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Titolo:
Clostridium neurotoxins influence serotonin uptake and release differentlyin rat brain synaptosomes
Autore:
Najib, A; Pelliccioni, P; Gil, C; Aguilera, J;
Indirizzi:
Univa,utonoma Barcelona, Fac Med, Dept Bioquim & Biol Mol, E-08193 Barcelon Univ Autonoma Barcelona Barcelona Spain E-08193 ol Mol, E-08193 Barcelon
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 5, volume: 72, anno: 1999,
pagine: 1991 - 1998
SICI:
0022-3042(199905)72:5<1991:CNISUA>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
KINASE-C ACTIVATION; TETANUS-TOXIN; BOTULINUM NEUROTOXIN; NEUROTRANSMITTER RELEASE; PROTEASE ACTIVITY; DOWN-REGULATION; SYNAPSIN-I; MECHANISM; CLEAVAGE; ZINC;
Keywords:
clostridium neurotoxins; 5-hydroxytryptamine (serotonin); [H-3]imipramine binding; uptake; release; tetanus toxin; botulinum neurotoxin type A;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Aguilera, J Univa,utonoma Barcelona, Fac Med, Dept Bioquim & Biol Mol, E-08193 Barcelon Univ Autonoma Barcelona Barcelona Spain E-08193 193 Barcelon
Citazione:
A. Najib et al., "Clostridium neurotoxins influence serotonin uptake and release differentlyin rat brain synaptosomes", J NEUROCHEM, 72(5), 1999, pp. 1991-1998

Abstract

Clostridium neurotoxins produce inhibition of both basal and K+-evoked serotonin release in rat brain synaptosomes. To produce these effects, tetanustoxin (TeTx), as well as botulinum neurotoxin type A (BoNT/A), added to brain synaptosomes, must be incubated at 37 degrees C over a long interval (hours). This serotonin exocytosis inhibition was abolished with previous treatment with specific Zn2+-metalloprotease inhibitors. Nevertheless, a shortincubation time produces different behavior of the indicated neurotoxins: TeTx significantly blocks the sodium-dependent, high-affinity serotonin uptake, whereas a small increase of this uptake was found with BoNT/A, Both Zn2+-metalloprotease active fragments, light chains of TeTx and BoNT/A, are unable to reproduce the block of the serotonin uptake, whereas the C-terminal portion of the TeTx heavy chain (H-c-TeTx), which;binds specifically to the target tissue, inhibited the serotonin uptake in a dose-dependent manner. The IC50 of H-c-TeTx ranges from 0.62 to 2.08 nM. Binding of [H-3]imipramine and [H-3]serotonin did not change after toxin treatments, which indicates that these clostridium neurotoxins do not act on the serotonin high-affinity site at the serotonin transporter or at other serotonin high-affinity sites. These results could indicate that TeTx and H-c-TeTx bind to different targets than BoNT/A in the plasma membrane.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 13:07:38