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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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{
"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 following primary antibody concentrations were used: antibodies against ) at 1:50, Kv3.2 ) at 1:50, parvalbumin (Sigma Immunochemicals) at 1:400. Secondary fluorescent antibodies were used at 1:500. The atlas by and the book edited by were used as guides to identify CNS neuronal populations and axonal projections. | [
"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"
} | Images were taken either with a Zeiss Axiophot fluorescent microscope or an Axiovert 35 M confocal microscope, with a ϫ40 (NA 1.3) or ϫ63 (NA 1.4) objective lenses. Fluorescent images were recorded using a scanning laser attachment (MRC-600 and MRC-1000, Bio-Rad Laboratories) and a krypton/argon mixed gas laser. Images were collected digitally and transferred to a graphics program (Adobe Photoshop 4.0). After brightness and contrast adjustments, the image files were printed on a Tektronix printer (Phaser 440). | [] | [
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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"
} | Rat brain membrane extracts were prepared from a P3 fraction of tissue homogenate solubilized for 1 h in a 2% Triton X-100 solution containing (in mM) 50 potassium phosphate buffer, pH 7.4; 50 KCl; 2 EDTA; 1 pepstatin A, 1 1,10phenanthroline, 0.2 phenylmethylsulfonyl fluoride (PMSF), and 1 iodoacetamide to inhibit proteases. The suspension was spun at 100,000 g to remove nonsolubilized material, and the top two-thirds of the supernatant used for further experiments. To prepare membrane extracts from the GP, the nucleus was dissected from slices prepared as described for the preparation of dissociated neurons and proteins solubilized as described in the preceding text. | [] | [
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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"
} | To prepare immunoblots, 50 g of membrane protein was mixed 1:1 with a sample buffer [10% (vol) glycerol, 5% (vol) b-mercaptoethanol; 60 mM Tris-HCl pH 6.8; 0.001% (weight) bromophenol blue and 3% SDS], heated for 3 min at 80°C, and electrophoresed in a 8% SDS polyacrylamide gel. The electrophoresed proteins were transferred onto a nitrocellulose filter (Bio Rad). Blots were incubated with either Kv3.2 antibodies at a 1:100 dilution or Kv3.1b antibodies at 1:2000, followed by incubation with horseradish peroxidase-linked anti-rabbit secondary antibodies (Promega). Bound antibodies were detected using chemilluminscence (Pierce). | [
"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"
} | Before immunoprecipitation, 300 l of solubilized membranes (ϳ400 g protein) in 1% Triton X-100 in (in mM) 50 Tris, 150 NaCl, 1 EDTA, and 1 EGTA, pH 7.4, were precleared for 30 min at 4°C with protein A-Sepharose beads (Sigma Chemicals). After removing the beads, the extracts were incubated for 4 h at 4°C with Kv3.2 antibodies at a 1:10 dilution or Kv3.1b antibodies at 1:50 dilution. At the end of the incubation period, fresh protein A-Sepharose beads were added, and the suspension was incubated for 2-3 h at 4°C with shaking. The complexed beads were collected and washed three times in 1% Triton X-100 in (in mM) 50 Tris, 150 NaCl, 1 EDTA, and 1 EGTA, pH 7.4. Proteins then were extracted by adding an equal volume of sample buffer, heated for 3 min at 80°C and processed for immunoblotting as described in the preceding text. | [
"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"
} | CHO cells were cultured in ␣-MEM (pH 7.4, GIBCO BRL, Gaithersburg, MD) supplemented with 10% of fetal bovine serum (FBS, GIBCO BRL) in the presence of penicillin and streptomycin at 37°C in a 95% O 2 with 5% of CO 2 atmosphere in 100-mm-diam culture dishes (Costar, Cambridge, MA). When the cells were confluent, the monolayer was incubated with trypsin-EDTA (GIBCO BRL) for Յ1 min, and the cells resuspended in ␣-MEM containing 10% of FBS and plated at a 1/5 dilution in new 100 mm dishes. The medium was changed every 2 days, and the cells passed every 4 days. | [] | [
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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"
} | To study Kv3.2 currents, we used the Kv3.2a stably transfected cell line previously described. To study Kv3.1 currents, wild-type CHO cells were transiently transfected with Kv3.1b cDNA. After reaching 90% confluence in 100 mm dishes, CHO cells were trypsinized and resuspended in 2 ml of ␣-MEM with 10% FBS. One milliliter of the cell suspension was diluted and plated in 30 mm dishes at 40% confluence. Two to 4 h later, when the cells had attached to the bottom of the dish, they were washed two times with ␣-MEM without serum and transfected with Lipofectamine (Life Technologies, Gaithersburg, MD) following the manufacturer's protocols. To identify transfected cells, they were cotransfected with a second plasmid containing the cDNA encoding the reporter protein Green Fluorescent Protein (GFP, Life Technologies, Gaithersburg, MD). Transfected cells were detected by the emission of green fluorescence (520 nm) under epifluorescence with 488 nm excitation light. Typically, electrophysiological recordings were carried out 1-2 days after transfection. | [
"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"
} | Young Sprague-Dawley rats 10 -16 days of age were used. The brain was quickly removed and submerged in ice-cold normal extracellular solution (NES) containing (in mM) 130 NaCl, 3 KCl, 2 MgCl 2 , 1 NaHCO 3 , 0.5 NaH 2 PO 4 , 5 HEPES, 2 CaCl 2 , and 5 glucose, pH 7.4. The solution was gassed with 95% O 2 -5% CO 2 for 15 min before starting the dissociation and then continuously during the procedure. Once the cerebellum had been removed, the brain hemispheres were separated along the midline and cut in the parasagittal plane with a vibratome (Campden Instruments, London, UK) in 400 m slices. The slices were collected and maintained in ice-cold NES solution. The GP was identified by visual inspection under a stereomicroscope (see. The GP from four to seven slices was dissected out and subjected to enzymatic digestion for 25-35 min (depending on the age of the animal) at 37°C in NES with Pronase (Sigma Chemicals, St. Louis, MO). The tissue then was washed three times in NES without calcium and triturated mechanically by means of glass Pasteur pipettes with tips of decreasing diameters in a final volume of 2 ml. An aliquot (ϳ500 l) of the cell suspension was seeded in a recording chamber (RC-13, Warner Instruments, Hamden, CT) and mounted on the plate of an inverted microscope for electrophysiological recording. The cells were perfused continuously (ϳ1 ml/min) with NES at room temperature. | [] | [
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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"
} | Electrophysiological recordings used voltage clamp under the whole cell configuration of the patch-clamp technique. The same extracellular and intracellular solutions were used for recordings with CHO cells and pallidal neurons. Extracellular solution (NES) was supplemented with 1 M tetrodotoxin (TTX; Alomone, Jerusalem, Israel) and 200 M of CdCl 2 (Sigma Chemical) to block voltage-dependent sodium and calcium currents, respectively. By inhibiting calcium influx, CdCl 2 also limited the activation of calcium-activated potassium currents. Potassium channel blockers (TEA, Sigma; 4-AP, Aldrich; charybdotoxin and dendrotoxin, Alomone) were dissolved in NES with TTX and CdCl 2. All the experiments were carried out at room temperature (21-23°C). | [] | [
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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 recording patch electrodes were made with borosilicate glass capillary tubes (GC120F-10, Warner Instrument) filled with an intracellular solution containing (in mM) 106 KH 2 PO 4 , 2 MgCl 2 , 10 HEPES-K, 10 BAPTA-K (Molecular Probes, Eugene, OR), 2 ATP-Mg, and 0.5 GTP (Sigma Chemicals); pH 7.35 with NaOH. The use of a high concentration of the fast calcium chelator bis-(o-aminophenoxy)-N,N,NЈ,NЈ-tetraacetic acid (BAPTA) was aimed at further limiting the activation of calcium-activated membrane conductances. The typical resistances of the electrodes when filled with this solution varied between 2.5 and 3.0 M⍀. The patch pipette Ag-Cl wire was connected to the input of an Axopatch-1D or Axoptach 200A amplifier (Axon Instruments, Foster City, CA). To generate voltage clamp protocols and for data acquisition and analysis, we used the pClamp software (Axon Instruments). Large neurons with short processes (Ͻ40 m) were selected for recording. Series resistance was estimated from the time constant of the capacity transient and ranged between 5 and 10 M⍀ in the cells used for analysis. The series resistance was compensated (70 -80%) and monitored throughout the course of the experiment. If the series resistance could not be compensated or if it changed by Ͼ20%, the cell was discarded. Input capacitance of the cells included in this study ranged between 15 and 33 pF and the time constant of the capacity current transient between 0.18 and 0.31 ms. Drugs were applied locally by means of a puffer pipette with a relatively wide tip (10 m), made of a pulled borosilicate glass capillary and placed with a second micromanipulator to a distance of 100 -200 m of the cell. The application was made either by gravity or pressure pulses (10 psi) controlled with a picospritzer device (General Valve). | [] | [
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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 presence of Kv3s mRNAs in dissociated GP cells was determined by single-cell RT-PCR. This was performed as described by Vega-Saenz de with the following modifications: the solutions were prepared in double-distilled RNase-free water from Sigma. The content of individual cells was collected from the recording chamber using gentle suction with a wide tip glass micropipette filled with 3 l of a solution containing 150 mM KCl, 30 mM Tris-HCl, pH 8.3, and 10 U of Promega RNase inhibitor. The tip of the pipette was broken inside a 500-l Eppendorf tube, and its contents emptied. The tubes were placed in dry ice-ethanol bath to freeze the contents and then stored at Ϫ70°C until use. | [] | [
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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"
} | For reverse transcription, 17 l of a solution containing 1.18 mM dNTP, 3.82 mM MgCl 2 , 50 U of Moloney Murine Leukemia Virus RNase H minus reverse transcriptase (Gibco-BRL), 4.4 M random hexamer primer (Pharmacia), 20 U/ml of RNase inhibitor, 30 mM KCl, and 6 mM Tris-HCl pH 8.3, were added to the Eppendorf tube containing the neuron's contents. Mineral oil (50 l) were laid on top of the aqueous solution and the tubes incubated successively at 25°C for 5 min, 37°C for 15 min, and 42°C for 15 min. The tubes then were heated at 94°C for 5 min and then cooled to 0°C until used for PCR amplification. | [] | [
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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"
