Patterns of Adsorption of Proteins From Human Plasma Onto Foreign Surfaces

Uniyal, S; Brash, John L.

doi:10.1055/s-0038-1657186

Cited by 157 publications

(49 citation statements)

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“…Understanding the mechanism of competitive protein adsorption is therefore of great interest for the development of biocompatible materials. Extensive work, including adsorption experiments in which single protein solutions and solutions of protein mixtures were used (1,2), has been carried out to obtain more insight into this phenomenon. Most investigations have been performed with three plasma proteins: (i) fibrinogen, due to its physiological role in hemostasis, (ii) albumin, due to its abundance in plasma, and (iii) IgG, since it is the most important among the globulins.…”

mentioning

confidence: 99%

Competitive adsorption of human immunoglobulin G and albumin: consequences for structure and reactivity of the adsorbed layer.

Lutanie

Voegel

Schaaf

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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The affinity of polyclonal anti-IgG for human IgG adsorbed on silica surfaces was investigated by two complementary techniques, scanning angle reflectometry and 125I radiotracing. Special attention was paid to compare the reactivity of IgG adsorbed directly or by exchange with already adsorbed albumin. In particular it was shown that (i) in the first case (direct adsorption) the reaction between anti-IgG and adsorbed IgG was in the ratio 1:1 and (it) in the second case (adsorption by exchange) there was no reaction.Most natural systems, essentially biofluids, contain different kinds of proteins mutually competing for adsorption at any exposed surface. Understanding the mechanism of competitive protein adsorption is therefore of great interest for the development of biocompatible materials. Extensive work, including adsorption experiments in which single protein solutions and solutions of protein mixtures were used (1, 2), has been carried out to obtain more insight into this phenomenon. Most investigations have been performed with three plasma proteins: (i) fibrinogen, due to its physiological role in hemostasis, (ii) albumin, due to its abundance in plasma, and (iii) IgG, since it is the most important among the globulins.From competitive adsorption experiments it is usually found that the sorbent surface is initially populated by the smaller and more abundantly occurring molecules, which exhibit a faster rate of diffusion. At later stages, these adsorbed molecules must be displaced by other molecules of higher molecular weight having a stronger tendency to adsorb but with a smaller diffusion coefficient. This phenomenon, which is representative of what has been termed the "Vroman effect," has been demonstrated by Vroman and Adams (3) for fibrinogen. In studies involving fibrinogen, IgG, and albumin at long adsorption times, it is observed that the preference for the adsorbent surface decreases in this order (4, 5). Nevertheless, when comparing the adsorption affinity of proteins ofdifferent sizes, the differences in their electrical charge and conformational stability and in their hydrophobicity or that of the surface must also be taken into account. Indeed, Brash and Uniyal (6) have shown that the exchange sequence (albumin, IgG, fibrinogen, fibronectin, factor XII, high molecular weight kininogen) commonly reported on hydrophilic surfaces like glass (7) does not apply to hydrophobic polystyrene or polyethylene.To our knowledge, no results have been reported on the relationship between competitive adsorption and antigenantibody reactions. Competitive adsorption may, however, have implications for the use of antigen-antibody assays involving the adsorption of protein antigens from blood plasma containing other proteins. In this regard, we studied the reactivity of adsorbed IgG toward anti-IgG (IgY) molecules in three situations: IgG molecules were immobilized either alone or from a binary IgG/albumin mixture on a bare silica surface or were adsorbed from an IgG solution onto an albumin-precoated surfa...

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mentioning

confidence: 99%

Competitive adsorption of human immunoglobulin G and albumin: consequences for structure and reactivity of the adsorbed layer.

Lutanie

Voegel

Schaaf

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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“…Adsorption/desorption experiments were carried out as described previously [15][16][17], In short, the clean films were exposed to protein mixture contain- ing 25 mg% albumin, 15mg% y-globulin and 7.5 mg% fibrinogen with a known amount of the single labeled protein in phosphate buffer (pH 7.4) at 37 °C. (Concentration of labeled albumin in the me dium was 40%, 0.46 pCi/ml and of fibrinogen 7%, 0.51 pCi/ml.)…”

Section: Adsorption Proceduresmentioning

confidence: 99%

“…The films were taken out and were shaken and rinsed in 3 separate beakers filled with approximately 30 ml of phosphate buffer; finally, they were rinsed in flowing buffer. A uniform rinsing procedure was adopted for all samples; this was necessary to achieve an irreduci ble level of surface concentration [15]. The experi ments were repeated in a similar fashion as those of control samples by adding blood cells inside the me dia in the presence and absence of 1.5 mg% vitamin C. The protein concentration inside the media was, compared to a normal blood concentration of cells kept quite low, in order to investigate the bare nature of the adsorption process.…”

