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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.
Bladder PAR (show JTB Proteins) activation elicits urothelial MIF (show AMH Proteins) release and urothelial MIF (show AMH Proteins) receptor signaling at least partly through CXCR4 (show CXCR4 Proteins) to result in abdominal hypersensitivity without overt bladder inflammation
The metabolic effects were associated with activation of the SIRT1 (show SIRT1 Proteins)-LKB1 (show STK11 Proteins)-AMPK (show PRKAA1 Proteins) signalling pathway in adipose tissue and liver.
Treg cells use LKB1 (show STK11 Proteins) signalling to coordinate their metabolic and immunological homeostasis and to prevent apoptotic and functional exhaustion, thereby orchestrating the balance between immunity and tolerance
renal proximal tubule cell CB1R (show CNR1 Proteins) contributes to the pathogenesis of obesity-induced renal lipotoxicity and nephropathy by regulating the liver kinase B1 (show STK11 Proteins)/AMP-activated protein kinase (show PRKAA2 Proteins) signaling pathway
Results reveal an important role for Lkb1 (show STK11 Proteins) in regulating cerebellar cortical size and foliation in a Hedgehog (show SHH Proteins)-independent manner.
beige adipocyte renaissance was governed by liver kinase b1 (show STK11 Proteins) and histone deacetylase 4 (show HDAC5 Proteins) in white adipocytes.
miR-17-92-dependent tuning of LKB1 (show STK11 Proteins) levels regulates both the metabolic potential of Myc (show MYC Proteins)+ lymphomas and tumor growth in vivo.
Findings indicate that the energy-sensing LKB1 (show STK11 Proteins)-AMPK (show PRKAA1 Proteins) pathway regulates IGF1 (show IGF1 Proteins) secretion in mouse primary hepatocytes, which in turn regulates activation of the IGF1R (show IGF1R Proteins)-PKB (show AKT2 Proteins) pathway.
These data suggest that nutrient availability dictates the mode of division and that LKB1 (show STK11 Proteins)-AMPK (show PRKAA1 Proteins) mediates this nutrient-driven effect on intestinal epithelial stem cell proliferation.
this study identified the molecular mechanism of increased angiogenesis and tumor growth with LKB1 (show STK11 Proteins) deficiency
These results suggest that although physiologic LKB1 (show STK11 Proteins) expression exerts a potent pro-survival effect in lymphocytes, LKB1 (show STK11 Proteins) inactivation nonetheless facilitates transformation of B, but not T, lymphocytes.
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
, coagulation factor II (thrombin)
, protease-activated receptor-4
, thrombin receptor-like 3
, coagulation factor II receptor-like 3
, protease-activated receptor 4
, LKB1 short isoform
, liver kinase B1 homolog
, serine/threonine-protein kinase 11
, serine/threonine-protein kinase LKB1
, serine/threonine-protein kinase STK11