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• W2003147287 abstract "Methods for the evaluation of competitive interactions at receptors associated with platelet activation and inhibition using aggregometry of human PRP have been developed. The evidence supports the suggestion that PGE1 and PGI2 share a common receptor for inhibition of platelet reactivity, but only a portion (if any) of the aggregation stimulation associated with PGE2 is the result of PGE2 binding (without efficacy) to this receptor. PGE2 (@.3–20 μM) is an effective antagonist of PGE1, PGI2, and PGD2 producing a shift of about one order of magnitude in the IC50-values obtained from complete aggregation inhibition dose response curves. The antagonism of PGD2 inhibition is particularly notable, 80 nM PGE2 levels are detectable. This and other actions of PGE2 indicate another platelet receptor for PGE2. PGE1 acts at both the PGE2 and PGI2 receptor. Other substances showing PGI2-like actions only at high doses (1–30 μM), display additive responses with PGI2 indicative of decreased affinity for the I2E1 receptor and the absence of PGE2-like aggregation stimulation activity. PGI2 methyl ester has intrinsic inhibitory action not associated with in situ ester hydrolysis. The methyl ester is dissaggregatory showing particular specificity for inhibition of release and second wave aggregation." @default.
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• W2003147287 date "1980-05-01" @default.
• W2003147287 modified "2023-10-17" @default.
• W2003147287 title "On the multiplicity of platelet prostaglandin receptors I. Evaluation of competitive antagonism by aggregometry" @default.
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• W2003147287 doi "https://doi.org/10.1016/0090-6980(80)90170-7" @default.
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