Section: Adsorption Proceduresmentioning

confidence: 99%

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Influence of <i>L</i>-Ascorbic Acid, Blood Cells and Components on Protein Adsorption/Desorption on Polycarbonate

Sharma¹,

Chandy²

1987

Pathophysiol Haemos Thromb

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In a previous study we have shown that vitamin C has some effect on the polymer surface by adsorption to it, which would probably affect the protein adsorption and platelet adhesion. The present work has been extended to demonstrate the influence of vitamin C on the kinetics of protein-polymer interaction, using labeled proteins, in the presence and absence of red blood cells, platelets and white blood cells. It appears that vitamin C causes an increase in albumin surface concentration compared to bare substrate which seems to decrease slightly in the presence of blood cells. On the other hand, the infusion of vitamin C to the fibrinogen blood cells system dramatically inhibits the fibrinogen surface binding. The role of L-ascorbic acid to reduce the protein adsorption in the presence of blood cells is discussed by taking into account (a) the interaction of vitamin C with the polymer surface, (b) the interaction of vitamin C with the proteins and cellular membrane, and (c) the interaction of proteins and cells with the polymer itself. The effect of various blood components also seems to be important, and slight differences in the adsorption pattern of proteins are observed in the presence of urea, creatinine, bilirubin, Fe⁺⁺⁺ ion and zinc at normal blood levels.

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“…For example, about 80% of preadsorbed fibrinogen was shown to be lost from a glass surface within 5 minutes of plasma contact. 47 Such preadsorbed proteins are almost certainly replaced by other blood constituents having higher binding affinity. Similar exchange phenomena occur when bare surfaces are contacted with blood.…”

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confidence: 99%

Delivery of passivating proteins to sutures during passage through the vessel wall reduces subsequent platelet deposition by blocking fibrinogen adsorption.

Johnson

Garrett

Brash

et al. 1992

Arterioscler Thromb

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Intraluminal vascular suture material, which attracts fewer than the expected number of platelets compared with the same biomaterial exposed to blood in vitro, differs from the untreated biomaterial in that it has been passed once through the vessel wall. The mechanism by which this apparently trivial maneuver reduces platelet deposition was investigated. Polypropylene suture (7-0 Prolene) was passed through human arteries (fetal and adult), and platelet deposition to the suture was measured in a standardized perfusion chamber. Single vessel passage of the sutures reduced platelet deposition by 68 ±23%, which contrasts sharply with the power of prostaglandin E, (1 (iM PGE, is sufficient to abolish platelet shape change and aggregation), which inhibited only 11% of platelet deposition to the sutures. Aspirin treatment of the vessel (to prevent PGI 2 formation) or endothelial stripping (to remove the ability to produce nitric oxide) had no effect on the degree of inhibition. Passage of the suture through a vessel analogue (expanded polytetrafluoroethylene) did not inhibit platelet deposition. I-fibrinogen adsorption to the suture after vessel passage was reduced to a degree similar to that of platelet deposition. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins eluted from vessel-passed sutures revealed bands at 66, 47, and 16 kd. Western blotting indicated the presence of large amounts of albumin and hemoglobin, a moderate amount of haptoglobin, and only trace amounts of fibrinogen. When sutures were exposed to each of these proteins in vitro before perfusion, albumin and hemoglobin were found to reproduce the effect of vessel passage alone on platelet deposition. We conclude that albumin and hemoglobin adsorb to sutures during their passage through the vessel subendothelium. This reduces the subsequent adsorption of fibrinogen from blood, thereby reducing the ability of platelets to attach to the suture. (Arteriosclerosis and Thrombosis 1992;12:727-735)

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Patterns of Adsorption of Proteins From Human Plasma Onto Foreign Surfaces

Cited by 157 publications

References 18 publications

Competitive adsorption of human immunoglobulin G and albumin: consequences for structure and reactivity of the adsorbed layer.

Competitive adsorption of human immunoglobulin G and albumin: consequences for structure and reactivity of the adsorbed layer.

Influence of <i>L</i>-Ascorbic Acid, Blood Cells and Components on Protein Adsorption/Desorption on Polycarbonate

Delivery of passivating proteins to sutures during passage through the vessel wall reduces subsequent platelet deposition by blocking fibrinogen adsorption.

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