Interaction of prostaglandin D2 with prostacyclin, carbacyclin and the hydantoin prostaglandin, BW245C, in guinea‐pig platelets

Article date: May 1985

By: S. Hamid, B.J.R. Whittle in Volume 85, Issue 1, pages 285-290

The anti‐aggregating actions of prostaglandin D2 (PGD2) have been compared to prostacyclin (PGI2), its stable analogue carbacyclin and a hydantoin prostaglandin, BW245C, in guinea‐pig platelets in vitro.

PGI2, carbacyclin and BW245C were potent inhibitors of ADP‐induced aggregation in guinea‐pig platelets, with ID50 values comparable to those obtained in human platelet‐rich‐plasma.

In contrast, PGD2 acted as a weak and partial inhibitor in guinea‐pig platelet aggregation, producing a bell‐shaped dose‐response relationship.

PGD2 induced a dose‐related antagonism of the inhibitory actions of BW245C, prostacyclin and carbacyclin on guinea‐pig platelets.

However, PGD2 did not antagonize the inhibitory actions of either forskolin or dibutyryl cyclic AMP on this platelet preparation.

The results suggest a non‐specific interaction of PGD2 with these prostanoid binding sites on guinea‐pig platelets.

The anti‐aggregating actions of prostaglandin D2 (PGD2) have been compared to prostacyclin (PGI2), its stable analogue carbacyclin and a hydantoin prostaglandin, BW245C, in guinea‐pig platelets in vitro.

PGI2, carbacyclin and BW245C were potent inhibitors of ADP‐induced aggregation in guinea‐pig platelets, with ID50 values comparable to those obtained in human platelet‐rich‐plasma.

In contrast, PGD2 acted as a weak and partial inhibitor in guinea‐pig platelet aggregation, producing a bell‐shaped dose‐response relationship.

PGD2 induced a dose‐related antagonism of the inhibitory actions of BW245C, prostacyclin and carbacyclin on guinea‐pig platelets.

However, PGD2 did not antagonize the inhibitory actions of either forskolin or dibutyryl cyclic AMP on this platelet preparation.

The results suggest a non‐specific interaction of PGD2 with these prostanoid binding sites on guinea‐pig platelets.

DOI: 10.1111/j.1476-5381.1985.tb08858.x

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