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Laminin promotes coagulation and thrombus formation in a factor XII-dependent manner
T C White-Adams1, M A Berny, I A Patel
1Division of Biomedical Engineering, School of Medicine, Oregon Health & Science University, Portland, OR, USA.
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.
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