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Laminin promotes coagulation and thrombus formation in a factor XII‐dependent manner
Author(s) -
WHITEADAMS T. C.,
BERNY M. A.,
PATEL I. A.,
TUCKER E. I.,
GAILANI D.,
GRUBER A.,
MCCARTY O. J. T.
Publication year - 2010
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/j.1538-7836.2010.03850.x
Subject(s) - laminin , coagulation , fibrin , thrombus , chemistry , factor xii , platelet adhesiveness , platelet , platelet activation , hemostasis , basement membrane , microbiology and biotechnology , gpvi , adhesion , immunology , biochemistry , extracellular matrix , medicine , biology , platelet aggregation , organic chemistry
Summary. 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.