TY - JOUR
T1 - The transglutaminase hypothesis for the action of tetanus toxin
AU - Facchiano, Francesco
AU - Valtorta, Flavia
AU - Benfenati, Fabio
AU - Luini, Alberto
PY - 1993
Y1 - 1993
N2 - Tetanus toxin potently and almost irreversibly inhibits the release of neurotransmitters from nerve terminals. The toxin binds to and activates transglutaminase, a Ca2+-dependent enzyme that can form stable crosslinks between substrate proteins. Transglutaminase is present in nerve terminals and recognizes synapsin I, an abundant synaptic vesicle phosphoprotein involved in neurotransmission, as an excellent substrate. The neuroparalytic action of tetanus toxin might be due, at least in part, to the stimulation of synaptic transglutaminase and the consequent crosslinking of synapsin I.
AB - Tetanus toxin potently and almost irreversibly inhibits the release of neurotransmitters from nerve terminals. The toxin binds to and activates transglutaminase, a Ca2+-dependent enzyme that can form stable crosslinks between substrate proteins. Transglutaminase is present in nerve terminals and recognizes synapsin I, an abundant synaptic vesicle phosphoprotein involved in neurotransmission, as an excellent substrate. The neuroparalytic action of tetanus toxin might be due, at least in part, to the stimulation of synaptic transglutaminase and the consequent crosslinking of synapsin I.
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U2 - 10.1016/0968-0004(93)90066-V
DO - 10.1016/0968-0004(93)90066-V
M3 - Article
C2 - 7901926
AN - SCOPUS:0027260842
SN - 0376-5067
VL - 18
SP - 327
EP - 329
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 9
ER -