} | For PCR amplification, 75 l of a solution containing 50 mM KCl, 0.85 mM MgCl 2 , 1.7 M of the sense and antisense external primers, and 10 mM Tris-HCl, pH 8.3 were added to the tubes containing the reverse-transcribed DNA. The tubes were heated for 5 min at 94°C. While the tubes were at 94°C, 5 l of a solution containing 2.5 units of Perkin Elmer Taq polimerase, 50 mM KCl, and 10 mM Tris-HCl pH 8.3 were introduced through the oil. The tubes then were subjected to 35 cycles of denaturalization at 94°C for 1 min, annealing at 48°C for 1 min, and extension at 72°C, for 1 min followed by one final incubation at 72°C for 7 min. One microliter of a 1:1 dilution of the previous reaction was used as template for the second PCR reaction in a new PCR tube. 94 l of a solution containing 2.63 mM MgCl 2 , 210 M dNTPs, 50 mM KCl, 10 mM Tris-HCl pH 8.3, and 160 nM of the specific primers were added to these tubes. Oil (50 l) was laid on top and the tubes heated and Taq polimerase added as described in the preceding text. The tubes were subjected to 35 cycles of PCR amplification (1 min each of denaturalization, annealing and extension at 94, 55, and 72°C, respectively) followed by a last extension period at 72°C for 7 min. The PCR products were analyzed by electrophoresis in 2% agarose gels. | [] | [
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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 external degenerate primers, designed to amplify all Kv3 sequences, from Drosophila to man, used in the first PCR reaction, had the following sequences: sense primer, CTC GAA TTC I TT(C/T) TG(C/T) (C/T)TN (A/G)A(A/G) ACN CA; antisense primer, CTC-GAATTC GGA (A/G)TA (A/G)TA CAT N(C/G)C (G/A)AA (G/A)TT. The sequence for the specific primers was: Kv3.1, sense primer: CGC TTC AAC CCC ATC GTG AAC (position 1801-1821 in Accession No. M68880); antisense primer: GTG TGT GTG TTC GCT GGC. The size of the expected product is 532bp. Kv3.2, sense primer CC AGC GCT GTT CTC CAG TAT (882-901 in No. M34052); antisense primer: C AAT GGG GAT GTT. The size of the expected product is 477 bp. Kv3.4, sense primer: CCT GAT ACG TTG GAC TTT GTC (1312-1333 in No. X62841), antisense primer: ATT GCC CCG TGG GTC AGA T (1629 -1647). The size of the expected product is 336 bp. | [
"Kv3.1",
"Kv3.2",
"Kv3.4"
] | [
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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 of Kv3.1 and Kv3.2 proteins in the rat GP Kv3 mRNAs are not expressed at significant levels before birth. Immunoblots using antibodies against Kv3.1 and Kv3.2 were used to study the postnatal developmental expression of Kv3.1 and Kv3.2 proteins in membrane extracts from the GP. Membranes were prepared from GP dissected in the same fashion as the tissue used to prepare dissociated neurons. The levels of both proteins increased significantly after postnatal days 6 -8, although it appears that the expression of Kv3.1 develops somewhat faster than the expression of Kv3.2. Maximum levels of Kv3.1 protein were seen around p15 , lanes 1-4), whereas for Kv3.2, maximum levels were not achieved until p20 , lanes 5-7). Both proteins were not detectable earlier than p6 -7. Similar results were obtained in three separate experiments with each antibody. | [
"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"
} | The bands observed with Kv3.1 or Kv3.2 antibodies are not seen when the immunoblots are reacted with antibodies preincubated with an excess of the Kv3.1 or Kv3.2 peptides , lane 2) used to prepare the antisera. Also, no bands are detected in immunoblots treated with the preimmune sera derived from the rabbit used to raise the Kv3.2 antibodies , lane 3). Moreover, the Kv3.2 protein is absent in membranes derived from Kv3.2 Ϫ/Ϫ mice , lane 5) but is present in membranes from Kv3.1 Ϫ/Ϫ mice , lane 4), whereas the reverse is seen with Kv3.1 antibodies , lanes 6 and 7). | [
"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"
} | Immunohistochemistry was used to study the cellular and subcellular localization of Kv3.1 and Kv3.2 proteins in the rat GP. Antibodies against Kv3.1 produced strong staining of the somatic membrane and the cytoplasm immediately beneath the membrane of neurons located throughout the GP. Fewer stained cells were seen in the most lateral border of the nucleus. The same section shown in was stained with antibodies against parvalbumin. Most neurons positive for Kv3.1 also are stained for parvalbumin and vice versa. As in other neurons expressing Kv3.1, there is little staining of the dendrites of pallidal neurons. There was a faint staining of the pallidal neuropile. Higher magnification images from another experiment confirmed that Kv3.1b proteins and parvalbumin are expressed in the same pallidal neurons , although parvalbumin staining tends to occupy most of the cytoplasm, whereas Kv3.1b staining is stronger in the proximity of the membrane. Antibodies against Kv3.2 also were expressed in parvalbumin-containing neurons , although Kv3.2 antibodies produced a somewhat stronger staining of the neuropile than the antibodies against Kv3.1. Background staining is observed when the sections are treated with antibodies preincubated with the corresponding immunogenic peptide (data not shown). Kv3.1 and Kv3.2 antibodies also stain the GP in mouse and. Kv3.1 or Kv3.2 staining is absent in tissue derived from the corresponding knockout mice , confirming the specificity of both antibodies for immunohistochemistry. | [
"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"
} | The immunohistochemical data suggest that both Kv3.1 and Kv3.2 are co-expressed in the same pallidal neurons, the projecting, parvalbumin-containing neurons, which are the main neuronal population in the GP ). Kv3 proteins form heteromultimeric channels in vitro with other Kv3 proteins but not with proteins of other subfamilies (K.. This is similar to what has been observed with other Kv proteins. Because both Kv3.1 and Kv3.2 proteins are expressed in the same pallidal neurons, it is likely that both proteins are part of the same heteromeric channels. To test this hypothesis, we used immunoprecipitation assays from pallidal membranes solubilized with nondenaturing detergents. As shown in , antibodies against Kv3.1 or Kv3.2 proteins immunoprecipitate both Kv3.1 and Kv3.2 proteins. Thus immunoblots with Kv3.1 antibodies stain Kv3.1 proteins immunoprecipitated with Kv3.1 , lane 1) or Kv3.2 antibodies , lane 2); and immunoblots with Kv3.2 antibodies identify Kv3.2 proteins in Kv3.1 , lane 6) and Kv3.2 , lane 5) immunoprecipitates. No channel protein is detected when the immunoprecipitation is done with antibodies preincubated with the corresponding immunogenic peptide , lanes 3 and 4 and 7 and 8). The coimmunoprecipitation studies demonstrate that heteromeric complexes. Expression of Kv3.1 and Kv3.2 proteins in the rat globus pallidus (GP). A: immunoblots of rat pallidal membrane extracts treated with Kv3.2 antibodies (lane 1), with Kv3.2 antibodies pretreated with Kv3.2 peptides (lane 2), with preimmune sera (lane 3), and immunoblots of pallidal membrane extracts obtained from Kv3.1 Ϫ/Ϫ mice ) (lanes 4 and 6) or Kv3.2 Ϫ/Ϫ mice ) (lanes 5 and 7) treated with Kv3.2 antibodies (lanes 4 and 5) or Kv3.1 antibodies (lanes 6 and 7). B: Kv3.1 proteins detected in immunoblots of rat brain membrane extracts obtained from postnatal day 8 rats (lane 1), postnatal day 11 (lane 2), postnatal day 15 (lane 3), and postnatal day 20 animals (lane 4); and Kv3.2 proteins detected in immunoblots of rat brain membrane extracts obtained from postnatal day 15 rats (lane 5), postnatal day 20 (lane 6), and adult (11 wk, lane 7). C: immunoblots of Kv3.1 proteins immunoprecipitated from GP membrane extracts from 2-wk-old rats with anti-Kv3.1b antibodies (lane 1), anti-Kv3.2 antibodies (lane 2), anti-Kv3.1b antibodies pretreatead with Kv3.1b peptide (lane 3), and anti-Kv3.2 antibodies pretreated with Kv3.2 peptides (lane 4). Immunoblots of Kv3.2 proteins immunoprecipitated from the same membrane extracts as in lanes 1-4 with anti-Kv3.2 antibodies (lane 5), anti-Kv3.1b antibodies (lane 6), anti-Kv3.2 antibodies pretreatead with Kv3.2 peptides (lane 7), and anti-Kv3.1b antibodies pretreated with Kv3.1b peptide (lane 8). | [
"Kv3.1",
"Kv3.2",
"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"
} | of both types of channel proteins exist in pallidal membranes. Taken together the data suggest that parvalbumin-containing projecting pallidal neurons have heteromeric channels containing both Kv3.1 and Kv3.2 subunits. | [
"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"
} | To compare the properties of the currents recorded from CHO cells transfected with Kv3.1 or Kv3.2 cDNAs with putative Kv3 currents in freshly dissociated pallidal neurons, all cells were recorded with identical intra-and extracellular solutions. CHO cells transfected with cDNAs encoding Kv3.2a or Kv3.1b proteins had large delayed rectifier-type voltagedependent K ϩ currents that resembled the currents observed in Xenopus oocytes injected with Kv3.2a or Kv3.1b cRNAs (reviewed in Vega-Saenz de ). Both Kv3.2a or Kv3.1b currents start activating when the membrane is depolarized to potentials more positive than Ϫ10 mV and rise relatively fast (as compared with other voltage-gated K ϩ channels) (see , with a similar time course, to a maximum level that is maintained for the duration of the pulses used in this experiment. A slow inactivation becomes evident with pulses of longer duration (data not shown). Untransfected CHO cells had negligible outward currents under the same pulse protocols (Ͻ100 pA for the largest depolarizations). | [
"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"
} | Preliminary studies with pallidal neurons showed that a large proportion of the outward current in these cells could be suppressed by holding the membrane at depolarized potentials. This could be a useful strategy to eliminate a fraction of the potassium currents if Kv3 currents are not affected by such treatment. We therefore tested the effect of varying the holding potential on Kv3.1 and Kv3.2 currents expressed in isolation. | [
"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"
} | of the form G/G max ϭ 1/[1 Ϫ exp(V m Ϫ V 1/2 )/k]. | [] | [
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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"
} | From these fits, we derived a midpoint of activation of V 1/2 ϭ 12.1 Ϯ 1.26 mV (n ϭ 6) for Kv3.2 currents and 18.1 Ϯ 1.01 mV (n ϭ 6) for Kv3.1 and a steepness parameter k of 8.4 Ϯ 0.25 mV for Kv3.2 and 11.0 Ϯ 0.2 mV for Kv3.1. Kv3 currents are unusual in requiring very depolarized potentials to start activating. However, the midpoints of the conductance-voltage relationships of Kv3 channels are not that different from those of other voltage-dependent K ϩ currents, reflecting a steep voltage dependence. This distinguishes mammalian Kv3 currents from the currents expressed by the Drosophila Shaw protein, which also starts activating at high voltages but has a very weak voltage dependence, producing a midpoint of activation above ϩ70 mV. | [
"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"
} | Another unusual feature of Kv3 currents is the fast rate of deactivation on repolarization, first described for Kv3.1 currents expressed in NIH-3T3 and L929 cells by. These authors found that Kv3.1 currents deactivated ϳ10 times faster than several other cloned mammalian voltage-gated K ϩ channels when compared at the same membrane potentials. Since then, many new voltage-gated channels have been identified in mammals; however, only one of them, Kv1.7, a nonneuronal member of the Kv1 family, deactivates fast (closing rates are ϳ3 times the deactivation rates of Kv3.1 channels) ). Kv3.1 currents also deactivate extremely fast in CHO cells under our recording conditions. Kv3.2 currents deactivate at rates somewhat slower than Kv3.1 but still significantly faster than K ϩ currents from channels of other subfamilies. | [
"Kv1.7",
"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"
