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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 is crucial for TGF-beta1 (Montrer TGFB1 Protéines)-induced cell motility by its ability to sustain expression of ALK5 (Montrer TGFBR1 Protéines). Therapeutically targeting PAR2 may thus be a promising approach in preventing TGF-beta (Montrer TGFB1 Protéines)-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 (Montrer MLXIP Protéines)-205/BMPR1B (Montrer BMPR1B Protéines) pathway in human colorectal carcinoma.
findings showed in intestinal epithelial cells that PAR-2 activation leads to polarized IL-8 (Montrer IL8 Protéines) 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 (Montrer IL8 Protéines) production and can affect proteasome system, particularly when PAR-2 activation was induced in the apical side
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.
Enhanced FXa (Montrer F10 Protéines) and PAR2 exacerbate DN and that both are promising targets for preventing diabetic nephropathy.
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