6533b85afe1ef96bd12b8d00
RESEARCH PRODUCT
Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells
Axel EckerBarbara Höhne-zellUlrich WellerManfred Gratzlsubject
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 medulladescription
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 inhibitor captopril and by synaptobrevin derived peptides. Our data indicate that the tetanus toxin light chain acts as a zinc dependent protease that cleaves synaptobrevin of secretory granules, an essential component of the exocytosis machinery in adrenal chromaffin cells.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1994-11-28 | FEBS Letters |