} | At present there are no specific blockers for Kv3.1 and Kv3.2 channels. However, in Xenopus oocytes all Kv3 currents are blocked by low concentrations of TEA or 4-aminopyridine (4-AP) (reviewed in Vega-Saenz de ). Kv3.1 and Kv3.2 currents in CHO cells, under our recording conditions, were also very sensitive to these channel blockers. TEA dose-response curves for Kv3.1 and Kv3.2 currents are shown in. From these curves, we derived IC 50 s of 0.28 mM (n ϭ 4) for Kv3.2 and 0.38 mM (n ϭ 4) for Kv3.1 currents. We also have confirmed that as in other experimental systems shown). The effects of 4-AP on these currents were not examined in detail. Preliminary experiments discarded 4-AP as a useful tool to distinguish native currents carried by channels of the Kv3 subfamily in pallidal neurons because the drug blocks, also at low concentrations, a component of the outward current that also is blocked by dendrotoxin. | [
"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"
} | The currents obtained when both Kv3.1 and Kv3.2 proteins are co-expressed in Xenopus oocytes (Vega-Saenz de or CHO cells (data not shown) are similar to those obtained in cells expressing only one of the two subunits. This is not surprising given the similarities between Kv3.1 and Kv3.2 currents and is consistent with the observation that heteromultimeric Kv channels have properties intermediate between those of the corresponding homomultimeric channels ). The properties of Kv3.1 and Kv3.2 currents in CHO cells are summarized in Table. | [
"Kv3.1",
"Kv3.2",
"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"
} | As a product of the enzymatic dissociation of the GP, we typically found two morphological subtypes of neurons , similar to those observed in previous studies of dissociated pallidal neurons. We also found astrocytes and a population of small cells (data not shown). All our records were obtained from the two mV. In all cases, depolarizing pulses were applied from Ϫ30 to ϩ40 mV in 10-mV increments. E and F: plots of normalized conductance (G/G max ) as a function of voltage obtained from current records from several Kv3.2 (E)-and Kv3.1-transfected (F) cells, (n ϭ 4). Conductance (G ϭ I/V Ϫ V K ) values were computed from current data using a potassium equilibrium potential (V K ) of Ϫ80 mV, which was the average reversal potential in these cells and is close to the expected K ϩ equilibrium potential of ϳϪ90 mV. main types shown in. Most neurons (type A, , A and B) had bipolar-fusiform or triangular shape and were similar in size and morphological appearance to pallidal GABAergic projecting neurons ). The second type, much less frequently encountered (type B, , consisted of multipolar cells that were distinguished mainly by having somas significantly larger than those of type A cells. These cells may correspond to the large cholinergic neurons that lie along the medial border of the GP ), but no evidence of this was obtained in this study. | [
"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"
} | It was also possible to group the dissociated GP neurons according to the amount and kinetics of the transient currents observed when the cells were depolarized from a holding potential of Ϫ80 mV. shows records from three different neurons at two holding potentials. The cell shown in A has very little low-voltage activating A-type current, whereas this current is large in the cells shown in C and E. In addition, All measurements are reported at room temperature. References: 1, this work; 2,. V on , minimum voltage at which there is significant activation of the current; V 1/2 , membrane potential at which the conductance is half maximal; k, slope of normalized G-V curve; t on , time for the current to rise from 10 to 90% of its final value for noninactivating currents and time to peak for inactivating currents, both at ϩ40 mV; off , time constant of deactivation at Ϫ40 mV; Inactivation , time constant of inactivation at ϩ40 mV; NA, not applicable. the cell shown in E has a substantial amount of a slowly inactivating A-type current similar to the I As described in pallidal neurons by. The records in also show that a holding potential of Ϫ40 mV and inactivates not only the transient currents but also a substantial portion of the sustained current. We did not observe a clear correlation between the phenotype of the currents at a holding potential of Ϫ80 mV and the cell's morphology. | [] | [
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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 experiments described next, aimed at searching for Kv3.1-and Kv3.2-like currents in dissociated pallidal neurons, asked whether in these cells there is a component of the potassium current whose kinetics, voltage dependence, and pharmacology resembles those of the currents recorded under the same experimental conditions in CHO cells expressing Kv3.1 or Kv3.2 proteins. The results will be presented in two parts each comprising results obtained from one of two distinct subpopulations of GP neurons, distinguishable by their morphology and electrophysiological characteristics: type A and type B cells. As indicated in METHODS, identical intra-and extracellular solutions to those used to record currents in CHO cells were used in pallidal neuron recordings. | [
"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"
} | This group was composed of cells with fusiform/bipolar and triangular/multipolar somata (such as those shown in and. Typical records obtained from a cell with these mor-phological characteristics are shown in. shows a family of currents obtained during depolarizing pulses from a holding potential of Ϫ40 mV, and illustrates the currents obtained in the same cell after the application of 1 mM TEA to the external solution. The studies with Kv3.1 and Kv3.2 currents in heterologous expression systems indicate that such a concentration of TEA should eliminate an important fraction (ϳ80%) of the current generated by Kv3 channels. A holding potential of Ϫ40 mV was used to reduce the components of the total K ϩ current and facilitate the isolation of Kv3-like currents, which are not significantly affected by holding the membrane at this potential (see. | [
"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"
} | The currents recorded under control conditions (I GPc ) begin to activate at about Ϫ20 mV and have characteristics of delayed rectifying currents. The TEA-resistant current component (I GP, R ) also possesses characteristics of a sustained current of the delayed rectifier-type, although its activation kinetics is slower than that of I GPc. shows the current component sensitive to TEA (I GP, TEA ), obtained by digital subtraction of the current traces shown in B from the corresponding traces in A. In type A cells, I GP, TEA is also a sustained current of the delayed rectifier type that represents in this cell ϳ50% of the total current from a holding potential (V H ) of Ϫ40 mV. Typically the activation kinetics of I GP, TEA was faster than that of I GP, R (compare and. It is also apparent from the records shown in , B and C, that the TEAresistant and -sensitive components of the current in this cell also differ in their rate of deactivation at Ϫ40 mV. The deactivation of I GP, R is slow as compared with the rate of deactivation of I GP, TEA (deact ϭ 25.64 Ϯ 3.38 ms (n ϭ 9) for I GP, R and 2.72 Ϯ 0.24 ms (n ϭ 6) for I GP, TEA ). While the proportion of I GP, R and I GP, TEA varied among type A cells (I GP, TEA ranged between 30 and 85% of total current at a V H of Ϫ40 mV, with a mean of 54%), the kinetic features illustrated here were reproducibly observed. | [] | [
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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"
} | Figure shows the normalized conductance (G/G max ) for I GP, TEA. This component of the current starts activating between Ϫ10 and Ϫ20 mV. The continuous line represents the fit of the data to a Boltzmann equation with a V 1/2 and k of 16.94 mV and 10.59 mV Ϫ1 , respectively (n ϭ 6). These data show that the component of the outward current from type A cells that is blocked by 1 mM TEA resembles in voltage dependence as well as in activation and deactivation kinetics the currents carried by Kv3.1 and Kv3.2 channels. | [
"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"
} | To explore this conclusion further, we compared more closely the kinetics of activation and deactivation of I GP, TEA with the kinetics of Kv3.1 and Kv3.2 currents in CHO cells. shows current records obtained with identical pulse protocols in CHO cells transfected with Kv3.1 and Kv3.2 cDNAs (A and B, respectively) and I GP, TEA in a type A GP neuron (C). In D-G, we have scaled and superimposed the first 150 ms of the current traces in A-C, at four different voltages. It is clear from this comparison that the TEA-sensitive component of the K ϩ current in type A GP neurons has activation kinetics that closely resembles the activation kinetics of Kv3.1 and Kv3.2 currents in CHO cells. | [
"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"
} | I GP, TEA also resembles Kv3.1 and Kv3.2 currents in deactivation kinetics. examines the kinetics of the tail current recorded under control conditions in a type A GP neuron. The tail current that results from repolarizing the membrane potential from ϩ40 to Ϫ40 mV was best fitted by the sum of two exponentials, suggesting that the deactivation process of this current includes two components with fast and slow time constants ( 1 ϭ 1.78 ms and 2 ϭ 21.8 ms, respectively). In contrast, the tail current of the TEAinsensitive component and the TEA-sensitive component can be fitted to a single exponential with time constants of 28.8 and 2.27 ms, respectively. These two values resemble the time constants of the two components seen in the total current. The time constant of deactivation of the TEA-sensitive current from a number of experiments (n ϭ 4) is plotted against the repolarizing membrane potential in. I GP, TEA deactivates very fast, at rates similar (and roughly intermediary) to those of Kv3.1 and Kv3.2 currents in CHO cells. A summary of the comparison of the properties of I GP, TEA in type A GP neurons with the properties of Kv3.1 and Kv3.2 currents is shown in Table. | [
"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"
} | The characteristics of the currents obtained from GP neurons described earlier were typical of the majority of the cells studied. However, we found that in a small group of cells, 1 mM TEA blocked a fast inactivating current. Many of these cells (type B) had a distinct morphology characterized by large multipolar somas with about four to five dendrites (such as the cell illustrated in. Typical records from one of these cells are shown in. Depolarizing pulses from a holding potential of Ϫ40 mV produced currents of the delayed rectifier type similar to those seen in type A cells , although the kinetics of activation of these currents was faster than that of the currents recorded in type A GP neurons (rise time between 10 and 90% at ϩ40 mV of 14.0 Ϯ 1.2 ms, n ϭ 3 for type B cells and 25 Ϯ 5 ms, n ϭ 6 for type A cells). The predominant time constant of deactivation of the currents in these cells is slow ( ϭ 25.86 Ϯ 1.17 ms after a pulse to ϩ40 mV; n ϭ 4). Application of 1 mM TEA inhibited ϳ10 -15% of the current. The TEA-resistant current had slower activation kinetics than the control (10 -90% rise time: 22.4 Ϯ 2.5 ms, n ϭ 3). The TEA-sensitive component (I GP, TEA ), obtained by digital subtraction , was composed predominantly of a current that activates very rapidly starting at voltages more positive than Ϫ10 mV (time to peak at ϩ40 mV of 3.6 Ϯ 0.7 ms, n ϭ 4) and presented marked and fast inactivation that could be fitted to a single exponential function. The transient currents recorded from type B neurons of the GP resemble the currents expressed by Kv3.4 proteins (Table. These are proteins of the Kv3 subfamily that express fast activating and inactivating currents resembling Kv3.1 and Kv3.2 in voltage dependence and pharmacology. This result was surprising at first because in situ hybridization studies reported that Kv3.4 was only expressed at very low levels in a scattered pattern in the GP. | [
