Surface Modification of CoCr Alloy Using Varying Concentrations of Phosphoric and Phosphonoacetic Acids: Albumin and Fibrinogen Adsorption, Platelet Adhesion, Activation, and Aggregation Studies

Langmuir ◽  
2014 ◽  
Vol 31 (1) ◽  
pp. 358-370 ◽  
Author(s):  
Eagappanath Thiruppathi ◽  
Mark K. Larson ◽  
Gopinath Mani
2011 ◽  
Vol 12 (12) ◽  
pp. 4348-4356 ◽  
Author(s):  
Wei-Hsuan Kuo ◽  
Meng-Jiy Wang ◽  
Hsiu-Wen Chien ◽  
Ta-Chin Wei ◽  
Chiapyng Lee ◽  
...  

1991 ◽  
Vol 65 (05) ◽  
pp. 608-617 ◽  
Author(s):  
Joseph A Chinn ◽  
Thomas A Horbett ◽  
Buddy D Ratner

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.


2008 ◽  
Vol 61 (6) ◽  
pp. 446 ◽  
Author(s):  
Ai-Fu Che ◽  
Xiao-Jun Huang ◽  
Zhen-Gang Wang ◽  
Zhi-Kang Xu

Poly(acrylonitrile-co-acrylic acid) (PANCAA) was synthesized and fabricated into nanofibrous membranes by an electrospinning technique. Scanning electron microscopy revealed that membranes composed of uniformly thin and smooth nanofibres were obtained under optimized processing parameters. Surface modification with chitosan on these nanofibrous membranes was accomplished by a coupling reaction between the carboxylic groups of PANCAA and the primary amino groups of chitosan. Fluorescent labelling, weight measurement, FT-IR/ATR spectroscopy, and X-ray photoelectron spectroscopy (XPS) were used to confirm the modification process and determine the immobilization degree of chitosan. Platelet adhesion experiments were further carried out to evaluate the hemocompatibility of the studied nanofibrous membranes. Preliminary results indicated that the immobilization of chitosan on the PANCAA nanofibrous membranes was favourable for platelet adhesion.


Blood ◽  
1986 ◽  
Vol 68 (2) ◽  
pp. 355-362 ◽  
Author(s):  
JN Lindon ◽  
G McManama ◽  
L Kushner ◽  
EW Merrill ◽  
EW Salzman

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.


2014 ◽  
Vol 9 (4) ◽  
pp. 041002 ◽  
Author(s):  
Megan S. Lord ◽  
John M. Whitelock ◽  
Anne Simmons ◽  
Rachel L. Williams ◽  
Bruce K. Milthorpe

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