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Thrombin (show F2 Proteins) binding to extra-cellular loop II (ECLII) of PAR4 (show PAWR Proteins) is important for its cleavage and activation of PAR4 (show PAWR Proteins).
PAR4 (show PAWR Proteins) has a role in mediating platelet aggregation; its blockade provides antithrombotic activity
PAR4 (show PAWR Proteins) is required for platelet procoagulant function during thrombus formation in human blood
Prospective study demonstrated that AHRR (show CYP1A1 Proteins) and F2RL3 methylation levels had inverse relationships with self-reported smoking status and accurately discriminated for both current- and former- smoking. Moreover, methylation markers distinguished former smokers from never-smokers with high accuracy and significantly associated with an increased risk of lung cancer.
F2RL3 variants have the potential to markedly alter platelet PAR4 (show PAWR Proteins) reactivity particularly after exposure to therapeutic PAR1 (show MARK2 Proteins) antagonists.
these findings are the first to show that internalization of activated PAR4 (show PAWR Proteins) is linked to proper ERK1/2 and Akt (show AKT1 Proteins) activation.
an intracellular PAR4 C-terminal motif that regulates calcium signaling and beta-arrestin interactions, was identified.
the contribution of PAR1 (show MARK2 Proteins) and PAR4 (show PAWR Proteins) to thrombin (show F2 Proteins)-mediated activation of the platelet fibrin receptor (GPIIbIIIa), is reported.
Suppression of PAR4 (show PAWR Proteins) expression has no significant effect on the proliferation of SW620 cells, but can inhibit the migration of the cells.
Both GPIbalpha (show GP1BA Proteins) and PAR4 (show PAWR Proteins) are required for thrombin (show F2 Proteins)-induced reactive oxygen species formation in human platelets.
these findings are the first to show that internalization of activated PAR4 is linked to proper ERK1/2 and Akt (show AKT1 Proteins) activation.
Par4 deficiency offers cardioprotection after acute ischemia reperfusion injury.
Bladder PAR4 stimulation affected urothelial HMGB1 (show HMGB1 Proteins) release.
Thrombin (show F2 Proteins) cleavage of platelet PAR4 promotes leukocyte recruitment to sites of vascular injury.
Bladder PAR (show AFG3L2 Proteins) activation elicits urothelial MIF (show MIF Proteins) release and urothelial MIF (show MIF Proteins) receptor signaling at least partly through CXCR4 (show CXCR4 Proteins) to result in abdominal hypersensitivity without overt bladder inflammation
PAR4 blockade impairs neutrophil migration in vivo, suggesting that PAR4 plays an important role in the regulation of inflammation
PAR-4 appears to play a hitherto unsuspected role in diabetic vasculopathy.
PAR-4 as a potential target for future therapeutic strategies against platelet-mediated liver injury on transplantation.
Results demonstrate that PAR-4 does not play a significant role during pulmonary fibrosis.
These data suggest a key role for PAR4 in mediating neutrophil recruitment in a mouse model of pleurisy induced by the activity of trypsin or trypsin-like enzymes
Coagulation factor II (thrombin) receptor-like 3 (F2RL3) is a member of the large family of 7-transmembrane-region receptors that couple to guanosine-nucleotide-binding proteins. F2RL3 is also a member of the protease-activated receptor family. F2RL3 is activated by proteolytic cleavage of its extracellular amino terminus. The new amino terminus functions as a tethered ligand and activates the receptor. F2RL3 is activated by thrombin and trypsin.
proteinase-activated receptor 4
, coagulation factor II (thrombin) receptor-like 3
, protease-activated receptor-4
, thrombin receptor-like 3
, coagulation factor II receptor-like 3
, protease-activated receptor 4