"Kv3.1",
"Kv3.2",
"Kv3.4"
] | [
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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"
} | Because there are no antibodies available against Kv3.4 proteins, we used single-cell RT-PCR to investigate whether type B cells in the GP contain Kv3.4 transcripts. Singlestranded cDNA synthesized from the mRNA obtained from the cytoplasm of several freshly dissociated type A and type B GP neurons was used as template for two rounds of PCR amplification. In the first round, we used a pair of primers designed to amplify the products of all Kv3 genes. This was followed by amplification using internal primers designed to amplify specifically the products of Kv3.1, Kv3.2, and Kv3.4 genes. The amplified products obtained when cDNA for each Kv3 gene was used as template are shown in. Each product has a different molecular weight facil-itating the identification of the transcript. ). These currents have several properties (see Table that distinguish them from those of other delayed rectifier K ϩ channels known. One property is an activation voltage range that is more positive than that of other heterologously expressed voltage-gated K ϩ channels, besides those of the Kv3 subfamily. The channels with the nearest activation voltage (Kv2.1 and Kv2.2) start activating at 10 -20 mV more negative potentials. Although Kv3 channel opening starts at high potentials (more positive than Ϫ10 mV), the probability of channel opening increases steeply with voltage, and Ͼ80% of the channels are opened at ϩ30 mV. The currents deactivate very fast, at rates that are Ն7-10 times faster (when compared at the same voltage) than those of other known mammalian voltage-gated K ϩ channels, except for Kv1.7 a nonneuronal member of the Kv1 subfamily (deactivation rates are 2-3 times slower than Kv3.1 or Kv3.2). The rate of rise of the currents is relatively fast; faster than many other voltage-gated K ϩ channels (e.g., Kv2.x; Kv1.2) but slower than that of other voltage-gated K ϩ channels such as several Kv1 channels like Kv1.1 and Kv1.5. In contrast to other FIG. 11. Deactivation kinetics of K ϩ currents recorded from a type A GP neuron. A: tail current obtained from a type A pallidal neuron during repolarization to Ϫ40 mV after a voltage step to ϩ40 mV from a holding potential of Ϫ40 mV. Deactivation can be fitted by the sum of 2 exponential functions. B: tail current obtained from the same cell and during the same voltage protocol as in A after application of 1 mM TEA. In this case, the tail current can be fitted to a single exponential function. C: tail current of the TEA-sensitive component obtained by subtraction of the current record obtained with TEA from the current record obtained before TEA application. Tail current is also well fitted by a single exponential function. | [
"Kv1.1",
"Kv1.2",
"Kv1.5",
"Kv1.7",
"Kv2.1",
"Kv2.2",
"Kv3.1",
"Kv3.2",
"Kv3.4"
] | [
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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"
} | -, curves fitted to the experimental points (E; sampling rate 60 s/point). D: voltage dependence of the time constants of deactivation of the TEA-sensitive current in several type A GP neurons (Ⅲ, n ϭ 4). Deactivation time constants for Kv3.1 (‚) and Kv3.2 (E) currents obtained in CHO cells shown in have been replotted here to facilitate comparison with the deactivation of the TEA-sensitive currents in type A GP 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"
} | delayed rectifiers, Kv3.1 and Kv3.2 currents are not significantly inactivated by depolarizing prepulses (see and do not show cumulative inactivation. These distinctive properties are likely to endow neurons with special electrophysiological properties. | [
"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"
} | The studies described here provide strong evidence that in pallidal neurons, Kv3.1-Kv3.2 proteins in heteromultimeric complexes form K ϩ channels mediating a high-voltage-activating component of the delayed rectifier current that closely resembles the currents expressed by these proteins in heterologous expression systems. The immunohistochemical studies demonstrated that there is expression of both Kv3.1 and Kv3.2 proteins in the GP and that both proteins are colocalized in the same cell type, the triangular and bipolar parvalbumin-containing (PVϩ) neurons, which constitute the major neuronal population in the rodent GP. Moreover, anti-bodies against Kv3.1 or Kv3.2 proteins coprecipitate both subunits, strongly suggesting that the proteins exist in heteromeric complexes. It remains to be shown, however, that the functional channels are heteromultimeric. This will be a difficult task unless major, notyet detected, differences between homomultimeric and heteromultimeric channels are discovered. We also have demonstrated that in acutely dissociated pallidal neurons having triangular or bipolar shapes (type A), shown to express Kv3.1 and Kv3.2 transcripts by single cell RT-PCR, a component of the current not inactivated when the cell is held at Ϫ40 mV and blocked by 1 mM TEA, has properties that closely resemble those of Kv3.1 and Kv3.2 channels in CHO cells (see Table. | [
"Kv3.1",
"Kv3.2",
"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"
} | The concentration of TEA used to isolate the current in pallidal neurons (1 mM) blocks Ͼ80% of Kv3.1 and Kv3.2 currents in heterologous expression systems. This concentration of TEA produces significant inhibition of only a few other known K ϩ channels. These include the large conductance Ca 2ϩ -activated K ϩ channels containing proteins of the slo family (K d 80 -330 M) and Kv1.1 channels (K d ϳ 0.5 mM). These channel types are unlikely to contribute to the current isolated from the pallidal neurons in these studies. In our experiments, the activation of Ca 2ϩactivated K ϩ channels was suppressed by using Cd 2ϩ in the extracellular solution and by using BAPTA in the intracellular solution. In the pallidal area Kv1.1 proteins apparently are expressed somatically only in the ventral pallidum. Moreover, Kv1.1 channels also are blocked by dendro- toxin (K d ϳ 10 -20 nM). In pallidal neurons, this toxin blocked a small inactivating current component (ϳ10 -15% of total outward current) resembling a D current , which was suppressed significantly by holding the cell at Ϫ40 mV. Dendrotoxin also blocks other channels of the Kv1 subfamily that are not highly sensitive to TEA ) and may mediate the D-like current in pallidal neurons. | [
"Kv1.1",
"Kv3.1",
"Kv3.2",
"Slo1"
] | [
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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"
} | This study confirms and extends the observations of , who showed that hippocampal interneurons expressing Kv3.1 proteins had a current that showed resemblance to Kv3.1 currents in heterologous expression systems. Also the l-type current in T lymphocytes was shown to be very similar to Kv3.1 currents in Xenopus oocytes when recordings in the two preparations were obtained with the same solutions ). Kv3.1-like currents also have been described in auditory neurons ). | [
"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"
} | It appears from these results that the properties of native channels containing Kv3.1 and Kv3.2 proteins are not significantly affected by factors such as associated subunits or postranslational modifications as might be the case for other cloned subunits, at least in the cells studied until now. It is therefore valid to ask why were Kv3.1-and Kv3.2-like currents not described in the many neuronal populations expressing these proteins prior to the cloning studies? Most likely the Kv3 channel-mediated current was buried in other components of the K ϩ current. This emphasizes the suggestion made in the introduction that experimental conditions and methods to isolate individual components of the K ϩ current tailored to search for specific current components are required before it is possible to determine whether native currents resemble those in heterologous expression systems. In the specific case of pallidal neurons, the Kv3.1-Kv3.2 current isolated in our study was most likely buried in the delayed rectifier component (I k ) isolated with 10 mM TEA by. | [
"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"
} | The GP in rodents consist of a main neuronal mass homologous to the external segment of the GP in primates and often is referred to simply as the GP. A smaller nuclear group situated at a certain distance and embedded among the fiber bundles of the internal capsule usually called entopeduncular nucleus (not included in most of our dissociations) is thought to correspond to the internal segment of the GP in primates. The GP proper contains several neuronal populations, the majority of which are medium to large neurons (20 -40 m in length along their longer axis) with a fusiform (bipolar) or triangular shape. There are also small neurons (12-16 m in length), which may correspond to the small dissociated cells that were excluded from the present study, and a few scattered large multipolar cells located mainly in the medial border in rat, which may correspond to cholinergic neurons. Most pallidal neurons, including the triangular and fusiform cells, are GABAergic. Many of these cells stain for parvalbumin, which labels about two-thirds of projecting pallidal neurons ). According to our immunohistochemical studies, Kv3.1 and Kv3.2 are present in the PVϩ neurons. Furthermore the morphology of the majority of the dissociated cells identified as type A in this study corresponds to the morphology of the PVϩ cells in situ. Together with the results from the single cell RT-PCR, this suggests that the neurons expressing Kv3.1-and Kv3.2-like currents correspond to the projecting GABAergic, PVϩ, neurons. The ventral pallidum, which may have contaminated some of our dissociations, contains similar GABAergic and cholinergic 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"
} | The Kv3.1-Kv3.2 component of the delayed rectifier current in pallidal neurons represents a significant component of the total K ϩ current (ϳ50% of the current when the cell was depolarized from a holding potential of Ϫ40 mV) and is therefore likely to contribute to the firing properties of these cells. Because Kv3.1-Kv3.2 channels are not opened until the membrane potential is depolarized beyond Ϫ10 mV, it has been suggested that these channels are activated late in the action potential and, when present in sufficient amounts, influence action potential repolarization. Thus Kv3.1-Kv3.2 channels would help dictate action potential duration without competing much with the Na ϩ current in generating the rising phase of an action potential and influencing firing threshold, in contrast to K ϩ channels that are activated earlier during a spike. These arguments, supported by computer modeling (A. , suggest that high-voltage-activating K ϩ channels would modulate firing properties more selectively than K ϩ channels that activate at more negative voltages. | [
"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"
