The mechanism of action of tetanus toxin: Effect on synaptic processes and some particular features of toxin binding by the nervous tissue

1973 ◽  
Vol 276 (3-4) ◽  
pp. 247-270 ◽  
Author(s):  
G. N. Kryzhanovsky
Keyword(s):  
Mechanism Of Action ◽  
Tetanus Toxin ◽  
Nervous Tissue ◽  
Toxin Binding

scholarly journals The Fixation of Tetanus Toxin by Nervous Tissue

1959 ◽  
Vol 20 (2) ◽  
pp. 291-300 ◽  
Author(s):  
W. E. van HEYNINGEN
Keyword(s):  
Tetanus Toxin ◽  
Nervous Tissue

scholarly journals Characterization of tetanus toxin binding to rat brain membranes. Evidence for a high-affinity proteinase-sensitive receptor

1986 ◽  
Vol 236 (3) ◽  
pp. 845-852 ◽  
Author(s):  
E J Pierce ◽  
M D Davison ◽  
R G Parton ◽  
W H Habig ◽  
D R Critchley
Keyword(s):  
Rat Brain ◽  
Tetanus Toxin ◽  
Binding Studies ◽  
Single Class ◽  
Toxin Binding ◽  
High Affinity ◽  
Brain Membranes ◽  
Protein Receptor ◽  
Rat Brain Membranes ◽  
Competition Binding

Binding of 125I-labelled tetanus toxin to rat brain membranes in 25 mM-Tris/acetate, pH 6.0, was saturable and there was a single class of high-affinity site (KD 0.26-1.14 nM) present in high abundance (Bmax. 0.9-1.89 nmol/mg). The sites were largely resistant to proteolysis and heating but were markedly sensitive to neuraminidase. Trisialogangliosides were effective inhibitors of toxin binding (IC50 10 nM) and trisialogangliosides inserted into membranes lacking a toxin receptor were able to bind toxin with high affinity (KD 2.6 nM). The results are consistent with previous studies and the hypothesis that di- and trisialogangliosides act as the primary receptor for tetanus toxin under these conditions. In contrast, when toxin binding was assayed in Krebs-Ringer buffer, pH 7.4, binding was greatly reduced, was non-saturable and competition binding studies showed evidence for a small number of high-affinity sites (KD 0.42 nM, Bmax. 0.90 pmol/mg) and a larger number of low-affinity sites (KD 146 nM, Bmax. 179 pmol/mg). Treatment of membranes with proteinases, heat, and neuraminidase markedly reduced binding. Trisialogangliosides were poor inhibitors of toxin binding (IC50 11.0 microM), and trisialogangliosides inserted into membranes bound toxin with low affinity. The results suggest that in physiological buffers tetanus toxin binds with high affinity to a protein receptor, and that gangliosides represent only a low-affinity site.

Tetanus toxin binding to isolated and cultured rat retinal glial cells

Glia ◽  
1988 ◽  
Vol 1 (2) ◽  
pp. 156-164 ◽  
Author(s):  
Reiner Huba ◽  
Hans-Dieter Hofmann
Keyword(s):  
Glial Cells ◽  
Tetanus Toxin ◽  
Toxin Binding
Sign in / Sign up

Export Citation Format

Share Document