Heparin interaction with protein-adsorbed surfaces

Lynn C. Winterton, Joseph D. Andrade, Jan Feijen, Sung Wan Kim

Research output: Contribution to journalArticleAcademic

36 Citations (Scopus)
34 Downloads (Pure)

Abstract

Albumin and fibrinogen show no binding affinity to varied molecular weights of heparin at physiological pH. Human plasma fibronectin was shown to bind heparins in both the solution and adsorbed states. Fibronectin was shown to have six active binding sites for heparins which may be sterically blocked in some adsorbed states. 125I-Fibronectin monolayer concentrations were shown to be significantly different on polyvinyl chloride surfaces when compared to hydrophilic/hydrophobic silica, Biomer, Silastic, and polystyrene surfaces. Preadsorbing fibronectin to various substrates and then allowing heparins to interact with the protein monolayer made it possible to bind up to 0.2 μg/cm2 heparin in a plasma environment. This fibronectin-heparin complex was at least 85% stable in plasma and buffer solutions for up to 8 h time. The complex was observed to prolong blood clotting times two to three times over that of controls as assayed by Activated Partial Thromboplastin Times. All of the bound heparin was observed to be active by its ability to bind Factor Xa in plasma. Monolayers of blood proteins adsorbed from human serum were not observed to be active in binding heparins. The fibronectin-heparin conjugate showed low activation of blood components compared to protein monolayers preadsorbed from human sera as assayed by Activated Partial Thromboplastin Time.
Original languageUndefined
Pages (from-to)314-342
JournalJournal of colloid and interface science
Volume111
Issue number2
DOIs
Publication statusPublished - 1986

Keywords

  • IR-69675

Cite this

Winterton, Lynn C. ; Andrade, Joseph D. ; Feijen, Jan ; Kim, Sung Wan. / Heparin interaction with protein-adsorbed surfaces. In: Journal of colloid and interface science. 1986 ; Vol. 111, No. 2. pp. 314-342.
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title = "Heparin interaction with protein-adsorbed surfaces",
abstract = "Albumin and fibrinogen show no binding affinity to varied molecular weights of heparin at physiological pH. Human plasma fibronectin was shown to bind heparins in both the solution and adsorbed states. Fibronectin was shown to have six active binding sites for heparins which may be sterically blocked in some adsorbed states. 125I-Fibronectin monolayer concentrations were shown to be significantly different on polyvinyl chloride surfaces when compared to hydrophilic/hydrophobic silica, Biomer, Silastic, and polystyrene surfaces. Preadsorbing fibronectin to various substrates and then allowing heparins to interact with the protein monolayer made it possible to bind up to 0.2 μg/cm2 heparin in a plasma environment. This fibronectin-heparin complex was at least 85{\%} stable in plasma and buffer solutions for up to 8 h time. The complex was observed to prolong blood clotting times two to three times over that of controls as assayed by Activated Partial Thromboplastin Times. All of the bound heparin was observed to be active by its ability to bind Factor Xa in plasma. Monolayers of blood proteins adsorbed from human serum were not observed to be active in binding heparins. The fibronectin-heparin conjugate showed low activation of blood components compared to protein monolayers preadsorbed from human sera as assayed by Activated Partial Thromboplastin Time.",
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Heparin interaction with protein-adsorbed surfaces. / Winterton, Lynn C.; Andrade, Joseph D.; Feijen, Jan; Kim, Sung Wan.

In: Journal of colloid and interface science, Vol. 111, No. 2, 1986, p. 314-342.

Research output: Contribution to journalArticleAcademic

TY - JOUR

T1 - Heparin interaction with protein-adsorbed surfaces

AU - Winterton, Lynn C.

AU - Andrade, Joseph D.

AU - Feijen, Jan

AU - Kim, Sung Wan

PY - 1986

Y1 - 1986

N2 - Albumin and fibrinogen show no binding affinity to varied molecular weights of heparin at physiological pH. Human plasma fibronectin was shown to bind heparins in both the solution and adsorbed states. Fibronectin was shown to have six active binding sites for heparins which may be sterically blocked in some adsorbed states. 125I-Fibronectin monolayer concentrations were shown to be significantly different on polyvinyl chloride surfaces when compared to hydrophilic/hydrophobic silica, Biomer, Silastic, and polystyrene surfaces. Preadsorbing fibronectin to various substrates and then allowing heparins to interact with the protein monolayer made it possible to bind up to 0.2 μg/cm2 heparin in a plasma environment. This fibronectin-heparin complex was at least 85% stable in plasma and buffer solutions for up to 8 h time. The complex was observed to prolong blood clotting times two to three times over that of controls as assayed by Activated Partial Thromboplastin Times. All of the bound heparin was observed to be active by its ability to bind Factor Xa in plasma. Monolayers of blood proteins adsorbed from human serum were not observed to be active in binding heparins. The fibronectin-heparin conjugate showed low activation of blood components compared to protein monolayers preadsorbed from human sera as assayed by Activated Partial Thromboplastin Time.

AB - Albumin and fibrinogen show no binding affinity to varied molecular weights of heparin at physiological pH. Human plasma fibronectin was shown to bind heparins in both the solution and adsorbed states. Fibronectin was shown to have six active binding sites for heparins which may be sterically blocked in some adsorbed states. 125I-Fibronectin monolayer concentrations were shown to be significantly different on polyvinyl chloride surfaces when compared to hydrophilic/hydrophobic silica, Biomer, Silastic, and polystyrene surfaces. Preadsorbing fibronectin to various substrates and then allowing heparins to interact with the protein monolayer made it possible to bind up to 0.2 μg/cm2 heparin in a plasma environment. This fibronectin-heparin complex was at least 85% stable in plasma and buffer solutions for up to 8 h time. The complex was observed to prolong blood clotting times two to three times over that of controls as assayed by Activated Partial Thromboplastin Times. All of the bound heparin was observed to be active by its ability to bind Factor Xa in plasma. Monolayers of blood proteins adsorbed from human serum were not observed to be active in binding heparins. The fibronectin-heparin conjugate showed low activation of blood components compared to protein monolayers preadsorbed from human sera as assayed by Activated Partial Thromboplastin Time.

KW - IR-69675

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DO - 10.1016/0021-9797(86)90038-X

M3 - Article

VL - 111

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JO - Journal of colloid and interface science

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