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- W2023130009 abstract "CA2+-permeable glutamate receptors assembled from subunits containing a GLN residue at the RNA editing site in membrane domain 2 show strong inward rectification. In HEK 293 cells transfected with the kainate receptor subunit GluR6(Q), inward rectification is lost in outside-out patches, suggesting a role for diffusible, cytoplasmic factors. Inclusion of different polyamines in the internal solution restored inward rectification, whereas Mg2+ (1 mM) was inactive. Spermidine (Kd[0 mV] = 5.5 microM) was of higher affinity than spermidine (Kd[0 mV] = 25.4 microM) or putrescine (Kd[0 mV] = 1.2 mM). AMPA receptors assembled from GluRA(flip) showed even higher affinity for spermine (Kd[0 mV] = 1.5 microM). Analysis of the voltage dependence of whole-cell responses predicted intracellular free spermine and spermidine concentrations of 51 and 153 muM, respectively." @default.
- W2023130009 created "2016-06-24" @default.
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- W2023130009 date "1995-08-01" @default.
- W2023130009 modified "2023-10-18" @default.
- W2023130009 title "Inward rectification of both AMPA and kainate subtype glutamate receptors generated by polyamine-mediated ion channel block" @default.
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- W2023130009 doi "https://doi.org/10.1016/0896-6273(95)90049-7" @default.
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