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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | A large number of subunits of mammalian K ϩ channels expressed in the CNS have been identified after the cloning of the Shaker gene in Drosophila in 1987 (reviewed in. This work has revealed the existence of an extraordinary diversity of molecular components of voltage-gated K ϩ channels, predicting a functional diversity well beyond that expected from prior functional studies. The cloning studies have allowed enormous progress in the understanding of the molecular mechanisms of channel function, including the recent crystallization and high resolution structural analysis of a K ϩ channel. Less progress has been obtained in understanding the physiological significance of the molecular diversity. A major task of future research is to identify physiological roles of the cloned proteins, starting with the identification of native channels containing specific types of cloned subunits. | [
"TASK1"
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | Among the cloned subunits are the members of the Kv and KCNQ (or KQT) families of K ϩ channel proteins, which are pore-forming components of voltage-gated K ϩ channels. The Kv family is divided into several subfamilies based on sequence similarities. Nearly 30 Kv proteins classified in eight subfamilies (Kv1-Kv6 and Kv8 -Kv9) are known to date. | [
"Kv"
] | [
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | The goal of this study was to identify the currents mediated by channels containing proteins of the Kv3 subfamily in neurons. There are four known Kv3 genes (Kv3.1-Kv3.4). In heterologous expression systems, Kv3.1 and Kv3.2 proteins express tetraethylammonium (TEA)-sensitive delayed rectifier type currents, whereas Kv3.3 and Kv3.4 proteins form transient, TEA-sensitive, A-type K ϩ channels (reviewed in Vega-Saenz de. However, native channels may differ from those formed by a given Kv subunit in heterologous expression systems. Kv proteins can form heteromeric channels with novel properties with other members of the same subfamily. Moreover the functional characteristics of K ϩ channels, including those of the Kv family, also can be modified by accessory subunits and postranslational modifications. | [
"Kv3.1",
"Kv3.2",
"Kv3.3",
"Kv3.4",
"Kv"
] | [
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | We have shown previously in a study combining immunohistochemical and electrophysiological analysis in slice preparations that drugs that block Kv3.1 currents in heterologous | [
"Kv3.1"
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked ''advertisement'' in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. | [] | [
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | expression systems blocked a fraction of the K ϩ current from hippocampal interneurons expressing Kv3.1b proteins that resembles Kv3.1 currents in activation and deactivation properties. However, limitations associated with voltage clamping intact neurons in slices prevented a detailed comparison of the properties of the putative Kv3.1-mediated currents in these cells with the properties of Kv3.1 currents in heterologous expression systems. Both Kv3.1 and Kv3.2 proteins are strongly expressed in neurons of the globus pallidus (GP), suggesting that these cells might be a good system to study the properties of native Kv3.1-Kv3.2 channels using voltage-clamp methods. Moreover, methods to dissociate these neurons from rat brain have been developed. Freshly dissociated and short term cultured cells are a good system for this kind of study, allowing improved conditions for space clamp and pharmacological analysis. | [
"Kv3.1",
"Kv3.2"
] | [
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | We have used whole cell patch-clamp methods to analyze the voltage-dependent K ϩ currents of freshly dissociated rat GP neurons to determine whether they contain currents with properties similar to those carried by Kv3.1-Kv3.2 channels. Because of its central roles in movement control and perhaps also cognitive functions, there is great interest in the anatomic and physiological characterization of the GP. The present studies contribute novel information on the classification and cellular properties of pallidal neurons. | [
"Kv3.1",
"Kv3.2"
] | [
