Search results for "Calmodulin"

showing 10 items of 83 documents

Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation

1996

Lethal toxin (LT) from Clostridium sordellii is one of the high molecular mass clostridial cytotoxins. On cultured cells, it causes a rounding of cell bodies and a disruption of actin stress fibers. We demonstrate that LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo. LT glucosylates Ras, Rap, and Rac. In Ras, threonine at position 35 was identified as the target amino acid glucosylated by LT. Other related members of the Ras GTPase superfamily, including RhoA, Cdc42, and Rab6, were not modified by LT. Incubation of serum-starved Swiss 3T3 cells with LT prevents the epidermal growth factor-induced phosphorylation of m…

ThreonineUridine Diphosphate GlucoseRHOABacterial ToxinsMolecular Sequence DataClostridium sordelliimacromolecular substancesCDC42GTPaseBiologyCell morphologyBiochemistryGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)MiceGTP-binding protein regulatorsGTP-Binding ProteinsAnimalsHumansAmino Acid SequenceMolecular BiologyClostridiumEpidermal Growth FactorKinase3T3 CellsCell Biologybiology.organism_classificationMolecular biologyActinsrac GTP-Binding ProteinsActin CytoskeletonKineticsGlucoserap GTP-Binding ProteinsGlucosyltransferasesCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinPhosphorylationGuanosine TriphosphateHeLa CellsJournal of Biological Chemistry
researchProduct

Ethylene modulates gene expression in cells of the marine sponge Suberites domuncula and reduces the degree of apoptosis.

1999

Sponges (phylum Porifera) live in an aqueous milieu that contains dissolved organic carbon. This is degraded photochemically by ultraviolet radiation to alkenes, particularly to ethylene. This study demonstrates that sponge cells (here the demosponge Suberites domuncula has been used), which have assembled to primmorphs, react to 5 microM ethylene with a significant up-regulation of intracellular Ca(2+) concentration and with a reduction of starvation-induced apoptosis. In primmorphs from S. domuncula the expression of two genes is up-regulated after exposure to ethylene. The cDNA of the first gene (SDERR) isolated from S. domuncula encodes a potential ethylene-responsive protein, termed ER…

Transcriptional ActivationEthyleneMolecular Sequence DataApoptosisMarine BiologyBiochemistryEvolution Molecularchemistry.chemical_compoundComplementary DNAGene expressionBotanyAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyGenePlant Proteinschemistry.chemical_classificationbiologySequence Homology Amino AcidKinaseProteinsCell BiologySequence Analysis DNAEthylenesbiology.organism_classificationAmino acidPoriferaSuberites domunculaSpongechemistryBiochemistryGene Expression RegulationProtein BiosynthesisCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Food DeprivationSignal TransductionThe Journal of biological chemistry
researchProduct

Histamine Upregulates Gene Expression of Endothelial Nitric Oxide Synthase in Human Vascular Endothelial Cells

2003

Background— Histamine has a short-term, transient, stimulating effect on endothelial nitric oxide synthase (eNOS) activity; however, long-term effects on eNOS have not been described yet. In addition, the vascular effect of histamine seems to depend critically on eNOS functionality. Therefore, we studied the effects of histamine on eNOS gene expression and function. Methods and Results— In human umbilical vein endothelial cells (HUVECs) and HUVEC-derived EA.hy 926 cells, histamine upregulated eNOS mRNA (RNase protection assay) and protein (electron microscopic immunocytochemistry) expression. The upregulation of eNOS could be prevented by mepyramine, a selective antagonist at the H 1 recep…

Transcriptional Activationmedicine.medical_specialtyNitric Oxide Synthase Type IIIEndotheliumHistamine H1 receptorNitric OxideCell LineNitric oxidechemistry.chemical_compoundEnosPhysiology (medical)Internal medicinemedicineHumansRNA MessengerReceptors Histamine H1Enzyme InhibitorsPromoter Regions GeneticProtein Kinase InhibitorsCells CulturedDose-Response Relationship DrugbiologyNitric Oxide Synthase Type IIIbiology.organism_classificationMolecular biologyUp-RegulationNitric oxide synthaseKineticsOxidative StressEndocrinologymedicine.anatomical_structurechemistryEnzyme InductionCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinEndothelium VascularNitric Oxide SynthaseHistamine H3 receptorCalcium-Calmodulin-Dependent Protein Kinase Type 2Reactive Oxygen SpeciesCardiology and Cardiovascular MedicineHistamineHistamineCirculation
researchProduct

rhoB encoding a UV-inducible Ras-related small GTP-binding protein is regulated by GTPases of the Rho family and independent of JNK, ERK, and p38 MAP…

