Protein-Phospholipid interactions in blood clotting
نویسندگان
چکیده
منابع مشابه
Protein-phospholipid interactions in blood clotting.
Most steps of the blood clotting cascade require the assembly of a serine protease with its specific regulatory protein on a suitable phospholipid bilayer. Unfortunately, the molecular details of how blood clotting proteins bind to membrane surfaces remain poorly understood, owing to a dearth of techniques for studying protein-membrane interactions at high resolution. Our laboratories are tackl...
متن کاملThe local phospholipid environment modulates the activation of blood clotting.
Examples abound of membrane-bound enzymes for which the local membrane environment plays an important role, including the ectoenzyme that triggers blood clotting, the plasma serine protease, factor VIIa, bound to the integral membrane protein, tissue factor. The activity of this enzyme complex is markedly influenced by lipid bilayer composition and further by tissue factor partitioning into mem...
متن کاملProteases in blood clotting.
The serine proteases, cofactors and cell-receptor molecules that comprise the haemostatic mechanism are highly conserved modular proteins that have evolved to participate in biochemical reactions in blood coagulation, anticoagulation and fibrinolysis. Blood coagulation is initiated by exposure of tissue factor, which forms a complex with factor VIIa and factor X, which results in the generation...
متن کاملBlood clotting in minimally altered whole blood.
The sequences of events regulating thrombin generation during tissue factor-initiated clotting in whole blood at 37 degrees C in which the contact pathway was suppressed with corn trypsin inhibitor are studied using quantitative Western blotting of factor V, prothrombin, platelet factor 4, antithrombin III, and fibrinogen. In addition, fibrinopeptide A (FPA), thrombin-antithrombin III (TAT) com...
متن کاملBlood Clotting in Minimally Altered Whole Blood
The sequences of events regulating thrombin generation during tissue factor-initiated clotting in whole blood at 37°C in which the contact pathway was suppressed with corn trypsin inhibitor are studied using quantitative Western blotting of factor V, prothrombin, platelet factor 4, antithrombin Ill, and fibrinogen. In addition, fibrinopeptide A (FPA), thrombin-antithrombin 111 (TAT) complex for...
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ژورنال
عنوان ژورنال: Thrombosis Research
سال: 2010
ISSN: 0049-3848
DOI: 10.1016/j.thromres.2010.01.027