January 1, 2008Thrombosis and Haemostasis
Detection of P2Y14 protein in platelets and investigation of the role of P2Y14 in platelet function in comparison with the EP3 receptor
Key result
Although P2Y14 receptor protein is present on platelets, the agonist UDP-glucose did not induce platelet aggregation or affect adenylate cyclase activity, unlike the EP3 agonist sulprostone.
Population
Platelets (in vitro)
Comparison
UDP-glucose (P2Y14 agonist, up to 100 muM) vs Sulprostone (selective EP3 receptor agonist)
Design
Preclinical
Authors
Discussion
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Member takes
Implication
P2Y14 unlikely to drive platelet activation; leaves open its role in vivo or with other ligands.
Structured PICO
P
Population
Platelets (in vitro)
I
Intervention
UDP-glucose (P2Y14 agonist, up to 100 muM)
C
Comparator
Sulprostone (selective EP3 receptor agonist)
O
Outcome
Platelet aggregation (in platelet-rich plasma and whole blood) and adenylate cyclase activity (VASP phosphorylation)surrogate
Although the P2Y14 receptor protein is present on platelets, its activation by UDP-glucose does not appear to contribute to platelet aggregation or adenylate cyclase activity in vitro.
Cite This Study
Wijeyeratne et al. (2008) studied this question. UDP-glucose vs. Sulprostone was evaluated on Platelet aggregation and adenylate cyclase activity. Although P2Y14 receptor protein is present on platelets, the agonist UDP-glucose did not induce platelet aggregation or affect adenylate cyclase activity, unlike the EP3 agonist sulprostone.