http://www.cnr.it/ontology/cnr/individuo/prodotto/ID45941
Transglutaminase participates in the blockade of neurotransmitter release by tetanus toxin: evidence for a novel biological function. (Articolo in rivista)
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- Label
- Transglutaminase participates in the blockade of neurotransmitter release by tetanus toxin: evidence for a novel biological function. (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s00726-009-0436-3 (literal)
- Alternative label
Facchiano F, Deloye F, Doussau F, Innamorati G, Ashton AC, Dolly JO, Beninati S, Facchiano A, Luini A, Poulain B, Benfenati F. (2010)
Transglutaminase participates in the blockade of neurotransmitter release by tetanus toxin: evidence for a novel biological function.
in Amino acids (Wien, Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Facchiano F, Deloye F, Doussau F, Innamorati G, Ashton AC, Dolly JO, Beninati S, Facchiano A, Luini A, Poulain B, Benfenati F. (literal)
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- (1) Department of Hematology, Oncology and Molecular Medicine, Istituto Superiore di Sanità, Viale Regina Elena 299, 00161 Rome, Italy
(2) Laboratory of Molecular Neurobiology, Mario Negri Institute, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro, Chieti, Italy
(3) CNRS UPR3212, Institut des Neurosciences Cellulaires et Intégratives, 5 rue Blaise Pascal, 67084 Strasbourg, France
(4) Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, SW7 2AY, UK
(5) Istituto di Scienze dell'Alimentazione, CNR, Avellino, Italy
(6) Department of Biology, University of Tor Vergata, Rome, Italy
(7) Department of Neuroscience and Brain Technologies, The Italian Institute of Technology, Via Morego 30, 16163 Genoa, Italy (literal)
- Titolo
- Transglutaminase participates in the blockade of neurotransmitter release by tetanus toxin: evidence for a novel biological function. (literal)
- Abstract
- Inhibition of neuroexocytosis by tetanus neurotoxin (TeNT) involves VAMP-2/synaptobrevin-2 cleavage. However, deletion of the TeNT activity does not completely abolish its inhibitory action. TeNT is a potent activator of the cross-linking enzyme transglutaminase 2 (TGase 2) in vitro. The role of the latter mechanism in TeNT poisoning was investigated in isolated nerve terminals and intact neurons. TeNT-induced inhibition of glutamate release from rat cortical synaptosomes was associated with a simultaneous activation of neuronal transglutaminase (TGase) activity. The TeNT-induced blockade of neuroexocytosis was strongly attenuated by pretreatment of either live Aplysia neurons or isolated nerve terminals with specific TGase inhibitors or neutralizing antibodies. The same treatments completely abolished the residual blockade of neuroexocytosis of a non-proteolytic mutant of TeNT light chain. Electrophysiological studies indicated that TGase activation occurs at an early step of TeNT poisoning and contributes to the inhibition of transmitter release. Bioinformatics and biochemical analyses identified synapsin I and SNAP-25 as potential presynaptic TGase substrates in isolated nerve terminals, which are potentially involved in the inhibitory action of TeNT. The results suggest that neuronal TGase activity plays an important role in the regulation of neuroexocytosis and is one of the intracellular targets of TeNT in neurons. (literal)
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