In addition to regulating platelet function, the G protein-coupled sub-family member Proteinase-activated receptor-1 (PAR1) has a proposed role in the development of various cancers, but its exact role and mechanism of action in the invasion, metastasis, and proliferation process in gastric cancer have yet to be completely elucidated. Here, we analyzed the relationship between PAR1 activation, proliferation, invasion, and the signaling pathways downstream of PAR1 activation in gastric cancer. We established a PAR1 stably transfected MKN45 human gastric cancer cell line (MKN45/PAR1) and performed cell proliferation and invasion assays employing this cell line and MKN28 cell line exposed to PAR1 agonists (α-thrombin and TFLLR-NH2). We also quantified NF-κB activation by electrophoretic mobility shift assay (EMSA) and the level of Tenascin-C (TN-C) expression in conditioned medium by ELISA of MKN45/PAR1 following administration of α-thrombin. A high molecular weight concentrate was derived from the
The proteinase-activated receptor 1 (PAR-1) plays a central role in melanoma progression and its expression level is believed to correlate with the degree of cancer invasiveness.
Ramachandran R, Hyun E, Zhao L, Lapointe TK, Chapman K, Hirota CL, Ghosh S, McKemy DD, Vergnolle N, Beck PL, Altier C, Hollenberg MD. TRPM8 activation attenuates inflammatory responses in mouse models of colitis. Proc Natl Acad Sci U S A. 110:7476-7481, 2013.. Fernández-Blanco JA, Hollenberg MD, Martínez V, Vergara P. PAR-2-mediated control of barrier function and motility differs between early and late phases of postinfectious gut dysfunction in the rat. Am J Physiol Gastrointest Liver Physiol. 304(4):G390-400, 2013.. Hollenberg MD. Mentors And The Butterfly Effect: Triggers For Discovering Signalling by Proteinases via Proteinase-Activated Receptors (PARs) And More. Clin Invest Med. 2012 Feb 1;35(6):E378.. Nichols HL, Saffeddine M, Theriot BS, Hegde A, Polley D, El-Mays T, Vliagoftis H, Hollenberg MD, Wilson EH, Walker JK, DeFea KA. β-Arrestin-2 mediates the proinflammatory effects of proteinase-activated receptor-2 in the airway. Proc Natl Acad Sci U S A. 109:16660-16665, 2012.. Russell ...
Receptor for trypsin and trypsin-like enzymes coupled to G proteins. Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho. Can also be transactivated by cleaved F2R/PAR1. Involved in modulation of inflammatory responses and regulation of innate and adaptive immunity, and acts as a sensor for proteolytic enzymes generated during infection. Generally is promoting inflammation. Can signal synergistically with TLR4 and probably TLR2 in inflammatory responses and modulates TLR3 signaling. Has a protective role in establishing the endothelial barrier; the activity involves coagulation factor X. Proposed to have a bronchoprotective role in airway epithelium, but also shown to compromise the airway epithelial barrier by interrupting E-cadherin adhesion. Involved in the regulation of vascular tone; activation results in hypotension presumably mediated ...
An excess of proteinase receptors in the brain aggravates demyelination in multiple sclerosis (MS), suggest Noorbakhsh and colleagues on page 425. Mice lacking proteinase-activated receptor-2 (PAR2), they show, are protected from the brain damage characteristic of experimental autoimmune encephalomyelitis (EAE), a model of MS.. PAR2, a G protein-coupled receptor activated by trypsin-like serine proteases, is best known as the primary pain receptor in the peripheral nervous system. But this receptor is also expressed on smooth muscle cells in the gut, where it stimulates muscle contraction, and on neurons and glial cells in the brain, where it is proposed to promote cell growth and survival.. This versatile receptor can also help promote inflammation. Indeed, activation of PAR2 on skin cells triggers the production of inflammatory cytokines, and PAR2-deficient mice are protected against allergic dermatitis. Noorbakhsh and colleagues now show that PAR2 also enhances inflammation in the ...
