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Research Article Free access | 10.1172/JCI106857

Platelet Interaction with Polymerizing Fibrin

Stefan Niewiarowski, Erwin Rogoeczi, Gwendolyn J. Steward, Andrew F. Senyi, and J. Fraser Mustard

Department of Pathology, McMaster University, Hamilton, Ontario, Canada

Find articles by Niewiarowski, S. in: PubMed | Google Scholar

Department of Pathology, McMaster University, Hamilton, Ontario, Canada

Find articles by Rogoeczi, E. in: PubMed | Google Scholar

Department of Pathology, McMaster University, Hamilton, Ontario, Canada

Find articles by Steward, G. in: PubMed | Google Scholar

Department of Pathology, McMaster University, Hamilton, Ontario, Canada

Find articles by Senyi, A. in: PubMed | Google Scholar

Department of Pathology, McMaster University, Hamilton, Ontario, Canada

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Published March 1, 1972 - More info

Published in Volume 51, Issue 3 on March 1, 1972
J Clin Invest. 1972;51(3):685–700. https://doi.org/10.1172/JCI106857.
© 1972 The American Society for Clinical Investigation
Published March 1, 1972 - Version history
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Abstract

Interaction of washed pig, rabbit, or human platelets with fibrinogen was studied during its transition to fibrin using photometric, isotopic, and electron microscopic techniques. Untreated fibrinogen and fully polymerized fibrin had no detectable effect on platelets. Fibrinogen, incubated with low concentrations of reptilase or thrombin, formed intermediate products which readily became associated with platelets and caused their aggregation. Neutralization of the thrombin did not prevent this interaction. In the absence of fibrinogen, reptilase did not affect platelets.

The interaction of polymerizing fibrin with platelets was accompanied by small losses of platelet constituents (serotonin, adenine nucleotides, platelet factor 4, and lactic dehydrogenase). This loss did not appear to be the result of the platelet release reaction. Inhibitors of the release reaction or of adenosine diphosphate (ADP)-induced aggregation did not prevent the interaction of platelets with polymerizing fibrin. Apyrase or prostaglandin E1 (PGE1) reduced the extent of platelet aggregation by polymerizing fibrin, but the amount of protein associated with platelets was slightly increased.

The interaction of polymerizing fibrin with platelets was completely inhibited by ethylenediaminetetraacetate (EDTA) or ethylene glycol bis (β-aminoethyl ether) N, N,N′,N′-tetraacetic acid (EGTA).

Fibers formed in solutions of polymerizing fibrin were larger in the presence than in the absence of washed platelets, suggesting that platelets affect fibrin polymerization. The adherence of platelets to polymerizing fibrin may be responsible for the establishment of links between platelets and fibrin in hemostatic plugs and thrombi.

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