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  Fractional calcium currents through recombinant GluR channels of the NMDA, AMPA and kainate receptor subtypes

Burnashev, N., Zhou, Z., Neher, E., & Sakmann, B. (1995). Fractional calcium currents through recombinant GluR channels of the NMDA, AMPA and kainate receptor subtypes. The Journal of Physiology, 485(2), 403-418. doi:10.1113/jphysiol.1995.sp020738.

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The Journal of Physiology - 1995 - Burnashev.pdf (Verlagsversion), 3MB
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Burnashev, N., Autor
Zhou, Z.1, Autor           
Neher, E.2, Autor           
Sakmann, B.3, Autor           
Affiliations:
1Abteilung Kinetik der Phasenbildung, MPI for biophysical chemistry, Max Planck Society, ou_578549              
2Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578579              
3Abteilung Zellphysiologie, MPI for biophysical chemistry, Max Planck Society, ou_578558              

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 Zusammenfassung: Simultaneous fluorescence and whole-cell current measurements using the calcium indicator dye fura-2 were made in HEK 293 cells expressing recombinant glutamate receptor (GluR) channels, and fractional Ca2+ currents (the proportion of whole-cell current carried by Ca2+; Pf) were determined. 2. Cells expressing N-methyl-D-aspartate receptor (NMDAR) channels showed glutamate activated Ca2+ inflow in the voltage range -60 to 40 mV in normal extracellular solution. Ca2+ inflow decreased in a voltage-dependent manner at membrane potentials more negative than -30 mV due to Mg2+ block. Voltage dependence of block at negative potentials was stronger in cells expressing the NR1-NR2A as compared with cells expressing NR1-NR2C subunits. 3. Fractional Ca2+ currents through NMDARs were independent of extracellular Mg2+ and varied between 8.2% (NR1-NR2C subunits) and 11% (NR1-NR2A subunits) in normal extracellular solution (1.8 mM Ca2+) at -60 mV membrane potential. Pf values increased with increasing [Ca2+]o in the range of 0.5-10mM [Ca2+]o in a saturating fashion. 4. In cells expressing alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate receptor (AMPAR) subunits which were unedited at the Q/R site of the putative transmembrane segment TM2 (Q-form), or in cells coexpressing unedited and edited subunits (R-form), the glutamate-evoked Ca2+ inflow increased from 20 to -80 mV in an almost linear way. 5. Fractional Ca2+ currents through AMPAR channels depended on subunit composition. Pf values of Q-form homomeric channels at -60 mV and 1.8 mM [Ca2+]o were between 3.2 and 3.9%. They were slightly voltage dependent and increased with [Ca2+]o in the range 1.8-10mM. Pf values in cells co-expressing Q- and R-form subunits were almost one order of magnitude smaller (0.54%). 6. Relative concentrations of Q-form and R-form GluR-B subunit-specific cDNAs used for cell transfection determined the expression of functionally different heteromeric AMPARS. Pf decreased with increasing relative concentration of R-form encoding CDNAs from 3.4 to 1.4%, demonstrating that editing of the Q/R site of GluR-B subunits decreases Ca2+ inflow through heteromeric AMPARs. 7. Cells expressing the GluR-6 subunit of the kainate receptor (KAR) family were characterized by Pf values which depended on the editing in the TM1 and TM2 segments. Pf values were largest for the Q-form (1.55-2.0%) and lowest for R-form channels (< 0.2%), suggesting that Q/R site editing also decreases Ca2+ inflow through KAR channels. Cells co-expressing both subunit forms showed an intermediate value (0.58%).(ABSTRACT TRUNCATED AT 400 WORDS)

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Sprache(n): eng - English
 Datum: 1995-06-01
 Publikationsstatus: Erschienen
 Seiten: -
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1113/jphysiol.1995.sp020738
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Titel: The Journal of Physiology
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Hoboken, New Jersey, Vereinigte Staaten : Wiley-Blackwell
Seiten: - Band / Heft: 485 (2) Artikelnummer: - Start- / Endseite: 403 - 418 Identifikator: ISSN: 0022-3751
CoNE: https://pure.mpg.de/cone/journals/resource/954925334693_2