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Titolo:
Regulation of kinetic properties of GluR2 AMPA receptor channels by alternative splicing
Autore:
Koike, M; Tsukada, S; Tsuzuki, K; Kijima, H; Ozawa, S;
Indirizzi:
Gunma Univ, Sch Med, Dept Physiol, Gunma 3718511, Japan Gunma Univ GunmaJapan 3718511 h Med, Dept Physiol, Gunma 3718511, Japan Japan Sci & Technol Corp, Core Res Evolut Sci & Technol, Kawaguchi, Saitama 3320012, Japan Japan Sci & Technol Corp Kawaguchi Saitama Japan 3320012 a 3320012, Japan Nagoya Univ, Grad Sch Sci, Dept Phys, Nagoya, Aichi 4648602, Japan Nagoya Univ Nagoya Aichi Japan 4648602 Phys, Nagoya, Aichi 4648602, Japan
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 6, volume: 20, anno: 2000,
pagine: 2166 - 2174
SICI:
0270-6474(20000315)20:6<2166:ROKPOG>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUTAMATE-OPERATED CHANNELS; SYNAPTIC TRANSMISSION; INWARD RECTIFICATION; KAINATE RECEPTORS; CA2+ PERMEABILITY; ACID RECEPTORS; FUNCTIONAL EXPRESSION; NEOCORTICAL NEURONS; SUBUNIT COMPOSITION; ION FLOW;
Keywords:
AMPA receptor channel; GluR2; flip/flop splice variants; Q/R site; desensitization; deactivation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Koike, M Gunma Univ, Sch Med, Dept Physiol, 3-39-22 Showa Machi, Gunma 3718511, Japan Gunma Univ 3-39-22 Showa Machi Gunma Japan 3718511 718511, Japan
Citazione:
M. Koike et al., "Regulation of kinetic properties of GluR2 AMPA receptor channels by alternative splicing", J NEUROSC, 20(6), 2000, pp. 2166-2174

Abstract

The four subunits of the AMPA-type glutamate receptor (GluR1-GluR4 or GluR-A-GluR-D) exist in two distinct forms, flip and flop, generated by alternative splicing of a 115 bp region. The GluR2 subunit plays a key role in determining the functional properties of the AMPA receptor channel. In this study, we examined the differences in kinetic properties between the flip andflop splice variants of the GluR2 subunit expressed in Xenopus oocytes using fast agonist application techniques. Glutamate was applied to outside-out patches from oocytes with piezo-driven double-barreled application pipettes. Because homomeric receptor channels composed of the edited form of GluR2 (GluR2R) produce no appreciable current responses, we expressed the unedited form of GluR2 (GluR2Q) in oocytes, which produced large current responses sufficient for analysis of the kinetic properties. The time constant fordesensitization during application of 1 mM glutamate was 5.89 +/- 0.17 msec (n = 50) in flip and 1.18 +/- 0.05 msec (n = 37) in flop. The deactivation time constant was 0.62 +/- 0.06 msec (n = 10) in flip and 0.54 +/- 0.05 msec (n = 10) in flop. The steady-state nondesensitizing current was 6.8 +/-0.4% (n = 53) of the peak current in flip, whereas it was almost negligible in flop, being only 1.1 +/- 0.1% (n = 36). The slower desensitization kinetics and larger steady-state current responses in the flip variant were also observed in heteromeric receptors assembled from GluR2Q/GluR2R. Thus, desensitization occurred much more prominently in the flop variant in the recombinant GluR2 receptor channels.

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Documento generato il 04/04/20 alle ore 14:55:21