Key result
Prostacyclin platelet anti-aggregatory activity was more stable in plasma than in buffer solutions, likely due to protection by a plasma protein rather than enzymatic conversion.
Prostacyclin's platelet anti-aggregatory activity is prolonged in human plasma likely due to non-enzymatic protection by plasma proteins.
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Does not support changes in prostacyclin use; hypothesis-generating for plasma protein stabilization of platelet inhibition.
The rate of decay of the platelet antiaggregatory activity of prostacyclin in plasma and buffer solutions was investigated. 2. Platelet anti-aggregatory activity of prostacyclin was more stable in plasma than in buffer solutions at physiological pH. 3. The rate of decay of this activity increased with an increase in incubation temperature. 4. Preheating of plasma at 65 degrees C led to a marked but not total loss of its ability to "protect" prostacyclin. 5. Incubation of 6-keto prostaglandin F 1 alpha in plasma did not result in the appearance of platelet anti-aggregatory activity; nor did the decay curves of prostacyclin activity indicate the emergence of any new platelet anti-aggregatory activity. 6. Incubation of 6-keto-prostaglandin E1 in plasma did not lead to any loss of its platelet anti-aggregatory activity for prolonged periods. 7. We conclude that the marked prolongation of platelet anti-aggregatory activity of prostacyclin in plasma is not due to its enzymatic conversion into 6-keto-prostaglandin E1 but due to 'protection' of prostacyclin itself. This 'protection' is probably due to an interaction with a plasma protein.
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Mikhailidis et al. (1982) studied this question. Prostacyclin in human plasma vs. Buffer solutions was evaluated on Rate of decay of platelet antiaggregatory activity. Prostacyclin platelet anti-aggregatory activity was more stable in plasma than in buffer solutions, likely due to protection by a plasma protein rather than enzymatic conversion.
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