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PMID:7531804

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Citation

Tsuzuki, K, Mochizuki, S, Iino, M, Mori, H, Mishina, M and Ozawa, S (1994) Ion permeation properties of the cloned mouse epsilon 2/zeta 1 NMDA receptor channel. Brain Res. Mol. Brain Res. 26:37-46

Abstract

The heteromeric mouse epsilon 2/zeta 1 N-methyl-D-aspartate (NMDA) receptor was expressed in Xenopus oocytes, and its channel properties were studied using both the outside-out patch-clamp and two-microelectrode voltage-clamp techniques. In the cloned receptor channel, permeation properties of monovalent and divalent cations, and voltage-dependent block by Mg2+ were similar to those reported previously in the native NMDA receptor channels. The sequence of single-channel conductances for alkali metals was Rb+ > Cs+ approximately K+ > Na+ > Li+, whereas the sequence of relative permeabilities was Cs+ > Rb+ > K+ approximately Na+ > Li+. The single-channel conductances measured in isotonic Ca2+, Sr2+ and Ba2+ solutions were almost equal, and approximately one-fifth of the value in the Na+ solution, although the permeabilities for these alkaline earth cations were higher than for Na+. It is likely that Ca2+, Sr2+ and Ba2+ would enter the NMDA receptor channel more easily than Na+, but would bind to a site in the channel more tightly, the net effect being a reduced value of the current.

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PubMed

Keywords

Animals; Cations, Divalent/metabolism; Cations, Monovalent/metabolism; Cell Membrane Permeability; Cloning, Molecular; Electric Conductivity; Evoked Potentials/drug effects; Female; Glutamic Acid/pharmacology; Glycine/pharmacology; Ion Channels/biosynthesis; Ion Channels/drug effects; Ion Channels/physiology; Mice; Oocytes/physiology; Patch-Clamp Techniques; Receptors, N-Methyl-D-Aspartate/biosynthesis; Receptors, N-Methyl-D-Aspartate/drug effects; Receptors, N-Methyl-D-Aspartate/physiology; Recombinant Proteins/biosynthesis; Recombinant Proteins/drug effects; Recombinant Proteins/metabolism; Xenopus laevis

Significance

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