The transglutaminase hypothesis for the action of tetanus toxin

Francesco Facchiano, Flavia Valtorta, Fabio Benfenati, Alberto Luini

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)327-329
Number of pages3
JournalTrends in Biochemical Sciences
Volume18
Issue number9
DOIs
Publication statusPublished - 1993

Fingerprint

Tetanus Toxin
Transglutaminases
Synapsins
Synaptic Vesicles
Phosphoproteins
Substrates
Synaptic Transmission
Crosslinking
Neurotransmitter Agents
Enzymes
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

The transglutaminase hypothesis for the action of tetanus toxin. / Facchiano, Francesco; Valtorta, Flavia; Benfenati, Fabio; Luini, Alberto.

In: Trends in Biochemical Sciences, Vol. 18, No. 9, 1993, p. 327-329.

Research output: Contribution to journalArticle

Facchiano, Francesco ; Valtorta, Flavia ; Benfenati, Fabio ; Luini, Alberto. / The transglutaminase hypothesis for the action of tetanus toxin. In: Trends in Biochemical Sciences. 1993 ; Vol. 18, No. 9. pp. 327-329.
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