F2RL3 / PAR-4 antibody (coagulation factor II (thrombin) receptor-like 3) for IHC-P. Anti-F2RL3 / PAR-4 pAb (GTX71163) is tested in Human samples. 100% Ab-Assurance.
NIH Funding Opportunities and Notices in the NIH Guide for Grants and Contracts: Gut Microbiota-Derived Factors in the Integrated Physiology and Pathophysiology of Diseases within NIDDKs Mission (R01) PAR-13-293. NIDDK
NIH Funding Opportunities and Notices in the NIH Guide for Grants and Contracts: Revision Applications to U01 Awards on Detection of Pathogen-Induced Cancer (DPIC) (U01) PAR-13-173. NCI
Abstract: : Purpose: Proteinase-activated receptors (PARs) are a recently described, novel family of G-protein-coupled receptors, which are activated by the cleavage of their N-terminal domain by serine proteases. These receptors are activated by serine proteases such as trypsin and thrombin released after tissue inflammation and injury. In this study we determined if human corneal cells express functional PAR-1 and PAR-2 receptors and examined the effects of receptor activation on corneal proinflammatory cytokine production. Methods: Human primary corneal epithelial cells (HCEC) and the human corneal epithelial cell line HCE-T were cultured to 80% confluence and then exposed to 10 nM thrombin, 100 M human PAR-1 peptide agonist TFLLRN-NH2, 10 nM trypsin, and 100 M murine PAR-2 peptide agonist SLIGRL-NH2 for 3, 6 and 24 hours. Cells treated with PMA (50ng/ml) and TNF-α-treated (10ng/ml) cells served as positive controls for these studies. PAR-1 and PAR-2 mRNA levels were determined by RT-PCR and ...
Author(s): Min, Jungah | Advisor(s): DeFea, Kathryn A | Abstract: β-arrestins, originally discovered in the context of G protein-coupled receptor (GPCR) desensitization and internalization, also function in signaling of these receptors independently of G protein coupling. These novel functions involve the roles for β-arrestins as scaffolds. It has been reported that β-arrestins interact with a number of binding partners including trafficking proteins, cytosolic kinases, cytoskeletal proteins, and non-receptor tyrosine kinase. Downstream of protease-activated receptor-2 (PAR-2), β-arrestin scaffolds the components of the ERK cascade, Raf-1, MEK1, and ERK1/2 with the receptor at the plasma membrane, leading to activation of cytoplasmic/membrane ERK1/2 signaling independent of G-protein coupling. Furthermore, we previously demonstrated that stimulation of PAR-2 resulted in prolonged activation of ERK1/2 in pseudopodia in a β-arrestin-dependent manner and β-arrestins were required in PAR-2 mediated
Proteinase-activated receptor-1 (PAR1), a G protein-coupled receptor activated by thrombin, is highly expressed in different cell types of the gastrointestinal tract. The activity of thrombin and of other proteinases is significantly increased in the colon of inflammatory bowel disease (IBD) patients. Since PAR1 activation in tissues other than the gut provoked inflammation, we hypothesized that PAR1 activation in the colon is involved in the pathogenesis of IBD. Here, we demonstrate that PAR1 is overexpressed in the colon of IBD patients. In mice, intracolonic administration of PAR1 agonists led to an inflammatory reaction characterized by edema and granulocyte infiltration. This PAR1 activation-induced inflammation was dependent on B and T lymphocytes. Moreover, PAR1 activation exacerbated and prolonged inflammation in a mouse model of IBD induced by the intracolonic administration of trinitrobenzene sulfonic acid (TNBS), while PAR1 antagonism significantly decreased the mortality and severity ...