1998

The small GTPase RhoB is immediate-early inducible by DNA damaging treatments and thus part of the early response of eukaryotic cells to genotoxic stress. To investigate the regulation of this cellular response, we isolated the gene for rhoB from a mouse genomic library. Sequence analysis of the rhoB gene showed that its coding region does not contain introns. The promoter region of rhoB harbors regulatory elements such as TATA, CAAT, and Sp1 boxes but not consensus sequences for AP-1, Elk-1, or c-Jun/ATF-2. The rhoB promoter was activated by UV irradiation, but not by 12-O-tetradecanoylphorbol-13-acetate treatment. rhoB promoter deletion constructs revealed a fragment of 0.17 kilobases in …

Ultraviolet RaysRHOBMolecular Sequence DataMAP Kinase Kinase Kinase 1BiologyProtein Serine-Threonine KinasesBiochemistryp38 Mitogen-Activated Protein KinasesGTP PhosphohydrolasesWortmanninchemistry.chemical_compoundMiceGTP-Binding ProteinsRhoB GTP-Binding ProteinAnimalsCloning MolecularEnzyme InhibitorsPromoter Regions GeneticrhoB GTP-Binding ProteinMolecular BiologyPhosphoinositide-3 Kinase InhibitorsMAP kinase kinase kinaseBase SequenceKinaseMEK inhibitorJNK Mitogen-Activated Protein KinasesMembrane ProteinsCell BiologyMolecular biologychemistryMitogen-activated protein kinaseCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinras ProteinsSignal transductionMitogen-Activated Protein KinasesThe Journal of biological chemistry
researchProduct

Characterization of Membrane-Bound Cyclic Nucleotide Phosphodiesterases from Bovine Aortic Smooth Muscle

1992

This study reports the isolation and characterization of cyclic nucleotide phosphodiesterases (PDEs) associated with membrane fraction in comparison to cytosolic forms from bovine aorta. DEAE-Sephacel chromatography of a solubilized membrane fraction from a homogenate, prepared under isotonic conditions in the presence of protease inhibitors, yielded one major peak of PDE activity that specifically hydrolyzed cAMP and was not stimulated by calmodulin: It appeared to contain two subtypes of PDE. The first subtype belonged to the cyclic GMP (cGMP)-inhibited PDE family, (PDE III): It had an apparent Km value of 0.4 microM and was potently inhibited by cGMP, LY186126, and cilostamide. The secon…

Vascular smooth muscleCalmodulinPhosphodiesterase InhibitorsMuscle Smooth Vascularchemistry.chemical_compoundCytosolCalmodulinCyclic AMPmedicineAnimalsheterocyclic compoundsCyclic GMPRolipramPharmacologyCilostamidebiologyCyclic nucleotide phosphodiesterasePhosphoric Diester HydrolasesHydrolysisCell MembraneBiological membranemusculoskeletal systemenzymes and coenzymes (carbohydrates)Mechanism of actionBiochemistrychemistryEnzyme inhibitorbiology.proteinCattleChromatography Thin Layersense organsmedicine.symptomCardiology and Cardiovascular Medicinecirculatory and respiratory physiologymedicine.drugJournal of Cardiovascular Pharmacology
researchProduct

Calcium, calmodulin-dependent protein phosphorylation in Neurospora crassa

1984

Abstract A calcium, calmodulin-dependent protein kinase activity has been partially purified by calmodulin-Sepharose affinity chromatography from the soluble fraction of Neurospora crassa . The phosphorylated peptide has an apparent molecular mass on SDS-polyacrylamide gel of 47 kDa. The apparent half maximal phosphorylation is obtained after 1.5 min at 30° C in the presence of calcium and calmodulin. The apparent half maximal activation of the phosphorylation is obtained at 1 μM calcium, and 0.1 or 0.2 μM calmodulin from bovine brain or Neurospora , respectively. The 32 P incorporation is enhanced about 10-fold by calmodulin.

