4348-4356 ◽  
Author(s):  
Wei-Hsuan Kuo ◽  
Meng-Jiy Wang ◽  
Hsiu-Wen Chien ◽  
Ta-Chin Wei ◽  
Chiapyng Lee ◽  
...  
Keyword(s):  
Surface Modification ◽  
Acrylic Acid ◽  
Platelet Adhesion ◽  
Plasma Coagulation ◽  
Fibrinogen Adsorption

scholarly journals Fibrinogen adsorption and platelet adhesion to silica surfaces with stochastic nanotopography

2014 ◽  
Vol 9 (4) ◽  
pp. 041002 ◽  
Author(s):  
Megan S. Lord ◽  
John M. Whitelock ◽  
Anne Simmons ◽  
Rachel L. Williams ◽  
Bruce K. Milthorpe
Keyword(s):  
Platelet Adhesion ◽  
Silica Surfaces ◽  
Fibrinogen Adsorption

scholarly journals Does the conformation of adsorbed fibrinogen dictate platelet interactions with artificial surfaces?

Blood ◽  
1986 ◽  
Vol 68 (2) ◽  
pp. 355-362 ◽  
Author(s):  
JN Lindon ◽  
G McManama ◽  
L Kushner ◽  
EW Merrill ◽  
EW Salzman
Keyword(s):  
Platelet Adhesion ◽  
Surface Coverage ◽  
Platelet Reactivity ◽  
Polymer Surfaces ◽  
Side Chain ◽  
Alkyl Side Chain ◽  
Fibrinogen Binding ◽  
Artificial Surfaces ◽  
Antibody Preparations ◽  
Fibrinogen Adsorption

Platelet activation by polymer surfaces is thought to require preliminary adsorption of fibrinogen and perhaps changes in fibrinogen conformation. We measured fibrinogen adsorption by a series of polymers by two methods, using either 125I-labeled fibrinogen or 125I-labeled antifibrinogen antibodies, and correlated the results with platelet reactivity (retention and secretion) in columns of beads coated with the polymers. For polyalkyl methacrylates with 1 to 4 carbon side chains, platelet reactivity varied directly with increasing length of the alkyl side chain and with the quantity of bound fibrinogen recognizable by antifibrinogen antibody but not with the total quantity of fibrinogen adsorbed. The same pattern of results was seen with five antibody preparations, including affinity-purified Fab fragments against the D or E domain of fibrinogen. Tests of platelet retention and fibrinogen binding to four polyalkyl acrylates and to three unrelated polymers (polystyrene, polymethyl methacrylate, and a polyether polyurethane) indicated that platelet retention correlated positively with both total fibrinogen binding and with the amount of antibody-recognizable fibrinogen bound. Drugs that block platelet aggregation, but not adhesion, did not alter the hierarchy of platelet retention to the polyalkyl methacrylates. These data suggest that, contrary to previous views, platelet adhesion to artificial surfaces increases with increasing surface coverage of adsorbed fibrinogen if the bound fibrinogen maintains a conformation such that its functional domains remain recognizable by antibody probes.

Fibrinogen adsorption and platelet adhesion at the surface of modified polypropylene glycol/polysiloxane networks

Biomaterials ◽  
1986 ◽  
Vol 7 (5) ◽  
pp. 379-385 ◽  
Author(s):  
R.W. Pekala ◽  
E.W. Merrill ◽  
J. Lindon ◽  
L. Kushner ◽  
E.W. Salzman
Keyword(s):  
Platelet Adhesion ◽  
Polypropylene Glycol ◽  
Fibrinogen Adsorption

Fibrinogen Adsorption, Platelet Adhesion and Thrombin Generation at Heparinized Surfaces Exposed to Flowing Blood

2002 ◽  
Vol 87 (04) ◽  
pp. 742-747 ◽  
Author(s):  
George Willems ◽  
Marco Morra ◽  
Jeffrey Keuren ◽  
Simone Wielders ◽  
Theo Lindhout
Keyword(s):  
Protein Adsorption ◽  
Whole Blood ◽  
Thrombin Generation ◽  
Platelet Adhesion ◽  
Platelet Rich Plasma ◽  
Thrombus Formation ◽  
Adhesion Assay ◽  
Flowing Blood ◽  
Fibrinogen Adsorption

SummaryThrombus formation at an artificial surface in contact with blood is a complex process that encompasses accretion of platelets from flowing blood and fibrin deposition. Platelet adhesion and fibrin formation are intimately intertwined reactions that are triggered by different sets of surface adsorbed plasma proteins. To dissect the contribution of protein adsorption and platelet adhesion to thrombin formation, a coherent study was performed with non-coated (NC) and heparin-coated (HC) surfaces. Thrombin production in whole blood, platelet adhesion and protein adsorption were studied using an amidolytic thrombin assay, a dynamic platelet adhesion assay and ellipsometry, respectively. Thrombin generation in flowing whole blood exposed to HC surfaces was greatly diminished when compared with NC surfaces. However, separate platelet adhesion and protein adsorption studies with anticoagulated whole blood revealed that platelets do not adhere because fibrinogen is not available in the protein layer that was deposited during the perfusion. These findings indicate that the in vitro thrombogenicity of a material cannot be predicted from platelet adhesion and protein adsorption data when these measurements are performed with anticoagulated blood or platelet rich plasma. Preincubation of NC and HC surfaces with fibrinogen or 2000-fold diluted plasma resulted in similar amounts of surface-bound fibrinogen and mediated massive platelet adhesion from flowing whole blood. These results indicate that a) platelet adhesion correlates with the availability of surface-bound fibrinogen and b) NC and HC surfaces are indistinguishable with respect to protein (fibrinogen) adsorption and platelet adhesion. It is apparent that the heparinized surface used in our studies exerts its anti-thrombogenic properties by neutralizing locally formed thrombin and not by reducing fibrinogen-dependent platelet adhesion.

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