Search results for "toxins"

showing 10 items of 799 documents

Reactive neurogenesis during regeneration of the lesioned medial cerebral cortex of lizards

1995

Abstract This study reports that lesion of the adult lizard medial cortex (lizard hipocampal fascia dentata) induces a short period of intensive neurogenesis which we have termed reactive neurogenesis; a cell proliferation event that occurs in the subjacent ependyma. Specific lesion of the medial cortex was achieved by intraperitoneal injection of the neurotoxin 3-acetylpyridine and proliferating cells were detected using tritiated thymidine or 5-bromodeoxiuridine pulse labelling. After lesion, granule neurons in the lizard medial cortex cell layer appeared pyknotic and died; they were then removed and progressively replaced by a set of new neurons. These neurons were mostly generated from …

Pathologymedicine.medical_specialtyPyridinesMedial cortexNeurotoxinsPodarcis hispanicaLesionNeuroblastmedicineAnimalsCerebral CortexbiologyGeneral NeuroscienceNeurogenesisLizardsDNAAnatomybiology.organism_classificationImmunohistochemistryNerve RegenerationMicroscopy Electronmedicine.anatomical_structureCerebral cortexAutoradiographyFascia dentatamedicine.symptomEpendymaCell DivisionNeuroscience
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Mycotoxin Incidence in Some Fish Products: QuEChERS Methodology and Liquid Chromatography Linear Ion Trap Tandem Mass Spectrometry Approach

2019

The inclusion of vegetal raw materials in feed for fish farming has increased the risk of mycotoxin occurrence in feed, as well as in edible tissues from fish fed with contaminated feed, due to the carry-over to muscle portions. Therefore, the objective of this study was to evaluate the occurrence of 15 mycotoxins in processed fish products, which are commonly consumed, such as smoked salmon and trout, different types of sushi, and gula substitutes. A QuEChERS method was employed to perform the mycotoxin extraction from fish samples. For mycotoxin identification and quantitation, the selected technique was the liquid chromatography-tandem mass spectrometry linear ion trap (LC-MS/MS-LIT). Sm…

Pharmaceutical ScienceTandem mass spectrometry01 natural sciencesAnalytical Chemistrysushichemistry.chemical_compoundTandem Mass SpectrometryDepsipeptidesDrug Discoverymass spectrometrybiologySolid Phase ExtractionFishesfood and beverages04 agricultural and veterinary sciencesFish products040401 food scienceSmoked salmonTroutChemistry (miscellaneous)Molecular Medicineendocrine systemanimal structuresFish farmingFood ContaminationQuechersSensitivity and SpecificityArticlelcsh:QD241-4410404 agricultural biotechnologyfoodlcsh:Organic chemistrymycotoxinsFish ProductsAnimalsHumansliquid chromatographyPhysical and Theoretical ChemistryMycotoxinMuscle SkeletalfishChromatography010401 analytical chemistryOrganic Chemistrybiology.organism_classificationsmoked salmonfood.food0104 chemical sciencesSmoked fishchemistryTrichothecenesChromatography LiquidMolecules
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Novel Analogs and Stereoisomers of the Marine Toxin Neodysiherbaine with Specificity for Kainate Receptors

2007

Antagonists for kainate receptors (KARs), a family of glutamategated ion channels, are efficacious in a number of animal models of neuropathologies, including epilepsy, migraine pain, and anxiety. To produce molecules with novel selectivities for kainate receptors, we generated three sets of analogs related to the natural marine convulsant neodysiherbaine (neoDH), and we characterized their pharmacological profiles. Radioligand displacement assays with recombinant alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) and KARs demonstrated that functional groups at two positions on the neoDH molecule are critical pharmacological determinants; only binding to the glutamate receptor …

PharmacologyAgonistAlaninemedicine.drug_classChemistryProtein subunitStereoisomerismKainate receptorAMPA receptorBridged Bicyclo Compounds HeterocyclicLigand (biochemistry)ArticleCell LineReceptors Kainic AcidBiochemistryConvulsantmedicineHumansMolecular MedicineMarine ToxinsReceptorMarine toxinJournal of Pharmacology and Experimental Therapeutics
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Temperature dependence of the toxic effects of phenytoin on peripheral neuromuscular function of the rat tail.