Partitioning defective 3 (Par-3), a crucial component of partitioning-defective complex proteins, controls cell polarity and contributes to cell migration and cancer cell epithelial-to-mesenchymal transition. However, the clinical relevance of Par-3 in tumor progression and metastasis has not been well elucidated. In this study, we investigated the impact and association of Par-3 expression and clinical outcomes with hepatocellular carcinoma (HCC). We first confirmed that Par-3 was abundantly expressed in HCC cell lines by Western blot analysis. We used immunohistochemistry to analyze the association of Par-3 expression and clinicopathological characteristics in primary and subsequent metastatic tumors of patients with HCC. Par-3 was overexpressed in 47 of 111 (42.3%) primary tumors. Increased expression of Par-3 in primary tumors predicted an increased five-year cumulative incidence of extrahepatic metastasis. In addition, multivariate analysis revealed that Par-3 overexpression was an independent
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Background The Protease-Activated Receptor 1 (PAR1) is activated by the proteolytic release of the N-terminal 41 amino acids. Exogenously administered PAR1(1- 41) peptides protect against myocardial ischemia and reperfusion injury in the rat. In the present study, we determined whether PAR1(1-26), the putative signal peptide of PAR1 contains the functional domain of PAR1(1- 41).. Methods and Results We assessed the protective role of a synthesized PAR1(1-26) peptide in an in vivo rat model of myocardial regional ischemia and reperfusion injury (n=6/group). PAR1(1-26) (0.01-10 μg/kg) treatment immediately before ischemia reduced infarct size from 58±1% to 13±1% area at risk (p,0.01) at an optimal dose of 10 μg/kg. Treatment with PAR1(1-26) after the onset of reperfusion decreased infarct size to 22±1% area at risk (p,0.01). We then explored the survival pathways known to be up-regulated by pharmacologic cardioprotectants. Inhibition of Gi proteins (pertussis toxin), PI3K/Akt (Wortmannin), ...
The generation of asymmetry in the one-cell embryo of Caenorhabditis elegans is necessary to establish the anterior-posterior axis and to ensure the proper identity of early blastomeres. Maternal-effect lethal mutations with a partitioning defective phenotype (par) have identified several genes involved in this process. We have identified a new gene, par-6, which acts in conjunction with other par genes to properly localize cytoplasmic components in the early embryo. The early phenotypes of par-6 embryos include the generation of equal-sized blastomeres, improper localization of P granules and SKN-1 protein, and abnormal second division cleavage patterns. Overall, this phenotype is very similar to that caused by mutations in a previously described gene, par-3. The probable basis for this similarity is revealed by our genetic and immunolocalization results; par-6 acts through par-3 by localizing or maintaining the PAR-3 protein at the cell periphery. In addition, we find that loss-of-function ...
Par 1 | Protease-activated receptor 1 stimulate phosphoinositide hydrolysis. Specific for platelets and vascular endothelial cells. Alternative names: Coagulation factor II receptor, Thrombin receptor. AS10 1572, P25116
PARs (protease-activated receptors) are a subfamily of related G protein-coupled receptors that are activated by cleavage of part of their extracellular domain. They are highly expressed in platelets, and also on endothelial cells, myocytes and neurons.
Protease-activated receptor-2 (PAR2) is a G protein-coupled receptor abundantly expressed in the kidney. The aim of this study was to profile inflammatory gene and protein expression induced by PAR2 activation in human kidney tubular epithelial cells (HTEC). A novel PAR2 antagonist, GB88, was used to confirm agonist specificity. Intracellular Ca(2+) (iCa(2+)) mobilization, confocal microscopy, gene expression profiling, qRTPCR, and protein expression were used to characterize PAR2 activation. PAR2 induced a pronounced increase in iCa(2+) concentration that was blocked by the PAR2 antagonist. Treatment with SLIGKV-NH2 at the apical or basolateral cell surface for 5 h induced expression of a range of inflammatory genes by greater than fourfold, including IL-1β, TRAF1, IL-6, and MMP-1, as assessed by cDNA microarray and qRTPCR analysis. Using antibody arrays, GM-CSF, ICAM-1, TNF-α, MMP-1, and MMP-10 were among the induced proteins secreted. Cytokine-specific ELISAs identified three- to sixfold increases
Proteinase-activated receptors (PARs) are a class of G-protein-coupled receptors which are involved in various physiological and pathophysiological processes. The new product monograph PAR-Activating-Peptides gives you an overview of Bachem´s PAR-activating-peptides and analogs useful for studying receptor function ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a member of the protease-activated receptor (PAR) family which is a subfamily of the seven transmembrane G protein-coupled cell surface receptor family. The encoded protein acts as a cofactor in the thrombin-mediated cleavage and activation of the protease-activated receptor family member PAR4. The encoded protein plays an essential role in hemostasis and thrombosis. Alternate splicing results in multiple transcript variants that encode different isoforms. [provided by RefSeq, Feb 2012 ...
