Thromb Haemost 1985; 53(01): 008-014
DOI: 10.1055/s-0038-1661226
Original Article
Schattauer GmbH Stuttgart

Effects of Plasmin on Rabbit Platelets

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

Publication History

Received 03 May 1984

Accepted 25 September 1984

Publication Date:
21 August 2018 (online)

Summary

The effects of plasmin have been examined because platelets may be exposed to plasmin in vivo and treatment of platelets with plasmin shortens platelet survival. Rabbit plasmin was prepared by urokinase activation of plasminogen immobilized on lysine- Sepharose. Plasmin caused rabbit platelets to aggregate and release the contents of their amine storage granules, but aggregation was slower than in response to ADP or thrombin. EDTA, prostaglandin E1, or creatine phosphate/creatine phosphokinase were inhibitory, but indomethacin was not. Deaggregation did not occur when platelets had been aggregated by a concentration of plasmin that caused extensive release of granule contents. EDTA or prostaglandin E1 caused deaggregation. Low concentrations of ADP and plasmin acted synergistically in causing platelet aggregation. Plasmin decreased the amounts of platelet membrane glycoproteins that stained with periodic acid-Schiff reagent; glycoprotein I was more susceptible than glycoproteins II and III. Concentrations of plasmin that induced the release of amine storage granule contents also released PAS- staining granule gylcoproteins.

Platelets incubated with plasmin, washed and resuspended, were not aggregated by ADP, but were aggregated strongly by the combination of fibrinogen and ADP, and bound 125I-fibrinogen to a greater extent than untreated platelets. Platelets preincubated with a high concentration of plasmin were unresponsive to thrombin, but were sometimes aggregated by fibrinogen.

Plasmin decreased the buoyant density and increased the median size of platelets. Thus plasmin, as well as ADP and thrombin, may contribute to the density shift observed in platelets from rabbits in which thrombosis and continuous vessel injury have been induced.

 
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