anti kv1 5  (Alomone Labs)


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    Structured Review

    Alomone Labs anti kv1 5
    Characterization of the Kv1.3 and <t>Kv1.5</t> mutant channels containing the YS segment. A , average normalized activation and inactivation curves are shown as conductance-voltage relationships for Kv1.3, Kv1.5, the truncated Kv1.3-YS channel, and the chimeras Kv1.5-YS 532 and Kv1.5-YS 613 . All datasets were fitted to Boltzmann functions. Each data point is the mean ± S.E. of 6–11 cells. B , confocal images of non-permeabilized cells transfected with Kv1.3-YS-Cherry, Kv1.5-YS 532 -EGFP, and Kv1.5-YS 613 -EGFP. An extracellular anti-Kv1.3 antibody was used to label Kv1.3-YS ( green ), whereas the extracellular anti-Kv1.5 antibody was used for Kv1.5-YS 532 and Kv1.5-YS 613 chimeras ( red ). Nuclei were stained by Hoechst ( blue ). C , proliferation rate of the indicated channels or GFP-transfected cells (control) was determined by measuring EdU incorporation. Significant differences when comparing to Kv1.3 (*) or to control (#) are indicated. Statistical analysis was performed with one-way ANOVA followed by a Tukey's HSD multiple comparison. Each bar is the average of 9–15 determinations from 5 different assays. D , the average peak current amplitude obtained in cell-attached experiments for Kv1.5 channels and all the Kv1.5 chimeras was plotted against the % of the channels expressed at the plasma membrane ( upper graph ) or their normalized effect on proliferation (taking 100% as the proliferation rate of GFP-transfected HEK cells, lower graph ). The correlation between expression and current was fit to a linear regression curve ( y = 18.54 + 0.0066x, R 2 = 0.85, p = 0.008), but there was no correlation between proliferation and current amplitude ( R 2 = 0.23, p = 0.19).
    Anti Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Molecular Determinants of Kv1.3 Potassium Channels-induced Proliferation *"

    Article Title: Molecular Determinants of Kv1.3 Potassium Channels-induced Proliferation *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M115.678995

    Characterization of the Kv1.3 and Kv1.5 mutant channels containing the YS segment. A , average normalized activation and inactivation curves are shown as conductance-voltage relationships for Kv1.3, Kv1.5, the truncated Kv1.3-YS channel, and the chimeras Kv1.5-YS 532 and Kv1.5-YS 613 . All datasets were fitted to Boltzmann functions. Each data point is the mean ± S.E. of 6–11 cells. B , confocal images of non-permeabilized cells transfected with Kv1.3-YS-Cherry, Kv1.5-YS 532 -EGFP, and Kv1.5-YS 613 -EGFP. An extracellular anti-Kv1.3 antibody was used to label Kv1.3-YS ( green ), whereas the extracellular anti-Kv1.5 antibody was used for Kv1.5-YS 532 and Kv1.5-YS 613 chimeras ( red ). Nuclei were stained by Hoechst ( blue ). C , proliferation rate of the indicated channels or GFP-transfected cells (control) was determined by measuring EdU incorporation. Significant differences when comparing to Kv1.3 (*) or to control (#) are indicated. Statistical analysis was performed with one-way ANOVA followed by a Tukey's HSD multiple comparison. Each bar is the average of 9–15 determinations from 5 different assays. D , the average peak current amplitude obtained in cell-attached experiments for Kv1.5 channels and all the Kv1.5 chimeras was plotted against the % of the channels expressed at the plasma membrane ( upper graph ) or their normalized effect on proliferation (taking 100% as the proliferation rate of GFP-transfected HEK cells, lower graph ). The correlation between expression and current was fit to a linear regression curve ( y = 18.54 + 0.0066x, R 2 = 0.85, p = 0.008), but there was no correlation between proliferation and current amplitude ( R 2 = 0.23, p = 0.19).
    Figure Legend Snippet: Characterization of the Kv1.3 and Kv1.5 mutant channels containing the YS segment. A , average normalized activation and inactivation curves are shown as conductance-voltage relationships for Kv1.3, Kv1.5, the truncated Kv1.3-YS channel, and the chimeras Kv1.5-YS 532 and Kv1.5-YS 613 . All datasets were fitted to Boltzmann functions. Each data point is the mean ± S.E. of 6–11 cells. B , confocal images of non-permeabilized cells transfected with Kv1.3-YS-Cherry, Kv1.5-YS 532 -EGFP, and Kv1.5-YS 613 -EGFP. An extracellular anti-Kv1.3 antibody was used to label Kv1.3-YS ( green ), whereas the extracellular anti-Kv1.5 antibody was used for Kv1.5-YS 532 and Kv1.5-YS 613 chimeras ( red ). Nuclei were stained by Hoechst ( blue ). C , proliferation rate of the indicated channels or GFP-transfected cells (control) was determined by measuring EdU incorporation. Significant differences when comparing to Kv1.3 (*) or to control (#) are indicated. Statistical analysis was performed with one-way ANOVA followed by a Tukey's HSD multiple comparison. Each bar is the average of 9–15 determinations from 5 different assays. D , the average peak current amplitude obtained in cell-attached experiments for Kv1.5 channels and all the Kv1.5 chimeras was plotted against the % of the channels expressed at the plasma membrane ( upper graph ) or their normalized effect on proliferation (taking 100% as the proliferation rate of GFP-transfected HEK cells, lower graph ). The correlation between expression and current was fit to a linear regression curve ( y = 18.54 + 0.0066x, R 2 = 0.85, p = 0.008), but there was no correlation between proliferation and current amplitude ( R 2 = 0.23, p = 0.19).

    Techniques Used: Mutagenesis, Activation Assay, Transfection, Staining, Expressing

    2) Product Images from "Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns"

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00464.2009

    Mutant KCNA5 is located in perinuclear packets and not on the cell surface of transfected HEK-293 cells and human (h)PASMC. A : HEK-293 cells transfected with WT KCNA5 ( a and c ) or G182R ( b and d ) were stained with anti-KCNA5 antibody (Ab-KCNA5, red) and
    Figure Legend Snippet: Mutant KCNA5 is located in perinuclear packets and not on the cell surface of transfected HEK-293 cells and human (h)PASMC. A : HEK-293 cells transfected with WT KCNA5 ( a and c ) or G182R ( b and d ) were stained with anti-KCNA5 antibody (Ab-KCNA5, red) and

    Techniques Used: Mutagenesis, Transfection, Staining

    G182R and E211D mutations cause incomplete processing of KCNA5 in HEK-293 cells. HEK-293 cells were transfected with WT KCNA5, G182R, E211D, or G182R/E211D and subjected to standard immunoblot procedures. A : representative immunoblot from cells transfected
    Figure Legend Snippet: G182R and E211D mutations cause incomplete processing of KCNA5 in HEK-293 cells. HEK-293 cells were transfected with WT KCNA5, G182R, E211D, or G182R/E211D and subjected to standard immunoblot procedures. A : representative immunoblot from cells transfected

    Techniques Used: Transfection

    Mutant KCNA5 forms functional homotetrameric channels. A : COS-1, HEK-293, and human pulmonary artery smooth muscle cells (PASMC) were transiently transfected with either empty vector [green fluorescent protein (GFP)] or WT KCNA5 (WT) as indicated. Whole
    Figure Legend Snippet: Mutant KCNA5 forms functional homotetrameric channels. A : COS-1, HEK-293, and human pulmonary artery smooth muscle cells (PASMC) were transiently transfected with either empty vector [green fluorescent protein (GFP)] or WT KCNA5 (WT) as indicated. Whole

    Techniques Used: Mutagenesis, Functional Assay, Transfection, Plasmid Preparation

    Mutations in KCNA5 at G182 and E211 do not affect the pharmacological effect of 4-aminopyridine (4-AP). A : a standard I-V pulse protocol was delivered to HEK-293 cells transiently transfected with the indicated vector [WT KCNA5 ( a ), G182R ( b ), E211D (
    Figure Legend Snippet: Mutations in KCNA5 at G182 and E211 do not affect the pharmacological effect of 4-aminopyridine (4-AP). A : a standard I-V pulse protocol was delivered to HEK-293 cells transiently transfected with the indicated vector [WT KCNA5 ( a ), G182R ( b ), E211D (

    Techniques Used: Transfection, Plasmid Preparation

    Decreased G182R expression in COS-1 cells cannot be rescued by overexpression of K V β subunits. A , a : HEK-293 cells were transfected with WT KCNA5 or K V β1.3-HA alone or cotransfected with WT KCNA5, G182R, E211D, or G182R/E211D and K V β1.3-HA.
    Figure Legend Snippet: Decreased G182R expression in COS-1 cells cannot be rescued by overexpression of K V β subunits. A , a : HEK-293 cells were transfected with WT KCNA5 or K V β1.3-HA alone or cotransfected with WT KCNA5, G182R, E211D, or G182R/E211D and K V β1.3-HA.

    Techniques Used: Expressing, Over Expression, Transfection

    Two nonsynonymous mutations identified in the KCNA5 gene from idiopathic pulmonary arterial hypertension (IPAH) patients localize to the NH 2 -terminal tetramerization domain (T1 domain). A , left : schematic diagram of voltage-gated K + (K V ) channel subunit
    Figure Legend Snippet: Two nonsynonymous mutations identified in the KCNA5 gene from idiopathic pulmonary arterial hypertension (IPAH) patients localize to the NH 2 -terminal tetramerization domain (T1 domain). A , left : schematic diagram of voltage-gated K + (K V ) channel subunit

    Techniques Used:

    Cotransfection of K V β subunits affects KCNA5 channel kinetics. HEK-293 cells were transfected with WT KCNA5 alone (KCNA5) or in the presence of K V β1.3-hemagglutinin (HA) (KCNA5/K V β1.3). A and B : representative current recordings
    Figure Legend Snippet: Cotransfection of K V β subunits affects KCNA5 channel kinetics. HEK-293 cells were transfected with WT KCNA5 alone (KCNA5) or in the presence of K V β1.3-hemagglutinin (HA) (KCNA5/K V β1.3). A and B : representative current recordings

    Techniques Used: Cotransfection, Transfection

    Voltage-dependent inactivation is accelerated in the G182R mutant KCNA5 channel. A standard 2-pulse inactivation protocol was used to determine channel availability after a 10-s prepulse in HEK-293 cells transiently transfected with WT KCNA5, G182R, E211D,
    Figure Legend Snippet: Voltage-dependent inactivation is accelerated in the G182R mutant KCNA5 channel. A standard 2-pulse inactivation protocol was used to determine channel availability after a 10-s prepulse in HEK-293 cells transiently transfected with WT KCNA5, G182R, E211D,

    Techniques Used: Mutagenesis, Transfection

    G182R protein expression is significantly decreased in COS-1 cells. A : COS-1 cells were transiently transfected with water (Mock), WT-KCNA5, G182R, E211D, or G182R/E211D. Representative images are shown at ×40 magnification. B : transfected cells
    Figure Legend Snippet: G182R protein expression is significantly decreased in COS-1 cells. A : COS-1 cells were transiently transfected with water (Mock), WT-KCNA5, G182R, E211D, or G182R/E211D. Representative images are shown at ×40 magnification. B : transfected cells

    Techniques Used: Expressing, Transfection

    3) Product Images from "K+ Channel Kv3.4 Is Essential for Axon Growth by Limiting the Influx of Ca2+ into Growth Cones"

    Article Title: K+ Channel Kv3.4 Is Essential for Axon Growth by Limiting the Influx of Ca2+ into Growth Cones