In the present study, we have demonstrated that PAR-3 knockdown results in a delay of VAC exocytosis and leads eventually to mislocalization of the apical membrane in both 2D monolayers and 3D cysts of MDCK cells. VACs were originally defined in MDCK cells cultured under non-physiological conditions that prevented the formation of cell-cell contacts (Vega-Salas et al., 1987). However, similar intracellular vacuoles have been described under normal culture conditions not only in vitro (Bayless and Davis, 2002; Folkman and Haudenschild, 1980) but also in vivo (Kamei et al., 2006). These observations suggest that the formation of easily detected VACs represents the normal process of lumen formation, in which smaller short-lived vacuoles are used to build the luminal surface of epithelial cells (Lakkaraju and Rodriguez-Boulan, 2007; Mostov and Martin-Belmonte, 2006). Here, we observed that aPKC and PAR-6, but not PAR-3, accumulated on VACs and were targeted to the PAR-3-containing regions in ...
History The upregulation of matrix metalloproteinase-1 (MMP-1) continues to be proven correlated with lymph node metastasis of nasopharyngeal carcinoma (NPC) as the activation of protease-activated receptor-1 (PAR-1) mediates proliferation and invasion of NPC cells. in 190 (71.43%) and 182 (68.42%) from the 266 NPC sufferers. Furthermore the mixed MMP-1 and PAR-1 appearance was significantly connected with advanced T-stage (= 0.01) advanced clinical stage (= 0.002) positive recurrence (= 0.01) and metastatic position (= 0.01) of NPC. Furthermore the overall success in NPC sufferers MAP3K8 with MMP-1 and PAR-1 dual overexpression was considerably shorter than in people that have dual low appearance (< 0.001). Furthermore the multivariate analyses indicated the fact that mixed MMP-1 and PAR-1 overexpression was an unbiased prognostic aspect for overall success (= 0.001) in NPC sufferers however the upregulation of MMP-1 and PAR-1 alone is at each case no independent prognostic aspect because of ...
1. van der Merwe, J. Q., Moreau, F., and MacNaughton, W. K. Protease-activated receptor-2 stimulates intestinal SCBN epithelial chloride transport through activation of PLC and selective PKC isoforms. Am J Physiol Gastrointest Liver Physiol, 296: G1258-1266, 2009. 2. van der Merwe, J. Q., Ohland, C. L., Hirota, C. L., and MacNaughton, W. K. Prostaglandin E2 derived from cyclooxygenases 1 and 2 mediates intestinal SCBN epithelial ion transport stimulated by the activation of protease-activated receptor 2. J Pharmacol Exp Ther, 329: 747-752, 2009. 3. Dong, X., Smoll, E. J., Ko, K. H., Lee, J., Chow, J. Y., Kim, H. D., Insel, P. A., and Dong, H. P2Y receptors mediate Ca2+ signaling in duodenocytes and contribute to duodenal mucosal SCBN bicarbonate secretion. Am J Physiol Gastrointest Liver Physiol, 296: G424-432, 2009. 4. Buret, A. and Lin, Y. C. Genotypic characterization of an epithelial cell line SCBN for the study of parasite-epithelial interactions. J Parasitol, 94: 545-548, 2008. 5. Smith, ...
A class of receptors that are activated by the action of PROTEINASES. The most notable examples are the THROMBIN RECEPTORS. The receptors contain cryptic ligands that are exposed upon the selective proteolysis of specific N-terminal cleavage sites ...
