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Titolo:
GYKI 52466 has positive modulatory effects on AMPA receptors
Autore:
Arai, AC;
Indirizzi:
So Illinois Univ, Sch Med, Dept Pharmacol, Springfield, IL 62794 USA So Illinois Univ Springfield IL USA 62794 acol, Springfield, IL 62794 USA
Titolo Testata:
BRAIN RESEARCH
fascicolo: 2, volume: 892, anno: 2001,
pagine: 396 - 400
SICI:
0006-8993(20010223)892:2<396:G5HPME>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUTAMATE-RECEPTOR; HIPPOCAMPAL-NEURONS; KAINATE RECEPTORS; PATCH-CLAMP; CYCLOTHIAZIDE; GYKI-52466; 2,3-BENZODIAZEPINE; ANTAGONISM; DRUG; RESPONSES;
Keywords:
pyramidal neuron; CA1; 2,3-benzodiazepine; outside-out patch; ampakine; glutamate receptor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Arai, AC So Illinois Univ, Sch Med, Dept Pharmacol, POB 19629, Springfield, IL 62794 USA So Illinois Univ POB 19629 Springfield IL USA 62794 IL 62794 USA
Citazione:
A.C. Arai, "GYKI 52466 has positive modulatory effects on AMPA receptors", BRAIN RES, 892(2), 2001, pp. 396-400

Abstract

The 2,3-benzodiazepine derivative GYKI 52466 has been well characterized as a negative modulator of AMPA-type glutamate receptors. The present study re-examined the effects of GYKI 52466 on AMPA receptor-mediated currents inpatches excised from pyramidal neurons in the hippocampal CA1 field and found that this drug has positive modulatory effects in addition to ifs receptor blocking action. A low concentration of GYKI 52466 (10 muM) reliably increased the steady-state current by about three-fold. while the peak current was reduced by 30% only. Higher drug concentrations produced parallel reductions in both the steady-state and peak currents. The increase in the steady-state current was not accompanied by a change in the deactivation time constant and thus, is more likely to result from a change in desensitization than a slowing of channel closing. The results indicate that GYKI 52466 modulates AMPA receptor-mediated currents in a complex manner, perhaps by acting through more than one binding site. (C) 2001 Elsevier Science B.V. Allrights reserved.

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Documento generato il 29/03/20 alle ore 15:08:23