期刊
JOURNAL OF THROMBOSIS AND HAEMOSTASIS
卷 8, 期 6, 页码 1295-1301出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1538-7836.2010.03850.x
关键词
factor XI; factor XII; fibrin; laminin; platelets
资金
- American Heart Association [0910025G, 09PRE2230117, 0850056Z, 09GRNT2150003]
- National Institutes of Health [HL58837]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL058837, R01HL081326] Funding Source: NIH RePORTER
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 plasmain 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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