1990

We studied the acute effects of a single dose of phenytoin (250 mg/kg) on peripheral neuromuscular function. The evoked muscle action potentials of the dorsal segmental muscles in the rat tail, and the conduction velocity of the dorsal nerve trunk which innervates them, were measured before and after the intraperitoneal injection of phenytoin. The experiments were performed at different temperatures, 27 (physiological tail temperature), 36 and 37 degrees C (physiological central temperature) in different groups of animals. The amplitudes of the evoked muscle action potentials in the treated groups showed no significant modifications at 27 degrees C, at 36 degrees C a small nonsignificant de…

PhenytoinMaleTailmedicine.medical_specialtyTime Factorsmedicine.medical_treatmentIntraperitoneal injectionCentral nervous systemNeurotoxinsNeural ConductionNeuromuscular JunctionAction PotentialsToxicologyNerve conduction velocityCellular and Molecular NeuroscienceDevelopmental NeuroscienceReference ValuesInternal medicinemedicineAnimalsEvoked PotentialsChemistryMusclesTemperatureRats Inbred StrainsRatsElectrophysiologyEndocrinologyAnticonvulsantmedicine.anatomical_structureAnesthesiaPeripheral nervous systemPhenytoinToxicitymedicine.drugNeurotoxicology and teratology
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Tyrosine-phosphorylation-dependent and Rho-protein-mediated control of cellular phosphatidylinositol 4,5-bisphosphate levels

1998

The polyphosphoinositide PtdIns(4,5)P2, best known as a substrate for phospholipase C isozymes, has recently been recognized to be involved in a variety of other cellular processes. The aim of this study was to examine whether the cellular levels of this versatile phospholipid are controlled by tyrosine phosphorylation. The studies were performed in human embryonic kidney (HEK)-293 cells stably expressing the M3 muscarinic acetylcholine receptor. Inhibition of tyrosine phosphatases by pervanadate induced an up-to-approx.-2.5-fold increase in the total cellular level of PtdIns(4,5)P2, which was both time- and concentration-dependent. In contrast, the tyrosine kinase inhibitors, genistein and…

Phosphatidylinositol 45-DiphosphateBacterial ToxinsBiologyBiochemistryCell LineGTP Phosphohydrolaseschemistry.chemical_compoundEnzyme activatorBacterial ProteinsGTP-Binding ProteinsPhospholipase DHumansPhosphorylationTyrosinerhoB GTP-Binding ProteinMolecular BiologyPhospholipase CADP-Ribosylation FactorsClostridioides difficilePhospholipase DMembrane ProteinsTyrosine phosphorylationCell BiologyTyrphostinsGenisteinCell biologyEnzyme ActivationBiochemistryPhosphatidylinositol 45-bisphosphatechemistryTyrosinePhosphorylationVanadatesTyrosine kinaseResearch ArticleBiochemical Journal
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A role for Rho in receptor- and G protein-stimulated phospholipase C Reduction in phosphatidylinositol 4,5-bisphosphate by Clostridium difficile toxi…

1996

Receptors coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins) activate phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)-hydrolyzing phospholipase C (PLC) enzymes by activated alpha of free beta gamma subunits of the relevant G proteins. To study whether low molecular weight G proteins of the Rho family are involved in receptor signaling to PLC, we examined the effect of Clostridium difficile toxin B, which glucosylates and thereby inactivates Rho proteins, on the regulation of PLC activity in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor (mAChR) subtype. Toxin B treatment of HEK cells did not affect basal PLC activi…

Phosphatidylinositol 45-DiphosphateBotulinum ToxinsG proteinBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BBiologychemistry.chemical_compoundBacterial ProteinsGTP-Binding ProteinsHeterotrimeric G proteinHumansPhosphatidylinositolCells CulturedADP Ribose TransferasesPharmacologyPhospholipase CHEK 293 cellsGeneral MedicineReceptors MuscarinicMolecular biologyCell biologychemistryPhosphatidylinositol 45-bisphosphateType C PhospholipasesrhoA GTP-Binding ProteinNaunyn-Schmiedeberg's Archives of Pharmacology
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Restoration of Clostridium difficile toxin-B-inhibited phospholipase D by phosphatidylinositol 4,5-bisphosphate.