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.1076-16.2017

    Kv3.4 in the axonal growth cones of dorsal spinal commissural neurons. A–F , Transverse sections of the spinal cord of chick embryos were immunostained for Kv3.4. A , Absence of Kv3.4-IR in the dorsal spinal cord at HH17. Kv3.4-IR in precrossing commissural axons ( B–F , arrowheads) is evident during HH19-HH25 but disappears at HH27. D , Arrows indicate postcrossing commissural axons projecting from the other side of spinal cord. FP, Floor plate. G–L , Transverse sections of the spinal cord at HH23 were immunostained as indicated. G , Absence of Kv1.5-IR. H , Kv4.2-IR in the somata and dendrites of motoneurons (MN). I , Kv4.3-IR in the bifurcation zone (BZ). In addition to the BZ, Kv3.1b-IR is strong in postcrossing commissural axons ( J , arrow) but weak in precrossing commissural axons ( J , arrowhead). K , Absence of Kv3.2-IR. L , Kv3.3 in motoneurons. M–M″ , Double staining in transverse sections of the spinal cord at HH21 shows colocalization of Kv3.4 and axonin-1 in the growth cones (arrowheads) of commissural axons. N–N″ , Colocalization of Kv3.4 and axonin-1 in cultured dorsal spinal neurons isolated from HH21-HH23 chick embryos. O–P″ , Red fluorescence-tagged phalloidin colabeling reveals enrichment of Kv3.4 in the growth cone ( O–O″ ) and Kv3.1b in the soma/axon shaft ( P–P″ ) of cultured dorsal spinal neurons. Q–Q″ , Kv3.4 and DiI colabeling. White represents Kv3.4-abundant regions. Blue represents Kv3.4-sparse regions ( Q″ ). R , Ratio of Kv3.4/DiI in the soma, axon shaft, or growth cone of each neuron was obtained by dividing the fluorescence intensity of Kv3.4 by that of DiI. Data are mean ± SEM ( n = 8 neurons, pooled from three independent experiments done on different days). *** p
    Figure Legend Snippet: Kv3.4 in the axonal growth cones of dorsal spinal commissural neurons. A–F , Transverse sections of the spinal cord of chick embryos were immunostained for Kv3.4. A , Absence of Kv3.4-IR in the dorsal spinal cord at HH17. Kv3.4-IR in precrossing commissural axons ( B–F , arrowheads) is evident during HH19-HH25 but disappears at HH27. D , Arrows indicate postcrossing commissural axons projecting from the other side of spinal cord. FP, Floor plate. G–L , Transverse sections of the spinal cord at HH23 were immunostained as indicated. G , Absence of Kv1.5-IR. H , Kv4.2-IR in the somata and dendrites of motoneurons (MN). I , Kv4.3-IR in the bifurcation zone (BZ). In addition to the BZ, Kv3.1b-IR is strong in postcrossing commissural axons ( J , arrow) but weak in precrossing commissural axons ( J , arrowhead). K , Absence of Kv3.2-IR. L , Kv3.3 in motoneurons. M–M″ , Double staining in transverse sections of the spinal cord at HH21 shows colocalization of Kv3.4 and axonin-1 in the growth cones (arrowheads) of commissural axons. N–N″ , Colocalization of Kv3.4 and axonin-1 in cultured dorsal spinal neurons isolated from HH21-HH23 chick embryos. O–P″ , Red fluorescence-tagged phalloidin colabeling reveals enrichment of Kv3.4 in the growth cone ( O–O″ ) and Kv3.1b in the soma/axon shaft ( P–P″ ) of cultured dorsal spinal neurons. Q–Q″ , Kv3.4 and DiI colabeling. White represents Kv3.4-abundant regions. Blue represents Kv3.4-sparse regions ( Q″ ). R , Ratio of Kv3.4/DiI in the soma, axon shaft, or growth cone of each neuron was obtained by dividing the fluorescence intensity of Kv3.4 by that of DiI. Data are mean ± SEM ( n = 8 neurons, pooled from three independent experiments done on different days). *** p

    Techniques Used: Double Staining, Cell Culture, Isolation, Fluorescence

    4) Product Images from "Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes"

    Article Title: Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes

    Journal: The Journal of Physiology

    doi: 10.1113/jphysiol.2007.134809

    Some Kv1.5 channel subunits are localized in lipid raft fractions in adult rat atrial myocytes Western blot analysis of the distribution of Kv1.5 subunits, connexin-43 and caveolin-3 on step sucrose gradient of proteins from atrial myocardium.
    Figure Legend Snippet: Some Kv1.5 channel subunits are localized in lipid raft fractions in adult rat atrial myocytes Western blot analysis of the distribution of Kv1.5 subunits, connexin-43 and caveolin-3 on step sucrose gradient of proteins from atrial myocardium.

    Techniques Used: Western Blot

    Kv1.5 do not co-localized with caveolin-3 in adult atrial tissue Immunolocalization of Kv1.5 subunits ( A ) and caveolin-3 ( B ) in cryosections of atrial myocardium. Double immunostaining of connexin-43 (FITC, C ) and caveolin-3 (Texas Red, D ) in cryosections of atrial myocardium. E , merged image of the same area of the section in C and D , showing the lack of overlap between connexin-43 and caveolin-3 stainings.
    Figure Legend Snippet: Kv1.5 do not co-localized with caveolin-3 in adult atrial tissue Immunolocalization of Kv1.5 subunits ( A ) and caveolin-3 ( B ) in cryosections of atrial myocardium. Double immunostaining of connexin-43 (FITC, C ) and caveolin-3 (Texas Red, D ) in cryosections of atrial myocardium. E , merged image of the same area of the section in C and D , showing the lack of overlap between connexin-43 and caveolin-3 stainings.

    Techniques Used: Double Immunostaining

    Surface expression of Kv1.5 subunits in neonatal cardiomyocytes A , in live cardiomyocytes, transfected GFP-tagged Kv1.5 subunits are clustered at the membrane surface adjacent to the bottom of laminin-coated glass support, as shown in the projection of Z sections in the lower panel. In contrast, GFP alone was homogeneously distributed in cardiomyocytes (inset). B , after the application of 2% MCD, clusters increased in size and were redistributed throughout the plasma membrane. C , bar graphs summarizing changes in cluster size upon MCD exposures; data are from 21 cardiomyocytes in control, and following incubation with 2% MCD for 7 min and 1 h 30 min. ** P
    Figure Legend Snippet: Surface expression of Kv1.5 subunits in neonatal cardiomyocytes A , in live cardiomyocytes, transfected GFP-tagged Kv1.5 subunits are clustered at the membrane surface adjacent to the bottom of laminin-coated glass support, as shown in the projection of Z sections in the lower panel. In contrast, GFP alone was homogeneously distributed in cardiomyocytes (inset). B , after the application of 2% MCD, clusters increased in size and were redistributed throughout the plasma membrane. C , bar graphs summarizing changes in cluster size upon MCD exposures; data are from 21 cardiomyocytes in control, and following incubation with 2% MCD for 7 min and 1 h 30 min. ** P

    Techniques Used: Expressing, Transfection, Incubation

    Effect of cholesterol depletion on outward current parameters resulting from Kv1.5 subunit overexpression in neonatal cardiomyocytes Current density–voltage relationships ( A ) and voltage dependence ( B ) of I Kur activation under control conditions (•) and following 7 min MCD application (^). In A and B , each point represents average data from 5 cells.
    Figure Legend Snippet: Effect of cholesterol depletion on outward current parameters resulting from Kv1.5 subunit overexpression in neonatal cardiomyocytes Current density–voltage relationships ( A ) and voltage dependence ( B ) of I Kur activation under control conditions (•) and following 7 min MCD application (^). In A and B , each point represents average data from 5 cells.

    Techniques Used: Over Expression, Activation Assay

    5) Product Images from "Hydrogen peroxide induces vasorelaxation by enhancing 4-aminopyridine-sensitive Kv currents through S-glutathionylation"

    Article Title: Hydrogen peroxide induces vasorelaxation by enhancing 4-aminopyridine-sensitive Kv currents through S-glutathionylation

    Journal: Pflugers Archiv

    doi: 10.1007/s00424-014-1513-3

    S -glutathionylation of the Kv 2.1 channel after exposure to H 2 O 2 . a Kv 2.1 channels were detected only from samples that were obtained from the cells treated with both BioGEE and H 2 O 2 in the streptavidin pull-down assay. In the streptavidin pull-down assay, Kv1.2 and Kv1.5 channels were not detected even from samples that were obtained from cells treated with both BioGEE and H 2 O 2 . b Kv channel subunits were detected through conventional Western blot using rat mesenteric arterial smooth muscle cell (MASMC) primary cultures pretreated with various concentrations of H 2 O 2 and untreated control. Band density did not change with H 2 O 2 treatment. The results are representative examples of three independent experiments
    Figure Legend Snippet: S -glutathionylation of the Kv 2.1 channel after exposure to H 2 O 2 . a Kv 2.1 channels were detected only from samples that were obtained from the cells treated with both BioGEE and H 2 O 2 in the streptavidin pull-down assay. In the streptavidin pull-down assay, Kv1.2 and Kv1.5 channels were not detected even from samples that were obtained from cells treated with both BioGEE and H 2 O 2 . b Kv channel subunits were detected through conventional Western blot using rat mesenteric arterial smooth muscle cell (MASMC) primary cultures pretreated with various concentrations of H 2 O 2 and untreated control. Band density did not change with H 2 O 2 treatment. The results are representative examples of three independent experiments

    Techniques Used: Pull Down Assay, Western Blot

    6) Product Images from "Interactions between the C-terminus of Kv1.5 and Kv? regulate pyridine nucleotide-dependent changes in channel gating"

    Article Title: Interactions between the C-terminus of Kv1.5 and Kv? regulate pyridine nucleotide-dependent changes in channel gating

    Journal: Pflugers Archiv

    doi: 10.1007/s00424-012-1093-z

    Binding of the C-terminal domain of Kv to Kvβ (a)  Western blots of Kvβ2 (upper panel) and Kvβ3 (middle panel) pulled down by the GST-Kv1.5 C-terminus fusion peptides. Fusion proteins containing 60, 38, or 19 terminal amino acid peptides from Kvα1.5 C-terminus attached to GST or GST with unrelated peptide (Control; 30μ g each) were incubated with lysate of Kvβ2 or Kvβ3 -expressing  E.coli  (350 μ g total protein). Protein complexes were pulled down using GST·Bind beads, washed and eluted with 10mM glutathione. The eluate was separated by SDS-PAGE and probed with anti-pan-Kvβ antibody, an antibody directed against the C-terminus of Kv1.5 (bait) or GST;  (b)  Densitometric analysis of the bands in panel a. The density of the Kvβ band precipitated with GST-C60 was assigned a 100% value. †, P
    Figure Legend Snippet: Binding of the C-terminal domain of Kv to Kvβ (a) Western blots of Kvβ2 (upper panel) and Kvβ3 (middle panel) pulled down by the GST-Kv1.5 C-terminus fusion peptides. Fusion proteins containing 60, 38, or 19 terminal amino acid peptides from Kvα1.5 C-terminus attached to GST or GST with unrelated peptide (Control; 30μ g each) were incubated with lysate of Kvβ2 or Kvβ3 -expressing E.coli (350 μ g total protein). Protein complexes were pulled down using GST·Bind beads, washed and eluted with 10mM glutathione. The eluate was separated by SDS-PAGE and probed with anti-pan-Kvβ antibody, an antibody directed against the C-terminus of Kv1.5 (bait) or GST; (b) Densitometric analysis of the bands in panel a. The density of the Kvβ band precipitated with GST-C60 was assigned a 100% value. †, P

    Techniques Used: Binding Assay, Western Blot, Incubation, Expressing, SDS Page

    7) Product Images from "Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury"

