Search results for "Clostridium tetani"

showing 3 items of 3 documents

Amylase release from streptolysin O-permeabilized pancreatic acinar cells. Effects of Ca2+, guanosine 5'-[gamma-thio]triphosphate, cyclic AMP, tetanu…

1992

The molecular requirements for amylase release and the intracellular effects of botulinum A toxin and tetanus toxin on amylase release were investigated using rat pancreatic acinar cells permeabilized with streptolysin O. Micromolar concentrations of free Ca2+ evoked amylase release from these cells. Maximal release was observed in the presence of 30 microM free Ca2+. Ca(2+)-stimulated, but not basal, amylase release was enhanced by guanosine 5′-[gamma-thio]triphosphate (GTP[S]) (3-4 fold) or cyclic AMP (1.5-2 fold). Neither the two-chain forms of botulinum A toxin and tetanus toxin, under reducing conditions, nor the light chains of tetanus toxin, inhibited amylase release triggered by Ca2…

MaleBotulinum ToxinsCell Membrane PermeabilityClostridium tetanimedicine.disease_causeBiochemistryNorepinephrineBacterial ProteinsTetanus ToxinAcinar cellmedicineCyclic AMPNeurotoxinAnimalsAmylaseMolecular BiologyPancreasbiologyToxinProteolytic enzymesRats Inbred StrainsCell BiologyRatsBiochemistryGuanosine 5'-O-(3-Thiotriphosphate)AmylasesStreptolysinsbiology.proteinClostridium botulinumStreptolysinCalciumResearch Article
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Noradrenaline release from permeabilized synaptosomes is inhibited by the light chain of tetanus toxin

1992

AbstractNoradrenaline release from rat brain cortical synaptosomes permeabilized with streptolysin O can be triggered by μM concentrations of free Ca2+. This process was inhibited within minutes by tetanus toxin and its isolated light chain, but not by its heavy chain. The data demonstrate that the effect of tetanus toxin on NA release from purified synaptosomes is caused by the intraterminal action of its light chain.

MaleCell Membrane PermeabilityClostridium tetaniBiophysicsBiologymedicine.disease_causeImmunoglobulin light chainBiochemistryExocytosisExocytosisGeneeskundeNorepinephrineStructural BiologyPermeabilizationGeneticsmedicineSynaptosomeAnimalsNeurotoxinRats WistarStreptolysin OMolecular BiologySynaptosomeToxinCell BiologyRatsTetanus toxinMechanism of actionBiochemistryStreptolysinmedicine.symptomSynaptosomesFEBS Letters
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Activation and Inactivation of Tetanus Toxin in Chromaffin Cells

1993

Tetanus toxin is produced by Clostridium tetani as a single chain, almost non-toxic, protein with a molecular weight of approximately 150.000 representing 1315 amino acids. Bacterial proteases cleave the molecule between positions A 457 and S 458 (extracellular activation), yielding a heavy chain (MW 100.000) and a light chain (MW 50.000) tetanus toxin (HC-TeTx, LC-TeTx). Both chains remain connected to each other by a disulphur bond between positions C 439 and C 467 (Dichain-TeTx)1. The cleavage or nicking dramatically increases the biological activity2. HC-TeTx is involved in binding DC-TeTx to gangliosides lodged in the plasma membrane, which is a prerequisite for incorporation into the …

education.field_of_studyClostridium tetaniChemistryPopulationEndocytosismedicine.disease_causeExocytosisCytosolmedicine.anatomical_structureChromaffin cellmedicineExtracellularBiophysicseducationIntracellular
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