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Neutrophil elastase (show ELANE Proteins) enhances IL-12p40 production by lipopolysaccharide-stimulated macrophages via transactivation of the PAR-2/EGFR (show EGFR Proteins)/TLR4 (show TLR4 Proteins) signaling pathway
PAR2 is crucial for TGF-beta1 (show TGFB1 Proteins)-induced cell motility by its ability to sustain expression of ALK5 (show TGFBR1 Proteins). Therapeutically targeting PAR2 may thus be a promising approach in preventing TGF-beta (show TGFB1 Proteins)-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 (show MLXIP Proteins)-205/BMPR1B (show BMPR1B Proteins) pathway in human colorectal carcinoma.
findings showed in intestinal epithelial cells that PAR-2 activation leads to polarized IL-8 (show IL8 Proteins) 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 (show IL8 Proteins) 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 (show SMAD3 Proteins) that is indispensable for the maintenance of vascular integrity.
PAR-2- and PAR-1 (show MARK2 Proteins)-mediated TNF-alpha (show TNF Proteins) release from monocytes suggests that these unique protease receptors are involved in the pathogenesis of inflammation.
Results indicate that chymotrypsin-like serine protease (show F2 Proteins) enhances soluble fms-like tyrosine kinase 1 (show FLT1 Proteins) 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
PAR-2 plays an important role in the progression of ovarian clear cell carcinoma.
Data show that activated protein C (show PROC Proteins) signals via protease activated receptors PAR2/PAR3 (show F2RL2 Proteins) to expand Treg cells, mitigating the disease in mice.
PAR2 plays an important and previously unrecognised anti-apoptotic role in T cell development
thrombin (show F2 Proteins) 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 (show F10 Proteins) 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 (show MLXIP Proteins)-223, miR (show MLXIP Proteins)-339 and miR (show MLXIP Proteins)-21, which are associated with platelet activation, were elevated in pooled mouse plasma exosomes before thrombosis and enriched in thrombin (show F2 Proteins)-stimulated platelet-derived exosomes in vitro.
Neutrophil elastase (show ELANE Proteins) induced acute inflammation and pain in knee joints of mice. These changes are PAR2-dependent and appear to involve activation of a p44 (show GTF2H4 Proteins)/42 MAPK (show MAPK1 Proteins) pathway. Blocking neutrophil elastase (show ELANE Proteins), PAR2 and p44 (show GTF2H4 Proteins)/42 MAPK (show MAPK1 Proteins) activity can reduce inflammation and pain, suggesting their utility as therapeutic targets.
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