Fibrin chain cross-linking, fibrinolysis, and in vivo sealing efficacy of differently structured fibrin sealants

J Biomed Mater Res B Appl Biomater. 2012 Aug;100(6):1507-12. doi: 10.1002/jbm.b.32719. Epub 2012 Jun 12.

Abstract

In this study, we compared the sealing characteristics and efficacy of a fibrin sealant with reduced plasminogen (FS-rplg) and a fibrin sealant with aprotinin as a fibrinolysis inhibitor (FS-apr). The relevant sealing characteristics including clot structure, fibrin chain cross-linking, and clot lysis were tested in the laboratory. The sealing efficacy was then investigated in a follow-up animal model to determine differences in the in vivo sealing properties. A total of 46 animals were available for the final analysis with 23 animals in each treatment arm. In conclusion, we saw differences in vitro between FS-rplg and FS-apr in ultrastructure and α-chain cross-linking rates as well as in the rate of fibrinolysis. These differences may explain the significantly enhanced sealing efficacy in FS-apr compared to FS-rplg shown in vivo in a rabbit intestinal model.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aprotinin / pharmacokinetics
  • Aprotinin / pharmacology*
  • Fibrin / pharmacokinetics
  • Fibrin / pharmacology*
  • Fibrin Tissue Adhesive / pharmacokinetics
  • Fibrin Tissue Adhesive / pharmacology*
  • Fibrinolysis / drug effects*
  • Fibrinolytic Agents / pharmacokinetics
  • Fibrinolytic Agents / pharmacology*
  • Materials Testing*
  • Plasminogen / pharmacokinetics
  • Plasminogen / pharmacology*
  • Rabbits
  • Serine Proteinase Inhibitors / pharmacokinetics
  • Serine Proteinase Inhibitors / pharmacology*
  • Tissue Adhesives / pharmacokinetics
  • Tissue Adhesives / pharmacology*

Substances

  • Fibrin Tissue Adhesive
  • Fibrinolytic Agents
  • Serine Proteinase Inhibitors
  • Tissue Adhesives
  • Fibrin
  • Plasminogen
  • Aprotinin