    Article Title: Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0049758

    OxLDL-induced mitochondrial ROS overproduction was attenuated by Kv1.5 siRNA, but exaggerated by Kv1.5 overexpression. The mitochondrial ROS generation was detected using MitoSOX reagents in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) The representative images from laser scanning confocal microscopy Kv1.5 siRNA significantly attenuated oxLDL-induced mitochondrial superoxide production in HPAECs. ( B ) ( C ). The mitochondrial ROS levels in HPAECs transfected with Kv1.5 siRNA (B) or infected with adnovirus overexpression of Kv1.5 (C) were quantified by the fluorescent plate reader and expressed as the ratio of MitoSOX to Mitotracker. The values are presented as means ± SEM of 6 independent experiments. * P
    Figure Legend Snippet: OxLDL-induced mitochondrial ROS overproduction was attenuated by Kv1.5 siRNA, but exaggerated by Kv1.5 overexpression. The mitochondrial ROS generation was detected using MitoSOX reagents in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) The representative images from laser scanning confocal microscopy Kv1.5 siRNA significantly attenuated oxLDL-induced mitochondrial superoxide production in HPAECs. ( B ) ( C ). The mitochondrial ROS levels in HPAECs transfected with Kv1.5 siRNA (B) or infected with adnovirus overexpression of Kv1.5 (C) were quantified by the fluorescent plate reader and expressed as the ratio of MitoSOX to Mitotracker. The values are presented as means ± SEM of 6 independent experiments. * P

    Techniques Used: Over Expression, Transfection, Infection, Confocal Microscopy

    OxLDL-induced ROS overproduction was attenuated by Kv1.5 siRNA, but exaggerated by Kv1.5 overexpression. Intracellular ROS levels were detected using DCFH-DA staining in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) ( B ). Kv1.5 siRNA significantly attenuated oxLDL-induced endothelial ROS overproduction in HPAECs, as demonstrated by representative images from laser scanning confocal microscopy and bar graph showing fluorescence intensity measured in Multi-Mode Microplate Reader. ( C ). Bar graph shows that adnoviral KCNA5 gene transfer exaggerated oxLDL-induced endothelial ROS overproduction in HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P
    Figure Legend Snippet: OxLDL-induced ROS overproduction was attenuated by Kv1.5 siRNA, but exaggerated by Kv1.5 overexpression. Intracellular ROS levels were detected using DCFH-DA staining in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) ( B ). Kv1.5 siRNA significantly attenuated oxLDL-induced endothelial ROS overproduction in HPAECs, as demonstrated by representative images from laser scanning confocal microscopy and bar graph showing fluorescence intensity measured in Multi-Mode Microplate Reader. ( C ). Bar graph shows that adnoviral KCNA5 gene transfer exaggerated oxLDL-induced endothelial ROS overproduction in HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P

    Techniques Used: Over Expression, Staining, Transfection, Infection, Confocal Microscopy, Fluorescence

    Effects of Kv1.5 siRNA adenoviral Kv1.5 overexpression on endogenous Kv1.5 protein expression in HPAECs. ( A ). HPAECs were treated with 2.5, 5, 10 nM Kv1.5 siRNA for 48 h and Kv1.5 protein expression was analyzed by western blot. * P
    Figure Legend Snippet: Effects of Kv1.5 siRNA adenoviral Kv1.5 overexpression on endogenous Kv1.5 protein expression in HPAECs. ( A ). HPAECs were treated with 2.5, 5, 10 nM Kv1.5 siRNA for 48 h and Kv1.5 protein expression was analyzed by western blot. * P

    Techniques Used: Over Expression, Expressing, Western Blot

    Ang II and oxLDL affected Kv1.5 protein expression, intracellular ROS production, and endothelial cell injury. HUVECs were incubated with AngII at different concentrations for different times. Ang II time (A)- or concentration (B)-dependently enhanced the Kv1.5 protein expression. Pretreatment with MT for 30 min inhibited Ang II (2 µM, 24 h)-induced increase in intracellular ROS levels in HUVECs in a concentration-dependent manner (C), as determined by DCF fluorescence. MT also significantly attenuated Ang II (2 µM, 24 h)-induced HUVEC injury. Incubation of HPAECs with oxLDL at the concentration of 37.5, 75 and 150 µg/ml significantly increased EC injury (D), intracellular ROS production (E) and Kv1.5 protein expression (F) in a concentration-dependent manner. The values were presented as ± SEM of 6 independent experiments for Ang II- or oxLDL-treatment, respectively. * P
    Figure Legend Snippet: Ang II and oxLDL affected Kv1.5 protein expression, intracellular ROS production, and endothelial cell injury. HUVECs were incubated with AngII at different concentrations for different times. Ang II time (A)- or concentration (B)-dependently enhanced the Kv1.5 protein expression. Pretreatment with MT for 30 min inhibited Ang II (2 µM, 24 h)-induced increase in intracellular ROS levels in HUVECs in a concentration-dependent manner (C), as determined by DCF fluorescence. MT also significantly attenuated Ang II (2 µM, 24 h)-induced HUVEC injury. Incubation of HPAECs with oxLDL at the concentration of 37.5, 75 and 150 µg/ml significantly increased EC injury (D), intracellular ROS production (E) and Kv1.5 protein expression (F) in a concentration-dependent manner. The values were presented as ± SEM of 6 independent experiments for Ang II- or oxLDL-treatment, respectively. * P

    Techniques Used: Expressing, Incubation, Concentration Assay, Fluorescence

    OxLDL-induced EC injury was attenuated by Kv1.5 siRNA, but aggravated by adnoviral Kv1.5 overexpression. HPAECs were transfected with Kv1.5 siRNA (10 nM) or control siRNA for 48 h, or infected with adnovirus containing KCNA5 and control–adnovirus for 24 h, then treated with oxLDL (150 µg/ml) for further 24 h. The oxLDL-induced EC injury was detected by optical microscopy and DAPI staining. The optical microscope observation (A) and DAPI staining (B) show the morphological changes in Kv1.5 siRNA pretreated HPAECs. The mean values of percentages of apoptotic cells were summarized after DAPI staining in Kv1.5 siRNA (C)- and KCNA5 adnovirus- pretreated (D) HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P
    Figure Legend Snippet: OxLDL-induced EC injury was attenuated by Kv1.5 siRNA, but aggravated by adnoviral Kv1.5 overexpression. HPAECs were transfected with Kv1.5 siRNA (10 nM) or control siRNA for 48 h, or infected with adnovirus containing KCNA5 and control–adnovirus for 24 h, then treated with oxLDL (150 µg/ml) for further 24 h. The oxLDL-induced EC injury was detected by optical microscopy and DAPI staining. The optical microscope observation (A) and DAPI staining (B) show the morphological changes in Kv1.5 siRNA pretreated HPAECs. The mean values of percentages of apoptotic cells were summarized after DAPI staining in Kv1.5 siRNA (C)- and KCNA5 adnovirus- pretreated (D) HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P

    Techniques Used: Over Expression, Transfection, Infection, Microscopy, Staining

    OxLDL-induced reduction in UCP2 protein was restored by Kv1.5 siRNA, but exaggerated by Kv1.5 overexpression. The UCP2 protein expression was detected by western blot in HPAECs transfected with Kv1.5-siRNA (A) and or infected with adnovirus containing KCNA5 (B). Digital photographs showing UCP2 protein expression are on the top panel and bar graph showing quantitative analysis of the total protein are on the lower panel. The values are presented as means ± SEM of 6 independent experiments. ** P
    Figure Legend Snippet: OxLDL-induced reduction in UCP2 protein was restored by Kv1.5 siRNA, but exaggerated by Kv1.5 overexpression. The UCP2 protein expression was detected by western blot in HPAECs transfected with Kv1.5-siRNA (A) and or infected with adnovirus containing KCNA5 (B). Digital photographs showing UCP2 protein expression are on the top panel and bar graph showing quantitative analysis of the total protein are on the lower panel. The values are presented as means ± SEM of 6 independent experiments. ** P

    Techniques Used: Over Expression, Expressing, Western Blot, Transfection, Infection

    Kv1.5 inhibitor, DPO-1 attenuated H 2 O 2 -induced in vivo EC apoptosis in rat carotid artery. DPO-1(0.3, 3 mg/kg) was i.p. dose administrated at 6 hours after H 2 O 2 injury. Representative morphological changes of apoptotic ECs were determined by en face Hoechst 33342 staining in Control (A), H 2 O 2 injury (B) and DPO-1 treatment (C) groups. The contralateral side of carotid artery at 6 h after injury served as control, nuclear morphology of normal ECs (round, shown by full line arrow in (A)) and VSMCs (spindle-shaped, shown by dotted line arrow in (A)) can be observed. In (B) (C), the white arrows show typical apoptotic morphological changes in apoptotic ECs, including chromatin condensation and nuclear fragmentation. The values were presented as ± SEM of 6 independent experiments. * P
    Figure Legend Snippet: Kv1.5 inhibitor, DPO-1 attenuated H 2 O 2 -induced in vivo EC apoptosis in rat carotid artery. DPO-1(0.3, 3 mg/kg) was i.p. dose administrated at 6 hours after H 2 O 2 injury. Representative morphological changes of apoptotic ECs were determined by en face Hoechst 33342 staining in Control (A), H 2 O 2 injury (B) and DPO-1 treatment (C) groups. The contralateral side of carotid artery at 6 h after injury served as control, nuclear morphology of normal ECs (round, shown by full line arrow in (A)) and VSMCs (spindle-shaped, shown by dotted line arrow in (A)) can be observed. In (B) (C), the white arrows show typical apoptotic morphological changes in apoptotic ECs, including chromatin condensation and nuclear fragmentation. The values were presented as ± SEM of 6 independent experiments. * P

    Techniques Used: In Vivo, Staining

    8) Product Images from "Effect of Methamphetamine on the Microglial Damage: Role of Potassium Channel Kv1.3"

    Article Title: Effect of Methamphetamine on the Microglial Damage: Role of Potassium Channel Kv1.3

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0088642

    Meth increased Kv1.3 protein expression rather than Kv1.5. Microglial cells were incubated with Meth, and the level of Kv1.3, Kv1.5 proteins were detected by western-blot. (A) Meth (0, 100,300 µM) up-regulated Kv1.3 protein in a concentration dependent manner. (B) Meth (300 µM) obviously up-regulated Kv1.3 protein expression in 12, 24 and 48 h, and displayed a time-dependent way. (C) Meth mediated up-regulation of Kv1.3 protein level was partly attenuated by MgTx (10 nM). (D) and (E) Meth (300 µM) showed no impact on Kv1.5 protein level. * and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p
    Figure Legend Snippet: Meth increased Kv1.3 protein expression rather than Kv1.5. Microglial cells were incubated with Meth, and the level of Kv1.3, Kv1.5 proteins were detected by western-blot. (A) Meth (0, 100,300 µM) up-regulated Kv1.3 protein in a concentration dependent manner. (B) Meth (300 µM) obviously up-regulated Kv1.3 protein expression in 12, 24 and 48 h, and displayed a time-dependent way. (C) Meth mediated up-regulation of Kv1.3 protein level was partly attenuated by MgTx (10 nM). (D) and (E) Meth (300 µM) showed no impact on Kv1.5 protein level. * and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p

    Techniques Used: Expressing, Incubation, Western Blot, Concentration Assay

    Meth increased Kv1.3 mRNA expression rather than Kv1.5. Microglial cells were incubated with Meth (300 µM) for 24 h, and the mRNA level was detected by realtime-PCR. (A) Meth significantly increased the Kv1.3 mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on Kv1.5 mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p
    Figure Legend Snippet: Meth increased Kv1.3 mRNA expression rather than Kv1.5. Microglial cells were incubated with Meth (300 µM) for 24 h, and the mRNA level was detected by realtime-PCR. (A) Meth significantly increased the Kv1.3 mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on Kv1.5 mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p

