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PAR4 (Montrer PAWR Protéines) has a role in mediating platelet aggregation; its blockade provides antithrombotic activity
PAR4 (Montrer PAWR Protéines) is required for platelet procoagulant function during thrombus formation in human blood
Prospective study demonstrated that AHRR (Montrer CYP1A1 Protéines) 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 (Montrer PAWR Protéines) reactivity particularly after exposure to therapeutic PAR1 (Montrer MARK2 Protéines) antagonists.
these findings are the first to show that internalization of activated PAR4 (Montrer PAWR Protéines) is linked to proper ERK1/2 and Akt (Montrer AKT1 Protéines) activation.
an intracellular PAR4 C-terminal motif that regulates calcium signaling and beta-arrestin interactions, was identified.
the contribution of PAR1 (Montrer MARK2 Protéines) and PAR4 (Montrer PAWR Protéines) to thrombin (Montrer F2 Protéines)-mediated activation of the platelet fibrin receptor (GPIIbIIIa), is reported.
Suppression of PAR4 (Montrer PAWR Protéines) expression has no significant effect on the proliferation of SW620 cells, but can inhibit the migration of the cells.
Both GPIbalpha (Montrer GP1BA Protéines) and PAR4 (Montrer PAWR Protéines) are required for thrombin (Montrer F2 Protéines)-induced reactive oxygen species formation in human platelets.
Bladder PAR (Montrer JTB Protéines) activation elicits urothelial MIF (Montrer AMH Protéines) release and urothelial MIF (Montrer AMH Protéines) receptor signaling at least partly through CXCR4 (Montrer CXCR4 Protéines) to result in abdominal hypersensitivity without overt bladder inflammation
The metabolic effects were associated with activation of the SIRT1 (Montrer SIRT1 Protéines)-LKB1 (Montrer STK11 Protéines)-AMPK (Montrer PRKAA1 Protéines) signalling pathway in adipose tissue and liver.
Treg cells use LKB1 (Montrer STK11 Protéines) 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 (Montrer CNR1 Protéines) contributes to the pathogenesis of obesity-induced renal lipotoxicity and nephropathy by regulating the liver kinase B1 (Montrer STK11 Protéines)/AMP-activated protein kinase (Montrer PRKAA2 Protéines) signaling pathway
Results reveal an important role for Lkb1 (Montrer STK11 Protéines) in regulating cerebellar cortical size and foliation in a Hedgehog (Montrer SHH Protéines)-independent manner.
beige adipocyte renaissance was governed by liver kinase b1 (Montrer STK11 Protéines) and histone deacetylase 4 (Montrer HDAC5 Protéines) in white adipocytes.
miR-17-92-dependent tuning of LKB1 (Montrer STK11 Protéines) levels regulates both the metabolic potential of Myc (Montrer MYC Protéines)+ lymphomas and tumor growth in vivo.
Findings indicate that the energy-sensing LKB1 (Montrer STK11 Protéines)-AMPK (Montrer PRKAA1 Protéines) pathway regulates IGF1 (Montrer IGF1 Protéines) secretion in mouse primary hepatocytes, which in turn regulates activation of the IGF1R (Montrer IGF1R Protéines)-PKB (Montrer AKT2 Protéines) pathway.
These data suggest that nutrient availability dictates the mode of division and that LKB1 (Montrer STK11 Protéines)-AMPK (Montrer PRKAA1 Protéines) 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 (Montrer STK11 Protéines) deficiency
These results suggest that although physiologic LKB1 (Montrer STK11 Protéines) expression exerts a potent pro-survival effect in lymphocytes, LKB1 (Montrer STK11 Protéines) 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