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Mast cells contribute to tissue repair in fibrous tissues by stimulating proliferation of fibroblasts through the release of tryptase which activates protease-activated receptor-2 (PAR-2). The possibility that a tryptase/PAR-2 signaling pathway exists in skeletal muscle cell has never been investigated. The aim of this study was to evaluate whether tryptase can stimulate myoblast proliferation and determine the downstream cascade. Proliferation of L6 rat skeletal myoblasts stimulated with PAR-2 agonists (tryptase, trypsin and SLIGKV) was assessed. The specificity of the tryptase effect was evaluated with a specific inhibitor, APC-366. Western blot analyses were used to evaluate the expression and functionality of PAR-2 receptor and to assess the expression of COX-2. COX-2 activity was evaluated with a commercial activity assay kit and by measurement of PGF2α production. Proliferation assays were also performed in presence of different prostaglandins (PGs). Tryptase increased L6 myoblast proliferation
Tissue factor (TF)-mediated protease-activated receptor (PAR)-2 signaling is associated with a promigratory, invasive and proangiogenic phenotype in experimental models of breast cancer and has been mechanistically coupled to phosphorylation of the TF cytoplasmic domain (pTF). However, the clinical relevance of these findings is unknown. Here, we provide the first in vivo evidence of TF phosphorylation in experimental as well as clinical breast cancer tumors. pTF was demonstrated in MDA-MB-231 xenografts and in tumors from the MMTV-PyMT transgene model of spontaneous murine breast adenocarcinoma. Tumors from PAR-2-deficient transgenic mice were negative for pTF, thus linking pTF to PAR-2 signaling. The clinical correlation between TF, pTF, PAR-1, PAR-2 and vascular endothelial growth factor (VEGF)-A was determined by immunohistochemistry on tumors from a cohort of 172 consecutive primary breast cancer patients, with a median follow-up time of 50 months. In 160 evaluable patient tumors, pTF was ...
TY - CONF. T1 - Protease-activated receptor-2 expression by oral epithelial cells is required for bone loss associated with periodontal disease. AU - Francis, Nidhish. AU - Ayodele, Babatunde. AU - Pike, Rob. AU - Pagel, Charles. AU - Mackie, Eleanor. PY - 2017/6/18. Y1 - 2017/6/18. M3 - Abstract. ER - ...
Protease-activated receptor-2 (PAR2) is activated by proteases, such as trypsin, human mast cell beta-tryptase, human kallikrein isoforms, coagulation factors VIIa and Xa, etc. PAR2 is believed to have an important role under inflammatory pathological conditions, but its role in metabolic syndrome remains uncertain. We have reported that PAR2-activating peptide, 2-furoyl-LIGRLO-amide (2fly) causes NO-mediated vasorelaxation in rat aortas similar to that observed with acetylcholine (ACh), and that 2fly-induced vasorelaxation is maintained in aortas from SHRSP.Z-Leprfa/IzmDmcr (SHRSP.ZF) rats with metabolic syndrome, even though ACh- and sodium nitroprusside (SNP)-induced vasodilation is lower than that in control (Wistar-Kyoto rats, WKY). In this study, we assessed the mechanisms involved in the preservation of PAR2-mediated vasorelaxation in metabolic syndrome.. Aortas were isolated from male WKY and SHRSP.ZF rats between 18-20 weeks of age. ACh- and 2fly-induced vasorelaxations were measured in ...
Mechanical strain on the artery wall is increased up to 30% in hypertension and is postulated to play a role in vascular injury.2-5 Thrombin is concentrated in vivo at sites of vascular injury, and its effects are mediated chiefly through PAR-1.21 PAR-1 is expressed at very low levels in normal arteries but increases after vascular injury12,18,22 and is increased in the arteries of hypertensive rats.11 Thus, we hypothesized that cyclic strain administered to VSMCs in vitro would increase PAR-1 expression.. Cyclic strain increased PAR-1 mRNA and protein levels (Figures 1 and 2⇑), and after 48 hours of cyclic strain, thrombin also produced a 50% increase in cell number (Figure 3). The significance of these findings is based on the opposite responses of PAR-1 expression to cyclic strain and shear stress. PAR-1 expression increases 2-fold under 20% cyclic strain for 24 hours, whereas it decreases by ≈4-fold under shear stress (25 dyne/cm2) for 24 hours.14 Thus, mechanical forces regulate the ...
