Search results for "Venom"

showing 10 items of 63 documents

Differential effects of calcium channel antagonists (omega-conotoxin GVIA, nifedipine, verapamil) on the electrically-evoked release of [3H]acetylcho…

1990

Electrically-evoked release of [3H]acetylcholine from autonomic neurons (myenteric plexus), motoneurons (phrenic nerve) and the central nervous system (neocortex) was investigated in the presence and absence of the calcium channel antagonists omega-conotoxin GVIA, nifedipine and verapamil, whereby the same species (rat) was used in all experiments. Release of [3H]acetylcholine was measured after incubation of the tissue with [3H]choline. omega-Conotoxin GVIA markedly reduced (70%) the evoked release of [3H]acetylcholine from the myenteric plexus of the small intestine (IC50: 0.7 nmol/l) with a similar potency at 3 and 10 Hz stimulation. An increase in the extracellular calcium concentration…

Malemedicine.medical_specialtyNifedipinechemistry.chemical_elementMollusk VenomsMyenteric PlexusCalciumAutonomic Nervous Systemcomplex mixturesNifedipineomega-Conotoxin GVIAInternal medicinemedicineAnimalsMyenteric plexusPhrenic nervePharmacologyCerebral CortexMotor NeuronsVoltage-dependent calcium channelCalcium channelRats Inbred StrainsGeneral MedicineCalcium Channel BlockersAcetylcholineElectric StimulationRatsPhrenic NerveEndocrinologynervous systemchemistryVerapamilAnesthesiaVerapamilFemaleAcetylcholinemedicine.drugNaunyn-Schmiedeberg's archives of pharmacology
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Inhibition of mechanical activity by neurotensin in rat proximal colon: involvement of nitric oxide.

1997

The aim of the present study was to define the nature of inhibitory action of neurotensin in rat proximal colon. Mechanical activity was detected as changes of intraluminal pressure. Neurotensin (10(-10) to 10(-7) M), in the presence of atropine (10(-6) M), guanethidine (10(-6) M), and nifedipine (10(-8) M), induced a tetrodotoxin-insensitive inhibitory effect characterized by the complete disappearance of the spontaneous phasic contractions. The inhibitory effect of neurotensin (10(-7) M) was abolished by scorpion venom (Leiurus quinquestriatus hebraeus) (10(-6) g/ml) or high K+ (40 mM KCl), whereas it persisted in the presence of omega-conotoxin GVIA, (10(-7) M). N omega-nitro-L-arginine…

Malemedicine.medical_specialtyPhysiologyColonNeuropeptideScorpion VenomsTetrodotoxinIn Vitro TechniquesInhibitory postsynaptic potentialNitric Oxidecomplex mixturesNitric oxidechemistry.chemical_compoundomega-Conotoxin GVIAPhysiology (medical)Internal medicinemedicineAnimalsOmega-Conotoxin GVIAEnzyme InhibitorsRats WistarGuanethidineNeurotensinHepatologybiologyGastroenterologyRatsNitric oxide synthaseEndocrinologyNG-Nitroarginine Methyl EsterMechanism of actionchemistrybiology.proteinPotassiumFemalemedicine.symptomGastrointestinal MotilityPeptidesmedicine.drugNeurotensinThe American journal of physiology
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Wasp venom injected into the prey's brain modulates thoracic identified monoaminergic neurons.

2005

The wasp Ampulex compressa injects a cocktail of neurotoxins into the brain of its cockroach prey to induce an enduring change in the execution of locomotory behaviors. Our hypothesis is that the venom injected into the brain indirectly alters the activity of monoaminergic neurons, thus changing the levels of monoamines that tune the central synapses of locomotory circuits. The purpose of the present investigation was to establish whether the venom alters the descending control, from the brain, of octopaminergic neurons in the thorax. This question was approached by recording the activity of specific identified octopaminergic neurons after removing the input from the brain or after a wasp s…

Malemedicine.medical_treatmentWaspsVenomSensory systemWasp VenomsMotor ActivityMembrane PotentialsCellular and Molecular Neurosciencebiology.animalMonoaminergicmedicineAnimalsPeriplanetaOctopamineNeuronsCockroachbiologyGeneral NeuroscienceBrainInsect Bites and StingsAxotomyThoraxElectrophysiologyElectrophysiologyMonoamine neurotransmittermedicine.anatomical_structurenervous systemNeuronAxotomyNeuroscienceJournal of neurobiology
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Zn(II) and Ni(II) complexes with poly-histidyl peptides derived from a snake venom

