Different sensitivities of prostaglandin-cyclooxygenases in blood platelets and coronary arteries against non-steroidal antiinflammatory drugs

Naunyn Schmiedebergs Arch Pharmacol. 1980 Aug;313(1):69-76. doi: 10.1007/BF00505806.

Abstract

The action of the non-steroidal antiinflammatory drugs indomethacin, tiaprofenic acid, diclofenac and meclofenamate on vascular and platelet-cyclooxygenases was studied by measuring the arachidonic acid-induced thromboxane A2 (TXA2)-formation of washed human platelets and prostacyclin (PGI2)-formation of bovine coronary artery rings. TXA2 was bioassayed as RCS on rabbit aorta strips, PGI2 in terms of its antiaggregatory activity on ADP-induced aggregation of human platelet-rich plasma. All of the substances studied produced concentration-dependent inhibition of PGI2- and RCS-release. The IC50 [micrometer] in inhibition of RCS-formation was 0.019 for indomethacin, 0.070 for tiaprofenic acid but 44.9 for meclofenamate and 63.2 for diclofenac. The IC50 [micrometer] in inhibition of PGI2-release was 0.42 for diclofenac, 0.63 for indomethacin and 0.99 for tiaprofenic acid. The data suggest (1) high sensitivity of human platelet-cyclooxygenase against indomethacin and tiaprofenic acid, (2) different sequence of the substances studied in inhibiting arachidonic acid-induced TXA2- and PGI2-formation. The possible therapeutic value of selective inhibition of platelets and vascular cyclooxygenases is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Inflammatory Agents / pharmacology*
  • Blood Platelets / enzymology*
  • Cattle
  • Coronary Vessels / drug effects
  • Coronary Vessels / enzymology*
  • Dose-Response Relationship, Drug
  • Epoprostenol / metabolism
  • Humans
  • Prostaglandin-Endoperoxide Synthases / metabolism*
  • Rabbits
  • Thromboxane A2 / antagonists & inhibitors
  • Thromboxane A2 / metabolism
  • Time Factors

Substances

  • Anti-Inflammatory Agents
  • Thromboxane A2
  • Epoprostenol
  • Prostaglandin-Endoperoxide Synthases