
IndraLab
Statements
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"We previously found that seizures in rats in vivo , or glutamate stimulation of cultured rat hippocampal pyramidal neurons, led to calcineurin-dependent dephosphorylation of Kv2.1, and dispersion of Kv2.1 clusters. xref Initial experiments showed that glutamate stimulation of cultured neurons also led to significant hyperpolarizing shifts in voltage-dependent activation of neuronal I K . xref However, the potential impact of these changes on neuronal function could not be accurately deduced without a more comprehensive analysis of the effects of glutamate stimulation on the gating properties of neuronal Kv2.1 channels."
reach
"It has been proposed that inhibition of N-type Ca channels, known to be located at C-bouton synapses (Wilson et al., 2004), by G -dependent pathways following M2 receptor activation could lower the levels of local intracellular Ca , thus reducing calcineurin-related dephosphorylation of Kv2.1 channels (Deardorff et al., 2014; Romer et al., 2019)."
sparser
"Our study demonstrates that SDF-1α acts upon neuronal CXCR4 to induce an NMDA receptor-dependent elevation in [Ca 2+ ] i , leading to calcineurin-dependent dephosphorylation of Kv2.1, dispersal of channel clusters and enhancement of voltage-dependent activation of Kv2.1/ I DR currents."
sparser
"For example, cytosolic Ca 2+ increase and subsequent calcineurin activation affects the gating kinetics of I DR channels via dephosphorylating Kv2.1 channels, since calcineurin-dependent dephosphorylation of Kv2.1 decreases the threshold for I DR channel opening and disrupts channel clustering, resulting in changes of activation kinetics [ xref xref ]."
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"We previously found that reversible calcineurin-dependent Kv2.1 dephosphorylation as induced by ischemic insult is neuroprotective. xref However, sustained activation of Kv2.1, as occurs upon induction of apoptosis xref , or prolonged treatment with high levels of glutamate xref , might lead to excessive K + efflux, and subsequent induction of apoptotic or excitotoxic cell death, as we suggested previously. xref "