[SDE] Environmental SciencesCalmodulin[SDV]Life Sciences [q-bio]Biophysicschemistry.chemical_elementCalciumBiochemistryNeurosporaProtein kinaseNeurospora crassa03 medical and health sciencesAffinity chromatographyCalmodulinStructural BiologyGenetics[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyProtein phosphorylation[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyProtein kinase AMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesbiologyNeurospora crassa030306 microbiologyCell Biologybiology.organism_classification[SDV] Life Sciences [q-bio]chemistryBiochemistry[SDE]Environmental Sciencesbiology.proteinPhosphorylationCalcium
researchProduct

IDENTIFICATION OF A CALMODULIN-BINDING SITE WITHIN THE DOMAIN I OF BACILLUS THURINGIENSISCry3Aa TOXIN

2012

Bacillus thuringiensis Cry3Aa toxin is a coleopteran specific toxin highly active against Colorado Potato Beetle (CPB).We have recently shown that Cry3Aa toxin is proteolytically cleaved by CPB midgut membrane associated metalloproteases and that this cleavage is inhibited by ADAM metalloprotease inhibitors. In the present study, we investigated whether the Cry3Aa toxin is a calmodulin (CaM) binding protein, as it is the case of several different ADAM shedding substrates. In pull-down assays using agarose beads conjugated with CaM, we demonstrated that Cry3Aa toxin specifically binds to CaM in a calcium-independent manner. Furthermore, we used gel shift assays and (1)H NMR spectra to demons…

chemistry.chemical_classificationCalmodulinmedicine.diagnostic_testPhysiologyToxinBinding proteinProteolysisPeptideGeneral MedicineTrifluoperazineBiologymedicine.disease_causebiology.organism_classificationBiochemistryMolecular biologychemistryBiochemistryInsect ScienceBacillus thuringiensismedicinebiology.proteinBinding sitemedicine.drugArchives of Insect Biochemistry and Physiology
researchProduct

Stabilization of an ?-helical conformation in an isolated hexapeptide inhibitor of calmodulin

2001

The conformational properties of two hexapeptides, Ac-LWRILW-NH(2) and its D-amino acid counterpart Ac-lwrilw-NH(2), identified as calmodulin inhibitors using mixture-based synthetic combinatorial library approaches, have been characterised by NMR and CD spectroscopy. The peptides fold into an alpha-helical conformation in aqueous solution. The observed short- and medium-range nuclear Overhauser effects were consistent with the formation of an alpha-helical structure and a reasonably well-defined set of structures was obtained by using restraints from the NMR data in simulated annealing calculations. Analysis of glycine-substitution analogues demonstrated that all the amino acids that make …

chemistry.chemical_classificationCircular dichroismAqueous solutionCalmodulinbiologyStereochemistryOrganic ChemistryBiophysicsGeneral MedicineNuclear magnetic resonance spectroscopyBiochemistryAmino acidPeptide ConformationBiomaterialschemistrybiology.proteinPeptide sequenceProtein secondary structureBiopolymers
researchProduct

Novel, potent calmodulin antagonists derived from an all-dhexapeptide combinatorial library that inhibitin vivocell proliferation: activity and struc…

2000

: Calmodulin is known to bind to various amphipathic helical peptide sequences, and the calmodulin–peptide binding surface has been shown to be remarkably tolerant sterically. d-Amino acid peptides, therefore, represent potential non-hydrolysable intracellular antagonists of calmodulin. In the present study, synthetic combinatorial libraries have been used to develop novel d-amino acid hexapeptide antagonists to calmodulin-regulated phosphodiesterase activity. Five hexapeptides were identified from a library containing over 52 million sequences. These peptides inhibited cell proliferation both in cell culture using normal rat kidney cells and by injection via the femoral vein following part…

chemistry.chemical_classificationCircular dichroismCalmodulinbiologyCell growthChemistryPeptideNuclear magnetic resonance spectroscopyBiochemistryEndocrinologyBiochemistryIn vivoAmphiphilebiology.proteinIntracellularThe Journal of Peptide Research
researchProduct

Neuronal Nitric Oxide Synthase

2007

Neuronal nitric oxides synthase (nNOS; also referred to as NOS1 or NOS I) is a low-output enzyme that is primarily expressed in neurons. Like eNOS, it is a low-output NOS whose activity is regulated by Ca++ and calmodulin, and that produces NO in a pulsatile fashion. nNOS has a widespread distribution in the central and peripheral nervous systems. In addition, nNOS mRNA transcripts and/or protein have also been detected in non-neuronal cell types, such as rhabdomyocytes, epithelial cells, mast cells, and neutrophils …

chemistry.chemical_classificationmedicine.medical_specialtyMessenger RNACell typeCalmodulinbiologyATP synthaseChemistryNOS1biology.organism_classificationCell biologyEndocrinologyEnzymenervous systemEnosInternal medicinemedicinebiology.proteinNeuronal Nitric Oxide Synthase
researchProduct