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The activation of PAR-1 (show MARK2 Proteins) on the cell surface of SGC7901 and AGS (show JAG1 Proteins) cells was significantly reduced after the knockdown of EPCR (show PROCR Proteins). By contrast, blockade of PAR-1 (show MARK2 Proteins) reduced the proliferation and migration of gastric cells in vitro
Our structural data showed subtle changes in the binding pose between Vorapaxar and F16357. Transmembrane helices 1, 2, 5, and 7 were most significantly affected; most notably a large kink at F279(5.47) in TM helix 5 of the Vorapaxar complex was completely absent in the F16357 complex. The results of this study facilitate the future development of other therapeutic PAR1 (show MARK2 Proteins) antagonists.
Platelets were activated in antineutrophil cytoplasmic antibody (ANCA)-associated vasculitis (AAV) patients, and such activation was at least partially attributed to the thrombin (show F2 Proteins)-protease-activated receptors (PARs (show EPRS Proteins)) pathway.
Using protein C (show PROC Proteins)-factor VII (show TH Proteins) chimera demonstrate that APC (show APC Proteins) light chain amino acid residues outside the EPCR (show PROCR Proteins)-binding site enable cytoprotective PAR1 (show MARK2 Proteins) signaling.
Study demonstrated that nerve activation by mucosal biopsy supernatants depends on proteases. This is a common feature of quiescent ulcerative colitis and irritable bowel syndrome (IBS) and may relate to some common gastrointestinal symptoms. However, only proteases in IBS supernatants signal through PAR1 (show MARK2 Proteins).
Data show there was no significant correlation of autoantibodies to coagulation factor II thrombin receptor (F2R; protease-activated receptor 1, PAR1) (PAR1-AB) level with , progression-free (PFS) and overall (OS) survival.
we found that activation of the protease-activated receptor 1 (PAR1) induced secretion of TSLP (show TSLP Proteins) by the corneal stromal cells... we proposed that TSLP (show TSLP Proteins) might function as the link between increased protease activity and inflammatory responses or itch sensation in the
PAR-1 (show MARK2 Proteins) in non-small-cell lung cancer is mainly expressed on cells that constitute the pulmonary tumor microenvironment, including vascular endothelial cells, macrophages and stromal fibroblasts.
thrombin (show F2 Proteins) binding to PAR-1 (show MARK2 Proteins) receptor activated Gi-protein/c (show PROC Proteins)-Src (show SRC Proteins)/Pyk2 (show PTK2B Proteins)/EGFR (show EGFR Proteins)/PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins)/p42/p44 (show PSMC6 Proteins) MAPK (show MAPK3 Proteins) cascade, which in turn elicited AP-1 (show FOSB Proteins) activation and ultimately evoked MMP-9 (show MMP9 Proteins) expression and cell migration in SK-N-SH cells.
this study demonstrates that TGFbeta (show TGFB1 Proteins) is a positive regulator of PAR-1 (show MARK2 Proteins) expression in A549 lung adenocarcinoma cells, which in turn increases the sensitivity of these cells to thrombin (show F2 Proteins) signalling
PAR-1 (show MARK2 Proteins) plays an important role in the development of diabetic nephropathy (DN) and PAR-1 (show MARK2 Proteins) might therefore be an attractive therapeutic target to pursue in DN.
Experimental TCDD-elicited steatohepatitis is associated with coagulation cascade activation and PAR-1 (show MARK2 Proteins)-driven hepatic inflammation and fibrosis.
PAR1 in its inactive unligated state functions as a scaffold for TGFbetaRII to downregulate TGF-beta (show TGFB1 Proteins) signaling, and thereby promote embryonic stem cell transition to functional endothelial cells.
this study shows that poly I:C treated PAR-1 (show MARK2 Proteins)-/- mice given the thrombin (show F2 Proteins) inhibitor dabigatran etexilate exhibited less IFNbeta and CXCL10 (show CXCL10 Proteins) expression in the spleen and plasma
Brain water content in the ipsilateral hemisphere and the tumor mass were significantly lower in PAR-1 (show MARK2 Proteins) KO than WT mice at day 12 after implantation of glioma cells.
The results of this study suggested that polarized microglia occur dynamically after ICH (show ACE Proteins) and that PAR-1 (show MARK2 Proteins) plays a role in the microglia activation and polarization.
In this study, we found upregulation of several hemostasis-related genes, including the thrombin (show F2 Proteins)-activatable receptor PAR-1 (protease-activated receptor-1), in Runx1 (show RUNX1 Proteins)/Cbfb (show CBFB Proteins)-deleted MLL (show MLL Proteins)-AF9 (show MLLT3 Proteins) cells. Similar to the effect of Runx1 (show RUNX1 Proteins)/Cbfb (show CBFB Proteins) deletion, PAR-1 (show MARK2 Proteins) overexpression induced CDKN1A/p21 (show CDKN1A Proteins) expression and attenuated proliferation in MLL (show MLL Proteins)-AF9 (show MLLT3 Proteins) cells
our findings define a detrimental role of thrombin (show F2 Proteins)-activated PAR-1 (show MARK2 Proteins) in wound healing in mice with spinal cord injuries.
thrombin (show F2 Proteins)/PAR-1 (show MARK2 Proteins) interaction regulated MCP-1 (show CPT1B Proteins), TF, MCSF (show CSF1 Proteins) and IL-6 (show IL6 Proteins) production.
Thrombin (show F2 Proteins) upregulates LCN2 (show LCN2 Proteins) through protease-activated receptor-1 activation and causes brain damage.
Thrombin stimulates swine smooth muscle cell differentiation from peripheral blood mononuclear cells via protease-activated receptor-1, RhoA, and myocardin.
Thrombin (show F2 Proteins) induces a sustained contraction in the normal pulmonary artery, by activating PAR(1) and thereby increasing the sensitivity of the myofilament to Ca(2 (show CA2 Proteins)+).
MMP-1 (show MMP1 Proteins) promotes VEGFR2 (show KDR Proteins) expression and proliferation of endothelial cells through stimulation of PAR-1 and activation of NF-kappaB (show NFKB1 Proteins)
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 receptor is a 7-transmembrane receptor involved in the regulation of thrombotic response. Proteolytic cleavage leads to the activation of the receptor. F2R is a G-protein coupled receptor family member.
protease-activated receptor 1
, proteinase-activated receptor 1
, Thrombin receptor
, coagulation factor II receptor
, thrombin receptor
, protease-activated receptor-1
, coagulation factor II (thrombin) receptor