The traditional view on the role of serine proteases in tumor biology has changed with the recent discovery of a family of protease-activated receptors (PARs). In this study we explored the expression and functional role of the thrombin receptor PAR-1 in human colon cancer cells. Reverse transcripta …
G protein-coupled receptors (GPCRs) are well recognized as being able to activate several signaling pathways through the activation of different G proteins as well as other signaling proteins such as beta-arrestins. Therefore, understanding how such multiple GPCR-mediated signaling can be integrated constitute an important aspect. Here, we applied bioluminescence resonance energy transfer (BRET) to shed more light on the G protein coupling profile of trypsin receptor, or protease-activated receptor 2 (PAR2), and its interaction with beta-arrestin1. Using YFP and Rluc fusion constructs expressed in COS-7 cells, BRET data revealed a pre-assembly of PAR2 with both Galphai1 and Galphao and a rapid and transient activation of these G proteins upon receptor activation. In contrast, no preassembly of PAR2 with Galpha12 could be detected and their physical association can be measured with a very slow and sustained kinetics similar to that of beta-arrestin1 recruitment. These data demonstrate the coupling of
Protease-activated receptors (PAR)-1 and -4 are the principal receptors for thrombin-mediated platelet activation. Functional genetic variation has been described in the human PAR1 gene, but not in the PAR4 gene (F2RL3). We sought to identify variants in and around F2RL3 and to determine their association with perioperative myocardial injury (PMI) after coronary artery bypass graft surgery. We further explored possible mechanisms for F2RL3 single nucleotide polymorphism (SNP) associations with PMI including altered receptor expression and platelet activation. Twenty-three SNPs in the F2RL3 gene region were genotyped in two phases in 934 Caucasian subjects. Platelets from 43 subjects (23 major allele, 20 risk allele) homozygous for rs773857 (SNP with the strongest association with PMI) underwent flow cytometry to assess PAR4 receptor number and response to activation by a specific PAR4 activating peptide (AYPGKF) measured by von Willebrand factor (vWf) binding and P-selectin release and PAC-1 ...
Proteinase-activated receptor 1 (PAR1) also known as Protease-activated receptor 1 or coagulation factor II (thrombin) receptor is a protein that in humans is encoded by the F2R gene. PAR1 is a G protein-coupled receptor involved in the regulation of thrombotic response. Proteolytic cleavage leads to the activation of the receptor. PAR-1 has multifaceted effects and plays a key role in mediating the interplay between coagulation and inflammation, which is important in the pathogenesis of inflammatory and fibrotic lung diseases. It is involved both in disruption and maintaining of endothelial barrier integrity, through interaction with either thrombin or activated protein C, respectively. Several selective antagonists for the PAR1 receptor have been developed, for use as anti-clotting agents for the treatment of heart disease. SCH-530,348 SCH530348 has been recently shown to attenuate the neutrophilic inflammatory response to Streptococcus pneumoniae by reducing levels of pro-inflamamtory ...
The importance of MCP-1 for mononuclear cell recruitment has been shown in various animal models of disease (9-13). Our results confirm that peritoneal MΦ recruitment after thioglycollate is significantly reduced in MCP-1 KO mice, and we demonstrate for the first time the importance of this chemokine for NK cell and MΦ recruitment during acute humoral rejection. By performing the transplant study in a xenogeneic model, it was possible to differentiate between MCP-1 made by donor tissue from that made by recipient. Only the former was associated with infiltration into rejecting hearts.. Results from complimentary but distinct experimental approaches, using either WT or PAR-1 KO hearts transplanted into defibinogenated rats or CD31-Hir-Tg hearts transplanted into unmanipulated rats, showed that PAR-1 activation on donor cells was necessary to generate sufficient quantities of donor MCP-1 to promote leukocyte infiltration. Similarly, MCP-1 generation and MΦ recruitment into the inflamed ...
