IndraLab

Statements

CACNA1A activates IK. 10 / 10
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"As expected, bath application of NMDA to hippocampal cultures reduced the size of Kv2.1 clusters and produced a hyperpolarizing shift in the voltage-dependent activation of I K that was associated with dephosphorylated Kv2.1 channels."
19185209
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"In the present study, we show that in hippocampus, ethanol prevents the NMDA-induced hyperpolarizing shift in the voltage-dependent activation of neuronal I K and reduces the unclustering and dephosphorylation of Kv2.1 channels."
19185209
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"In addition, ischemic conditions produced calcineurin-dependent dephosphorylation and unclustering of Kv2.1, hyperpolarizing shifts in voltage-dependent activation of I K , and reduced spontaneous calcium transients ( xref )."
18753382
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"In agreement with previous studies using exogenously applied glutamate, we observed that bath application of NMDA potently and rapidly unclustered and dephosphorylated Kv2.1 channels and produced a hyperpolarizing shift in the voltage-dependent activation of neuronal I K . Previous studies have shown that hyperactivity associated with seizures or KCl-induced membrane depolarization causes dephosphorylation and unclustering of Kv2.1 channels ( xref )."
18753382
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"Bath application of NMDA potently unclustered and dephosphorylated Kv2.1 and produced a hyperpolarizing shift in voltage-dependent activation of I K . In contrast, driving synaptic activity in Mg 2+ -free media to hyperactivate synaptic NMDA receptors had no effect on Kv2.1 channels, and moderate pentylenetetrazole-induced seizure activity in adult mice did not dephosphorylate hippocampal Kv2.1 channels."
18753382
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"Glutamate-stimulation of hippocampal neurons has diverse effects on voltage-dependent activation and inactivation of I K via Ca 2+ /calcineurin-dependent intracellular signaling."
19276663
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"A submaximal concentration of Compound II (50 nM) had a significant effect on the time and voltage dependent activation of iK and caused a positive shift of the iK activation curve."
9550297
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"Hyperpolarizing shifts in the voltage-dependent activation of neuronal I K are associated with a dephosphorylation of the Kv2.1 channel ( xref , xref )."
20092568
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"Indeed, we found that the cell-permeable Zn 2+ chelator TPEN significantly attenuated the hyperpolarizing shift in the voltage-dependent activation of I K to the same extent as calcineurin inhibition."
20092568
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"The voltage-dependent activation of the ATP-induced IK during 500 ms depolarizing test pulses could be described by a Boltzmann equation with a half-activation voltage (V1/2) of 11.5 mV and slope factor (k) of 12.0 mV, which were close to those of IKs (V1/2 of 12.1 mV and k of 12.3 mV), determined as an E-4031-resistant IK, under the same isochronal (500 ms) activation conditions."
9288673