    Techniques Used: Expressing, Incubation, Polymerase Chain Reaction

    9) Product Images from "Modulation of Kv1.5 Currents by Src Tyrosine Phosphorylation: Potential Role in the Differentiation of Astrocytes"

    Article Title: Modulation of Kv1.5 Currents by Src Tyrosine Phosphorylation: Potential Role in the Differentiation of Astrocytes

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.20-14-05245.2000

    Src inhibitor acutely decreases Kv1.5 currents. A , Representative recording of currents in response to the voltage protocols shown ( insets to the right ). Currents were recorded after achieving whole-cell configuration ( Control ) and at 12 min after dialyzing
    Figure Legend Snippet: Src inhibitor acutely decreases Kv1.5 currents. A , Representative recording of currents in response to the voltage protocols shown ( insets to the right ). Currents were recorded after achieving whole-cell configuration ( Control ) and at 12 min after dialyzing

    Techniques Used:

    Src family-specific inhibitor PP2 decreases phosphorylation of Kv1.5 without affecting channel expression within the membrane. A , Kv1.5 protein levels in cell lysates are unaltered by incubation with the Src-specific inhibitor PP2. B , Tyrosine phosphorylation
    Figure Legend Snippet: Src family-specific inhibitor PP2 decreases phosphorylation of Kv1.5 without affecting channel expression within the membrane. A , Kv1.5 protein levels in cell lysates are unaltered by incubation with the Src-specific inhibitor PP2. B , Tyrosine phosphorylation

    Techniques Used: Expressing, Incubation

    Immunoreactivity for Kv1.5 did not change with proliferative status. A , B , Proliferating astrocytes as well as actively dividing cells ( arrows ) demonstrate diffuse Kv1.5 staining. C , Staining is seen in acutely dissociated spinal cord cells, implying
    Figure Legend Snippet: Immunoreactivity for Kv1.5 did not change with proliferative status. A , B , Proliferating astrocytes as well as actively dividing cells ( arrows ) demonstrate diffuse Kv1.5 staining. C , Staining is seen in acutely dissociated spinal cord cells, implying

    Techniques Used: Staining

    Increased Src activity increases astrocyte proliferation. A , Transfecting Src Y529F, a constitutively active Src ( Src* ), into quiescent astrocytes ( 27 DIV ) restores immunoreactivity of Kv1.5 for phosphotyrosine, as analyzed by Western blot. B , Astrocytes
    Figure Legend Snippet: Increased Src activity increases astrocyte proliferation. A , Transfecting Src Y529F, a constitutively active Src ( Src* ), into quiescent astrocytes ( 27 DIV ) restores immunoreactivity of Kv1.5 for phosphotyrosine, as analyzed by Western blot. B , Astrocytes

    Techniques Used: Activity Assay, Western Blot

    Kv1.5 antisense oligodeoxynucleotides inhibit astrocyte potassium currents and proliferation. A , Whole-cell current traces from a representative nonsense-treated control and antisense-treated cell as elicited by the voltage protocol ( inset above ). Antisense
    Figure Legend Snippet: Kv1.5 antisense oligodeoxynucleotides inhibit astrocyte potassium currents and proliferation. A , Whole-cell current traces from a representative nonsense-treated control and antisense-treated cell as elicited by the voltage protocol ( inset above ). Antisense

    Techniques Used:

    Kv1.5 protein expression is unaltered during astrocyte differentiation. A , A protein band at a molecular weight of 67 kDa was specific for Kv1.5 immunoreactivity and was unaltered neither on cell cycle arrest with RA or TEA nor on differentiation in culture
    Figure Legend Snippet: Kv1.5 protein expression is unaltered during astrocyte differentiation. A , A protein band at a molecular weight of 67 kDa was specific for Kv1.5 immunoreactivity and was unaltered neither on cell cycle arrest with RA or TEA nor on differentiation in culture

    Techniques Used: Expressing, Molecular Weight

    Coprecipitation of Kv1.5 and native Src throughout astrocyte differentiation. A , Immobilized Kv1.5 antibody is able to precipitate Kv1.5 channel protein in actively proliferating cells ( 5 DIV ), throughout differentiation (at 14, 20, and 33 DIV ), in astrocytes
    Figure Legend Snippet: Coprecipitation of Kv1.5 and native Src throughout astrocyte differentiation. A , Immobilized Kv1.5 antibody is able to precipitate Kv1.5 channel protein in actively proliferating cells ( 5 DIV ), throughout differentiation (at 14, 20, and 33 DIV ), in astrocytes

    Techniques Used:

    Increased Src activity increases Kv1.5 currents. A , Representative recording of currents in response to the voltage protocols shown ( insets to the right ). Currents were recorded within 1 min of achieving whole-cell configuration ( Control ) and at 35 min
    Figure Legend Snippet: Increased Src activity increases Kv1.5 currents. A , Representative recording of currents in response to the voltage protocols shown ( insets to the right ). Currents were recorded within 1 min of achieving whole-cell configuration ( Control ) and at 35 min

    Techniques Used: Activity Assay

    10) Product Images from "Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes"

    Article Title: Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes

    Journal: The Journal of Physiology

    doi: 10.1113/jphysiol.2007.134809

    Some Kv1.5 channel subunits are localized in lipid raft fractions in adult rat atrial myocytes Western blot analysis of the distribution of Kv1.5 subunits, connexin-43 and caveolin-3 on step sucrose gradient of proteins from atrial myocardium.
    Figure Legend Snippet: Some Kv1.5 channel subunits are localized in lipid raft fractions in adult rat atrial myocytes Western blot analysis of the distribution of Kv1.5 subunits, connexin-43 and caveolin-3 on step sucrose gradient of proteins from atrial myocardium.

    Techniques Used: Western Blot

    Kv1.5 do not co-localized with caveolin-3 in adult atrial tissue Immunolocalization of Kv1.5 subunits ( A ) and caveolin-3 ( B ) in cryosections of atrial myocardium. Double immunostaining of connexin-43 (FITC, C ) and caveolin-3 (Texas Red, D ) in cryosections of atrial myocardium. E , merged image of the same area of the section in C and D , showing the lack of overlap between connexin-43 and caveolin-3 stainings.
    Figure Legend Snippet: Kv1.5 do not co-localized with caveolin-3 in adult atrial tissue Immunolocalization of Kv1.5 subunits ( A ) and caveolin-3 ( B ) in cryosections of atrial myocardium. Double immunostaining of connexin-43 (FITC, C ) and caveolin-3 (Texas Red, D ) in cryosections of atrial myocardium. E , merged image of the same area of the section in C and D , showing the lack of overlap between connexin-43 and caveolin-3 stainings.

    Techniques Used: Double Immunostaining

    Surface expression of Kv1.5 subunits in neonatal cardiomyocytes A , in live cardiomyocytes, transfected GFP-tagged Kv1.5 subunits are clustered at the membrane surface adjacent to the bottom of laminin-coated glass support, as shown in the projection of Z sections in the lower panel. In contrast, GFP alone was homogeneously distributed in cardiomyocytes (inset). B , after the application of 2% MCD, clusters increased in size and were redistributed throughout the plasma membrane. C , bar graphs summarizing changes in cluster size upon MCD exposures; data are from 21 cardiomyocytes in control, and following incubation with 2% MCD for 7 min and 1 h 30 min. ** P
    Figure Legend Snippet: Surface expression of Kv1.5 subunits in neonatal cardiomyocytes A , in live cardiomyocytes, transfected GFP-tagged Kv1.5 subunits are clustered at the membrane surface adjacent to the bottom of laminin-coated glass support, as shown in the projection of Z sections in the lower panel. In contrast, GFP alone was homogeneously distributed in cardiomyocytes (inset). B , after the application of 2% MCD, clusters increased in size and were redistributed throughout the plasma membrane. C , bar graphs summarizing changes in cluster size upon MCD exposures; data are from 21 cardiomyocytes in control, and following incubation with 2% MCD for 7 min and 1 h 30 min. ** P

    Techniques Used: Expressing, Transfection, Incubation

    Effect of cholesterol depletion on outward current parameters resulting from Kv1.5 subunit overexpression in neonatal cardiomyocytes Current density–voltage relationships ( A ) and voltage dependence ( B ) of I Kur activation under control conditions (•) and following 7 min MCD application (^). In A and B , each point represents average data from 5 cells.
    Figure Legend Snippet: Effect of cholesterol depletion on outward current parameters resulting from Kv1.5 subunit overexpression in neonatal cardiomyocytes Current density–voltage relationships ( A ) and voltage dependence ( B ) of I Kur activation under control conditions (•) and following 7 min MCD application (^). In A and B , each point represents average data from 5 cells.

    Techniques Used: Over Expression, Activation Assay

    11) Product Images from "Cortactin Is Required for N-cadherin Regulation of Kv1.5 Channel Function *"

    Article Title: Cortactin Is Required for N-cadherin Regulation of Kv1.5 Channel Function *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M111.218560

    Differential expression of Kv channels in N-cad CKO myocytes. A–H , immunostaining of Kv1.5 ( A and B ), kcne2 ( C and D ), Kv1.4 ( E and F ), and Kir2.1 ( G and H ) in WT and N-cad CKO. I , relative cell surface fluorescence intensity was quantified from eight optical slices through the cardiomyocyte ( n = 10–12). **, p
    Figure Legend Snippet: Differential expression of Kv channels in N-cad CKO myocytes. A–H , immunostaining of Kv1.5 ( A and B ), kcne2 ( C and D ), Kv1.4 ( E and F ), and Kir2.1 ( G and H ) in WT and N-cad CKO. I , relative cell surface fluorescence intensity was quantified from eight optical slices through the cardiomyocyte ( n = 10–12). **, p

    Techniques Used: Expressing, Immunostaining, Fluorescence

    Knockdown of cortactin ablated the N-cadherin regulation of Kv1.5 channel activity. A , ionic current generated by injecting cRNA encoding Kv1.5 and N-cadherin in Xenopus oocytes. B , co-injection of Xenopus cortactin-specific antisense DNA oligonucleotides with cRNA encoding Kv1.5 and N-cadherin. C , co-injection with scrambled control oligonucleotides showed no effect on current enhancement by N-cadherin. D , average current-voltage relationships in different groups. ■, Kv1.5 + N-cadherin, n = 16; □, Kv1.5 + N-cadherin +cortactin-specific antisense DNA oligonucleotides, n = 30; ○, Kv1.5 + N-cadherin + negative control, n = 18.
    Figure Legend Snippet: Knockdown of cortactin ablated the N-cadherin regulation of Kv1.5 channel activity. A , ionic current generated by injecting cRNA encoding Kv1.5 and N-cadherin in Xenopus oocytes. B , co-injection of Xenopus cortactin-specific antisense DNA oligonucleotides with cRNA encoding Kv1.5 and N-cadherin. C , co-injection with scrambled control oligonucleotides showed no effect on current enhancement by N-cadherin. D , average current-voltage relationships in different groups. ■, Kv1.5 + N-cadherin, n = 16; □, Kv1.5 + N-cadherin +cortactin-specific antisense DNA oligonucleotides, n = 30; ○, Kv1.5 + N-cadherin + negative control, n = 18.

    Techniques Used: Activity Assay, Generated, Injection, Negative Control

    Kv1.5 and kcne2 expression were reduced in N-cad CKO ventricles. A , quantitative Western blot analysis was performed on fractionated ventricular membrane from WT and N-cad CKO hearts. B , quantification of the Western blot data. Transferrin receptor signal was used to normalize for loading differences between lanes.
    Figure Legend Snippet: Kv1.5 and kcne2 expression were reduced in N-cad CKO ventricles. A , quantitative Western blot analysis was performed on fractionated ventricular membrane from WT and N-cad CKO hearts. B , quantification of the Western blot data. Transferrin receptor signal was used to normalize for loading differences between lanes.

