Aggregation of platelets by muscle actin. A multivalent interaction model of platelet aggregation by ADP |
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Authors: | Victoria D Scarborough Harvey R Bradford Pankaj Ganguly |
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Institution: | 1. Department of Hematology, St. Jude Children''s Research Hospital, Memphis, Tennessee 38101 USA;2. the Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38101 USA |
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Abstract: | Filamentous muscle actin (F-actin) aggregated blood platelets while G-actin was ineffective. This aggregation could be blocked by ATP suggesting a possible role of actin-bound ADP in this process. Actin-bound ADP caused platelet aggregation at concentrations significantly lower than equivalent concentrations of free ADP. Thus, actin potentiates the aggregating action of ADP. An actin antibody or DNase I inhibited this aggregation showing the requirement of actin in this process. Like other physiological agents, Ca++ was necessary for platelet aggregation by actin. Platelets fixed in formaldehyde were not aggregated by actin showing the need for viable platelets. Since F-actin contains 1 mole of bound ADP/mole protein, it is postulated that actin potentiates ADP-induced aggregation by providing multiple interaction sites for platelets. |
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