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Single channel analysis of a novel NMDA channel from Xenopus oocytes expressing recombinant NR1a, NR2A and NR2D subunits.
J Physiol. 2000 Aug 01; 526 Pt 3:481-91.JP

Abstract

Two types of subunit (an NR1 subunit and one of the NR2 subunits) are sufficient to form efficient NMDA receptors. In order to investigate whether functional receptors may contain more than one sort of NR2 subunit, NR1, NR2A and NR2D subunits were co-expressed in Xenopus oocytes. Single channel recordings from the oocytes showed, as expected, channel openings that are characteristic of NR1/NR2A receptors (ca 50 and 40 pS conductances), and channels characteristic of NR1/NR2D receptors (ca 40 and 20 pS conductances). However, they also contained a novel channel that contained conductances of ca 30, 40 and 50 pS, with direct transitions between all three levels. It is postulated that the novel channel contains NR1, NR2A and NR2D subunits. The implications of this for receptor stoichiometry are discussed. The novel channel was intermediate between the NR1/NR2A and NR1/NR2D 'duplet' receptors in the length of the channel activations, and in the probability of being open during activation. Its glycine sensitivity was much higher than that of NR1/NR2A, and was comparable with that of the other 'duplet' receptors.

Authors+Show Affiliations

Department of Pharmacology, University College London, Gower Street, London WC1E 6BT, UK.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10922001

Citation

Cheffings, C M., and D Colquhoun. "Single Channel Analysis of a Novel NMDA Channel From Xenopus Oocytes Expressing Recombinant NR1a, NR2A and NR2D Subunits." The Journal of Physiology, vol. 526 Pt 3, 2000, pp. 481-91.
Cheffings CM, Colquhoun D. Single channel analysis of a novel NMDA channel from Xenopus oocytes expressing recombinant NR1a, NR2A and NR2D subunits. J Physiol. 2000;526 Pt 3:481-91.
Cheffings, C. M., & Colquhoun, D. (2000). Single channel analysis of a novel NMDA channel from Xenopus oocytes expressing recombinant NR1a, NR2A and NR2D subunits. The Journal of Physiology, 526 Pt 3, 481-91.
Cheffings CM, Colquhoun D. Single Channel Analysis of a Novel NMDA Channel From Xenopus Oocytes Expressing Recombinant NR1a, NR2A and NR2D Subunits. J Physiol. 2000 Aug 1;526 Pt 3:481-91. PubMed PMID: 10922001.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Single channel analysis of a novel NMDA channel from Xenopus oocytes expressing recombinant NR1a, NR2A and NR2D subunits. AU - Cheffings,C M, AU - Colquhoun,D, PY - 2000/8/2/pubmed PY - 2000/10/21/medline PY - 2000/8/2/entrez SP - 481 EP - 91 JF - The Journal of physiology JO - J Physiol VL - 526 Pt 3 N2 - Two types of subunit (an NR1 subunit and one of the NR2 subunits) are sufficient to form efficient NMDA receptors. In order to investigate whether functional receptors may contain more than one sort of NR2 subunit, NR1, NR2A and NR2D subunits were co-expressed in Xenopus oocytes. Single channel recordings from the oocytes showed, as expected, channel openings that are characteristic of NR1/NR2A receptors (ca 50 and 40 pS conductances), and channels characteristic of NR1/NR2D receptors (ca 40 and 20 pS conductances). However, they also contained a novel channel that contained conductances of ca 30, 40 and 50 pS, with direct transitions between all three levels. It is postulated that the novel channel contains NR1, NR2A and NR2D subunits. The implications of this for receptor stoichiometry are discussed. The novel channel was intermediate between the NR1/NR2A and NR1/NR2D 'duplet' receptors in the length of the channel activations, and in the probability of being open during activation. Its glycine sensitivity was much higher than that of NR1/NR2A, and was comparable with that of the other 'duplet' receptors. SN - 0022-3751 UR - https://www.unboundmedicine.com/medline/citation/10922001/Single_channel_analysis_of_a_novel_NMDA_channel_from_Xenopus_oocytes_expressing_recombinant_NR1a_NR2A_and_NR2D_subunits_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0022-3751&date=2000&volume=526&spage=481 DB - PRIME DP - Unbound Medicine ER -