2018

Abstract The snake venoms are complex mixtures containing many bioactive peptides and proteins; some of them are aimed to protect the snake glands, where the venom is stored, until the latter is inoculated in the victim. In the venom of some vipers of the genus Atheris , a set of peptides containing poly-His and poly-Gly segments was recently found. Poly-His peptides are not rare in Nature. Although their exact biological function is most often unknown, one thing is certain: they have good binding properties towards the transition metal ions. As a matter of fact, the imidazole side chain of histidine is one of the groups most frequently involved in metal complexation in the active sites of …

Materials Chemistry2506 Metals and AlloysSnake venomNickel ionPoly-His peptidesStereochemistryMetal ions in aqueous solutionComplex-formation equilibriaPeptideVenom010402 general chemistrycomplex mixtures01 natural sciencesNOInorganic ChemistryMetalchemistry.chemical_compoundMaterials ChemistryComplex-formation equilibria; Nickel ion; Poly-His peptides; Snake venom; Zinc ion; Physical and Theoretical Chemistry; Inorganic Chemistry; Materials Chemistry2506 Metals and AlloysImidazolePhysical and Theoretical ChemistryHistidinechemistry.chemical_classification010405 organic chemistryChemistryLigand (biochemistry)0104 chemical sciencesZinc ionSnake venomvisual_artvisual_art.visual_art_mediumInorganica Chimica Acta
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Role of murine macrophages and complement in experimental campylobacter infection

1988

Summary. The roles of macrophages and the complement system as potential host defence mechanisms in mice against campylobacter infection were studied in vivo, by depleting the murine serum-complement or the phagocytic cells. Macrophage-depletion was performed by intraperitoneal (i.p.) injection of silica dust, Liquoid or dextran sulphate. During 5 days after infection, such mice showed a significant increase in mortality, compared with controls. In contrast, mice that were previously decomplemented by i.p. injection of Cobra Venom Factor showed no significant increase in mortality. The results with combined macrophage depletion and decomplementation did not differ from those with macrophage…

Microbiology (medical)PolymersVirulenceMice Inbred StrainsBiologymedicine.disease_causeMicrobiologyMicrobiologyMiceCampylobacter fetusInbred strainIn vivoCampylobacter InfectionsmedicineAnimalsElapid VenomsVirulenceMacrophagesCampylobacterComplement C3General MedicineHost defenceSilicon DioxidePolyelectrolytesComplement systemSilica dustDextran sulphateImmunologyFemaleJournal of Medical Microbiology
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"RKKH" peptides from the snake venom metalloproteinase of Bothrops jararaca bind near the metal ion-dependent adhesion site of the human integrin alp…

1999

Integrin alpha(1)beta(1) and alpha(2)beta(1) are the major cellular receptors for collagen, and collagens bind to these integrins at the inserted I-domain in their alpha subunit. We have previously shown that a cyclic peptide derived from the metalloproteinase domain of the snake venom protein jararhagin blocks the collagen-binding function of the alpha(2) I-domain. Here, we have optimized the structure of the peptide and identified the site where the peptide binds to the alpha(2) I-domain. The peptide sequence Arg-Lys-Lys-His is critical for recognition by the I-domain, and five negatively charged residues surrounding the "metal ion-dependent adhesion site" (MIDAS) of the I-domain, when mu…

Models MolecularIntegrinsReceptors CollagenIntegrinMolecular Sequence DataIntegrin alpha2PeptidePeptide bindingBiochemistryAntigens CDCrotalid VenomsAnimalsHumansBothropsComputer SimulationAmino Acid SequenceMolecular BiologyPeptide sequencechemistry.chemical_classificationMetalloproteinaseBinding SitesbiologySequence Homology Amino AcidChemistryActive siteMetalloendopeptidasesCell BiologyCyclic peptidePeptide FragmentsCell biologyBiochemistryJararhaginbiology.proteinMutagenesis Site-DirectedCell Adhesion MoleculesProtein BindingThe Journal of biological chemistry
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Snake venom disintegrins: evolution of structure and function.

2005

Disintegrins represent a family of polypeptides present in the venoms of various vipers that selectively block the function of integrin receptors. Here, we review our current view and hypothesis on the emergence and the structural and functional diversification of disintegrins by accelerated evolution and the selective loss of disulfide bonds of duplicated genes. Research on disintegrins is relevant for understanding the biology of viper venom toxins, but also provides information on new structural determinants involved in integrin recognition that may be useful in basic and clinical research. The role of the composition, conformation, and dynamics of the integrin inhibitory loop acting in …

Models MolecularIntegrinsStereochemistryDisintegrinsIntegrinAmino Acid MotifsMolecular Sequence DataSequence alignmentVenomToxicologyViper VenomsEvolution MolecularStructure-Activity RelationshipProtein structureGenes DuplicateAnimalsAmino Acid SequencePeptide sequencePhylogenybiologyBase SequenceSnakesCell biologyProtein Structure TertiarySnake venombiology.proteinSequence AlignmentFunction (biology)Snake VenomsToxicon : official journal of the International Society on Toxinology
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2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes.

