Either your web browser doesn't support Javascript or it is currently turned off. In the latter case, please turn on Javascript support in your web browser and reload this page. Overexpression of the carboxyl terminus CT of the cognate channel Kv2. Here, we define a seven—amino acid declustering domain within Kv2. We present the first evidence of targeted disruption of Kv2. Stroke is the primary cause of serious long-term disability in the United States 1. While thrombolytic therapy i. Food and Drug Administration—approved neuroprotective drugs are available with the capability to mitigate the irreversible neuronal cell loss commonly associated with this neurological disorder. A hallmark of neuronal tissue damage following brain ischemia is the advent of excitotoxic injury and delayed apoptosis in the ischemic penumbra, a peri-infarct zone of collaterally perfused tissue surrounding the central necrotic core 2. A known key regulator of neuronal apoptosis is the delayed-rectifying voltage-gated potassium channel Kv2. Although this channel normally functions to modulate cell excitability 4 , 5 , it also plays a critical role in neuronal demise by allowing a loss of cytoplasmic potassium, optimizing intracellular conditions for programmed cell death 3 , 6 , 7. Neurons with decreased functional expression of Kv2. As a result, delayed proapoptotic Kv2. Exploration of neuroprotective strategies that mitigate delayed apoptotic cell death by inhibiting proapoptotic Kv2. Two separate membrane populations of Kv2. This second, much larger population of clustered Kv2. Critically, overexpression of the C terminus of the cognate channel Kv2. Here, we identify a critical seven—amino acid sequence within the Kv2. We show that this drug provides robust neuroprotection in vitro and, most critically, provide the first evidence of targeted disruption of Kv2. We first defined the minimal sequence within Kv2. To accomplish this, we analyzed the CT domains of both Kv2. S1A and Kv2. Both Kv2. Specifically, four critical residues exist within the PRC domain of Kv2. A seven—amino acid sequence that includes these four residues from Kv2. Notably, these sequences are also conserved for both Kv2. With this information, we hypothesized that the region encompassing amino acids to within Kv2. As these sequences omit one critical residue strongly implicated in cluster formation S in Kv2. We also generated plasmids encoding the DP-2 and Sc-2 sequences for comparative purposes, as prior work had used a Kv2. These expression vectors include the native upstream sequence containing the most proximal methionine to act as the start codon. These were tested first for their declustering properties by transfecting primary cortical neurons with a green fluorescent protein GFP —tagged Kv2.

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