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | Previous electrophysiological analysis of the K ϩ currents of pallidal neurons, in the same species, revealed a low voltageactivating fast inactivating current (I A ), a component with slower inactivation and slow recovery from inactivation that is blocked by micromolar concentrations of 4-AP (I As ), and two maintained components one blocked (I K ) and one not blocked by 10 mM TEA. None of these components resembles Kv3 currents. These observations do not necessarily indicate that Kv3 currents are either absent in pallidal neurons or have properties different from those of Kv3 currents in heterologous expression systems because the methods that are used in a given study to isolate individual components of the total K ϩ current are tailored to the goals of the particular investigation. Therefore electrophysiological experiments specifically designed to search for native currents with properties similar to those of Kv3.1-Kv3.2 currents in vitro are required before we can conclude whether or not native Kv3.1-Kv3.2 channels in pallidal neurons have properties similar to those in heterologous expression systems. | [
"Kv3.1",
"Kv3.2"
] | [
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | In this study, we first analyzed the expression of Kv3.1 and Kv3.2 proteins in the rat GP with specific antibodies. We also determined the developmental expression of these proteins, allowing us to select tissue at developmental stages in which the proteins are robustly expressed in pallidal neurons. We used pharmacological and electrophysiological protocols on freshly dissociated neurons appropriate for the isolation of Kv3-like currents and compared these currents to those recorded under identical conditions from mammalian cells trans-fected with Kv3.1 and Kv3.2 cDNAs. The expression of Kv3 transcripts in the same cells was confirmed by single cell RT-PCR. The studies described here have been previously presented in abstract form (Herna ´ndez-. | [
"Kv3.1",
"Kv3.2"
] | [
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | Site-specific antibodies against Kv3.1b proteins were prepared by injecting into rabbits the peptide CKESPVIAKYMPTEAVRVT coupled via the cysteine to keyhole limpet hemocyanin (KLH). The peptide corresponds to the carboxyl terminal sequence of the Kv3.1b protein (residues 567-585). The characterization of this antibody was described previously. To raise antibodies against Kv3.2 proteins, rabbits were injected with the peptides: CTPDLIGGDPGDDEDLGGKR and CTPDLIGGDPGD-DEDLAAKR coupled via the cysteine to KLH. The peptides correspond to a sequence present in the constant region of the rat and mouse Kv3.2 proteins, respectively (residues 171-189 plus an N-terminal cysteine added to facilitate coupling), before the first membrane-spanning domain in an area not conserved among different K ϩ channel proteins (Vega-Saenz de for the rat sequence). The mouse sequence has not been published, but it is identical to that in rat except for the substitution of glycines (186 -187 by alanines). For affinity purification, the respective peptides were coupled to Sulfolink Sepharose resin (Pierce, Rockford, IL) via the cysteine residue and the sera purified following supplier's protocols. | [
"Kv3.2"
] | [
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{
"section": "INTRO",
"title": "Kv3.1-Kv3.2 Channels Underlie a High-Voltage-Activating Component of the Delayed Rectifier K ϩ Current in Projecting Neurons From the Globus Pallidus"
} | Male Sprague-Dawley rats (2-3 wk old) or male C57Bl6 mice (6 -8 wk old), as well as Kv3.1 Ϫ/Ϫ or Kv3.2 Ϫ/Ϫ ) mice, were anesthetized with an injection of pentobarbital sodium (120 mg/kg ip) and perfused transcardially with 10 -20 ml Heparin (1 U/ml) in phosphate-buffered saline (PBS: 0.06 M sodium phosphate buffer, 0.85% sodium chloride, pH 7.35) at room temperature followed by 100 -200 ml of 4% paraformaldehyde in 0.1 M sodium phosphate buffer, pH 7.4. The brain was dissected out and blocked coronally into ϳ5 mm portions, postfixed for 30 min in the same fixative at room temperature and placed in 30% sucrose in PBS for 12-24 h at 4°C. When the tissue had sunk in the sucrose solution, 50-m sections were produced using a freezing microtome and collected in PBS. The sections were washed twice for 15 min in PBS and incubated in a blocking solution containing 10% normal goat serum (Jackson Immuno Research), 1% bovine serum albumin (Jackson Immuno Research), 0.2% cold water fish gelatin (Sigma Chemicals), and 0.2% Triton X-100 (Sigma Chemicals) in PBS for 1 h to minimize nonspecific binding. The sections then were incubated with primary antibody at the appropriate dilution in a working buffer (0.1ϫ blocking solution in PBS) for 12-24 h at 4°C. For double-labeled sections, a primary rabbit antibody, anti-Kv3.1b or anti-Kv3.2, and a primary mouse antibody, anti-parvalbumin (Sigma Immunochemicals) were added simultaneously. After three 15 min washes in PBS, secondary antibodies diluted in working buffer were applied for 15 min at room temperature. The following secondary antibodies were used, Cy2conjugated goat anti-mouse IgG and Cy3-conjugated goat anti-rabbit IgG (Jackson Immuno Research). After two 15 min washes in PBS, the sections were mounted onto glass slides and coverslipped with elvanol. | [
"Kv3.1",
"Kv3.2"
] | [
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