Facchiano F, Valtorta F, Benfenati F, Luini A
Laboratory of Molecular Neurobiology, Mario Negri Institute of Pharmacological Research, Consorzio Mario Negri Sud, S. Maria Imbaro (Chieti), Italy.
Trends Biochem Sci. 1993 Sep;18(9):327-9. doi: 10.1016/0968-0004(93)90066-v.
Tetanus toxin potently and almost irreversibly inhibits the release of neurotransmitters from nerve terminals. The toxin binds to and activates transglutaminase, a Ca(2+)-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.
破伤风毒素能有效且几乎不可逆地抑制神经末梢释放神经递质。该毒素与转谷氨酰胺酶结合并激活它，转谷氨酰胺酶是一种依赖钙离子的酶，能在底物蛋白之间形成稳定的交联。转谷氨酰胺酶存在于神经末梢，并将突触素I识别为一种极好的底物，突触素I是一种参与神经传递的丰富的突触小泡磷蛋白。破伤风毒素的神经麻痹作用可能至少部分归因于对突触转谷氨酰胺酶的刺激以及随之而来的突触素I的交联。
