0000000001054397

AUTHOR

Barbara Höhne-zell

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Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells

1994

AbstractExocytosis of secretory granules by adrenal chromaffin cells is blocked by the tetanus toxin light chain in a zinc specific manner. Here we show that cellular synaptobrevin is almost completely degraded by the tetanus toxin light chain within 15 min. We used highly purified adrenal secretory granules to show that synaptobrevin, which can be cleaved by the tetanus toxin light chain, is localized in the vesicular membrane. Proteolysis of synaptobrevin in cells and in secretory granules is reversibly inhibited by the zinc chelating agent dipicolinic acid. Moreover, cleavage of synaptobrevin present in secretory granules by the tetanus toxin light chain is blocked by the zinc peptidase …

SynaptobrevinProteolysismedicine.medical_treatmentMolecular Sequence DataBiophysicsSynaptobrevinNerve Tissue ProteinsIn Vitro Techniquesmedicine.disease_causeImmunoglobulin light chainBiochemistryExocytosisExocytosisR-SNARE ProteinsStructural BiologyGeneticsmedicineAnimalsChromaffin GranulesAmino Acid SequenceMolecular BiologySecretory granuleR-SNARE ProteinsAdrenal medullaProteasemedicine.diagnostic_testChemistryToxinMembrane ProteinsCell BiologyPeptide FragmentsTetanus toxinmedicine.anatomical_structureBiochemistryCattleAdrenal medullaFEBS Letters
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