Thrombin flux and wall shear rate regulate fibrin fiber deposition state during polymerization under flow

Biophys J. 2010 Apr 7;98(7):1344-52. doi: 10.1016/j.bpj.2009.12.4275.

Abstract

Thrombin is released as a soluble enzyme from the surface of platelets and tissue-factor-bearing cells to trigger fibrin polymerization during thrombosis under flow conditions. Although isotropic fibrin polymerization under static conditions involves protofibril extension and lateral aggregation leading to a gel, factors regulating fiber growth are poorly quantified under hemodynamic flow due to the difficulty of setting thrombin fluxes. A membrane microfluidic device allowed combined control of both thrombin wall flux (10(-13) to 10(-11) nmol/mum(2) s) and the wall shear rate (10-100 s(-1)) of a flowing fibrinogen solution. At a thrombin flux of 10(-12) nmol/mum(2) s, both fibrin deposition and fiber thickness decreased as the wall shear rate increased from 10 to 100 s(-1). Direct measurement and transport-reaction simulations at 12 different thrombin flux-wall shear rate conditions demonstrated that two dimensionless numbers, the Peclet number (Pe) and the Damkohler number (Da), defined a state diagram to predict fibrin morphology. For Da < 10, we only observed thin films at all Pe. For 10 < Da < 900, we observed either mat fibers or gels, depending on the Pe. For Da > 900 and Pe < 100, we observed three-dimensional gels. These results indicate that increases in wall shear rate quench first lateral aggregation and then protofibril extension.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biophysics / methods*
  • Blood Platelets / metabolism
  • Cell Membrane / metabolism
  • Computer Simulation
  • Fibrin / chemistry*
  • Fibrinogen / chemistry*
  • Gels
  • Humans
  • Microfluidics
  • Microscopy, Electron, Scanning / methods
  • Polymers / chemistry*
  • Stress, Mechanical
  • Thrombin / chemistry*
  • Thrombosis / pathology

Substances

  • Gels
  • Polymers
  • Fibrin
  • Fibrinogen
  • Thrombin