Laminin promotes coagulation and thrombus formation in a factor XII-dependent manner

J Thromb Haemost. 2010 Jun;8(6):1295-301. doi: 10.1111/j.1538-7836.2010.03850.x.

Abstract

Background: Laminin is the most abundant non-collagenous protein in the basement membrane. Recent studies have shown that laminin supports platelet adhesion, activation and aggregation under flow conditions, highlighting a possible role for laminin in hemostasis.

Objective: To investigate the ability of laminin to promote coagulation and support thrombus formation under shear.

Results and methods: Soluble laminin accelerated factor (F) XII activation in a purified system, and shortened the clotting time of recalcified plasma in a FXI- and FXII-dependent manner. Laminin promoted phosphatidylserine exposure on platelets and supported platelet adhesion and fibrin formation in recalcified blood under shear flow conditions. Fibrin formation in laminin-coated capillaries was abrogated by an antibody that interferes with FXI activation by activated FXII, or an antibody that blocks activated FXI activation of FIX.

Conclusion: This study identifies a role for laminin in the initiation of coagulation and the formation of platelet-rich thrombi under shear conditions in a FXII-dependent manner.

Publication types

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

MeSH terms

  • Blood Coagulation / physiology*
  • Factor XII / physiology*
  • Humans
  • Laminin / physiology*
  • Thrombosis*

Substances

  • Laminin
  • Factor XII