Search results for "Protease-activated receptor 2"

showing 10 items of 11 documents

Macrophage protease-activated receptor 2 regulates fetal liver erythropoiesis in mice.

2020

AbstractDeficiencies in many coagulation factors and protease-activated receptors (PARs) affect embryonic development. We describe a defect in definitive erythropoiesis in PAR2-deficient mice. Embryonic PAR2 deficiency increases embryonic death associated with variably severe anemia in comparison with PAR2-expressing embryos. PAR2-deficient fetal livers display reduced macrophage densities, erythroblastic island areas, and messenger RNA expression levels of markers for erythropoiesis and macrophages. Coagulation factor synthesis in the liver coincides with expanding fetal liver hematopoiesis during midgestation, and embryonic factor VII (FVII) deficiency impairs liver macrophage development…

0301 basic medicinemedicine.medical_specialtyBiologyThrombosis and Hemostasis03 medical and health sciencesMice0302 clinical medicineHepcidinInternal medicinemedicineMacrophageAnimalsReceptor PAR-2ErythropoiesisProtease-activated receptor 2Mice KnockoutFetusMacrophagesHematologymedicine.diseaseHemolysisHaematopoiesis030104 developmental biologyEndocrinologymedicine.anatomical_structureLiver030220 oncology & carcinogenesisbiology.proteinErythropoiesisBone marrowBlood advances
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High density of tryptase-positive mast cells in human colorectal cancer: a poor prognostic factor related to protease-activated receptor 2 expression

2013

Tryptase(+) mast cells (MCs), abundant in the invasive front of tumours, contribute to tissue remodelling. Indeed, protease-activated receptor- 2 (PAR-2) activation by MC-tryptase is considered an oncogenic event in colorectal cancer (CRC). Recently, we have suggested NHERF1 as a potential new marker in CRC. In this study, we aimed to determine the distribution of tryptase(+) MCs and PAR-2 and to examine the relationship between PAR-2 and NHERF1, investigating their reputed usefulness as tumour markers. We studied a cohort of 115 CRC specimens including primary cancer (C) and adjacent normal mucosa (NM) by immunohistochemical double staining, analyzing the protein expression of MC-tryptase,…

AdultMaleCytoplasmPathologymedicine.medical_specialtySodium-Hydrogen ExchangersColorectal cancerLymphovascular invasionSettore MED/06 - Oncologia MedicainvasivenesstryptasePAR-2Cell CountTryptaseModels BiologicalImmunophenotypingNHERF1Intestinal mucosamedicineHumansReceptor PAR-2Mast CellsIntestinal Mucosaprognostic factorProtease-activated receptor 2AgedAged 80 and overbiologyColorectal cancer PAR-2 mast cell tryptase NHERF1 prognostic factor invasiveness aggressivenessOriginal ArticlesCell BiologyaggressivenessMiddle AgedPhosphoproteinsPrognosismedicine.diseaseMast cellColorectal cancermedicine.anatomical_structurebiology.proteinMolecular MedicineImmunohistochemistryFemaleTryptasesmast cellColorectal Neoplasms
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Homodimeric murine interleukin-3 agonists indicate that ligand dimerization is important for high-affinity receptor complex formation.

1994

Homodimeric murine interleukin 3 (mIL-3) agonists were generated by intermolecular cystine-bonding. Steady-state binding assays and association kinetics performed at 4 degrees C using these agonists revealed specific binding to both the high- and low-affinity receptor. DSS-mediated crosslinking studies performed at 4 degrees C with agonist concentrations compatible with high-affinity receptor complex formation allowed to detect protein complexes of the alpha chain, the beta chain(s) and the high-affinity receptor complex migrating with apparent molecular weights of 90 kDa, 140 kDa, and above 180 kDa, respectively. In contrast, monomeric mIL-3 was crosslinked to the alpha chain receptor only…

AgonistReceptor complexmedicine.drug_classMacromolecular SubstancesClinical BiochemistryInterleukin-17 receptorLigandsProtein Structure SecondaryCell LineMiceEndocrinologymedicineAnimalsReceptorProtease-activated receptor 2Interleukin 3Cell Line TransformedMolecular massChemistryGranulocyte-Macrophage Colony-Stimulating FactorCell BiologyLigand (biochemistry)Receptors Interleukin-3Recombinant ProteinsKineticsBiochemistryCystineBiological AssayElectrophoresis Polyacrylamide GelInterleukin-3Interleukin-5Cell DivisionThymidineGrowth factors (Chur, Switzerland)
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Isolation of the Endothelin B Receptor from Bovine Lung Structure, Signal Sequence, and Binding Site