2013

AbstractSticholysin II (StnII) is a pore-forming toxin from the sea anemone Stichodactyla heliantus which belongs to the large actinoporin family. The toxin binds to sphingomyelin (SM) containing membranes, and shows high binding specificity for this lipid. In this study, we have examined the role of the hydrogen bonding groups of the SM long-chain base (i.e., the 2NH and the 3OH) for StnII recognition. We prepared methylated SM-analogs which had reduced hydrogen bonding capability from 2NH and 3OH. Both surface plasmon resonance experiments, and isothermal titration calorimetry measurements indicated that StnII failed to bind to bilayers containing methylated SM-analogs, whereas clear bind…

Models MolecularPore Forming Cytotoxic ProteinsMembrane permeabilizationLipid BilayersBiophysicsCalorimetryta3111Biochemistrychemistry.chemical_compoundCnidarian VenomsAnimalsComputer SimulationLipid bilayerta116Binding selectivityUnilamellar LiposomesPhosphocholineBinding SitesMolecular StructureChemistryHydrogen bondVesicleta1182Isothermal titration calorimetryHydrogen BondingCell BiologySurface Plasmon ResonanceProtein Structure TertiarySphingomyelinsKineticsMembraneSea AnemonesBiochemistryMolecular dockingIsothermal titration calorimetryBiophysicsPhosphatidylcholinesSphingomyelinProtein BindingBiochimica et biophysica acta
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Evolution of Snake Venom Disintegrins by Positive Darwinian Selection

2008

PII-disintegrins, cysteine-rich polypeptides broadly distributed in the venoms of geographically diverse species of vipers and rattlesnakes, antagonize the adhesive functions of beta(1) and beta(3) integrin receptors. PII-disintegrins evolved in Viperidae by neofunctionalization of disintegrin-like domains of duplicated PIII-snake venom hemorrhagic metalloproteinase (SVMP) genes recruited into the venom proteome before the radiation of the advanced snakes. Minimization of the gene (loss of introns and coding regions) and the protein structures (successive loss of disulfide bonds) underpins the postduplication divergence of disintegrins. However, little is known about the underlying genetic …

Models MolecularProtein ConformationDisintegrinsMolecular Sequence DataEvolution MolecularNegative selectionPhylogeneticsMolecular evolutionViperidaeGeneticsDisintegrinAnimalsAmino Acid SequenceSelection GeneticMolecular BiologyGenePhylogenyEcology Evolution Behavior and SystematicsGeneticsEvolution of snake venomBinding SitesbiologyPhylogenetic treeMultigene Familybiology.proteinNeofunctionalizationProtein MultimerizationSnake VenomsMolecular Biology and Evolution
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NMR Solution Structure of the Non-RGD Disintegrin Obtustatin

2003

The solution structure of obtustatin, a novel non-RGD disintegrin of 41 residues isolated from Vipera lebetina obtusa venom, and a potent and selective inhibitor of the adhesion of integrin alpha(1)beta(1) to collagen IV, has been determined by two-dimensional nuclear magnetic resonance. Almost the whole set of chemical shifts for 1H, 13C and 15N were assigned at natural abundance from 2D homonuclear and heteronuclear 500 MHz, 600 MHz and 800 MHz spectra at pH 3.0 recorded at 298 K and 303 K. Final structural constraints consisted of 302 non-redundant NOE (95 long-range, 60 medium, 91 sequential and 56 intra-residue), four disulfide bond distances, five chi1 dihedral angles and four hydroge…

Models MolecularProtein ConformationStereochemistryDisintegrinsMolecular Sequence DataStatic ElectricityViper VenomsDihedral angleCrystallography X-RayStructural BiologyDisintegrinAnimalsAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyProtein secondary structureConformational isomerismRGD motifMolecular StructureSequence Homology Amino AcidbiologyHydrogen bondChemistryCircular DichroismChemical shiftHydrogen BondingHydrogen-Ion ConcentrationSolutionsKineticsHeteronuclear moleculebiology.proteinOligopeptidesJournal of Molecular Biology
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