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anti-Human F2RL3 Anticorps:
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Human Monoclonal F2RL3 Primary Antibody pour IHC, ELISA - ABIN1724706
Xie, Guo: Par-4 inhibits choline uptake by interacting with CHT1 and reducing its incorporation on the plasma membrane. dans The Journal of biological chemistry 2004
Show all 4 Pubmed References
Human Monoclonal F2RL3 Primary Antibody pour 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. dans American journal of hematology 2013
Human Polyclonal F2RL3 Primary Antibody pour 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. dans Journal of Alzheimer's disease : JAD 2014
Endogenous H2S generated by CBS or CSE caused referred hyperalgesia mediated through MIF in mice with PAR4-induced bladder pain, without causing bladder injury or altering micturition behavior.
This study found divergent and inverse allele frequencies of the PAR4 rs773902 single nucleotide polymorphism (SNP) in the Somali population compared with data previously reported for blacks in the United States. The A allele frequency of the PAR4 rs773902 SNP in Somalis was 38% compared with the previously reported 63% for blacks.
The signaling difference by the PAR4-120 variant results in the enhancement of both Gq and G13 activation and an increase in thrombus formation resulting in a potential resistance to traditional antiplatelet therapies targeting COX-1 and the P2Y12 receptor.
methylation of F2RL3 can affect the prognosis of different types of acute coronary syndrome and is closely related to mortality
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
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
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