THE TRANSGLUTAMINASE HYPOTHESIS FOR THE ACTION OF TETANUS TOXIN

被引:28
作者
FACCHIANO, F
VALTORTA, F
BENFENATI, F
LUINI, A
机构
[1] UNIV MILAN,S RAFFAELE SCI INST,CTR CYTOPHARMACOL,NATL RES COUNCIL,I-20129 MILAN,ITALY
[2] UNIV MODENA,INST HUMAN PHYSIOL,I-41100 MODENA,ITALY
[3] UNIV ROMA TOR VERGATA,DEPT EXPTL MED,I-00173 ROME,ITALY
关键词
D O I
10.1016/0968-0004(93)90066-V
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:327 / 329
页数:3
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