The single prostacyclin receptor of gel-filtered platelets provides a correlation with antiaggregatory potency of PGI2 mimics

Thomas L. Eggerman, Cynthia J Hartzell, Sara Selfe, Niels H. Andersen

Research output: Contribution to journalArticle

8 Scopus citations


Gel-filtered human platelets (GFP) display only a single binding site for [3H]-PGI2: KD=61nM, 234 fmol/108 platelets (1410 sites/platelet). Platelet-rich plasma (PRP) displays the same receptor density but the KD value increases to 123 nM due to protein binding of PGI2 which lowers its effective concentration. The [3H]-PGI2/GFP binding assay has been used to evaluate the molecular basis of aggregation inhibition for prostacyclin analogs and mimics, three PGE type structures, and PGD2. Antiaggregatory IC50s and radioligand binding IC50s correlate for PGE2, E1 and six PGI2 analogs. PGD2, and to a lesser extent 6-oxo-PGE1, display greater antiaggregatory potency than expected based on PGI2-binding site affinity data.

Original languageEnglish (US)
Pages (from-to)645-659
Number of pages15
JournalThrombosis Research
Issue number5
StatePublished - Mar 1 1987
Externally publishedYes



  • aggregation inhibition
  • platelets
  • prostacyclin
  • receptor
  • structure-activity-relationships

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine
  • Hematology

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