Search results for "Phosphoinositide Phospholipase C"

showing 4 items of 4 documents

Arginine vasopressin, via activation of post-junctional V1 receptors, induces contractile effects in mouse distal colon

2013

The aim of this study was to analyze whether arginine vasopressin (AVP) may be considered a modulator of intestinal motility. In this view, we evaluated, in vitro, the effects induced by exogenous administration of AVP on the contractility of mouse distal colon, the subtype(s) of receptor(s) activated and the action mechanism. Isometric recordings were performed on longitudinal and circular muscle strips of mouse distal colon. AVP (0.001 nM-100 nM) caused concentration-dependent contractile effects only on the longitudinal muscle, antagonized by the V1 receptor antagonist, V-1880. AVP-induced effect was not modified by tetrodotoxin, atropine and indomethacin. Contractile response to AVP was…

AtropineMaleReceptors Vasopressinmedicine.medical_specialtyVasopressinCarbacholNifedipineColonPhysiologyIndomethacinClinical BiochemistryMuscarinic AntagonistsTetrodotoxinCholinergic AgonistsIn Vitro TechniquesBiologyBiochemistryContractilityMiceCellular and Molecular Neurosciencechemistry.chemical_compoundPhosphoinositide Phospholipase CEndocrinologyInternal medicinemedicineAnimalsCyclooxygenase InhibitorsReceptorVasopressin receptorPhospholipase CArginine vasopressin receptor 1AMuscle SmoothCalcium Channel BlockersArginine vasopressinIntestinalcontractility V1 receptorsPhospholipase C Mouse colonArginine VasopressinEnzyme ActivationMice Inbred C57BLEndocrinologychemistryCarbacholGastrointestinal MotilityCyclopiazonic acidhormones hormone substitutes and hormone antagonistsMuscle ContractionSignal Transductionmedicine.drugRegulatory Peptides
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Heat-stable antigen is expressed by murine keratinocytes and delivers costimulatory signals in T-cell activation.

1995

Heat-stable antigen (HSA), expressed by various antigen-presenting cells (APC), has been described as a costimulatory molecule for CD4+ T cells. Recently, we observed that HSA also serves as an important costimulatory molecule on epidermal Langerhans cells (LC). During these studies, low levels of HSA staining were also detected on normal murine keratinocytes (KC). To investigate whether HSA also is involved in T-cell activation by KC, normal murine KC or the spontaneously transformed KC cell-line PAM 212 were treated with PDB or PMA to induce HSA-expression. FACS analyses showed induction of HSA expression on normal murine KC, as well as PAM 212 cells. In functional assays PDB or PMA-treat…

Keratinocytesmedicine.drug_classT cellT-LymphocytesMolecular Sequence DataProtein Data Bank (RCSB PDB)DermatologyBiologyCleavage (embryo)Monoclonal antibodyLymphocyte ActivationBiochemistryMicePhosphoinositide Phospholipase CAntigenAntigens CDPhorbol EstersmedicineAnimalsInducerRNA MessengerMolecular BiologyCells CulturedMice Inbred BALB CMice Inbred C3HPhospholipase CBase SequencePhosphoric Diester HydrolasesPhosphatidylinositol Diacylglycerol-LyaseAntibodies MonoclonalMolecular biologyStainingbody regionsmedicine.anatomical_structureMolecular Probesembryonic structuresImmunizationLymph NodesExperimental dermatology
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Phospholipase D in rat myocardium: formation of lipid messengers and synergistic activation by G-protein and protein kinase C.

1998

Activation of phospholipase D (PLD) and phosphoinositide-specific phospholipase C (PI-PLC) by fluoride, to stimulate heterotrimeric G-proteins, and by phorbol esters, to stimulate protein kinase C (PKC), was studied in rat atria. Fluoride and 4beta-phorbol-12beta,13alpha-dibutyrate (PDB), in contrast to 4beta-phorbol-13alpha-acetate (PAc), activated PLD, catalyzing the formation of [3H]-phosphatidylethanol ([3H]-PETH), [3H]-phosphatidic acid ([3H]-PA), choline and sn-1,2-diacylglycerol (DAG). Basal PLD activity was resistant to drastic changes in Ca2+ and to Ro 31-8220, a PKC inhibitor, but was decreased by genistein, an inhibitor of tyrosine kinase, and increased by vanadate, a tyrosine ph…

MaleG proteinProtein tyrosine phosphataseBiologyBiochemistrySecond Messenger Systemschemistry.chemical_compoundPhosphoinositide Phospholipase CGTP-Binding ProteinsPhorbol EstersPhospholipase DAnimalsRats WistarProtein kinase CPhorbol 1213-DibutyrateProtein Kinase CDiacylglycerol kinasePharmacologyPhospholipase CPhospholipase DMyocardiumPhosphatidylinositol Diacylglycerol-LyaseTyrosine phosphorylationDrug SynergismLipid MetabolismLipidsRatsEnzyme ActivationBiochemistrychemistryType C PhospholipasesSecond messenger systemlipids (amino acids peptides and proteins)Biochemical pharmacology
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Control of cellular phosphatidylinositol 4,5-bisphosphate levels by adhesion signals and Rho GTPases in NIH 3T3 fibroblasts

2000

The involvement of small GTPases of the Rho family in the control of phosphoinositide metabolism by adhesion signals was examined in NIH 3T3 fibroblasts. Abrogation of adhesion signals by detachment of cells from their substratum resulted in a time-dependent decrease in the cellular level of PtdIns(4,5)P2 by approximately 50%. This effect could be mimicked by treatment of adherent cells with Clostridium difficile toxin B and toxin B-1470, which inhibit specific subsets of Rho and Ras GTPases. Detachment of cells that had been pretreated with the clostridial toxins did not cause a further reduction in PtdIns(4,5)P2 levels, suggesting that the target GTPases are integrated into the control of…

Phosphatidylinositol 45-Diphosphaterac1 GTP-Binding Proteinrho GTP-Binding ProteinsBacterial ToxinsCellClostridium difficile toxin BRAC1GTPasePhospholipaseBiologyTransfectionBiochemistryMicechemistry.chemical_compoundPhosphoinositide Phospholipase CBacterial ProteinsCell AdhesionmedicineAnimalsPhosphorylationInositol phosphatechemistry.chemical_classificationPhospholipase CCytotoxinsPhosphoric Diester Hydrolases3T3 CellsMolecular biologyRecombinant ProteinsCell biologyKineticsPhosphotransferases (Alcohol Group Acceptor)medicine.anatomical_structurechemistryPhosphatidylinositol 45-bisphosphateType C PhospholipasesCalciumSignal TransductionEuropean Journal of Biochemistry
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