    Techniques Used: Expressing, Western Blot

    Cortactin associates with Kv1.5 channel. A , upper panel , extracts of HEK-293 cells transfected with Kv1.5-GFP were immunoprecipitated ( IP ) using a polyclonal anti-cortactin antibody and immunoblotted with anti-Kv1.5 antibody first and then stripped and reprobed with anti-GFP antibody. Total input ( In ) HEK-293/Kv1.5-GFP cell extract was also probed with anti-Kv1.5 and anti-GFP antibodies. Immunoprecipitation minus cortactin antibody was used as a negative control. Lower panel , to control for nonspecific binding of cortactin to GFP, HEK-293 cells were transfected with GFP or Kv1.5-GFP followed by immunoprecipitation with anti-GFP antibody and immunoblotted for cortactin. Total input ( In ) HEK-293/Kv1.5-GFP cell extract was also probed with the anti-cortactin antibody. Note that GFP alone does not interact with cortactin. B , upper panel , extracts of adult mouse ventricles were immunoprecipitated with anti-cortactin antibody and immunoblotted with anti-Kv1.5, anti-Arp2, and anti-N-cadherin antibodies. Lower panel , extracts of adult mouse ventricles were immunoprecipitated with anti-N-cadherin antibody and immunoblotted with anti-Kv1.5, anti-cortactin, and anti-β-catenin antibodies. As a direct binding partner of N-cadherin, β-catenin was used as a positive control.
    Figure Legend Snippet: Cortactin associates with Kv1.5 channel. A , upper panel , extracts of HEK-293 cells transfected with Kv1.5-GFP were immunoprecipitated ( IP ) using a polyclonal anti-cortactin antibody and immunoblotted with anti-Kv1.5 antibody first and then stripped and reprobed with anti-GFP antibody. Total input ( In ) HEK-293/Kv1.5-GFP cell extract was also probed with anti-Kv1.5 and anti-GFP antibodies. Immunoprecipitation minus cortactin antibody was used as a negative control. Lower panel , to control for nonspecific binding of cortactin to GFP, HEK-293 cells were transfected with GFP or Kv1.5-GFP followed by immunoprecipitation with anti-GFP antibody and immunoblotted for cortactin. Total input ( In ) HEK-293/Kv1.5-GFP cell extract was also probed with the anti-cortactin antibody. Note that GFP alone does not interact with cortactin. B , upper panel , extracts of adult mouse ventricles were immunoprecipitated with anti-cortactin antibody and immunoblotted with anti-Kv1.5, anti-Arp2, and anti-N-cadherin antibodies. Lower panel , extracts of adult mouse ventricles were immunoprecipitated with anti-N-cadherin antibody and immunoblotted with anti-Kv1.5, anti-cortactin, and anti-β-catenin antibodies. As a direct binding partner of N-cadherin, β-catenin was used as a positive control.

    Techniques Used: Transfection, Immunoprecipitation, Negative Control, Binding Assay, Positive Control

    N-cadherin specifically enhanced Kv1.5 currents. cRNA encoding Kv1.5 and Kv1.5+ N-cad ( A ), Kv2.1 and Kv2.1+N-cad ( B ), and Kv4.2 and Kv4.2+N-cad ( C ) was injected into Xenopus oocytes. The details of the voltage clamp protocols are described in the legends (not to scale). In general, to record the current-voltage ( I-V ) relationship, the oocytes were voltage-clamped at a negative holding potential (−80 mV). Test potentials were applied to a variable potential with a fixed incremental increase between successive pulses at variable durations.
    Figure Legend Snippet: N-cadherin specifically enhanced Kv1.5 currents. cRNA encoding Kv1.5 and Kv1.5+ N-cad ( A ), Kv2.1 and Kv2.1+N-cad ( B ), and Kv4.2 and Kv4.2+N-cad ( C ) was injected into Xenopus oocytes. The details of the voltage clamp protocols are described in the legends (not to scale). In general, to record the current-voltage ( I-V ) relationship, the oocytes were voltage-clamped at a negative holding potential (−80 mV). Test potentials were applied to a variable potential with a fixed incremental increase between successive pulses at variable durations.

    Techniques Used: Injection

    Disruption of cortactin-actin cytoskeleton organization in N-cad CKO ventricular myocytes. Cardiomyocytes from WT and N-cad CKO mice were co-stained for actin ( A and D ) and Kv1.5 ( B and E ) or cortactin ( G and J ) and Kv1.5 ( H and K ). C , F , I , and L , insets show higher magnification of intercalated disc staining. M , Western blot analysis of actin, cortactin, and Arp2 in cortical cytoskeleton enriched fractions from WT and N-cad CKO ventricles. The arrow denotes the protein band corresponding to cortactin targeted by the antibody.
    Figure Legend Snippet: Disruption of cortactin-actin cytoskeleton organization in N-cad CKO ventricular myocytes. Cardiomyocytes from WT and N-cad CKO mice were co-stained for actin ( A and D ) and Kv1.5 ( B and E ) or cortactin ( G and J ) and Kv1.5 ( H and K ). C , F , I , and L , insets show higher magnification of intercalated disc staining. M , Western blot analysis of actin, cortactin, and Arp2 in cortical cytoskeleton enriched fractions from WT and N-cad CKO ventricles. The arrow denotes the protein band corresponding to cortactin targeted by the antibody.

    Techniques Used: Mouse Assay, Staining, Western Blot

    12) Product Images from "Cholesterol modulates the recruitment of Kv1.5 channels from Rab11-associated recycling endosome in native atrial myocytes"

    Article Title: Cholesterol modulates the recruitment of Kv1.5 channels from Rab11-associated recycling endosome in native atrial myocytes

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.0902809106

    Cholesterol depletion reduces the mobility and redistributes Kv1.5 channels in atrial myocytes. ( A ) Sequential images from FRAP experiments obtained in control prebleach (prebl.) and at various times postbleach (postbl.) in hKv1.5-EGFP expressing myocytes
    Figure Legend Snippet: Cholesterol depletion reduces the mobility and redistributes Kv1.5 channels in atrial myocytes. ( A ) Sequential images from FRAP experiments obtained in control prebleach (prebl.) and at various times postbleach (postbl.) in hKv1.5-EGFP expressing myocytes

    Techniques Used: Expressing

    13) Product Images from "Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns"

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00464.2009

    Mutant KCNA5 is located in perinuclear packets and not on the cell surface of transfected HEK-293 cells and human (h)PASMC. A : HEK-293 cells transfected with WT KCNA5 ( a and c ) or G182R ( b and d ) were stained with anti-KCNA5 antibody (Ab-KCNA5, red) and
    Figure Legend Snippet: Mutant KCNA5 is located in perinuclear packets and not on the cell surface of transfected HEK-293 cells and human (h)PASMC. A : HEK-293 cells transfected with WT KCNA5 ( a and c ) or G182R ( b and d ) were stained with anti-KCNA5 antibody (Ab-KCNA5, red) and

    Techniques Used: Mutagenesis, Transfection, Staining

    G182R and E211D mutations cause incomplete processing of KCNA5 in HEK-293 cells. HEK-293 cells were transfected with WT KCNA5, G182R, E211D, or G182R/E211D and subjected to standard immunoblot procedures. A : representative immunoblot from cells transfected
    Figure Legend Snippet: G182R and E211D mutations cause incomplete processing of KCNA5 in HEK-293 cells. HEK-293 cells were transfected with WT KCNA5, G182R, E211D, or G182R/E211D and subjected to standard immunoblot procedures. A : representative immunoblot from cells transfected

    Techniques Used: Transfection

    Mutant KCNA5 forms functional homotetrameric channels. A : COS-1, HEK-293, and human pulmonary artery smooth muscle cells (PASMC) were transiently transfected with either empty vector [green fluorescent protein (GFP)] or WT KCNA5 (WT) as indicated. Whole
    Figure Legend Snippet: Mutant KCNA5 forms functional homotetrameric channels. A : COS-1, HEK-293, and human pulmonary artery smooth muscle cells (PASMC) were transiently transfected with either empty vector [green fluorescent protein (GFP)] or WT KCNA5 (WT) as indicated. Whole

    Techniques Used: Mutagenesis, Functional Assay, Transfection, Plasmid Preparation

    Mutations in KCNA5 at G182 and E211 do not affect the pharmacological effect of 4-aminopyridine (4-AP). A : a standard I-V pulse protocol was delivered to HEK-293 cells transiently transfected with the indicated vector [WT KCNA5 ( a ), G182R ( b ), E211D (
    Figure Legend Snippet: Mutations in KCNA5 at G182 and E211 do not affect the pharmacological effect of 4-aminopyridine (4-AP). A : a standard I-V pulse protocol was delivered to HEK-293 cells transiently transfected with the indicated vector [WT KCNA5 ( a ), G182R ( b ), E211D (

    Techniques Used: Transfection, Plasmid Preparation

    Decreased G182R expression in COS-1 cells cannot be rescued by overexpression of K V β subunits. A , a : HEK-293 cells were transfected with WT KCNA5 or K V β1.3-HA alone or cotransfected with WT KCNA5, G182R, E211D, or G182R/E211D and K V β1.3-HA.
    Figure Legend Snippet: Decreased G182R expression in COS-1 cells cannot be rescued by overexpression of K V β subunits. A , a : HEK-293 cells were transfected with WT KCNA5 or K V β1.3-HA alone or cotransfected with WT KCNA5, G182R, E211D, or G182R/E211D and K V β1.3-HA.

    Techniques Used: Expressing, Over Expression, Transfection

    Two nonsynonymous mutations identified in the KCNA5 gene from idiopathic pulmonary arterial hypertension (IPAH) patients localize to the NH 2 -terminal tetramerization domain (T1 domain). A , left : schematic diagram of voltage-gated K + (K V ) channel subunit
    Figure Legend Snippet: Two nonsynonymous mutations identified in the KCNA5 gene from idiopathic pulmonary arterial hypertension (IPAH) patients localize to the NH 2 -terminal tetramerization domain (T1 domain). A , left : schematic diagram of voltage-gated K + (K V ) channel subunit

    Techniques Used:

    Cotransfection of K V β subunits affects KCNA5 channel kinetics. HEK-293 cells were transfected with WT KCNA5 alone (KCNA5) or in the presence of K V β1.3-hemagglutinin (HA) (KCNA5/K V β1.3). A and B : representative current recordings
    Figure Legend Snippet: Cotransfection of K V β subunits affects KCNA5 channel kinetics. HEK-293 cells were transfected with WT KCNA5 alone (KCNA5) or in the presence of K V β1.3-hemagglutinin (HA) (KCNA5/K V β1.3). A and B : representative current recordings

    Techniques Used: Cotransfection, Transfection

    Voltage-dependent inactivation is accelerated in the G182R mutant KCNA5 channel. A standard 2-pulse inactivation protocol was used to determine channel availability after a 10-s prepulse in HEK-293 cells transiently transfected with WT KCNA5, G182R, E211D,
    Figure Legend Snippet: Voltage-dependent inactivation is accelerated in the G182R mutant KCNA5 channel. A standard 2-pulse inactivation protocol was used to determine channel availability after a 10-s prepulse in HEK-293 cells transiently transfected with WT KCNA5, G182R, E211D,

    Techniques Used: Mutagenesis, Transfection

    G182R protein expression is significantly decreased in COS-1 cells. A : COS-1 cells were transiently transfected with water (Mock), WT-KCNA5, G182R, E211D, or G182R/E211D. Representative images are shown at ×40 magnification. B : transfected cells
    Figure Legend Snippet: G182R protein expression is significantly decreased in COS-1 cells. A : COS-1 cells were transiently transfected with water (Mock), WT-KCNA5, G182R, E211D, or G182R/E211D. Representative images are shown at ×40 magnification. B : transfected cells

