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anti-Human F2RL3 Antikörper:
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Human Monoclonal F2RL3 Primary Antibody für IHC, ELISA - ABIN1724706
Xie, Guo: Par-4 inhibits choline uptake by interacting with CHT1 and reducing its incorporation on the plasma membrane. in The Journal of biological chemistry 2004
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Human Polyclonal F2RL3 Primary Antibody für WB - ABIN2801951
Kahn, Hammes, Botka, Coughlin: Gene and locus structure and chromosomal localization of the protease-activated receptor gene family. in The Journal of biological chemistry 1998
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Human Monoclonal F2RL3 Primary Antibody für ELISA, WB - ABIN563904
Muehlschlegel, Perry, Liu, Fox, Smith, Lichtner, Collard, Shernan, Hartwig, Body, Hoffmeister: Polymorphism in the protease-activated receptor-4 gene region associates with platelet activation and perioperative myocardial injury. in American journal of hematology 2013
Human Polyclonal F2RL3 Primary Antibody für IF (p), IHC (p) - ABIN673224
Oláh, Kálmán, Tóth, Zvara, Sántha, Ivitz, Janka, Pákáski: Proteomic Analysis of Cerebrospinal Fluid in Alzheimer's Disease: Wanted Dead or Alive. in Journal of Alzheimer's disease : JAD 2014
lower major bleeding rates were observed in the overall TRACER cohort with the hyperreactive PAR4 Thr120 variant
Allergen Der p3 from house dust mites activates store-operated calcium channels and protease-activated 4 receptors, stimulating mast cell migration.
Creosote-exposed workers (73.3%), but not chimney sweeps (76.6%) had lower methylation of F2RL3 cg03636183 than controls (76.7%).
Data suggested that PAR4-AP-induced platelet reactivity between PAR4 rs773902 was associated with altered intensity of Ca(2+) mobilization and ERK activation.
Thrombin binding to extra-cellular loop II (ECLII) of PAR4 is important for its cleavage and activation of PAR4.
PAR4 has a role in mediating platelet aggregation; its blockade provides antithrombotic activity
PAR4 is required for platelet procoagulant function during thrombus formation in human blood
Prospective study demonstrated that AHRR 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 reactivity particularly after exposure to therapeutic PAR1 antagonists.
these findings are the first to show that internalization of activated PAR4 is linked to proper ERK1/2 and Akt activation.
an intracellular PAR4 C-terminal motif that regulates calcium signaling and beta-arrestin interactions, was identified.
the contribution of PAR1 and PAR4 to thrombin-mediated activation of the platelet fibrin receptor (GPIIbIIIa), is reported.
Suppression of PAR4 expression has no significant effect on the proliferation of SW620 cells, but can inhibit the migration of the cells.
Both GPIbalpha and PAR4 are required for thrombin-induced reactive oxygen species formation in human platelets.
Bladder PAR activation elicits urothelial MIF release and urothelial MIF receptor signaling at least partly through CXCR4 to result in abdominal hypersensitivity without overt bladder inflammation
protease-activated receptor 4 and Trefoil factor 2 are expressed in human colorectal cancer
The PAR4 expression and activation via intracellular signaling pathways and the role of PAR4 signaling pathways in the development and maintenance of pain.
This review summarizes the roles of PAR4 in coagulation and other extracellular protease pathways.
Findings suggested that F2RL3 methylation is a very strong predictor of lung cancer risk and mortality, particularly at older age.
Lower F2RL3 methylation is a strong predictor of mortality, including all-cause, cardiovascular, cancer and other mortality. Systemic adverse effects of smoking may be mediated by pathways associated with F2RL3 methylation.
Par-4 activation and binding to TERT are key steps required for inducing the apoptosis of islet beta cells under high-glucose/fatty acid conditions in type 2 diabetes.
Par4 deficiency offers cardioprotection after acute ischemia reperfusion injury.
Bladder PAR4 stimulation affected urothelial HMGB1 release.
Thrombin cleavage of platelet PAR4 promotes leukocyte recruitment to sites of vascular injury.
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.
mPAR4 contributes to antibacterial defence during murine pneumococcal pneumonia
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
Data suggest that PAR-4 activation is endogenously involved as a feedback loop to attenuate inflammatory colonic hyperalgesia to colorectal distension.
PARs are involved in the modulation of joint pain, with PAR-4 being pronociceptive in this tissue. Thus, blockade of articular PAR-4 may be a useful means of controlling joint inflammation and pain [PAR-4].
arrestin-2 regulates PAR4-dependent signaling pathways, but not responses to ADP alone, and contributes to thrombus formation in vivo.
this work demonstrates a key role for PAR-4 in mediating eosinophil recruitment in an allergic pleurisy model in mice
Data indicate that deficiency of PAR4 protects mice from cerebral ischemia/reperfusion (I/R) injury, partially through inhibition of platelet activation and attenuation of microvascular inflammation.
The current study proves for the first time that PAR4 is localised in mossy fibre axons. The altered expression in CA3 neurons after ischaemia indicates that PAR4 may be involved in post-ischaemic adaptive mechanisms.
mediates factor Xa signaling in endothelial cells
PAR4 activation mediates the potentially detrimental effects of thrombin on microglia, implying that perspectives of exploiting PAR1 as a potential anti-inflammatory target should be shifted toward PAR4
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