Factor VIII-induced superaggregation of human platelets
نویسندگان
چکیده
منابع مشابه
Factor VIII-induced superaggregation of human platelets.
High concentrations of bovine factor VIII cause clumping of platelets into a few very large aggregates. This response is termed superaggregation. It is distinct from factor-VIII-induced agglutination but is also independent of both extracellular calcium ions and platelet energy metabolism. Neither agglutinating lectins nor aggregating agents, including thrombin, ADP, the ionophore A23187, and U...
متن کاملFactor Vill - Induced Superaggregation of Human Platelets
High concentrations of bovine factor VIII cause clumping of platelets into a few very large aggregates. This response is termed superaggregation. It is distinct from factor-VIIIinduced agglutination but is also independent of both extracellular calcium ions and platelet energy metabolism. Neither agglutinating lectins nor aggregating agents. including thrombin. ADP. the ionophore A231 87. and U...
متن کاملThe interaction of bovine factor VIII with human platelets.
Treatment of human platelets with purified bovine Factor VIII caused three types of aggregation: (a) primary agglutination; (b) secondary aggregation involving the platelet release reaction; and (c) super-aggregation, in which the platelets were gathered into only a few large clumps. Removal of calcium ions or treatment with p-hydroxymercuiriphenyl sulfonate blocked the release reaction, but no...
متن کاملThrombin-induced exposure and prostacyclin inhibition of the receptor for factor VIII/von Willebrand factor on human platelets.
The receptor for Factor VIII/von Willebrand factor (F. VIIIVWF) is readily available on circulating platelets. We have found that the stimulation of platelets with traces of thrombin at concentrations that are generated physiologically (0.008 U-0.05 U/ml) induced concentration-dependent binding of 125I-labeled F. VIIIVWF in a steady-state system. The binding induced by thrombin was specific bec...
متن کاملDemonstration and characterization of specific binding sites for factor VIII/von Willebrand factor on human platelets.
The presence of specific Factor VIII/von Willebrand factor (FVIII/vWF) binding sites on human platelets has been demonstrated by using 125I-FVIII/vWF and washed human platelets. Binding is ristocetin-dependent and increases in proportion to the concentration of ristocetin from 0.2 to 1 mg/ml. Binding of 125I-FVIII/vWF to platelets can be competitively inhibited by unlabeled human or bovine FVII...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Blood
سال: 1982
ISSN: 0006-4971,1528-0020
DOI: 10.1182/blood.v60.6.1359.bloodjournal6061359