} | Many of the neuronal populations expressing Kv3.1 and Kv3.2 channels fire trains of brief action potentials at high rates , such as fastspiking interneurons in the cortex and the hippocampus. Kv3.1-Kv3.2 channels may help maintain high firing rates by keeping action potentials short, reducing Na ϩ channel inactivation, and facilitating fast recovery of Na ϩ channels from inactivation by hyperpolarizing the cell following the spike. Their fast deactivation on repolarization will quickly eliminate the increase in K ϩ conductance, and therefore these channels will contribute little to increasing the refractory period. K ϩ channels that are open at lower potentials or do not deactivate as fast could repolarize the spike but at the same time also limit firing frequency by contributing to the refractory period. In fact pharmacological treatments that suppress Kv3 currents impair fast spiking in neocortical neurons, but blockade of other K ϩ currents actually increases firing frequency. | [
"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"
} | Although there has not been a study combining immunohistochemistry and electrophysiology of pallidal neurons, it is likely that the PVϩ pallidal neurons correspond to the repetitive firing group of cells recorded in an in vivo intracellular study in rats by because they both represent the largest cell population and they have similar morphologies. These cells, which probably correspond to the type II neurons observed in intracellular recordings from guinea pig slices , show fast repetitive firing (Յ200 Hz) with weak accommodation when depolarized. | [] | [
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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"
} | It is possible that the role of Kv3.1-Kv3.2 channels in PVϩ pallidal neurons is similar to their proposed role in cortical interneurons to facilitate sustained high firing rates. The firing frequency of the repetitive firing cells in the GP is not as high or sustained as that of fast-spiking cortical neurons. Analysis of the currents in the latter cells shows that they have a significantly higher proportion of Kv3-like currents than pallidal neurons and lack subthreshold-activating A-type currents (A.. These differences in channel composition may explain the differences in spike frequency adaptation of the two cell types. The resting potential of pallidal neurons will change the contribution of Kv3 currents to the total current, it is therefore also possible that the firing frequency or adaptation of PVϩ pallidal neurons will depend on the resting potential. | [
"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"
} | The most surprising result of this study was the finding of fast, transient, high-voltage-activating, TEA-sensitive currents in a small subpopulation of the dissociated cells. The currents resemble those expressed by Kv3.4 subunits in heterologous expression systems (Table (see also Vega-Saenz de. The hypothesis that these transient currents in GP neurons are mediated by channels containing Kv3.4 proteins is supported by the findings from single-cell RT-PCR, which showed that Kv3.4 transcripts are present only in the cells having the high-voltage activating transient current. We did not expect to find Kv3.4 channels in pallidal neurons because reported very weak expression of Kv3.4 transcripts in the GP (in situ hybridization signals for these mRNAs were reported as ''weakly above background''). However, cautioned in their paper that low expression of Kv3.4 transcripts in neurons expressing other Kv3 proteins could be of physiological significance because Kv3.4 subunits can form heteromultimeric channels with other Kv3 proteins resulting in a large amplification of the transient current. Type B pallidal neurons might be an example of the situation predicted in this paper. | [
"Kv3.4"
] | [
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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"
} | Nevertheless relative to the other outward currents, the Kv3.4-like current in type B pallidal neurons contributes such a small proportion of the total current that one could be tempted to suggest it could play little role in the excitability of these cells. However, although the Kv3.4-like current contributes little current, it produces a large effect on the rise time of the total current. The currents remaining after 1 mM TEA are not very different in magnitude from the original current; however, they are clearly much slower (see. This suggests a new role for Kv3.4-like currents: to accelerate the rate of rise of the repolarizing currents. Further studies of type B pallidal neurons or other cells expressing Kv3.4 channels will allow future tests of this hypothesis. | [
"Kv3.4"
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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"
} | 0022-3077/99 $5.00 Copyright © 1999 The American Physiological Society on May 11, 2009 jn.physiology.org Downloaded from | [] | [
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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"
} | on May 11, 2009 jn.physiology.org Downloaded from | [] | [
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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"
} | NATIVE HETEROMULTIMERIC KV3.1-KV3.2 CHANNELS on May 11, 2009 jn.physiology.org Downloaded from | [] | [
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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"
} | HERNA ´NDEZ-PINEDA ET AL. on May 11, 2009 jn.physiology.org Downloaded from | [] | [
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{
"section": "INTRO",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Depolarization-activated outward K + currents contribute to determining the height and the duration of the plateau phase of the action potential in cardiac cells. In the mammalian myocardium, various types of depolarizationactivated outward K + currents have been distinguished based on differences in time-and voltage-dependent properties and pharmacological sensitivities. In previous studies completed on adult rat ventricular myocytes, for example, transient (Iio) and delayed (IK) type K + currents were distinguished based on *Dr. Merlie died on Address correspondence to Jeanne M. Nerbonne, Department of Molecular Biology and Pharmacology, Box 8103, Washington University School of Medicine, 660 South Euclid Avenue, Saint Louis, MO 63110; Fax: 314-362-7058; E-mail:jnerbonn@pharmdec.wustl.edu differential sensitivities to 4-aminopyridine and tetraethylammonium. lto and IK also display markedly different time-and voltage-dependent properties, and functional studies revealed that these conductance pathways subserve distinct roles in action potential repolarization: Ito underlies the early phase of repolarization and is largely inactivated at later times, whereas IK underlies the latter phase of repolarization back to the resting potential. | [] | [
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{
"section": "INTRO",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Interestingly, molecular cloning of cardiac K + channel pore-forming (t~) subunits has revealed even greater potential for diversity than expected based on the numbers of depolarization-activated K + currents/ channels distinguished electrophysiologically. Five different voltage-gated K + channel (Kv) ct subunits, for example, have been cloned from or shown to be expressed at the message level in adult rat heart; three of these belong to the Shaker subfamily, one (Kv2.1) to the Shab subfamily, and one (Kv4.2) to the Shal subfamily. There are, therefore, more Kv 0L subunits expressed than expected given that only two types of depolarization-activated K + channels have been distinguished electrophysiologically in adult rat ventricular myocytes. This discrepancy raises the interesting questions of what are the functional roles of the various Kv ~ subunits and, specifically, what underlies Ito and IK? Recently, we exploited K + channel subunit-specific antibodies to examine the distributions of Kvl.2, Kvl.4, Kvl.5, Kv2.1, and Kv4.2 in adult rat heart. Immunohistochemistry and Western analysis revealed that Kvl.2, Kvl.5, Kv2.1, and Kv4.2 are readily detected in adult rat ventricular myocytes. Kvl.4, in contrast, was barely detectable, suggesting that this subunit does not contribute to the formation of Ito or IK in these cells. Based on the relative distributions of Kvl.2, Kvl.5, Kv2.1, and Kv4.2 and on the properties of the K + channels formed on heterologous expression of these subunits, we suggested that Kv4.2 likely underlies rat ventricular Ito and that Kv2.1 underlies IK. | [
"Kv2.1",
"Kv4.2",
"Kv"
] | [
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{
"section": "INTRO",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | The experiments here were undertaken to examine quantitatively the developmental expression of Ito and I K and of the Kv (x subunits, Kvl.2, Kvl.4, Kvl.5, Kv2.1, and Kv4.2 in rat ventricular myocytes at the mRNA and protein levels and to provide further insights into the relationship between these subunits and the functional K + channels in these cells. The electrophysiological studies revealed that Ito and IK are the only K + currents expressed in -->postnatal day 5 (P5) 1 rat ventricular myocytes and that these two conductance pathways develop independently. Although Ito densities increase severalfold between P5 and adult, the properties of Ito and IK do not change appreciably as a function of age, suggesting that the subunits underlying functional Ito and IK channels are the same throughout development. RNase protection assays revealed that Kvl.2, Kvl.5, Kv2.1, and Kv4.2 mRNA levels all increase (in parallel) during postnatal development. Western analyses, however, revealed that the developmental expression patterns of the corresponding subunit proteins are distinct. The levels of the Kvl.2 and Kv4.2 proteins, for example, increase with age, whereas Kv2.1 decreases, and Kvl.5 is invariant. The mismatch between the number of Kv 0~ subunits and functional voltage-gated K + chan-~ Abtrreviations used in this paper: DTX, dendrotoxin; HP, holding potential; P, postnatal day; TEA, tetraethylammonium; 4-AP, 4-aminopyridine. nels expressed in rat ventricular myocytes and the functional implications of this mismatch are discussed. | [
"Kv2.1",
"Kv4.2",
"Kv"
] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | To examine the developmental expression of the Ca 2+independent, depolarization-activated outward K + currents, ventricular myocytes were isolated from postnatal day 5 (P5), 10 (P10), 15 (P15), 20 (P20), 25, (P25), 30 (P30), and adult rat hearts. Using the described procedures, 50--90% of the ventricular myocytes isolated from animals of all ages were rod-shaped and had clear cross striations; electrophysiological recordings were obtained only from Ca 2+tolerant rod-shaped cells, and, in general, smaller cells were selected for recordings to ensure the fidelity of the voltage-clamp recordings. Visual inspection did re- opmental ages are displayed in. As is evident, outward K + current amplitudes increase markedly from P5 to adult, and the peak outward currents increase to a greater extent than the plateau currents as a function of postnatal age. The (mean -SEM) peak current amplitude evoked at +30 mV from an HP of -70 mV, for example, increased more than sevenfold from 346 -+ 52 (n = 9) at P5 to 2,484 + 212 pA (n = 9) at P30. Mean (-SEM) plateau current amplitudes evoked at +30 mV from an HP of-70 mV, in contrast, increased threefold during the same developmental period from 194 -+ 32 (n = 9) at P5 to 618 -+ 37 pA (n = 9) at P30. Both the peak and the plateau current amplitudes increased progressively throughout postnatal development. | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | As noted above, ventricular myocytes isolated from early (-P15) postnatal animals appeared smaller than those isolated from older (->P20) animals. Examination of whole-cell membrane capacitances confirmed substantial differences in cell size as a function of age: mean (+SEM) whole-cell membrane capacitance increased significantly (P < 0.001, ANOVA) from 28.8 + 2.8 pF (n = 9) at P5 to 124.6 -+ 4.9 pF (n = 13) for adult cells. To facilitate comparisons between cells of different sizes, peak and plateau current amplitudes in each cell were measured and normalized to the whole-cell membrane capacitance (of that cell). There was no correlation between cell size (as assessed by the whole-cell membrane capacitance) and the peak or plateau current density. Mean (-+SEM) peak and plateau outward current densities are plotted in B. Peak current densities increase significantly (ANOVA, P< 0.01) from 12.0 -+ 1.2 (n = 9) in P5 cells to 28.7 -+ 1.7 pA/pF (n = 10) in P25 cells; peak outward current densities did not change appreciably between P25 and adult. Plateau current densities, in contrast, increased slightly from 6.9 -+ 0.7 (n = 9) at P5 to 13.4 -+ 1.1 pA/ pF (n = 14) at P15 and then decreased again to 7.3 -+ 0.3 pA/pF (n = 10) at P25; no further changes in plateau current densities were evident in cells isolated at times later than P25. The increase in plateau current density between P5 and P15 is statistically significant (P < 0.01), as is the decrease in plateau current density between P15 and P25. Interestingly, however, plateau current densities are not significantly (Student's t test) different in P5 and adult rat ventricular myocytes. | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Previously, we demonstrated that the total CaZ+-independent, depolarization-activated outward K + currents in adult rat ventricular myocytes reflect the activation of two distinct K + current components, Ito and IK. In adult rat ventricular myocytes, the peak outward current amplitudes evoked during depolarizing voltage steps largely reflect the activation of Ito, whereas IK underlies the plateau currents. In addition, the rapidly decaying component of the total outward current reflects Ito exclusively, uncontaminated by IK. In adult cells, therefore, determination of the amplitudes of the rapidly decaying current component in records such as those in provides a direct way to estimate Ito amplitudes (densities). Assuming that this would also be the case in cells isolated at P5 through P30 (if the properties of Ito were unchanged as a function of postnatal age), the decay phases of the currents evoked at +30 mV from an HP of -70 mV were analyzed. These analyses revealed that Ito amplitudes and densities increase markedly as a function of age: mean -+ SEM Ito densities increased from 6.0 + 0.8 (n = 9) at P5 to 23.8 + 2.1 pA/pF (n = 9) at P30. These results support the hypothesis that the rapidly decaying component of the currents indeed reflects Ito at all ages, and, in addition, suggest that the time-and voltage-dependent properties of this component do not change appreciably during development. Subsequent experiments, therefore, were focussed on examining the time-and voltage-dependent properties of the currents in greater detail. | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | To determine the voltage dependences of activation of the currents in developing and adult rat ventricular myocytes, the peak and plateau amplitudes of the currents evoked during depolarizations to test potentials between -40 and +30 mV from an HP of -70 mV were measured in individual cells and subsequently normalized to their respective (peak and plateau) amplitudes recorded during depolarization to +30 mV (in the same cell). Mean (-+SEM) normalized peak and plateau current amplitudes determined in P5 and adult rat ventricular myocytes are plotted in. The normalized current-voltage relations for the peak (Ito) and the plateau (IK) currents in P5 (n = 5) and adult (n = 10) cells are indistinguishable. Similar results were obtained when cells isolated from P10 (n = 7), P15 (n = 14), P20 (n = 10), P25 (n = 10), and P30 (n = 9) were examined (not illustrated). To determine the voltage dependences of steady-state inactivation of the currents in P10 and P20 myocytes, currents were evoked at +30 mV from various holding potentials (-120 to 0 mV). Peak and plateau currents were measured, normalized to their respective amplitudes for currents evoked from -120 mV, and plotted as a function of prepulse (holding) potential. Similar to our previous findings in adult cells , inactivation of the peak currents in P10 and P20 myocytes is well described by the sum of two Boltzmanns (reflecting contributions from both Ito and IK, the latter only at hyperpolarized prepulse potentials), whereas the plateau current is well described by a single Boltzmann (corresponding to inactivation of IK). In P20 cells (n = 4), the V]/2 values for the peak currents were -78 mV (k = 12.4) and -28 mV (k = 4.8). In P10 cells (n = 4), the best double Boltzmann fit to the data pointsyielded V]/2 values of -78 mV (k = 8.9) and -33 mV (k = 5.8). These values are nearly identical to those obtained on adult cells where V]/e values of -77 mV (k = 12.9) and -29 mV (k = 5.5) were obtained. Changes in the voltage dependences of activation and/or inactivation of the currents, therefore, cannot account for the increases in current amplitudes and densities observed during postnatal development. | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Similar to our findings in adult myocytes, we found that Ito in postnatal cells is selectively blocked by 4-aminopyridine (4-AP). Typical effects of 0.5 mM 4-AP (which blocks "-~50% of the peak current [and Ito]) are displayed in. At all ages, 0.5 mM 4-AP selectively attenuates the peak outward currents and is without effects on the plateau currents. The amplitudes of the 4-AP-sensitive currents , obtained by subtraction of the currents recorded in the presence of 0.5 mM 4-AP from the controls , increase markedly between P5 and P30; the mean (+SEM) amplitude of the current sensitive to 0.5 mM 4-AP increased significantly (P < 0.001, ANOVA) from 109 + 32 (n = 4) at P5 to 1,886 -+ 233 pA (n = 7) at P30. Even taking into account the large change in cell size observed during postnatal development, the mean (+SEM) 0.5 mM 4-AP-sensitive current density increased significantly (P < 0.001, ANOVA) from 2.8 + 0.8 pA/pF (n = 4) at P5 to 18.4 -+ 2.0 pA/pF (n = 7) at P30. Qualitatively, the waveforms of the total depolarization-activated outward K + currents and and the 0.5 mM 4-AP-sensitive currents appear similar at all developmental ages. To determine the kinetic properties of the currents, time constants (tau) for activation and inactivation of the peak outward currents were determined from single exponential fits to the rising and decaying phases, respectively, of the total outward currents. Activation and inactivation of the peak outward currents in adult rat ventricular myocytes are dominated by Ito. Analyzing these rates, therefore, gives reliable estimates of the kinetics of Ito activation and inactivation. As reported previously , the time constants for activation of the peak currents in adult cells are voltage dependent, decreasing with increasing depolarization (Table. Similar voltage dependences were seen at all developmental stages studied (Table. These analyses also revealed that the time constants for | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | (n = 9) (n = 9) (n = 9) (n = 9) Adult 8.5 • 1.4 5.2 • 0.7 3.2 • 0.4 1.9 • 0.2 1.4 • 0.1 (n = 8) (n = 8) (n = 8) (n = 8) (n = 8) | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Values are means • SEM. Time constants for outward current activation in individual cells were determined from single exponential fits to the rising phases of the total outward currents evoked at potentials between -10 and + 30 mV from an HP of -70 mV. | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | peak outward current activation are invariant between P10 and adult (Table. In P5 cells, however, the activation time constants, although clearly also voltage dependent, are approximately twofold longer than those determined in ->P10 cells. Although the differences between the activation time constants in P5 and >P10 are small, they are statistically significant (P < 0.01, ANOVA). Because of the small amplitudes of the currents, particularly Ito , in P5 cells , it seemed likely that the peak outward currents (and, therefore, the activation of the peak currents) might be contaminated by the presence and the activation of I K. To provide an independent measure of Ito activation rates, therefore, the rising phases of the 0.5 mM 4-AP-sensifive currents (in subtracted records such as those in were also analyzed. These analyses revealed time constants for Ito activation in P5 cells (n = 4) that are not significantly (ANOVA) different from the activation time constants determined for P10 to adult cells, suggesting that the slower activation of the total outward currents determined in P5 cells reflect contamination from the slower activating I K. The rising phases of the total outward currents in P10 through adult cells, in contrast, are dominated by activation of [to-The time constants for inactivation of the peak outward currents were determined from single exponential fits to the decay phases of the total outward currents. These analyses revealed that inactivation is voltage independent (Table and that there are no significant differences in the inactivation time constants in cells isolated at various stages of development | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | (n = 8) (n = 8) (n = 8) (n = 8) | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Values are means _+ SEM. Time constants for outward current inactivation in individual cells were determined from single exponential fits to the decay phases of the total outward currents evoked at potentials between 0 and +30 mV from an HP of -70 mV. | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | from P5 through adult (Table. Inactivation time constants for Ito , determined from single exponential fits to the decaying phases of the 4-AP-sensitive currents in subtracted currents, were indistinguishable from those determined from analyses of the decay phases of the total currents. Taken together, these results confirm that the voltage-independent inactivation of Ito underlies the inactivation of the total outward currents. In addition, these experiments revealed that the time constants for Ito inactivation are the same at all stages of postnatal development, from P5 through the adult. The finding that Ito inactivation rates are invariant during postnatal development validates the analyses above of the rapidly decaying component of the total outward currents as a way to estimate Ito amplitudes (densities) as a function of postnatal age. | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | In adult rat ventricular myocytes, IK is selectively blocked by mM concentrations of TEA. To provide an independent way to assess whether the time-dependent properties of IK vary during postnatal development, cells were exposed to TEA. The waveforms of the total depolarization-activated K + currents were recorded under control conditions and in the presence of 50 mM TEA. As reported previously , these experiments revealed that TEA selectively attenuates the plateau currents; there is little effect of TEA on the peak currents. The waveforms of the "TEA-sensitive" currents were then obtained by subtraction of the currents recorded in the presence of TEA from the controls. As illustrated if , the waveforms of the TEA-sensitive currents in P10 , P20 , and adult rat ventricular myocytes are indistinguishable. Taken together, therefore, the electrophysiological experiments suggest that neither the time-nor the voltage-dependent properties of Ito or IK varies measurably during postnatal development. | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Previously, demonstrated