Polyphosphate is a cofactor for the activation of factor XI by thrombin

被引:195
作者
Choi, Sharon H. [1 ]
Smith, Stephanie A. [1 ]
Morrissey, James H. [1 ]
机构
[1] Univ Illinois, Coll Med, Dept Biochem, Urbana, IL 61801 USA
基金
美国国家卫生研究院;
关键词
COAGULATION FACTOR-XI; BLOOD-COAGULATION; INORGANIC POLYPHOSPHATE; SACCHAROMYCES-CEREVISIAE; MEDIATED ACTIVATION; TISSUE FACTOR; DEFICIENCY; PLASMA; FIBRINOLYSIS; PLATELETS;
D O I
10.1182/blood-2011-07-368811
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Factor XI deficiency is associated with a bleeding diathesis, but factor XII deficiency is not, indicating that, in normal hemostasis, factor XI must be activated in vivo by a protease other than factor XIIa. Several groups have identified thrombin as the most likely activator of factor XI, although this reaction is slow in solution. Although certain nonphysiologic anionic polymers and surfaces have been shown to enhance factor XI activation by thrombin, the physiologic cofactor for this reaction is uncertain. Activated platelets secrete the highly anionic polymer polyphosphate, and our previous studies have shown that polyphosphate has potent procoagulant activity. We now report that polyphosphate potently accelerates factor XI activation by alpha-thrombin, beta-thrombin, and factor XIa and that these reactions are supported by polyphosphate polymers of the size secreted by activated human platelets. We therefore propose that polyphosphate is a natural cofactor for factor XI activation in plasma that may help explain the role of factor XI in hemostasis and thrombosis. (Blood. 2011;118(26):6963-6970)
引用
收藏
页码:6963 / 6970
页数:8
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