title: Quality assessment of heparin coatings by their binding capacities of coagulation and complement enzymes.
abstract: In vitro testing of blood contacting materials before clinical application is generally advisable. Four heparin coatings from different manufacturers were tested for adsorbed proteins and soluble activation markers. The surface with the highest antithrombin, thrombin, high-molecular-weight-kininogen (HMWK) and the lowest fibrinogen binding capacity (Carmeda, Medtronic) showed significantly lower levels of granulocytes and platelet activation (beta-TG, PMN-elastase release). No statistically significant differences in soluble markers of the coagulation system could be detected (F1 + 2, TAT). Interestingly, complement activation (TCC) was significantly reduced within the group of the lowest adsorption of the complement factor C3. Our data demonstrate that there is a relation between the binding affinity of proteins (C1-inhibitor, C3-complement) and the consecutive changes in complement activation (TCC). Therefore, measuring adsorbed proteins on artificial surfaces is a suitable, sensitive and very reproducible method for assessing the thrombogenicity of biomaterials.
authors.affiliation: Department of Surgery, Eberhard-Karls-University, Tuebingen, Germany.
authors.forename: N
authors.initials: N
authors.lastname: Weber
authors.forename: H P
authors.initials: HP
authors.lastname: Wendel
authors.forename: G
authors.initials: G
authors.lastname: Ziemer
mesh_terms: D000327:Adsorption; D000925:Anticoagulants / Q000737:chemistry*; D000990:Antithrombin III / Q000737:chemistry; D000991:Antithrombins / Q000737:chemistry; D001779:Blood Coagulation Factors / Q000737:chemistry*; D020099:Coated Materials, Biocompatible / Q000737:chemistry*; D003167:Complement Activation; D003174:Complement C1 Inactivator Proteins / Q000737:chemistry; D003176:Complement C3 / Q000737:chemistry; D003165:Complement System Proteins / Q000737:chemistry*; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry; D005340:Fibrinogen / Q000737:chemistry; D006098:Granulocytes / Q000473:pathology; D006493:Heparin / Q000737:chemistry*; D006801:Humans; D007704:Kininogens / Q000737:chemistry; D019272:Leukocyte Elastase / Q000737:chemistry; D008422:Materials Testing; D010446:Peptide Fragments / Q000737:chemistry; D010447:Peptide Hydrolases / Q000737:chemistry; D015539:Platelet Activation; D011485:Protein Binding; D011516:Prothrombin / Q000737:chemistry; D012680:Sensitivity and Specificity; D012995:Solubility; D018709:Statistics, Nonparametric; D013917:Thrombin / Q000737:chemistry; D013927:Thrombosis / Q000097:blood; D001620:beta-Thromboglobulin / Q000737:chemistry
chemical_list: D000925:Anticoagulants; D000991:Antithrombins; D001779:Blood Coagulation Factors; D020099:Coated Materials, Biocompatible; D003174:Complement C1 Inactivator Proteins; D003176:Complement C3; D015853:Cysteine Proteinase Inhibitors; D007704:Kininogens; D010446:Peptide Fragments; C046193:antithrombin III-protease complex; D001620:beta-Thromboglobulin; C045879:prothrombin fragment 1.2; D000990:Antithrombin III; D011516:Prothrombin; D005340:Fibrinogen; D006493:Heparin; D003165:Complement System Proteins; D010447:Peptide Hydrolases; D019272:Leukocyte Elastase; D013917:Thrombin