NDLI: Altered voltage dependence of fractional Ca2+ current in N-methyl-D-aspartate channel pore mutants with a decreased Ca2+ permeability.

Content Provider	PubMed Central
Author	Schneggenburger, R.
Abstract	The Ca2+ permeability properties of an N-methyl-D-aspartate (NMDA) channel pore mutant (NR1E603K-NR2A) were studied using whole-cell patch-clamp recordings in human embryonic kidney cells. Measurements of reversal potential shifts indicated that the relative permeability of Ca2+ over monovalent ions, P(Ca)/P(M), was 1.6, a value reduced by a factor of approximately 2 with respect to the wild-type channel. The ratio of Ca2+ current over total current (fractional Ca2+ current), however, was 19.7 +/- 1% at -50 mV and 2 mM external Ca2+ concentration, a value similar to that of the wild-type channel, but 2.3-fold larger than that predicted by simple permeation models for the corresponding P(Ca)/P(M) value. The deviation from predicted values gradually disappeared with membrane depolarization. Similar results were obtained for two cysteine mutations at asparagine residues of the NR1 and NR2A subunits. When interpreted in terms of a two-barrier one-site model for ion permeation, the results indicate that changes in the relative Ca2+ permeability occur close to an internal energy barrier limiting ion permeation.
Related Links	http://dx.doi.org/10.1016/s0006-3495(98)77889-0
Ending Page	1794
Page Count	5
Starting Page	1790
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	4
Volume Number	74
Language	English
Publisher Date	1998-04-01
Access Restriction	Open
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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