Studies on fibrin network structure: the effect of some plasma proteins

Abstract

Significant differences were found between characteristics of networks developed in plasma and those developed in pure fibrinogen solution. Networks in plasma have thicker fibres, are more permeable and have lower tensile strength. In this investigation determinants of network structure under physiological conditions of clotting have been examined in an attempt to account for the differences in network structure in plasma and fibrinogen solution. Effect of antithrombin III and of physiological concentrations of fibronectin, albumin and gamma-globulin on fibrin network structure was examined using mass-length ratio (microT) from turbidity, bulk permeability of networks (tau) and kinetics of network development. At physiological concentrations effect of ATIII was too pronounced to allow this method to quantify changes in network characteristics. Whilst fibronectin and gamma-globulins increased fibrin fibre thickness and network permeability, albumin caused opposite effects. It is concluded that the final network structure is determined by kinetics of fibrin fibre growth and is highly responsive to the presence of plasma proteins.