Abstract
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 [3H]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.
| Original language | English |
|---|---|
| Pages (from-to) | 1770-1774 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 270 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - Jan 1 1995 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
IgA protease from Neisseria gonorrhoeae inhibits exocytosis in bovine chromaffin cells like tetanus toxin. / Binscheck, T.; Bartels, F.; Bergel, H.; Bigalke, H.; Yamasaki, S.; Hayashi, T.; Niemann, H.; Pohlner, J.
In: Journal of Biological Chemistry, Vol. 270, No. 4, 01.01.1995, p. 1770-1774.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - IgA protease from Neisseria gonorrhoeae inhibits exocytosis in bovine chromaffin cells like tetanus toxin
AU - Binscheck, T.
AU - Bartels, F.
AU - Bergel, H.
AU - Bigalke, H.
AU - Yamasaki, S.
AU - Hayashi, T.
AU - Niemann, H.
AU - Pohlner, J.
PY - 1995/1/1
Y1 - 1995/1/1
N2 - 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 [3H]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.
AB - 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 [3H]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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UR - http://www.scopus.com/inward/citedby.url?scp=0028918032&partnerID=8YFLogxK
U2 - 10.1074/jbc.270.4.1770
DO - 10.1074/jbc.270.4.1770
M3 - Article
C2 - 7829513
AN - SCOPUS:0028918032
VL - 270
SP - 1770
EP - 1774
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 4
ER -