    Techniques Used: Expressing, Transfection

    14) Product Images from "Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns"

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00464.2009

    Mutant KCNA5 is located in perinuclear packets and not on the cell surface of transfected HEK-293 cells and human (h)PASMC. A : HEK-293 cells transfected with WT KCNA5 ( a and c ) or G182R ( b and d ) were stained with anti-KCNA5 antibody (Ab-KCNA5, red) and
    Figure Legend Snippet: Mutant KCNA5 is located in perinuclear packets and not on the cell surface of transfected HEK-293 cells and human (h)PASMC. A : HEK-293 cells transfected with WT KCNA5 ( a and c ) or G182R ( b and d ) were stained with anti-KCNA5 antibody (Ab-KCNA5, red) and

    Techniques Used: Mutagenesis, Transfection, Staining

    G182R and E211D mutations cause incomplete processing of KCNA5 in HEK-293 cells. HEK-293 cells were transfected with WT KCNA5, G182R, E211D, or G182R/E211D and subjected to standard immunoblot procedures. A : representative immunoblot from cells transfected
    Figure Legend Snippet: G182R and E211D mutations cause incomplete processing of KCNA5 in HEK-293 cells. HEK-293 cells were transfected with WT KCNA5, G182R, E211D, or G182R/E211D and subjected to standard immunoblot procedures. A : representative immunoblot from cells transfected

    Techniques Used: Transfection

    Mutant KCNA5 forms functional homotetrameric channels. A : COS-1, HEK-293, and human pulmonary artery smooth muscle cells (PASMC) were transiently transfected with either empty vector [green fluorescent protein (GFP)] or WT KCNA5 (WT) as indicated. Whole
    Figure Legend Snippet: Mutant KCNA5 forms functional homotetrameric channels. A : COS-1, HEK-293, and human pulmonary artery smooth muscle cells (PASMC) were transiently transfected with either empty vector [green fluorescent protein (GFP)] or WT KCNA5 (WT) as indicated. Whole

    Techniques Used: Mutagenesis, Functional Assay, Transfection, Plasmid Preparation

    Mutations in KCNA5 at G182 and E211 do not affect the pharmacological effect of 4-aminopyridine (4-AP). A : a standard I-V pulse protocol was delivered to HEK-293 cells transiently transfected with the indicated vector [WT KCNA5 ( a ), G182R ( b ), E211D (
    Figure Legend Snippet: Mutations in KCNA5 at G182 and E211 do not affect the pharmacological effect of 4-aminopyridine (4-AP). A : a standard I-V pulse protocol was delivered to HEK-293 cells transiently transfected with the indicated vector [WT KCNA5 ( a ), G182R ( b ), E211D (

    Techniques Used: Transfection, Plasmid Preparation

    Decreased G182R expression in COS-1 cells cannot be rescued by overexpression of K V β subunits. A , a : HEK-293 cells were transfected with WT KCNA5 or K V β1.3-HA alone or cotransfected with WT KCNA5, G182R, E211D, or G182R/E211D and K V β1.3-HA.
    Figure Legend Snippet: Decreased G182R expression in COS-1 cells cannot be rescued by overexpression of K V β subunits. A , a : HEK-293 cells were transfected with WT KCNA5 or K V β1.3-HA alone or cotransfected with WT KCNA5, G182R, E211D, or G182R/E211D and K V β1.3-HA.

    Techniques Used: Expressing, Over Expression, Transfection

    Two nonsynonymous mutations identified in the KCNA5 gene from idiopathic pulmonary arterial hypertension (IPAH) patients localize to the NH 2 -terminal tetramerization domain (T1 domain). A , left : schematic diagram of voltage-gated K + (K V ) channel subunit
    Figure Legend Snippet: Two nonsynonymous mutations identified in the KCNA5 gene from idiopathic pulmonary arterial hypertension (IPAH) patients localize to the NH 2 -terminal tetramerization domain (T1 domain). A , left : schematic diagram of voltage-gated K + (K V ) channel subunit

    Techniques Used:

    Cotransfection of K V β subunits affects KCNA5 channel kinetics. HEK-293 cells were transfected with WT KCNA5 alone (KCNA5) or in the presence of K V β1.3-hemagglutinin (HA) (KCNA5/K V β1.3). A and B : representative current recordings
    Figure Legend Snippet: Cotransfection of K V β subunits affects KCNA5 channel kinetics. HEK-293 cells were transfected with WT KCNA5 alone (KCNA5) or in the presence of K V β1.3-hemagglutinin (HA) (KCNA5/K V β1.3). A and B : representative current recordings

    Techniques Used: Cotransfection, Transfection

    Voltage-dependent inactivation is accelerated in the G182R mutant KCNA5 channel. A standard 2-pulse inactivation protocol was used to determine channel availability after a 10-s prepulse in HEK-293 cells transiently transfected with WT KCNA5, G182R, E211D,
    Figure Legend Snippet: Voltage-dependent inactivation is accelerated in the G182R mutant KCNA5 channel. A standard 2-pulse inactivation protocol was used to determine channel availability after a 10-s prepulse in HEK-293 cells transiently transfected with WT KCNA5, G182R, E211D,

    Techniques Used: Mutagenesis, Transfection

    G182R protein expression is significantly decreased in COS-1 cells. A : COS-1 cells were transiently transfected with water (Mock), WT-KCNA5, G182R, E211D, or G182R/E211D. Representative images are shown at ×40 magnification. B : transfected cells
    Figure Legend Snippet: G182R protein expression is significantly decreased in COS-1 cells. A : COS-1 cells were transiently transfected with water (Mock), WT-KCNA5, G182R, E211D, or G182R/E211D. Representative images are shown at ×40 magnification. B : transfected cells

    Techniques Used: Expressing, Transfection

    15) Product Images from "Potassium Channels Kv1.3 and Kir2.1 But Not Kv1.5 Contribute to BV2 Cell Line and Primary Microglial Migration"

    Article Title: Potassium Channels Kv1.3 and Kir2.1 But Not Kv1.5 Contribute to BV2 Cell Line and Primary Microglial Migration

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms22042081

    Immunolabeling of potassium channels in cultured BV2 microglial cells. The cells were stained with antibodies targeting Kv1.3 ( A ), Kv1.5 ( B ), Kir2.1 ( C ) and the negative control with Alexa 568 ( D ). The coverslips were mounted using the Prolong antifade with DAPI in blue. The channel was pseudo-colored in green for improved visualization. The images are representative of three independent experiments. Scale bar: 40 µm.
    Figure Legend Snippet: Immunolabeling of potassium channels in cultured BV2 microglial cells. The cells were stained with antibodies targeting Kv1.3 ( A ), Kv1.5 ( B ), Kir2.1 ( C ) and the negative control with Alexa 568 ( D ). The coverslips were mounted using the Prolong antifade with DAPI in blue. The channel was pseudo-colored in green for improved visualization. The images are representative of three independent experiments. Scale bar: 40 µm.

    Techniques Used: Immunolabeling, Cell Culture, Staining, Negative Control

    The contribution of potassium channels in BV2 microglial migration. The representative images show the robust and repetitive scratch made with the 200 µL sterile pipette tip at t0h ( A ) and the cell migration in control conditions ( E ) and after the inhibitor at t24h ( F – H ). The histograms show that BV2 microglial cells migrate less after the inhibition of Kv1.3 and Kir2.1 ( B , D ), whereas blocking Kv1.5 has no effect on cellular migration ( C ). Scale bar: 100 µm. All the statistical analysis is represented as Mean ± SD, ***: p
    Figure Legend Snippet: The contribution of potassium channels in BV2 microglial migration. The representative images show the robust and repetitive scratch made with the 200 µL sterile pipette tip at t0h ( A ) and the cell migration in control conditions ( E ) and after the inhibitor at t24h ( F – H ). The histograms show that BV2 microglial cells migrate less after the inhibition of Kv1.3 and Kir2.1 ( B , D ), whereas blocking Kv1.5 has no effect on cellular migration ( C ). Scale bar: 100 µm. All the statistical analysis is represented as Mean ± SD, ***: p

    Techniques Used: Migration, Transferring, Inhibition, Blocking Assay

    Electrophysiological properties of BV2 cells. For all Kv1.3, Kv1.5 and Kir2.1 potassium channels, the electrophysiological characteristics are represented by the intensity/voltage (I/V) curves extracted from the step recordings, representing the total current elicited by a voltage protocol starting from −120 mV, in 10 mV increments, to +40 mV ( A – C ), in control conditions and after each specific inhibitor. The inhibition effect of the of each blocker can be seen from the I/V curves. The insets represent the comparison of the current amplitude elicited by a voltage step at −160 mV and +40 mV. All the data are represented as Mean ± SD ( n = 3 independent experiments).
    Figure Legend Snippet: Electrophysiological properties of BV2 cells. For all Kv1.3, Kv1.5 and Kir2.1 potassium channels, the electrophysiological characteristics are represented by the intensity/voltage (I/V) curves extracted from the step recordings, representing the total current elicited by a voltage protocol starting from −120 mV, in 10 mV increments, to +40 mV ( A – C ), in control conditions and after each specific inhibitor. The inhibition effect of the of each blocker can be seen from the I/V curves. The insets represent the comparison of the current amplitude elicited by a voltage step at −160 mV and +40 mV. All the data are represented as Mean ± SD ( n = 3 independent experiments).

    Techniques Used: Inhibition

    The migration of primary microglial cells through inserts with 8 µm pores. ( A ) The migration rate of primary microglial cells after the spared nerve injury (SNI) surgery is reduced compared with sham conditions. Histograms showing the contribution of each potassium channel, Kv1.3, Kv1.5 and Kir2.1, to microglial migration, in both sham ( B – D ) and SNI conditions ( E – G ). All the statistical analysis is represented as Mean ± SD, *: p
    Figure Legend Snippet: The migration of primary microglial cells through inserts with 8 µm pores. ( A ) The migration rate of primary microglial cells after the spared nerve injury (SNI) surgery is reduced compared with sham conditions. Histograms showing the contribution of each potassium channel, Kv1.3, Kv1.5 and Kir2.1, to microglial migration, in both sham ( B – D ) and SNI conditions ( E – G ). All the statistical analysis is represented as Mean ± SD, *: p