1995

Bovine lung endothelin-B receptor has been isolated in good yield with a new procedure involving the use of endothelin-1 coupled to iminobiotin with a long spacer and avidin-agarose affinity chromatography. Contrary to previous reports, evidence has been obtained that the native form of this receptor corresponds to the full-length transcript expected on the basis of cDNA clones. The binding of endothelin to a variety of shortened fragments of the full receptor suggests that the long N-terminal sequence of this receptor has very little influence on the binding of endothelin and that the main determinants of the endothelin binding site might be constituted by residues in the sixth, and possib…

Binding SitesDNA ComplementaryEndothelin receptor type AReceptors EndothelinEndothelinsMolecular Sequence DataBiologyReceptor Endothelin BBiochemistryEndothelin 1Molecular biologyChromatography AffinityBiochemistrycardiovascular systemEnzyme-linked receptorAnimalsCattleElectrophoresis Polyacrylamide Gel5-HT5A receptorAmino Acid SequenceBinding siteGABBR1Endothelin receptorLungProtease-activated receptor 2European Journal of Biochemistry
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Role of the protein C receptor in cancer progression

2014

The hemostatic system plays pleiotropic roles in cancer progression by shaping the tumor microenvironment and metastatic niches through thrombin-dependent fibrin deposition and platelet activation. Expanding experimental evidence implicates coagulation protease receptors expressed by tumor cells as additional players that directly influence tumor biology. Pro-angiogenic G protein-coupled signaling of TF through protease activated receptor 2 and regulation of tumor cell and vascular integrins through ligation by alternative spliced TF are established pathways driving tumor progression. Our recent work shows that the endothelial protein C receptor (EPCR), a stem cell marker in hematopoietic, …

Endothelial protein C receptorTumor microenvironmentCD30Endothelial Protein C ReceptorBreast NeoplasmsReceptors Cell SurfaceHematologyBiologyStem cell markerArticleAntigens CDTumor progressionCancer stem cellDisease ProgressionTumor MicroenvironmentCancer researchAnimalsHumansFemalePlatelet activationBlood CoagulationProtease-activated receptor 2Signal TransductionThrombosis Research
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Subtype-specific endothelin-A and endothelin-B receptor desensitization correlates with differential receptor phosphorylation.

1998

In the rat cardiovascular system endothelin-1 (ET-1) elicits prolonged physiologic responses mediated by the ET A receptor, whereas the effects mediated by the ET B receptor are transient. The molecular mechanisms for the subtype-specific responses are not yet clear. However, post-translational modifications such as phosphorylation and palmitoylation may play an important role. In Sf9 cells overexpressing the human ET A and ET B receptors, both subtypes are palmitoylated. However, only the ET B but not the ET A receptor is phosphorylated in a ligand-dependent manner. Because phosphorylation is believed to play an important role in ligand-dependent receptor inactivation, we analyzed whether …

Endothelin Receptor Antagonistsmedicine.medical_specialtyTropomyosin receptor kinase BCHO CellsBiologyEstrogen-related receptor alphaInternal medicineCricetinaemedicineEnzyme-linked receptorAnimalsHumansCloning MolecularPhosphorylationReceptorProtease-activated receptor 2Insulin-like growth factor 1 receptorPharmacologyReceptors EndothelinInterleukin-13 receptorReceptor Endothelin AReceptor Endothelin BCell biologyRatsInterleukin 10KineticsEndocrinologyCardiology and Cardiovascular MedicineSignal TransductionJournal of cardiovascular pharmacology
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Structural features of the human bradykinin B2 receptor probed by agonists, antagonists, and anti-idiotypic antibodies

1993

The human bradykinin B2 receptor belongs to the family of G-protein-coupled receptors. To characterize the receptor protein, we have solubilized the membranes of cultured human foreskin fibroblasts bearing the B2 receptor. Affinity cross-linking of the solubilized receptor with the labeled agonist, 125I-Tyr0-bradykinin, or the labeled antagonist, 125I-(4-hydroxy-phenyl-propionyl)-HOE140, revealed major bands of apparent molecular mass of 69 kDa in SDS-polyacrylamide gel electrophoresis under reducing conditions, and of 59 kDa under non-reducing conditions. A 1000-fold molar excess of each of the unlabeled ligands quenched the specific labeling suggesting that the agonist and the antagonist …

