European Journal of Biochemistry · 1981 · 41 citations · 11 references
Life SciencesBiochemistryCell BiologyCell SignalingCytoskeletonHemostasisActin FilamentsActin PolymerizationPlatelet ActivationPlatelet AggregationPlatelet FunctionPlatelet PhysiologyAdenosine Diphosphate-induced Platelet AggregationCytoskeletal Rearrangement In PlateletsPlatelet Actin CytoskeletonPlatelet Cytoskeletal DynamicsPlatelet Cytoskeleton DynamicsPlatelet Responses To AgonistsThrombin-induced Platelet Aggregation
The state of platelet actin was determined using a fluorescent method of DNAse I inhibition. Activation of human platelets resulted in mobilization of DNAse-available actin. When platelets were activated with ADP the change in the state of actin was gradual and preceded the secretion. When thrombin was used as an activator, a sharp and rapid decrease in the DNAse-available actin was observed which paralleled the secretion. Inhibition of ADP-induced aggregation (and secretion) by EDTA resulted in a decrease in the rate of change on actin. Inhibition of the thrombin-induced aggregation (but not secretion) by EDTA did not affect the change in the state of actin.
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Fine Structural Alterations Induced in Platelets by Adenosine Diphosphate
James G. White · Blood · 1968 · 343 citations · Full text
Medicine, Biochemistry, Hematology +14
Depolymerization of F-actin by deoxyribonuclease I
Sarah E. Hitchcock, Lars Carlsson, Uno Lindberg · Cell · 1976 · 263 citations