that the mRNAs for voltage-gated K + channel et-subunits Kvl.2, Kvl.4, Kvl.5, Kv2.1, and Kv4.2 are readily detected in adult rat ventricular myocytes using quantitative RNase protection assays. To determine whether the expression patterns of these subunits vary during postnatal development, RNase protection assays were performed on samples prepared from P0, P5, P10, P16, P24, P30, and adult rat ventricles. These experiments revealed significant increases in. The timing of the increases was similar for Kvl.2, Kvl.5, and Kv2.1 in that the largest (percent) increases were observed between P5 and P15. Overall, the largest changes were evident for Kvl.2 mRNA, which increases approximately 8 fold between birth and adult , upper left). The Kvl.5 and Kv2.1 mRNAs showed smaller increases over the same time period. For Kv4.2, there was also an increase between P5 and P15, but the increase was modest c o m p a r e d to that seen with Kvl.2, Kvl.5, and Kv2.1. There was a slightly more p r o m i n e n t increase in Kv4.2 mRNA between P20 and adult , lower right). The observed increases in Kvl.2, Kvl.5, Kv2.1, and Kv4.2 mRNAs were not due to generalized increases in mRNA abundance, as evidenced by the fact that a marked decline in the abundance of Kvl.4 mRNA was observed: Kvl.4 mRNA peaked at P5-P10 and steadily declined during develo p m e n t (see below and. when the antibody was preincubated with the peptide against which the antibody was generated. As is also evident in , the a m o u n t of the Kvl.2 protein increases markedly as a function of age. Similar results were obtained in several experiments, and mean normalized data are presented in (upper/eft). The density of Kvl.2 increases approximately fourfold between P5 and P20 and then decreases slightly to its adult level. Interestingly, variations in the Kvl.2 protein and parallel those seen for the Kvl.2 mRNA. | [
"Kv2.1",
"Kv4.2"
] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | In parallel experiments, Western blots of ventricular membrane proteins revealed that Kvl.5, Kv2.1, and Kv4.2 are also readily detected at all developmental ages. The anti-Kv4.2 antibody specifically labels a single band at 74 kD in rat ventricular m e m b r a n e s at all developmental ages , lower right). In addition, the labeling was eliminated when the anti-Kv4.2 antibody was preincubated with the peptide against which the antibody was generated (data not shown). Similar results were obtained in several experiments, and mean normalized data for Kv4.2 expression are presented in Fig. | [
"Kv2.1",
"Kv4.2"
] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | between P5 and P20, and the increase in Kv4.2 expression appears to be complete by P20 , lower right). | [
"Kv4.2"
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Similar to the findings with Kvl.2, therefore, the developmental expression of the Kv4.2 protein closely parallels the observed increase in Kv4.2 mRNA. | [
"Kv4.2"
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | A specific protein band at 75 kD is recognized by the anti-Kvl.5 antibody in developing adult rat ventricular m e m b r a n e s , upper right). This band is eliminated when the antibody is preincubated with the fusion protein against which the antibody was generated. There are also two low molecular weight bands identified in Western blots with FIGURE 7. Westerns blots reveal marked differences in the postnatal expression patterns of the Kvl.2, Kvl.5, Kv2.1, and the Kv4.2 proteins. Ventricular membrane proteins prepared from P5, P10, P15, P20, P25, P30, and adult animals were fractionated on SDS-Page gels, transferred to PVDF membranes and immunoblotted with the anti-Kvl.2 (upper /eft), anti-Kvl.5 (upper right), anti-Kv2.1 (/0wet /eft), or anti-Kv4.2 (lower right) antibodies. To facilitate quantification of subunit expression, 20 ~g of ventricular membrane proteins prepared from the hearts of P5, P10, PI5, P20, P25, P30, or adult animals were loaded onto each gel. All antibodies were used at a concentration of 1:100 except Kv4.2, which was used at 1:500. Bound antibodies were detected using a chemiluminescence assay ( s e e MATERIALS AND M E T H O D S ) anti-Kvl.5 , upper right) ; these bands a p p e a r to reflect nonspecific binding, as evidenced by the fact that they are not eliminated by preincnbation of the antibody with the fusion protein against which the antibody was generated (data not shown). Quantification o f Western blots using the anti-Kvl.5 antibody confirmed that the level o f Kvl.5 protein expression does n o t vary appreciably d u r i n g postnatal d e v e l o p m e n t , upper right). In contrast to the findings with Kvl.2 and Kv4.2, therefore, Kvl.5 protein levels do not vary in parallel with the observed developmental increases in Kvl.5 m R N A. This discrepancy between the protein and the m R N A data suggests posttranscriptional regulation o f Kvl.5. | [
"Kv2.1",
"Kv4.2"
] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | The anti-Kv2.1 antibody specifically labels a single protein b a n d at 130 kD in adult rat ventricular membranes. Interestingly, and as clearly illustrated in , there are two bands recognized by the anti-Kv2.1 antibody in the P5 and P10 m e m b r a n e preparations, one at 130 kD and the second at 110 kD; only the 130 kD b a n d is detected at later ages. Both the 130-and the ll0-kD bands reflect specific labeling as evidenced by the fact that both bands are eliminated when the antibody was preincubated with the fusion protein against which the antibody was generated (data not shown). In addition, the l l0-kD band is p r o m i n e n t in ventricular m e m b r a n e s isolated at P0 (data not shown). These findings suggest that there are two distinct isoforms of Kv2.1 in the heart and that expression o f these is developmentally regulated. Quantification o f the 130-kD b a n d revealed a threefold decrease in Kv2.1 between P5 and P15; the level o f Kv2.1 is invariant at later ages. T h e variation in the Kv2.1 protein level during postnatal development, therefore, is directly opposite to the observed developmental changes in Kv2.1 Changes in Kv c~ subunit expression patterns during postnatal development are distinct. Western blots of ventricular membrane proteins were completed as described in the legend of. Films were scanned directly into a Molecular Dynamics densitometer using Image Quant. The density of each band was measured and subsequendy normalized to the density of the corresponding band in the adult sample on the same gel. For the Kv2.1 blots, only the high molecular weight band (130 kD) was included in the analyses. Mean (_+SEM) values from three to six separate determinations are plotted. vealed that Kvl.4 message levels decrease during postnatal development , top). In parallel with the decline in Kvl.4 message, there is a marked decrease in the level of the Kvl.4 protein during the same developmental period , bottom). A very faint band was detected at 97 kD in the P5 sample with the anti-Kvl.4 antibody at a much lower dilution (1:200) than those (1: 500 to 1:1,000) that we have previously demonstrated reveal robust labeling of a 97-kD band in adult rat brain (but not heart) membranes. This band was eliminated when the antibody was preincubated with the peptide against which the antibody was generated (data not shown). As also previously demonstrated, these experiments reveal that high concentrations of anti-Kvl.4 labels several other nonspecific bands in Western blots of P5, P10, P15, P20, P25, P30, and adult rat ventricular membrane proteins. | [
"Kv2.1",
"Kv"
] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Interestingly, several members of the Shaker subfamily of voltage-gated K + channel subunit proteins, including Kvl.2 , have been reported to be sensitive to blockade by nM concentrations of dendrotoxin, K + channel toxins isolated from the mamba Dendroaspis angusticeps. To determine if there are dendrotoxin-sensitive K + channel sub-FIGURE 9. The levels of Kvl.4 message and protein decrease markedly and in parallel during postnatal development. In the upper panel, the relative level of Kvl.4 mRNA expression in rat ventricles at various developmental ages is plotted. The data points are the means (-+ SEM) of four to six separate determinations; in each determination, the data were normalized to the adult value which was set equal to unity. A sample RNase protection assay is shown beneath the plot of the mean data. In the lower panel, Western blots of ventricular membrane proteins (20 p.g) isolated at various developmental ages using the anti-Kvl.4 antibody (at 1:200) are displayed. Kvl.4, although readily detected in the P5 sample (arrow), is not evident at later ages. mRNA levels , suggesting posttranscriptional regulation of Kv2.1. | [
"Kv2.1"
] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Interestingly, and in sharp contrast to the findings with the other four subunits, RNase protection assays re- units that contribute to the formation of the depolarization-activated K + channels, Ito and I K, in rat ventricular myocytes, the effects of 20 nM (n = 3) and 200 nM [3-dendrotoxin (n = 3) on the voltage-gated K + currents in these cells were examined. These experiments revealed no measurable effects of [3-dendrotoxin on the depolarization-activated outward K + currents in these cells at concentrations up to 200 nM. | [] | [
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{
"section": "RESULTS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | The outward K + currents recorded in the presence of 200 nM [3-dendrotoxin are indistinguishable from the control currents recorded in the same cell. To evaluate toxin efficacy, experiments were also performed on Ltkcells transfected with Kvl.2 cDNA (kindly provided by M. Tamkun, Vanderbilt University, Nashville, TN). These experiments revealed that, indeed, nM concentrations of [3-, c~-, or g-dendrotoxin reduced the amplitudes of heterologously expressed Kvl.2 currents by >50% (J.M. Nerbonne, unpublished observations). Thus, we conclude that the negative results obtained on rat ventricular myocytes do not reflect a problem with the purity or the activity of the toxins. Rather, we interpret these results as suggesting that there are no voltage-gated K + currents in rat ventricular myocytes that are sensitive to the dendrotoxins at concentrations up to 200 nM. | [] | [
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | The experiments described here demonstrate that the Ca2+-independent, depolarization-activated outward K + currents in rat ventricular myocytes, Ito and I K, develop independently, consistent with previous suggestions that distinct molecular entities underlie the expression of these two conductance pathways. I K density, for example, varies only slightly throughout from postnatal day 5 to the adult; Ito density, in contrast, increases more than fourfold during the same developmental period. Qualitatively similar changes in Ito density in developing rat ventricular myocytes have been described previously , although the increases in Ito density reported in the present study are somewhat larger. Also, as suggested previously , the results presented here demonstrate that the time-and voltagedependent properties of [to do not vary measurably between postnatal day 5 and the adult. | [] | [
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Developmental Expression of | [] | [