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0104 is needed to induce significant PAR-4 expression. As it is unlikely to accumulate such a high concentration of the allergens in the body, upregulated PAR-1 and PAR-4 expression should not play an important role in cockroach allergy. In contrast, Per a 1.0101-induced upregulation of expression of PAR-2 may be involved in cockroach allergy as only 100 ng/ml. of Per a 1.0101 is required to induce significant increase in PAR-2 expression. Activation of PAR-2 has been recognized to play an important role in allergic diseases. Patients with asthma express an increased amount of PAR-2 on respiratory epithelial cells [20], and PAR-2 activation in human airways is associated with contraction learn more Obeticholic Acid of human airways and contributes to the hyperplasia and hyper-responsiveness evident in the asthmatic airway [21]. Furthermore, our results indicate that Per a 1.0101 and Per a 1.0104 are not proteases. Therefore, their actions on PARs should not depend on enzymatic activity. Once ...
臺大位居世界頂尖大學之列,為永久珍藏及向國際展現本校豐碩的研究成果及學術能量,圖書館整合機構典藏(NTUR)與學術庫(AH)不同功能平台,成為臺大學術典藏NTU scholars。期能整合研究能量、促進交流合作、保存學術產出、推廣研究成果。. To permanently archive and promote researcher profiles and scholarly works, Library integrates the services of "NTU Repository" with "Academic Hub" to form NTU Scholars.. ...
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Principal Investigator:KATAOKA Kazuo, Project Period (FY):2002 - 2005, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Cerebral neurosurgery
Aberrant phosphorylation of tau protein is associated with a number of neurodegenerative disorders. The molecular mechanism by which tau phosphorylation is regulated under physiological and pathological conditions is not understood. Here we show that phosphorylation of a conserved T408 residue in the activation loop of the kinase domain of PAR-1, an established tau kinase, is critical for its activity. Mutations that render this site unphosphorylatable abolished the biological activity of PAR-1 and its biochemical activity in phosphorylating tau. Using a combination of biochemical and genetic analyses, we found that the tumor suppressor protein LKB1 is an upstream activating kinase that acts on the T408 site of PAR-1. Consistent with LKB1 acting upstream of PAR-1, we found that LKB1 promotes tau phosphorylation at PAR-1-dependent sites and that tauS2A, which is nonphosphorylatable by PAR-1, blocked the effect of LKB1 on tau toxicity.. Our results also demonstrate that PAR-1 activation and tau ...
Luo, W., Wang, Y., Hanck, T., Stricker, R. and Reiser, G. (2006) JAB1, A Novel Protease-Activated Receptor-2 (PAR-2) - Interacting Protein Is Involved in PAR-2-Induced Activation of AP-1. J. Biol. Chem. Papers in press. Published on January 12, 2006 as Manuscript M510784200 ...
heart attack or blockages in the arteries to the legs.. Zontivity is the first in a new class of drug, called a protease-activated receptor-1 (PAR-1) antagonist. It is an anti-platelet agent, designed to decrease the tendency of platelets to clump together to form a blood clot. By decreasing the formation of blood clots, Zontivity decreases the risk of heart attack and stroke.. Like other drugs that inhibit blood clotting, Zontivity increases the risk of bleeding, including life-threatening and fatal bleeding. Bleeding is the most commonly reported adverse reaction in people taking Zontivity. The drugs prescribing information (label) includes a Boxed Warning to alert health care professionals about this risk.. http://www.fda.gov/NewsEvents/Newsroom/PressAnnouncements/ucm396585.htm. ...
Platelets are central to thrombus formation, the leading cause of global mortality. PAR4 (protease-activated receptor 4) is a G-protein coupled receptor. Meanwhile, PAR4 together with PAR1 is responsible for thrombin-mediated…. Read More Read More. ...
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The Italian minister of health, Livia Turco, has announced that she will make use of an administrative procedure to change the tough drug law passed through par...