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Volume 270,
Number 4,
Issue of January 27, 1995 pp. 1770-1774
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
IgA Protease from Neisseria gonorrhoeae Inhibits Exocytosis in Bovine Chromaffin
Cells Like Tetanus Toxin
(Received for publication, August 3,
1994)
Torsten
Binscheck ,
Frank
Bartels,
Heidrun
Bergel ,
Hans
Bigalke ,
Shinji
Yamasaki,
Tetsuya
Hayashi ,
Heiner
Niemann,
Johannes
Pohlner
When tetanus toxin from Clostridium tetani or IgA
protease from Neisseria gonorrhoeae is translocated
artificially into the cytosol of chromaffin cells, both enzymes inhibit
calcium-induced exocytosis, which can be measured by changes in
membrane capacitance. The block of exocytosis caused by both proteases
cannot be reversed by enforced stimulation with increased calcium
concentration. This effect differs from the botulinum A
neurotoxin-induced block of exocytosis that can be overcome by
elevation of the intracellular calcium concentration. Tetanus toxin is
about 50-fold more potent than IgA protease in cells stimulated by
carbachol. In this case, the release of
[ H]noradrenaline was determined. Trypsin and
endoprotease Glu-C are hardly effective and only at concentrations that
disturb the integrity of the cells. Like tetanus toxin, IgA protease
also splits synaptobrevin II, though at a different site of the
molecule. However, unlike tetanus toxin, it does not cleave
cellubrevin. It is concluded that the membranes of chromaffin vesicles
contain synaptobrevin II, which, as in neurons, appears to play a
crucial part in exocytosis.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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