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The effect of thrombin on the release of adenine nucleotides from cultured human umbilical vein endothelium was studied. When endothelial cell monolayers were incubated with 3H-adenosine for two hours at 37°C, fifty percent of the radioactivity was incorporated into the cell. Thin-layer radiochromatography revealed that greater than 90% of the tritium was associated with ADP and ATP.  Addition of thrombin to the monolayers resulted in the release of tritium into the medium. This effect was dose-dependent and saturable, with a maximal response seen at 1 × 10-8 M thrombin. Diisopropylphosphoryl thrombin (DIP-thrombin) , which is enzymatically inactive, did not cause a release of tritium. Blocking the high-affinity thrombin binding sites which are present on the endothelial cell surface was done with DIP-thrombin. Saturating these binding sites by greater than 95% with a fifty-fold excess of DIP-thrombin had no effect on thrombin-induced release, indicating that the high-affinity binding sites are not involved in the release of adenine nucleotides by thrombin.

Thrombin-Induced Release Of Adenine Nucleotides From Cultured Human Endothelial Cells