SPECIAL ARTICLE ON BIOCOLLOIDS AND BIOSURFACES: FIBRINOGEN ADSORPTION ON ARTIFICIAL SURFACES AND ITS EFFECTS ON PLATELETS

1993 ◽  
Vol 14 (1) ◽  
pp. 117-128 ◽  
Author(s):  
H. Sato ◽  
J. Kojima ◽  
A. Nakajima
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.


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

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.


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.


2018 ◽  
pp. 14-23
Author(s):  
А. Богоявленский ◽  
A. Bogoyavlenskiy

One of the most important characteristics of the runways with artificial turf of civil airfields is their evenness. Passengers of the mainline aircraft – both in domestic and foreign airportssubjectively assess the airfield pavements evenness by the presence or absence of shaking during the movement of the aircraft on the runway both during takeoff and landing. In units of what physical quantities, by what means and methods is measured (estimated) the evenness of aerodrome surfaces? How to ensure of the traceability of measurements from the primary national etalon of parameter to the value of the measured value. About it-this publication.


1992 ◽  
Vol 42 (1) ◽  
pp. 87-92 ◽  
Author(s):  
F. Boumaza ◽  
Ph. Déjardin ◽  
F. Yan ◽  
F. Bauduin ◽  
Y. Holl

2012 ◽  
Vol 1376 ◽  
Author(s):  
P. Silva-Bermudez ◽  
S. Muhl ◽  
M. Rivera ◽  
S. E. Rodil

ABSTRACTIn the present work, the adsorption of albumin and fibrinogen on Ta, Nb, Ti and Zr oxidesthin films deposited on Si (100) wafers by magnetron sputtering was studied in order to get a better understanding of the correlation among the surface properties of these oxides and the protein adsorption phenomena on their surfaces. The surface energy, hydrophobicity, chemical composition, roughness and atomic order of the films were characterized. The films were immersedfor 45 minutes in single protein solutions; either albumin or fibrinogenand the adsorbed protein layer on the films was studied ex-situ in a dry ambient using bothX-ray photoelectron spectroscopy and atomic force microscopy.The adsorption of albumin and fibrinogen on the films modified the surface morphology and decreased the surface roughness for all the four different metal oxides. The XPS results confirmed the presence of the protein on the surface of the films and showed that the two proteins studied were adsorbed without undergoing a major chemical decomposition. A correlation between the surface roughness,the polar component of the surface energy of the films and the atomic percentage of nitrogen on the films after protein adsorption, an indirect signal of the amount of protein adsorbed, was found for albumin and fibrinogen adsorption on Ta, Nb and Ti oxides; the largest the roughness or the polar component the largest amount of adsorbed protein.


2010 ◽  
Vol 81 (2) ◽  
pp. 607-613 ◽  
Author(s):  
V. Deshmukh ◽  
D.W. Britt ◽  
V. Hlady

2011 ◽  
Vol 3 (4) ◽  
pp. 1254-1260 ◽  
Author(s):  
Long Yin ◽  
Lin Zhu ◽  
Qingjun Wang ◽  
Jianfu Ding ◽  
Qingmin Chen
Keyword(s):  

1984 ◽  
Vol 18 (6) ◽  
pp. 695-705 ◽  
Author(s):  
Hanson Y. K. Chuang ◽  
Sankar P. Mitra
Keyword(s):  

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