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PAR2 contributes to G-CSF expression in breast cancer cells, possibly favoring tumor progression
Cells with reduced PAR-2 expression showed significantly reduced release of IL-6, TNF-alpha, IL-1beta, and MMP-9 into culture medium in response to acute CTSS, while IL-6, TNF-alpha, and MMP-9 were reduced in culture medium, and IL-6 and MMP-9 in cell lysates, after chronic CTSS.
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 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+) release and Ca(2+) 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-induced ERK activation and cell motility. Functional cooperation of PAR2 and TGF-beta1 involves a physical interaction between PAR2 and ALK5.
Activation of PAR2 inhibits the expression of IL-10 in B cells, which can be reversed by treating B cells with Bcl2L12 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.
plays a direct role in melanogenesis by increasing stem cell factor secretion from keratinocytes
Neutrophil elastase enhances IL-12p40 production by lipopolysaccharide-stimulated macrophages via transactivation of the PAR-2/EGFR/TLR4 signaling pathway
PAR2 is crucial for TGF-beta1-induced cell motility by its ability to sustain expression of ALK5. Therapeutically targeting PAR2 may thus be a promising approach in preventing TGF-beta-dependent driven metastatic dissemination in PDAC and possibly other stroma-rich tumour types.
Protease-activated receptor 2 (PAR2) is present in human skin.
PAR2 signaling promotes cancer cell migration through miR-205/BMPR1B pathway in human colorectal carcinoma.
findings showed in intestinal epithelial cells that PAR-2 activation leads to polarized IL-8 secretion in accordance with the side of PAR-2 activation, apical or basolateral, but do not affect ubiquitin proteasome system; demonstrate that PAR-2 activation leads to an increased IL-8 production and can affect proteasome system, particularly when PAR-2 activation was induced in the apical side
TF-induced microvessel stabilization is regulated via PAR2-SMAD3 that is indispensable for the maintenance of vascular integrity.
PAR-2- and PAR-1-mediated TNF-alpha release from monocytes suggests that these unique protease receptors are involved in the pathogenesis of inflammation.
Results indicate that chymotrypsin-like serine protease enhances soluble fms-like tyrosine kinase 1 production through protease-activated receptor-2 in trophoblast cells and thus plays an important additional role in preeclampsia pathogenesis.
crystal structures of PAR2 in complex with two distinct antagonists and a blocking antibody
High PAR-1 expression is associated with atherogenesis.
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 in aortas from Tsk mice. PAR2 could represent a possible target for novel drugs in the treatment of vascular complications in fibrosis.
thrombin is increased in a mouse model of cancer cachexia in a partially interleukin-6 dependent manner
Data show that activated protein C signals via protease activated receptors PAR2/PAR3 to expand Treg cells, mitigating the disease in mice.
PAR2 plays an important and previously unrecognised anti-apoptotic role in T cell development
thrombin 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.
Enhanced FXa and PAR2 exacerbate DN and that both are promising targets for preventing diabetic nephropathy.
PAR2 is critically important in the pathogenesis of adenine-induced tubular injury
The levels of miR-223, miR-339 and miR-21, which are associated with platelet activation, were elevated in pooled mouse plasma exosomes before thrombosis and enriched in thrombin-stimulated platelet-derived exosomes in vitro.
Neutrophil elastase induced acute inflammation and pain in knee joints of mice. These changes are PAR2-dependent and appear to involve activation of a p44/42 MAPK pathway. Blocking neutrophil elastase, PAR2 and p44/42 MAPK activity can reduce inflammation and pain, suggesting their utility as therapeutic targets.
Reductions in astrogliosis, inflammation and neuromotor recovery observed in protease Activated Receptor 2 knockout mice after spinal cord injury suggests that this receptor and its agonists represent new drug targets to foster neuromotor recovery.
Stimulation of PAR-2 activates Nf-kappaB signaling, resulting in RelA nuclear translocation and enhanced expression of pro-inflammatory mRNAs in oral squamous cell carcinoma.
Tryptase and protease-activated receptor-2 stimulate scratching behavior in a murine model of ovalbumin-induced atopic-like dermatitis
This study reveals, for the first time, an important role for PAR2 in allergic lung inflammation
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