    Techniques Used: Migration

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    Alomone Labs anti kv1 5
    Characterization of the Kv1.3 and <t>Kv1.5</t> mutant channels containing the YS segment. A , average normalized activation and inactivation curves are shown as conductance-voltage relationships for Kv1.3, Kv1.5, the truncated Kv1.3-YS channel, and the chimeras Kv1.5-YS 532 and Kv1.5-YS 613 . All datasets were fitted to Boltzmann functions. Each data point is the mean ± S.E. of 6–11 cells. B , confocal images of non-permeabilized cells transfected with Kv1.3-YS-Cherry, Kv1.5-YS 532 -EGFP, and Kv1.5-YS 613 -EGFP. An extracellular anti-Kv1.3 antibody was used to label Kv1.3-YS ( green ), whereas the extracellular anti-Kv1.5 antibody was used for Kv1.5-YS 532 and Kv1.5-YS 613 chimeras ( red ). Nuclei were stained by Hoechst ( blue ). C , proliferation rate of the indicated channels or GFP-transfected cells (control) was determined by measuring EdU incorporation. Significant differences when comparing to Kv1.3 (*) or to control (#) are indicated. Statistical analysis was performed with one-way ANOVA followed by a Tukey's HSD multiple comparison. Each bar is the average of 9–15 determinations from 5 different assays. D , the average peak current amplitude obtained in cell-attached experiments for Kv1.5 channels and all the Kv1.5 chimeras was plotted against the % of the channels expressed at the plasma membrane ( upper graph ) or their normalized effect on proliferation (taking 100% as the proliferation rate of GFP-transfected HEK cells, lower graph ). The correlation between expression and current was fit to a linear regression curve ( y = 18.54 + 0.0066x, R 2 = 0.85, p = 0.008), but there was no correlation between proliferation and current amplitude ( R 2 = 0.23, p = 0.19).
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    Characterization of the Kv1.3 and Kv1.5 mutant channels containing the YS segment. A , average normalized activation and inactivation curves are shown as conductance-voltage relationships for Kv1.3, Kv1.5, the truncated Kv1.3-YS channel, and the chimeras Kv1.5-YS 532 and Kv1.5-YS 613 . All datasets were fitted to Boltzmann functions. Each data point is the mean ± S.E. of 6–11 cells. B , confocal images of non-permeabilized cells transfected with Kv1.3-YS-Cherry, Kv1.5-YS 532 -EGFP, and Kv1.5-YS 613 -EGFP. An extracellular anti-Kv1.3 antibody was used to label Kv1.3-YS ( green ), whereas the extracellular anti-Kv1.5 antibody was used for Kv1.5-YS 532 and Kv1.5-YS 613 chimeras ( red ). Nuclei were stained by Hoechst ( blue ). C , proliferation rate of the indicated channels or GFP-transfected cells (control) was determined by measuring EdU incorporation. Significant differences when comparing to Kv1.3 (*) or to control (#) are indicated. Statistical analysis was performed with one-way ANOVA followed by a Tukey's HSD multiple comparison. Each bar is the average of 9–15 determinations from 5 different assays. D , the average peak current amplitude obtained in cell-attached experiments for Kv1.5 channels and all the Kv1.5 chimeras was plotted against the % of the channels expressed at the plasma membrane ( upper graph ) or their normalized effect on proliferation (taking 100% as the proliferation rate of GFP-transfected HEK cells, lower graph ). The correlation between expression and current was fit to a linear regression curve ( y = 18.54 + 0.0066x, R 2 = 0.85, p = 0.008), but there was no correlation between proliferation and current amplitude ( R 2 = 0.23, p = 0.19).

    Journal: The Journal of Biological Chemistry

    Article Title: Molecular Determinants of Kv1.3 Potassium Channels-induced Proliferation *

    doi: 10.1074/jbc.M115.678995

    Figure Lengend Snippet: Characterization of the Kv1.3 and Kv1.5 mutant channels containing the YS segment. A , average normalized activation and inactivation curves are shown as conductance-voltage relationships for Kv1.3, Kv1.5, the truncated Kv1.3-YS channel, and the chimeras Kv1.5-YS 532 and Kv1.5-YS 613 . All datasets were fitted to Boltzmann functions. Each data point is the mean ± S.E. of 6–11 cells. B , confocal images of non-permeabilized cells transfected with Kv1.3-YS-Cherry, Kv1.5-YS 532 -EGFP, and Kv1.5-YS 613 -EGFP. An extracellular anti-Kv1.3 antibody was used to label Kv1.3-YS ( green ), whereas the extracellular anti-Kv1.5 antibody was used for Kv1.5-YS 532 and Kv1.5-YS 613 chimeras ( red ). Nuclei were stained by Hoechst ( blue ). C , proliferation rate of the indicated channels or GFP-transfected cells (control) was determined by measuring EdU incorporation. Significant differences when comparing to Kv1.3 (*) or to control (#) are indicated. Statistical analysis was performed with one-way ANOVA followed by a Tukey's HSD multiple comparison. Each bar is the average of 9–15 determinations from 5 different assays. D , the average peak current amplitude obtained in cell-attached experiments for Kv1.5 channels and all the Kv1.5 chimeras was plotted against the % of the channels expressed at the plasma membrane ( upper graph ) or their normalized effect on proliferation (taking 100% as the proliferation rate of GFP-transfected HEK cells, lower graph ). The correlation between expression and current was fit to a linear regression curve ( y = 18.54 + 0.0066x, R 2 = 0.85, p = 0.008), but there was no correlation between proliferation and current amplitude ( R 2 = 0.23, p = 0.19).

    Article Snippet: Non-permeabilized cells were incubated with anti-Kv1.3 or anti Kv1.5 extracellular primary antibodies (APC101 or APC150, Alomone Labs), whereas permeabilized cells were incubated with anti-Kv1.3 COOH (75-009, NeuroMab) or anti-Kv1.5 COOH (APC004, Alomone Labs), all at a final concentration of 1:50.

    Techniques: Mutagenesis, Activation Assay, Transfection, Staining, Expressing

    Mutant KCNA5 is located in perinuclear packets and not on the cell surface of transfected HEK-293 cells and human (h)PASMC. A : HEK-293 cells transfected with WT KCNA5 ( a and c ) or G182R ( b and d ) were stained with anti-KCNA5 antibody (Ab-KCNA5, red) and

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    doi: 10.1152/ajpcell.00464.2009

    Figure Lengend Snippet: Mutant KCNA5 is located in perinuclear packets and not on the cell surface of transfected HEK-293 cells and human (h)PASMC. A : HEK-293 cells transfected with WT KCNA5 ( a and c ) or G182R ( b and d ) were stained with anti-KCNA5 antibody (Ab-KCNA5, red) and

    Article Snippet: After cells were fixed in 4% paraformaldehyde-PBS for 15 min at room temperature, coverslips were incubated in blocking solution (2% BSA, 2% FBS, 0.1% Triton X-100 in PBS) for 1 h. Coverslips were then exposed to rabbit anti-KV1.5 antibody (Alomone Labs) at a dilution of 1:100 in blocking solution for 2 h at room temperature.

    Techniques: Mutagenesis, Transfection, Staining

    G182R and E211D mutations cause incomplete processing of KCNA5 in HEK-293 cells. HEK-293 cells were transfected with WT KCNA5, G182R, E211D, or G182R/E211D and subjected to standard immunoblot procedures. A : representative immunoblot from cells transfected

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    doi: 10.1152/ajpcell.00464.2009

    Figure Lengend Snippet: G182R and E211D mutations cause incomplete processing of KCNA5 in HEK-293 cells. HEK-293 cells were transfected with WT KCNA5, G182R, E211D, or G182R/E211D and subjected to standard immunoblot procedures. A : representative immunoblot from cells transfected

    Article Snippet: After cells were fixed in 4% paraformaldehyde-PBS for 15 min at room temperature, coverslips were incubated in blocking solution (2% BSA, 2% FBS, 0.1% Triton X-100 in PBS) for 1 h. Coverslips were then exposed to rabbit anti-KV1.5 antibody (Alomone Labs) at a dilution of 1:100 in blocking solution for 2 h at room temperature.

    Techniques: Transfection

    Mutant KCNA5 forms functional homotetrameric channels. A : COS-1, HEK-293, and human pulmonary artery smooth muscle cells (PASMC) were transiently transfected with either empty vector [green fluorescent protein (GFP)] or WT KCNA5 (WT) as indicated. Whole

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    doi: 10.1152/ajpcell.00464.2009

    Figure Lengend Snippet: Mutant KCNA5 forms functional homotetrameric channels. A : COS-1, HEK-293, and human pulmonary artery smooth muscle cells (PASMC) were transiently transfected with either empty vector [green fluorescent protein (GFP)] or WT KCNA5 (WT) as indicated. Whole

    Article Snippet: After cells were fixed in 4% paraformaldehyde-PBS for 15 min at room temperature, coverslips were incubated in blocking solution (2% BSA, 2% FBS, 0.1% Triton X-100 in PBS) for 1 h. Coverslips were then exposed to rabbit anti-KV1.5 antibody (Alomone Labs) at a dilution of 1:100 in blocking solution for 2 h at room temperature.

    Techniques: Mutagenesis, Functional Assay, Transfection, Plasmid Preparation

    Mutations in KCNA5 at G182 and E211 do not affect the pharmacological effect of 4-aminopyridine (4-AP). A : a standard I-V pulse protocol was delivered to HEK-293 cells transiently transfected with the indicated vector [WT KCNA5 ( a ), G182R ( b ), E211D (

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    doi: 10.1152/ajpcell.00464.2009

    Figure Lengend Snippet: Mutations in KCNA5 at G182 and E211 do not affect the pharmacological effect of 4-aminopyridine (4-AP). A : a standard I-V pulse protocol was delivered to HEK-293 cells transiently transfected with the indicated vector [WT KCNA5 ( a ), G182R ( b ), E211D (

    Article Snippet: After cells were fixed in 4% paraformaldehyde-PBS for 15 min at room temperature, coverslips were incubated in blocking solution (2% BSA, 2% FBS, 0.1% Triton X-100 in PBS) for 1 h. Coverslips were then exposed to rabbit anti-KV1.5 antibody (Alomone Labs) at a dilution of 1:100 in blocking solution for 2 h at room temperature.

    Techniques: Transfection, Plasmid Preparation

    Decreased G182R expression in COS-1 cells cannot be rescued by overexpression of K V β subunits. A , a : HEK-293 cells were transfected with WT KCNA5 or K V β1.3-HA alone or cotransfected with WT KCNA5, G182R, E211D, or G182R/E211D and K V β1.3-HA.

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    doi: 10.1152/ajpcell.00464.2009

    Figure Lengend Snippet: Decreased G182R expression in COS-1 cells cannot be rescued by overexpression of K V β subunits. A , a : HEK-293 cells were transfected with WT KCNA5 or K V β1.3-HA alone or cotransfected with WT KCNA5, G182R, E211D, or G182R/E211D and K V β1.3-HA.

    Article Snippet: After cells were fixed in 4% paraformaldehyde-PBS for 15 min at room temperature, coverslips were incubated in blocking solution (2% BSA, 2% FBS, 0.1% Triton X-100 in PBS) for 1 h. Coverslips were then exposed to rabbit anti-KV1.5 antibody (Alomone Labs) at a dilution of 1:100 in blocking solution for 2 h at room temperature.

    Techniques: Expressing, Over Expression, Transfection

    Two nonsynonymous mutations identified in the KCNA5 gene from idiopathic pulmonary arterial hypertension (IPAH) patients localize to the NH 2 -terminal tetramerization domain (T1 domain). A , left : schematic diagram of voltage-gated K + (K V ) channel subunit

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    doi: 10.1152/ajpcell.00464.2009

    Figure Lengend Snippet: Two nonsynonymous mutations identified in the KCNA5 gene from idiopathic pulmonary arterial hypertension (IPAH) patients localize to the NH 2 -terminal tetramerization domain (T1 domain). A , left : schematic diagram of voltage-gated K + (K V ) channel subunit

    Article Snippet: After cells were fixed in 4% paraformaldehyde-PBS for 15 min at room temperature, coverslips were incubated in blocking solution (2% BSA, 2% FBS, 0.1% Triton X-100 in PBS) for 1 h. Coverslips were then exposed to rabbit anti-KV1.5 antibody (Alomone Labs) at a dilution of 1:100 in blocking solution for 2 h at room temperature.

    Techniques:

    Cotransfection of K V β subunits affects KCNA5 channel kinetics. HEK-293 cells were transfected with WT KCNA5 alone (KCNA5) or in the presence of K V β1.3-hemagglutinin (HA) (KCNA5/K V β1.3). A and B : representative current recordings

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    doi: 10.1152/ajpcell.00464.2009

    Figure Lengend Snippet: Cotransfection of K V β subunits affects KCNA5 channel kinetics. HEK-293 cells were transfected with WT KCNA5 alone (KCNA5) or in the presence of K V β1.3-hemagglutinin (HA) (KCNA5/K V β1.3). A and B : representative current recordings

    Article Snippet: After cells were fixed in 4% paraformaldehyde-PBS for 15 min at room temperature, coverslips were incubated in blocking solution (2% BSA, 2% FBS, 0.1% Triton X-100 in PBS) for 1 h. Coverslips were then exposed to rabbit anti-KV1.5 antibody (Alomone Labs) at a dilution of 1:100 in blocking solution for 2 h at room temperature.

