Botulinum neurotoxin light chains inhibit both Ca2+‐induced and GTP analogue‐induced catecholamine release from permeabilised adrenal chromaffin cells

FEBS Letters

Burgoyne, Robert D.¹  Glenn, Daphne E.¹ 

[1] The Physiological Laboratory, University of Liverpool, Crown Street, Liverpool L69 3BX, UK

关键词: Exocytosis;    Chromaffin cell;    Neurotoxin;    VAMP;    Secretion;    GTPγS;    guanosine 5′-[γ-thio]triphosphate;    GppNHp;    guanosine 5′-[βγ-imido]triphosphate;   

DOI  :  10.1016/0014-5793(96)00432-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Using digitonin-permeabilised bovine adrenal chromaffin cells, the effects of botulinum neurotoxin light chains on exocytosis triggered by Ca²⁺ or by GppNHp were examined. Botulinum neurotoxin D light chain, prepared as a His₆-tagged recombinant protein, cleaved VAMP and substantially inhibited catecholamine release due to Ca²⁺ and GppNHp. Botulinum neurotoxin C1 and E light chains produced partial inhibition of both Ca²⁺- and GppNHp-induced catecholamine release. These results suggest that Ca ²⁺-dependent exocytosis and Ca²⁺-independent exocytosis triggered by a non-hydrolysable GTP analogue occurs via a SNARE-dependent mechanism in chromaffin cells.

【 授权许可】

Unknown