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Botulinum neurotoxin light chains inhibit both Ca 2+ ‐induced and GTP analogue‐induced catecholamine release from permeabilised adrenal chromaffin cells
Author(s) -
Glenn Daphne E.,
Burgoyne Robert D.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00432-2
Subject(s) - exocytosis , chromaffin cell , gtp' , digitonin , neurotoxin , catecholamine , chemistry , biophysics , immunoglobulin light chain , botulinum neurotoxin , biochemistry , adrenal medulla , biology , endocrinology , toxin , membrane , enzyme , antibody , immunology
Using digitonin‐permeabilised bovine adrenal chromaffin cells, the effects of botulinum neurotoxin light chains on exocytosis triggered by Ca 2+ or by GppNHp were examined. Botulinum neurotoxin D light chain, prepared as a His 6 ‐tagged recombinant protein, cleaved VAMP and substantially inhibited catecholamine release due to Ca 2+ and GppNHp. Botulinum neurotoxin C1 and E light chains produced partial inhibition of both Ca 2+ ‐ and GppNHp‐induced catecholamine release. These results suggest that Ca 2+ ‐dependent exocytosis and Ca 2+ ‐independent exocytosis triggered by a non‐hydrolysable GTP analogue occurs via a SNARE‐dependent mechanism in chromaffin cells.