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

T. C. White-Adams, M. A. Berny, I. A. Patel, E. I. Tucker, D. Gailani, A. Gruber, O. J.T. McCarty

Research output: Contribution to journalArticle

42 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1295-1301
Number of pages7
JournalJournal of Thrombosis and Haemostasis
Volume8
Issue number6
DOIs
StatePublished - Jun 1 2010

Keywords

  • Factor XI
  • Factor XII
  • Fibrin
  • Laminin
  • Platelets

ASJC Scopus subject areas

  • Hematology

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