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

FEBS Letters

Ecker, Axel²  Gratzl, Manfred²  Weller, Ulrich¹  Höhne-Zell, Barbara² 

[1] Institut für Medizinische Mikrobiologie der Universität, 55101 Mainz, Germany;Abteilung Anatomie und Zellbiologie der Universität, 89069 Ulm, Germany

关键词: Adrenal medulla;    Exocytosis;    Secretory granule;    Synaptobrevin;    Tetanus toxin;   

DOI  :  10.1016/0014-5793(94)01192-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Exocytosis 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.

【 授权许可】

Unknown