Gel electrophoresisAgonistmedicine.drug_classChemistryInsulin-like growth factor 2 receptorCell BiologyBiochemistryMolecular biologyBiochemistrymedicineBradykinin receptorBinding siteReceptorMolecular BiologyProtease-activated receptor 2Cation-dependent mannose-6-phosphate receptorJournal of Biological Chemistry
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Immunological Probes for the Bradykinin B2 Receptor. A Toolbox

1997

Publisher Summary This chapter provides an overview of the immunological tools for bradykinin (BK) B 2 receptor. Receptors for kinins are classified as two major subtypes, B 1 and B 2 , although other subtypes may exist. B 1 receptors are activated by carboxyterminally truncated kinins, whereas BK and kallidin (Lys-BK) are B 2 receptor agonists. Molecular cloning has revealed the primary structures of B 1 and B 2 receptors and identified them as members of the G protein-coupled receptor family, characterized by seven membrane-spanning α-helices. In some tissues, B 1 receptor expression is induced by cytokines, such as interleukin-1, whereas the B 2 receptor is thought to be expressed consti…

Interleukin-21 receptorReceptor expressionB-cell receptor5-HT5A receptorImmune receptorGABBR1BiologyBradykinin receptorMolecular biologyProtease-activated receptor 2
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Structural requirements for V2 vasopressin receptor proteolytic cleavage.

1999

The ligand-induced proteolytic cleavage of the V2 vasopressin receptor transiently expressed in COS cells was investigated. After incubation of the cell membranes with a photoreactive ligand possessing full agonistic properties for V2 receptors, approximately 90% of the porcine and bovine V2 vasopressin receptors were cleaved in the upper part of transmembrane helix 2 at a heptapeptide sequence conserved in both vasopressin and oxytocin receptors. The oxytocin receptor was completely resistant to proteolysis after binding the same photoreactive ligand, which is only a partial agonist for this receptor. Chimeric V2/oxytocin receptors obtained by transfer of extracellular domains of the oxyto…

Models MolecularReceptors VasopressinDNA ComplementaryTime FactorsProtein ConformationSwineMolecular Sequence DataBiologyLigandsTransfectionBiochemistryArginine vasopressin receptor 2Enzyme-linked receptorCyclic AMPAnimalsHumansPoint Mutation5-HT5A receptorAmino Acid SequenceCloning MolecularReceptorProtease-activated receptor 2Vasopressin receptorArginine vasopressin receptor 1BDose-Response Relationship DrugSequence Homology Amino AcidProteinsOxytocin receptorProtein Structure TertiaryEnzyme ActivationBiochemistryMicroscopy FluorescenceReceptors OxytocinType C PhospholipasesCOS CellsMutagenesis Site-DirectedCattlehormones hormone substitutes and hormone antagonistsAdenylyl CyclasesProtein BindingEuropean journal of biochemistry
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A New Type of Cytokine Receptor Antagonist Directly Targeting gp130

1998

The interleukin-6-type family of cytokines bind to receptor complexes that share gp130 as a common signal-transducing subunit. So far, receptor antagonists for interleukin-6-type cytokines have been constructed that still bind to the specific ligand binding subunit of the receptor complex, but have lost the ability to stimulate gp130. Such receptor antagonists compete for a specific receptor of a member of the cytokine family. Interleukin-6 only binds to gp130 when complexed with the interleukin-6 receptor that exists as a membrane bound and soluble molecule. Here we have constructed fusion proteins that consist of the soluble form of the human interleukin-6 receptor covalently linked to in…

Receptor complexRecombinant Fusion ProteinsNerve Tissue ProteinsOncostatin MBiologyLeukemia Inhibitory FactorBiochemistryAntigens CDCytokine Receptor gp130Enzyme-linked receptorHumansPoint Mutation5-HT5A receptorCiliary Neurotrophic FactorMolecular BiologyProtease-activated receptor 2Common gamma chainLymphokinesMembrane GlycoproteinsDose-Response Relationship DrugJanus kinase 1Interleukin-6digestive oral and skin physiologyCell BiologyReceptors Interleukin-6Growth Inhibitorsbiological factorsBiochemistryInterleukin-21 receptorCytokinesPeptidesCytokine receptorProtein BindingJournal of Biological Chemistry
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