Relationship of ADP-induced fibrinogen binding to platelet shape change and aggregation elucidated by use of colchicine and cytochalasin B

E. L. Peerschke, M. B. Zucker

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

ADP causes human, aspirin-treated, gel-filtered platelets to change from their native discoid shape to spiny spheres with pseudopods, bind 125I-labeled fibrinogen, and aggregate if shaken with sufficient fibrinogen. After destruction of the added ADP with the enzyme apyrase, the platelets revert to a disc shape and lose much of their bound fibrinogen. Colchicine (208 μM or 83 μg/ml) prevented ADP-induced shape change but not ADP-induced fibrinogen binding or aggregation. Thus, these findings support earlier studies with thrombasthenic and EDTA-treated platelets and with normal platelets at low pH, or in the presence of EDTA to indicate that fibrinogen binding is associated with aggregability but not with platelet shape.

Original languageEnglish
Pages (from-to)58-60
Number of pages3
JournalThrombosis and Haemostasis
Volume43
Issue number1
DOIs
StatePublished - 1980
Externally publishedYes

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