1996

Receptor signalling to phospholipase D (PLD) in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor apparently involves Rho proteins. Since phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] has been recognized as an essential cofactor for PLD activity and since activated Rho proteins have been reported to stimulate the synthesis of PtdIns(4,5)P2, we studied whether in HEK cells PLD activity is regulated by PtdIns(4,5)P2 and, in particular, whether PtdIns(4,5)P2 can restore PLD activity inhibited by Clostridium difficile toxin B, which inactivates Rho proteins. Addition of MgATP to permeabilized HEK cells increased basal PLD activity and potentia…

Phosphatidylinositol 45-DiphosphateGTP'Bacterial ToxinsClostridium difficile toxin BBiologyBiochemistryCell Linechemistry.chemical_compoundBacterial ProteinsGTP-Binding ProteinsPhosphatidylcholineRhoB GTP-Binding ProteinPhospholipase DHumansPhosphatidylinositolEnzyme InhibitorsrhoB GTP-Binding ProteinPhospholipase DClostridioides difficileHEK 293 cellsCell MembraneMembrane ProteinsReceptors MuscarinicCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)chemistryPhosphatidylinositol 45-bisphosphateGuanosine 5'-O-(3-Thiotriphosphate)lipids (amino acids peptides and proteins)European journal of biochemistry
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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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A new gene superfamily of pathogen-response (repat) genes in Lepidoptera: Classification and expression analysis

2012

Repat (REsponse to PAThogens) genes were first identified in the midgut of Spodoptera exigua (Lepidoptera: Noctuidae) in response to Bacillus thuringiensis and baculovirus exposure. Since then, additional repat gene homologs have been identified in different studies. In this study the comprehensive larval transcriptome from S. exigua was analyzed for the presence of novel repat-homolog sequences. These analyses revealed the presence of at least 46 repat genes in S. exigua, establishing a new gene superfamily in this species. Phylogenetic analysis and studies of conserved motifs in these hypothetical proteins have allowed their classification in two main classes, αREPAT and βREPAT. Studies o…

PhysiologyBacillus thuringiensisGenes InsectSpodopteradigestive systemBiochemistryTranscriptomeHemolysin ProteinsBacterial ProteinsBacillus thuringiensisGene expressionExiguaAnimalsMolecular BiologyGeneGeneticsBacillus thuringiensis ToxinsbiologyGene Expression ProfilingStem CellsfungiMidgutbiology.organism_classificationMolecular biologyEndotoxinsIntestinesLepidopteraGene expression profilingLarvaMetagenomeComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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Mannose phosphate isomerase isoenzymes in Plutella xylostella support common genetic bases of resistance to Bacillus thuringiensis toxins in Llpidopt…

2001

ABSTRACT A strong correlation between two mannose phosphate isomerase (MPI) isoenzymes and resistance to Cry1A toxins from Bacillus thuringiensis has been found in a Plutella xylostella population. MPI linkage to Cry1A resistance had previously been reported for a Heliothis virescens population. The fact that the two populations share similar biochemical, genetic, and cross-resistance profiles of resistance suggests the occurrence of homologous resistance loci in both species.

PopulationBacterial ToxinsBacillus thuringiensisDrug ResistanceIsomeraseApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalseducationPest Control BiologicalGeneticseducation.field_of_studyMannose-6-Phosphate IsomeraseEcologyHeliothis virescensbiologyBacillus thuringiensis ToxinsMannose phosphate isomeraseParasporal bodyfungiPlutellaMannose-6-Phosphate Isomerasebiology.organism_classificationEndotoxinsIsoenzymesLepidopteraElectrophoresis Polyacrylamide GelFood ScienceBiotechnologyApplied and environmental microbiology
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