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