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Study findings point out that PAR2 could play an essential role in gastroesophageal reflux disease (GERD) pathogenesis - even repeated short-term exposure to weakly acidic conditions lead to the upregulation of PAR2 and subsequent activation of the intense IL-8 (Montrer IL8 Protéines) release in the esophageal mucosa and initiation of mucosal immune response in GERD.
PAR-2 is expressed basolaterally in airway cells, where it stimulates both intracellular Ca(2 (Montrer CA2 Protéines)+) release and Ca(2 (Montrer CA2 Protéines)+) influx, which activates low-level nitric oxide production, increases apical membrane Cl(-) permeability approximately 3-5-fold, and increases ciliary beating approximately 20-50%.
PAR2 signaling from endosomes underlies the persistent hyperexcitability of nociceptors that mediates chronic pain of irritable bowel syndrome.
PAR2 plays an important role in the proliferation and metastasis of hepatocellular carcinoma.
PAR2 expression is crucial for TGF-beta1 (Montrer TGFB1 Protéines)-induced ERK (Montrer EPHB2 Protéines) activation and cell motility. Functional cooperation of PAR2 and TGF-beta1 (Montrer TGFB1 Protéines) involves a physical interaction between PAR2 and ALK5 (Montrer TGFBR1 Protéines).
Activation of PAR2 inhibits the expression of IL-10 (Montrer IL10 Protéines) in B cells, which can be reversed by treating B cells with Bcl2L12 (Montrer BCL2L12 Protéines) shRNA-carrying liposomes.
High Expressions of PAR2 is associated with cancer.
activation of PAR2 compromises the vascular endothelial barrier function by suppressing the expression of Ve-cadherin (Montrer CDH5 Protéines).
plays a direct role in melanogenesis by increasing stem cell factor (Montrer KITLG Protéines) secretion from keratinocytes
Neutrophil elastase (Montrer ELANE Protéines) enhances IL-12p40 production by lipopolysaccharide-stimulated macrophages via transactivation of the PAR-2/EGFR (Montrer EGFR Protéines)/TLR4 (Montrer TLR4 Protéines) signaling pathway
PAR2 activation in the prostate may contribute to the development of lower urinary tract dysfunction through proinflammatory as well as profibrotic pathways.
Our data show that PAR2 counterbalanced enhanced contractions to ET-1 (Montrer EDN1 Protéines) in aortas from Tsk (Montrer FBN1 Protéines) mice. PAR2 could represent a possible target for novel drugs in the treatment of vascular complications in fibrosis.
thrombin (Montrer F2 Protéines) is increased in a mouse model of cancer cachexia in a partially interleukin-6 (Montrer IL6 Protéines) dependent manner
Data show that activated protein C (Montrer PROC Protéines) signals via protease activated receptors PAR2/PAR3 (Montrer F2RL2 Protéines) to expand Treg cells, mitigating the disease in mice.
PAR2 plays an important and previously unrecognised anti-apoptotic role in T cell development
thrombin (Montrer F2 Protéines) has a role in diet-induced obesity through fibrin-driven inflammation
PAR2 modulation was sufficient to induce islet cell transdifferentiation in the absence of beta-cells.
Our results are suggestive that PAR2 inhibition may play a role in the treatment of diseases with increased inflammatory responses in renal systems
PAR2/GSK3beta is a novel pathway that plays a critical role in the regulation of stem/progenitor cell survival and proliferation in normal colon crypts and colon cancer.
PAR1 and PAR2 regulate endothelial NO synthase phosphorylation and activity through G(12/13) and G(q), delineating the signaling pathways by which the proteases act on protease-activated receptors to modulate endothelial functions.
Coagulation factor II (thrombin) receptor-like 1 (F2RL1) is a member of the large family of 7-transmembrane-region receptors that couple to guanosine-nucleotide-binding proteins. F2RL1 is also a member of the protease-activated receptor family. It is activated by trypsin, but not by thrombin. It is activated by proteolytic cleavage of its extracellular amino terminus. The new amino terminus functions as a tethered ligand and activates the receptor. The F2RL1 gene contains two exons and is widely expressed in human tissues. The predicted protein sequence is 83% identical to the mouse receptor sequence.
Proteinase-activated receptor 2
, G-protein coupled receptor 11
, coagulation factor II receptor-like 1
, protease-activated receptor 2
, proteinase-activated receptor 2
, thrombin receptor-like 1
, Protease-activated receptor-2
, proteinase-activated receptor-2
, Proteinase-activated receptor-2 G protein-coupled receptor 11
, Proteinase-activated receptor-2, G protein-coupled receptor 11