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | The results presented here also demonstrate that the K + channel subunits, Kvl.2, Kvl.4, Kvl.5, Kv2.1, and Kv4.2, shown to be expressed at the mRNA level in the adult rat heart are also readily detected in developing rat ventricles. In addition, although the expression levels of all five subunits were found to vary during postnatal development, the specific patterns and the time courses of the observed changes are variable. The mRNA levels of four of the five subunits, Kvl.2, Kvl.5, Kv2.1, and Kv4.2, for example, increase with increasing postnatal age. Overall, the largest change was seen for the Kvl.2 mRNA, which increased ~10-fold between birth and the adult. Similar increases in Kvl.2 mRNA levels during postnatal development were reported recently by. | [
"Kv2.1",
"Kv4.2"
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | More modest (approximately three-to fourfold) increases were observed for Kvl.5 and Kv2.1, although for these two subunits, expression reached the adult level at P15 to P20. A threefold increase in Kv4.2 mRNA was also documented, although for this subunit, most of the increase was detected between P15 and the adult. Qualitatively similar results have been reported previously. In sharp contrast to the findings with Kvl.2, Kvl.5, Kv2.1, and Kv4.2, however, we found that Kvl.4 message levels are high at birth (P0), increase between P0 and P10, and subsequently decrease to very low levels in adult ventricles. Although these findings are in direct conflict with at least one previous report using Northern analysis , a more recent study using quantitative reverse transcription also found that the Kvl.4 message is much more abundant in neonatal than in adult rat ventricles , consistent with the findings here. | [
"Kv2.1",
"Kv4.2"
] | [
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Developmental Expression of Proteins Previously, we demonstrated that the Kvl.2, Kvl.5, Kv2.1, and Kv4.2 subunits are readily detected in adult rat ventricular membranes whereas Kvl.4 was barely detectable. The results presented here confirm these previous findings and, in addition, demonstrate that the expression patterns of these subunits vary in distinct ways during postnatal development. The level of the Kvl.2 protein, for example, increases markedly between P5 and P20 in parallel with the increase in Kvl.2 mRNA. The Kv4.2 protein also increases during this period, albeit to a smaller extent than Kvl.2. The expression patterns of Kvl.5 and Kv2.1, however, are quite distinct: Kvl.5 protein levels are invariant throughout postnatal development, and Kv2.1 protein levels decrease. These findings suggest posttranscriptional regulation of Kvl.5 and Kv2.1, but not of Kvl.2 or Kv4.2, expression. Interestingly, there are also two isoforms of the Kv2.1 protein in early (<--P10) rat ventricles, whereas in older animals only a single Kv2.1 species is evident. These differences may reflect the expression of two splice variants of Kv2.1 in neonatal ventricles or, alternatively, developmentally regulated posttranslational modifications of this subunit. Further experiments will be necessary to distinguish between these possibilities. In contrast to the findings for the other four subunits, the Kvl.4 protein was barely detectable in rat ventricles throughout postnatal development; a weak signal was detected with the anti-Kvl.4 antibody in P5 ventricular membranes. It seems unlikely that the weak/ absent signals with this antibody on Western blots of ventricular membrane proteins reflects the experimental conditions used because all of the other antibodies gave unambiguous results. In addition, the anti-Kvl.4 antibody works well in Westerns of rat brain membrane proteins. The apparent absence of Kvl.4 in membranes prepared from P10 to adult ventricles, therefore, cannot be explained by problems with the antibody or with the methods in general. Rather, we suggest that Kvl.4 is not an abundant protein in -->P10 rat ventricles and, further, that this subunit likely does not play an important role in the formation of functional depolarization-activated K + channels in rat ventricular myocytes. | [
"Kv2.1",
"Kv4.2"
] | [
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | A goal of the experiments here was to provide further insights into the likely subunits that underlie rat ventricular Ito and Ix channels. Previously, we suggested that, of the subunits expressed, Kv2.1 seemed the most likely candidate for I K primarily because heterologous expression of Kv2.1 reveals slowly activating, TEA-sensitive K + currents. Heterologous expression of Kv4.2 , Kvl.2 , or Kvl.5 , in contrast, yields rapidly activating K + currents that are sensitive to 4-AP and relatively insensitive to TEA. Also, expressed Kvl.2 currents are sensitive to nM concentrations of DTX , whereas Ix in rat ventricular myocytes is insensitive to DTX. If the hypothesis that Kv2.1 underlies I K is correct, then one might have expected that Kv2.1 expression, like Ix density, would change little during postnatal development. The experiments here, however, revealed that Kv2.1 protein levels decrease markedly during postnatal development. These results suggest either that Kv2.1 does not play a role in the generation of Ix channels or, alternatively, that the number of functional Ix channels is highly regulated by posttranslational mechanisms. Further experiments are necessary to distinguish between these possibilities. | [
"Kv2.1",
"Kv4.2"
] | [
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Previously, we also suggested that Kv4.2, rather than Kvl.4, likely underlies rat ventricular Ito primarily because this subunit is abundant in rat ventricles at both the message and protein levels and because expression of Kv4.2 in Xenopus oocytes reveals transient K + currents that are similar to Ito. In addition, Kv4.2 mRNA expression varies through the thickness of the ventricular wall in a manner analogous to the variation in Ito density. Although the results here are consistent with a role for Kv4.2 in the formation of Ito channels, the (fourfold) increase in Ito density between P5 and P30 is larger than that expected based on Kv4.2 protein expression patterns (if one assumes that there should be a direct relationship between protein levels and channel densities). One interesting possibility to consider is that there are accessory [3 subunits associated with Kv4.2 in vivo and that these function to increase the density of functional Ito channels, analogous to the role ascribed to [3 subunits of L type, voltage-gated Ca 2+ channels. Biochemical studies have demonstrated that there are accessory [3 subunits of brain voltage-gated K + channels of the Shaker and Shab subfamilies, and several Shaker subfamily [3 subunits have now been cloned from brain and heart. Although there is no direct evidence for [3 subunits of the Shal subfamily, it has been shown that coexpression of low molecular weight brain poly(A) + RNA with Kv4.1 (or Kv4.2) modulates the properties and the densities of functional Kv4.1 (or Kv4.2) channels , consistent with the expression of an accessory subunit. Further experiments will be necessary to explore the possibility that there are [3 subunits that associate with Kv4.2 in the heart. | [
"Kv4.1",
"Kv4.2"
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | The finding that Kvl.2 is also abundant in adult rat ventricle and that the expression of this subunit increases during postnatal development in parallel with the increase in Ito density suggests that Kvl.2 (either alone or in combination with Kvl.5 and/or a [3 subunit) should also be considered a candidate for Ito. Heterologous expression of Kvl.2, however, yields rapidly activating, very slowly inactivating K + currents with properties quite different from rat ventricular Ito. The strongest argument against a role for Kvl.2 is that heterologously expressed Kvl.2 currents are sensitive to nM concentrations of DTX , whereas DTX at concentrations up to 200 nM has no effect on Ito (or IK) in rat ventricular myocytes. Nevertheless, it is certainly possible that Kvl.2 contributes to rat ventricular Ito and that the DTX binding site is rendered inaccessible by association with Kvl.5 and/or a/3 subunit or possibly as a result of posttranslational processing. Although we favor the hypothesis that Kv4.2 underlies Ito, it is clear that alternative experimental strategies will be necessary to explore directly the roles of Kv4.2 and Kvl.2 (alone or in combination with Kvl.5 and/or a [3 subunit) in the formation of functional Ito channels. | [
"Kv4.2"
] | [
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | The analysis of the developmental expression voltagegated K + channel currents and Kv 0~ subunits completed here has revealed that the Ito and IK develop independently in rat ventricular myocytes, consistent with previous suggestions that distinct molecular entities underlie these two conductance pathways. In addition, the finding that the time-and voltage-dependent properties of the currents do not change measurably suggests that the molecular compositions of functional Ito and I~ channels are the same from postnatal day 5 to adult. The biochemical studies completed here, however, have not provided clear insight into the Kv tx subunits that contribute to functional Ito and/or IK channels. Rather, these analyses have revealed that, throughout postnatal development there is a mismatch between the numbers of Kv e~ subunits and functional voltagegated K + channels expressed, if we assume that Kv ~x subunits in different subfamilies do not combine, as has been demonstrated for Kv et subunits in heterologous systems. We recognize that it might be suggested that the discrepancy between the biochemical and electrophysiological data reflects contamination from cell types other than ventricular myocytes in the biochemical studies. This possibility seems quite unlikely, however, because we have previously demonstrated that Kv et subunit expression patterns in Western blots of membrane proteins prepared from whole ventricles and isolated myocytes are indistinguishable. Thus, although we still favor the hypotheses (above) concerning the roles of Kv2.1 and Kv4.2 in the formation of functional I~ and Ito channels, it is clear that alternative experimental strategies must be applied to test these hypotheses directly, as well as to define the functional roles of Kvl,2 and Kvl.5. These must involve identifying and exploiting K + channel toxins that specifically target Kv2.1 or Kv4.2, as well as molecular approaches focussed on manipulating Kv c~ subunit expression directly and assessing the functional consequences of these manipulations. | [
"Kv2.1",
"Kv4.2",
"Kv"
] | [
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | Finally, it is important to emphasize that the studies described here have also revealed clear mismatches between Kv ~t subunit expression at the mRNA and protein levels (most notably for Kvl.5 and Kv2.1). These findings clearly suggest that there are posttranscriptional mechanisms in place for regulating Kv e~ subunit expression (at least for Kvl.5 and Kv2.1). These observations emphasize the need to proceed cautiously when attempting to draw conclusions about the expression of functional channels based on analyses of changes in message levels alone. | [
"Kv2.1",
"Kv"
] | [
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{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | In Memoriam: This work is dedicated to the memory of our former colleague, collaborator and friend, John P. Merlie, who died suddenly and unexpectedly on May 27, 1995. | [] | [
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] |
{
"section": "DISCUSS",
"title": "Developmental Analysis Reveals Mismatches in the Expression of K + Channel et Subunits and Voltage-gated K + Channel Currents in Rat Ventricular Myocytes"
} | J. GEN. PHYSIOL. 9 The Rockefeller University Press 9 0022-1295/96/11/405/15 $2.00 Volume 108 November 1996 405-419 | [] | [
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