Inhibition of purified factor Xa amidolytic activity may not be predictive of inhibition of in vivo thrombosis: implications for identification of therapeutically active inhibitors

Arterioscler Thromb Vasc Biol. 2003 Jun 1;23(6):1098-104. doi: 10.1161/01.ATV.0000077248.22632.88. Epub 2003 May 15.

Abstract

Objective: In this study we test the hypothesis that blood/plasma-based prothrombinase assays, rather than inhibition of purified factor Xa (fXa), are predictive of in vivo antithrombotic activity.

Methods and results: Six fXa inhibitors with equivalent nanomolar Ki were studied in thrombin generation assays using human plasma/blood and endogenous macromolecular substrate. In all assays, benzamidine inhibitors were more potent (100 to 800 nmol/L) than the aminoisoquinolines (5 to 58 micromol/L) or neutral inhibitors (3 to 10 micromol/L). A similar rank order of compound inhibition was also seen in purified prothrombinase assays as well as in a rabbit model of deep vein thrombosis.

Conclusions: Assays using prothrombinase with protein substrates are better predictors of in vivo efficacy than fXa Ki using amidolytic substrates.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Benzamidines / pharmacology*
  • Binding Sites / drug effects
  • Dose-Response Relationship, Drug
  • Drug Evaluation, Preclinical
  • Enzyme Inhibitors / classification
  • Enzyme Inhibitors / pharmacology*
  • Factor Xa Inhibitors*
  • Fibrinolytic Agents / classification
  • Fibrinolytic Agents / pharmacology*
  • Humans
  • Isoquinolines / pharmacology*
  • Male
  • Molecular Structure
  • Prothrombin / metabolism*
  • Sensitivity and Specificity
  • Substrate Specificity
  • Thrombin / biosynthesis
  • Thromboplastin / antagonists & inhibitors*
  • Venous Thrombosis / prevention & control

Substances

  • Benzamidines
  • Enzyme Inhibitors
  • Factor Xa Inhibitors
  • Fibrinolytic Agents
  • Isoquinolines
  • Prothrombin
  • Thromboplastin
  • Thrombin