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Comparison of structure, strength and cytocompatibility of a fibrin matrix supplemented either with tranexamic acid or aprotinin
Author(s) -
Furst Walter,
Banerjee Asmita,
Redl Heinz
Publication year - 2007
Publication title -
journal of biomedical materials research part b: applied biomaterials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.665
H-Index - 108
eISSN - 1552-4981
pISSN - 1552-4973
DOI - 10.1002/jbm.b.30711
Subject(s) - fibrin , aprotinin , fibrinolysis , fibrin tissue adhesive , ultimate tensile strength , fibrin glue , tranexamic acid , plasmin , chemistry , biomedical engineering , materials science , pharmacology , surgery , medicine , biochemistry , composite material , immunology , blood loss , enzyme
Fibrin sealants are used as hemostats, sealants, tissue adhesives, and as matrix for substances/cells in a number of surgical and tissue engineering procedures. Main characteristics of fibrin are high tensile strength, adhesive strength, biocompatibility, and resorption. A major adverse event would be premature fibrin lysis and recurrent bleeding. This must be prevented by fibrinolysis inhibitors. The most common fibrinolysis inhibitors used are aprotinin and tranexamic acid (t‐AMCA). Comparison of commercially available fibrin sealants utilizing aprotinin or t‐AMCA revealed a lower sealing efficacy in an in vivo lung resection model for a t‐AMCA containing product. Therefore, we compared the influence of t‐AMCA and aprotinin on structure, mechanical properties, and cytocompatibility of a fibrin matrix. In our experiments, we found that substitution of aprotinin with t‐AMCA reduced the tensile strength and formation of fibrin fibers and affected viability of a fibroblast cell‐line. In conclusion, t‐AMCA negatively affects physical and biological properties of fibrin relevant for clinical application as well as tissue regeneration. © 2006 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater 2006