Interaction of antithrombin III with preadsorbed albumin-heparin conjugates

Hennink, Wim E.; Ebert, C. D.; Kim, S.W.; Breemhaar, W.; Bantjes, A.; Feijén, Jan

doi:10.1016/0142-9612(84)90070-x

Cited by 17 publications

(6 citation statements)

References 19 publications

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“…This is in contrast to the findings by Hennink et al. (19) recording AT3 adsorption to preadsorbed polystyrene surfaces—using a different method, that is, a two‐stage enzyme immunoassay.…”

Section: Discussioncontrasting

confidence: 99%

Plasma Protein Binding Properties to Immobilized Heparin and Heparin–Albumin Conjugate

et al. 2007

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Selective adhesion of plasma proteins to immobilized heparin is considered to be beneficial regarding hemocompatibility of foreign materials in contact with blood. Prothrombin, thrombin, antithrombin III (AT3), and fibrinogen were selected for analysis in an experimental model. Biomolecular interaction analysis employing surface plasmon resonance was utilized to record and analyze their binding properties in real time. Biotinylated heparin, heparin-albumin conjugate, and albumin, respectively, were immobilized onto streptavidin-coated sensors as ligands. Prothrombin did not bind to any of the ligand surfaces and no specific binding of any of the plasma proteins to albumin was observed. Binding kinetics of thrombin to heparin and to heparin-albumin conjugate were calculated using two different methods. For heparin, identical K(D)(equilibrium dissociation constant) values of 61 x 10(-9) M were obtained with both methods. For the conjugate, only slightly different K(D) values of 111 x 10(-9) and 104 x 10(-9) M, respectively, were calculated. The affinity of thrombin toward the heparin-coated surface proved to be higher than its affinity toward the heparin conjugate. The binding pattern of AT3 to both heparin and heparin-albumin conjugate, although specific, was biphasic, possibly due to a conformational change during the binding process. Steady-state kinetic analysis revealed a K(D) value of 281 +/- 24 x 10(-9) M for the heparin surface. For the conjugate surface, a K(D) of 53 +/- 5 x 10(-9) M was calculated, indicating a higher affinity toward heparin-albumin conjugate. A high-affinity binding of fibrinogen to high-density surfaces of both heparin and the conjugate was observed. However, as binding to low-density surfaces was considerably reduced, specificity remained uncertain.

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Section: Discussioncontrasting

confidence: 99%

Plasma Protein Binding Properties to Immobilized Heparin and Heparin–Albumin Conjugate

et al. 2007

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“…This is probably due to preferential adsorption, or perhaps preferential binding of AT III onto the PS matrix of the PSsE 2 coated surfaces. As was already reported by Hennink et al [23], a significant adsorption of AT III from PBS solution onto polystyrene was observed. When plasma or plasma dilutions were used as a source of AT III, no adsorption was detected.…”

Section: Adsorption Of At III Onto Heparin-containing Surfacessupporting

confidence: 71%

“…1 it appears that there are no significant differences in the adsorption of AT III from PBS solutions containing different concentrations of AT III (1 IUm1-1 and 0.067 IUm1-1) onto glass and PDMS coated with PSsE ~ and PSsE2H 1 and hydrated surfaces, after 1 h contact time at ambient temperature. Studies by Hennink et al [23] demonstrated that immobilized heparin was able to bind AT III. This binding was dependent on the type of heparin (low and high affinity for AT III) used.…”

Section: Adsorption Of At III Onto Heparin-containing Surfacesmentioning

confidence: 99%

“…The adsorption of AT III, either from PBS (0.9% NaCI, 10raM Na2HPO4 adjusted to pH 7.4) solutions or from plasma (Bloodbank Twente and Aehterhoek, Enschede, Holland, containing 0.15 g AT III 1-1, as determined spectrophotometrically at 280 nm using an extinction coefficient [21] ~1%280n m = 6.10), for 1 h, onto the coated plates as well as onto hydrated coated plates was determined by means of specially constructed 24 well chamber in which each test surface area is 1 cm 2. Experimental details of the two-step ELISA have been given in the literature [22][23][24]. In order to detect AT III (human AT III, KabiVitrum) adsorbed onto the test surfaces, these surfaces were exposed to rabbit serum directed against human AT III (KH53P, Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam, Holland).…”

Section: Adsorption Of At III Onto Heparin-containing Surfacesmentioning

confidence: 99%

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Heparin-containing block copolymers

Vulić

Okano²,

Gaag

et al. 1993

J Mater Sci: Mater Med

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Newly synthesized heparin-containing block copolymers, consisting of a hydrophobic block of polystyrene (PS), a hydrophilic spacer-block of poly(ethylene oxide) (PEO) and covalently bonded heparin (Hep) as bioactive block, were coated either onto glass, poly (dimethylsiioxane), polyurethane or PS substrates. Coated surfaces were characterized by determination of the surface-bound heparin activity, adsorption of AT III, plasma recalcification time assays, adhesion of platelets and by an ex vivo rabbit A-A shunt model.It was demonstrated that heparin was available at the surface of all heparin-bound surfaces to interact with AT III and thrombin and to prevent the formation of clots. The maximum immobilized heparin activity was found to be 5.5 x 10 -3 U cm -2. Coated surfaces showed a significant prolongation of the plasma reclacification times as compared to control surfaces, due to surface-immobilized heparin. The platelet adhesion demonstrated that platelets reacted only minimally with the heparin-containing block copolymers in the test system and that the heparin-containing block copolymers seemed to passify the surface as compared to control surfaces. In the ex vivo A-A shunt experiments, which were carried out under low flow and low shear conditions, the heparin-containing block copolymers exhibited prolonged occlusion times, indicating the ability of the heparin-containing block copolymers to reduce thrombus formation at the surface.

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“…In this case, the heterogenicity of heparin must be taken into consideration. The high adsorption values were measured on high affinity albumin-heparin conjugate pretreated surfaces [94]. Less ATIII adsorption was found on nonfractionated albumin-heparin conjugate preadsorbed surfaces.…”

Section: Interaction Of Heparinized Polymer With Coagulation Factors mentioning

confidence: 99%

Antithrombogenic Heparin-Bound Polyurethanes

Ito

1987

J Biomater Appl

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Many kinds of heparin-bound polyurethanes have been developed. Polyurethanes are a family of elastomers displaying better blood-compatibility than other polymeric materials. It is useful to modify this material by heparinization. Several approaches to heparinization have been devised: 1) a general method of heparinization, applicable to all polymeric materials, 2) a heparinization method specific to polyurethanes, and 3) the design of heparinizable polyurethane derivatives. These three approaches are first explained in detail. Then, the antithrombogenic mechanism of the heparinized polymers is discussed. Finally, the interactions of the heparinized polymers with blood coagulation factors, plasma proteins, and platelets are discussed.

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Interaction of antithrombin III with preadsorbed albumin-heparin conjugates

Cited by 17 publications

References 19 publications

Plasma Protein Binding Properties to Immobilized Heparin and Heparin–Albumin Conjugate

Plasma Protein Binding Properties to Immobilized Heparin and Heparin–Albumin Conjugate

Heparin-containing block copolymers

Antithrombogenic Heparin-Bound Polyurethanes

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