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Thromb Haemost 1983; 49(03): 162-167
DOI: 10.1055/s-0038-1657353
Original Article
Schattauer GmbH Stuttgart

Factors Influencing the Deaggregation of Human and Rabbit Platelets

R L Kinlough-Rathbone
The Department of Pathology, McMaster University, Hamilton, Canada and the Department of Biochemistry, University of Toronto, Toronto, Canada
,
J F Mustard
The Department of Pathology, McMaster University, Hamilton, Canada and the Department of Biochemistry, University of Toronto, Toronto, Canada
,
D W Perry
The Department of Pathology, McMaster University, Hamilton, Canada and the Department of Biochemistry, University of Toronto, Toronto, Canada
,
E Dejana
The Department of Pathology, McMaster University, Hamilton, Canada and the Department of Biochemistry, University of Toronto, Toronto, Canada
,
J-P Cazenave
The Department of Pathology, McMaster University, Hamilton, Canada and the Department of Biochemistry, University of Toronto, Toronto, Canada
,
M A Packham
The Department of Pathology, McMaster University, Hamilton, Canada and the Department of Biochemistry, University of Toronto, Toronto, Canada
,
E J Harfenist
The Department of Pathology, McMaster University, Hamilton, Canada and the Department of Biochemistry, University of Toronto, Toronto, Canada
› Author Affiliations
Further Information

Publication History

Received 14 December 1982

Accepted 09 March 1983

Publication Date:
18 July 2018 (online)

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Summary

The mechanisms involved in platelet deaggregation are unclear. Washed platelets from rabbits or humans aggregated by ADP can be deaggregated by EDTA or PGI2 if the release reaction has not occurred; during deaggregation 125I-fibrinogen dissociates from the platelets. Human platelets suspended in a medium without calcium undergo the release reaction during ADP-induced aggregation; EDTA, PGE, or PGI2 do not deaggregate these platelets although EDTA displaces much of the 125I-fibrinogen that associates with them during aggregation. Rabbit platelets aggregated by low concentrations of releaseinducing stimuli (sodium arachidonate, collagen or thrombin) can be deaggregated by EDTA, PGI2 or PGE1 and 125I-fibrinogen dissociates from them; with high concentrations of collagen or thrombin, deaggregation and dissociation of l25I-fibrinogen is slower. Human platelets that have undergone the release reaction in response to thrombin, collagen or a combination of sodium arachidonate and ADP are not readily deaggregated by EDTA or PGE1. Since aggregation and fibrinogen binding involving the glycoprotein IIb/IIIa complex are readily reversed by EDTA, and since Ca2+ is required for thrombospondin binding to activated platelets, there may be a third type of platelet-platelet adherence that is not disrupted by EDTA; this type of binding plays a greater role with human than with rabbit platelets.

Keywords

Platelets - Deaggregation - Fibrinogen - Release reaction - Prostaglandin E1 - Thrombin - ADP
 

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