    Techniques: Cotransfection, Transfection

    Voltage-dependent inactivation is accelerated in the G182R mutant KCNA5 channel. A standard 2-pulse inactivation protocol was used to determine channel availability after a 10-s prepulse in HEK-293 cells transiently transfected with WT KCNA5, G182R, E211D,

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    doi: 10.1152/ajpcell.00464.2009

    Figure Lengend Snippet: Voltage-dependent inactivation is accelerated in the G182R mutant KCNA5 channel. A standard 2-pulse inactivation protocol was used to determine channel availability after a 10-s prepulse in HEK-293 cells transiently transfected with WT KCNA5, G182R, E211D,

    Article Snippet: After cells were fixed in 4% paraformaldehyde-PBS for 15 min at room temperature, coverslips were incubated in blocking solution (2% BSA, 2% FBS, 0.1% Triton X-100 in PBS) for 1 h. Coverslips were then exposed to rabbit anti-KV1.5 antibody (Alomone Labs) at a dilution of 1:100 in blocking solution for 2 h at room temperature.

    Techniques: Mutagenesis, Transfection

    G182R protein expression is significantly decreased in COS-1 cells. A : COS-1 cells were transiently transfected with water (Mock), WT-KCNA5, G182R, E211D, or G182R/E211D. Representative images are shown at ×40 magnification. B : transfected cells

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns

    doi: 10.1152/ajpcell.00464.2009

    Figure Lengend Snippet: G182R protein expression is significantly decreased in COS-1 cells. A : COS-1 cells were transiently transfected with water (Mock), WT-KCNA5, G182R, E211D, or G182R/E211D. Representative images are shown at ×40 magnification. B : transfected cells

    Article Snippet: After cells were fixed in 4% paraformaldehyde-PBS for 15 min at room temperature, coverslips were incubated in blocking solution (2% BSA, 2% FBS, 0.1% Triton X-100 in PBS) for 1 h. Coverslips were then exposed to rabbit anti-KV1.5 antibody (Alomone Labs) at a dilution of 1:100 in blocking solution for 2 h at room temperature.

    Techniques: Expressing, Transfection

    Kv3.4 in the axonal growth cones of dorsal spinal commissural neurons. A–F , Transverse sections of the spinal cord of chick embryos were immunostained for Kv3.4. A , Absence of Kv3.4-IR in the dorsal spinal cord at HH17. Kv3.4-IR in precrossing commissural axons ( B–F , arrowheads) is evident during HH19-HH25 but disappears at HH27. D , Arrows indicate postcrossing commissural axons projecting from the other side of spinal cord. FP, Floor plate. G–L , Transverse sections of the spinal cord at HH23 were immunostained as indicated. G , Absence of Kv1.5-IR. H , Kv4.2-IR in the somata and dendrites of motoneurons (MN). I , Kv4.3-IR in the bifurcation zone (BZ). In addition to the BZ, Kv3.1b-IR is strong in postcrossing commissural axons ( J , arrow) but weak in precrossing commissural axons ( J , arrowhead). K , Absence of Kv3.2-IR. L , Kv3.3 in motoneurons. M–M″ , Double staining in transverse sections of the spinal cord at HH21 shows colocalization of Kv3.4 and axonin-1 in the growth cones (arrowheads) of commissural axons. N–N″ , Colocalization of Kv3.4 and axonin-1 in cultured dorsal spinal neurons isolated from HH21-HH23 chick embryos. O–P″ , Red fluorescence-tagged phalloidin colabeling reveals enrichment of Kv3.4 in the growth cone ( O–O″ ) and Kv3.1b in the soma/axon shaft ( P–P″ ) of cultured dorsal spinal neurons. Q–Q″ , Kv3.4 and DiI colabeling. White represents Kv3.4-abundant regions. Blue represents Kv3.4-sparse regions ( Q″ ). R , Ratio of Kv3.4/DiI in the soma, axon shaft, or growth cone of each neuron was obtained by dividing the fluorescence intensity of Kv3.4 by that of DiI. Data are mean ± SEM ( n = 8 neurons, pooled from three independent experiments done on different days). *** p

    Journal: The Journal of Neuroscience

    Article Title: K+ Channel Kv3.4 Is Essential for Axon Growth by Limiting the Influx of Ca2+ into Growth Cones

    doi: 10.1523/JNEUROSCI.1076-16.2017

    Figure Lengend Snippet: Kv3.4 in the axonal growth cones of dorsal spinal commissural neurons. A–F , Transverse sections of the spinal cord of chick embryos were immunostained for Kv3.4. A , Absence of Kv3.4-IR in the dorsal spinal cord at HH17. Kv3.4-IR in precrossing commissural axons ( B–F , arrowheads) is evident during HH19-HH25 but disappears at HH27. D , Arrows indicate postcrossing commissural axons projecting from the other side of spinal cord. FP, Floor plate. G–L , Transverse sections of the spinal cord at HH23 were immunostained as indicated. G , Absence of Kv1.5-IR. H , Kv4.2-IR in the somata and dendrites of motoneurons (MN). I , Kv4.3-IR in the bifurcation zone (BZ). In addition to the BZ, Kv3.1b-IR is strong in postcrossing commissural axons ( J , arrow) but weak in precrossing commissural axons ( J , arrowhead). K , Absence of Kv3.2-IR. L , Kv3.3 in motoneurons. M–M″ , Double staining in transverse sections of the spinal cord at HH21 shows colocalization of Kv3.4 and axonin-1 in the growth cones (arrowheads) of commissural axons. N–N″ , Colocalization of Kv3.4 and axonin-1 in cultured dorsal spinal neurons isolated from HH21-HH23 chick embryos. O–P″ , Red fluorescence-tagged phalloidin colabeling reveals enrichment of Kv3.4 in the growth cone ( O–O″ ) and Kv3.1b in the soma/axon shaft ( P–P″ ) of cultured dorsal spinal neurons. Q–Q″ , Kv3.4 and DiI colabeling. White represents Kv3.4-abundant regions. Blue represents Kv3.4-sparse regions ( Q″ ). R , Ratio of Kv3.4/DiI in the soma, axon shaft, or growth cone of each neuron was obtained by dividing the fluorescence intensity of Kv3.4 by that of DiI. Data are mean ± SEM ( n = 8 neurons, pooled from three independent experiments done on different days). *** p

    Article Snippet: After wash in low-salt Tris-buffered saline (LTBS; 25 m m Tris, 0.85% NaCl, pH 7.5) and then LTBS containing 0.1% Triton X-100 (LTBST), sections on slides were treated with 0.2% hydrogen peroxide in LTBS for 30 min. Nonspecific binding was blocked by 3% normal donkey serum and 2% BSA in LTBST for 1.5 h. Primary antibodies included rabbit anti-Kv1.5 (1:100), rabbit anti-Kv3.1b (1:100), rabbit anti-Kv3.2 (1:100), rabbit anti-Kv3.3 (1:100), rabbit anti-Kv3.4 (1:100), rabbit anti-Kv4.2 (1:250), and rabbit anti-Kv4.3 (1:1500).

    Techniques: Double Staining, Cell Culture, Isolation, Fluorescence

    Some Kv1.5 channel subunits are localized in lipid raft fractions in adult rat atrial myocytes Western blot analysis of the distribution of Kv1.5 subunits, connexin-43 and caveolin-3 on step sucrose gradient of proteins from atrial myocardium.

    Journal: The Journal of Physiology

    Article Title: Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes

    doi: 10.1113/jphysiol.2007.134809

    Figure Lengend Snippet: Some Kv1.5 channel subunits are localized in lipid raft fractions in adult rat atrial myocytes Western blot analysis of the distribution of Kv1.5 subunits, connexin-43 and caveolin-3 on step sucrose gradient of proteins from atrial myocardium.

    Article Snippet: Then slides were incubated with rabbit anti-Kv1.5 polyclonal antibodies (pAbs) (1: 20), with mouse anti-caveolin-3 monoclonal antibodies (mAbs) (1: 50), with a mixture of mouse anti-caveolin-3 and rabbit anti-connexin-43 (1: 50) antibodies, or with a mixture of mouse anti-α-actinin sarcomeric and rabbit anti-Kv1.5 antibodies for 1 h at RT.

    Techniques: Western Blot

    Kv1.5 do not co-localized with caveolin-3 in adult atrial tissue Immunolocalization of Kv1.5 subunits ( A ) and caveolin-3 ( B ) in cryosections of atrial myocardium. Double immunostaining of connexin-43 (FITC, C ) and caveolin-3 (Texas Red, D ) in cryosections of atrial myocardium. E , merged image of the same area of the section in C and D , showing the lack of overlap between connexin-43 and caveolin-3 stainings.

    Journal: The Journal of Physiology

    Article Title: Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes

    doi: 10.1113/jphysiol.2007.134809

    Figure Lengend Snippet: Kv1.5 do not co-localized with caveolin-3 in adult atrial tissue Immunolocalization of Kv1.5 subunits ( A ) and caveolin-3 ( B ) in cryosections of atrial myocardium. Double immunostaining of connexin-43 (FITC, C ) and caveolin-3 (Texas Red, D ) in cryosections of atrial myocardium. E , merged image of the same area of the section in C and D , showing the lack of overlap between connexin-43 and caveolin-3 stainings.

    Article Snippet: Then slides were incubated with rabbit anti-Kv1.5 polyclonal antibodies (pAbs) (1: 20), with mouse anti-caveolin-3 monoclonal antibodies (mAbs) (1: 50), with a mixture of mouse anti-caveolin-3 and rabbit anti-connexin-43 (1: 50) antibodies, or with a mixture of mouse anti-α-actinin sarcomeric and rabbit anti-Kv1.5 antibodies for 1 h at RT.

    Techniques: Double Immunostaining

    Surface expression of Kv1.5 subunits in neonatal cardiomyocytes A , in live cardiomyocytes, transfected GFP-tagged Kv1.5 subunits are clustered at the membrane surface adjacent to the bottom of laminin-coated glass support, as shown in the projection of Z sections in the lower panel. In contrast, GFP alone was homogeneously distributed in cardiomyocytes (inset). B , after the application of 2% MCD, clusters increased in size and were redistributed throughout the plasma membrane. C , bar graphs summarizing changes in cluster size upon MCD exposures; data are from 21 cardiomyocytes in control, and following incubation with 2% MCD for 7 min and 1 h 30 min. ** P

    Journal: The Journal of Physiology

    Article Title: Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes

    doi: 10.1113/jphysiol.2007.134809

    Figure Lengend Snippet: Surface expression of Kv1.5 subunits in neonatal cardiomyocytes A , in live cardiomyocytes, transfected GFP-tagged Kv1.5 subunits are clustered at the membrane surface adjacent to the bottom of laminin-coated glass support, as shown in the projection of Z sections in the lower panel. In contrast, GFP alone was homogeneously distributed in cardiomyocytes (inset). B , after the application of 2% MCD, clusters increased in size and were redistributed throughout the plasma membrane. C , bar graphs summarizing changes in cluster size upon MCD exposures; data are from 21 cardiomyocytes in control, and following incubation with 2% MCD for 7 min and 1 h 30 min. ** P

    Article Snippet: Then slides were incubated with rabbit anti-Kv1.5 polyclonal antibodies (pAbs) (1: 20), with mouse anti-caveolin-3 monoclonal antibodies (mAbs) (1: 50), with a mixture of mouse anti-caveolin-3 and rabbit anti-connexin-43 (1: 50) antibodies, or with a mixture of mouse anti-α-actinin sarcomeric and rabbit anti-Kv1.5 antibodies for 1 h at RT.

    Techniques: Expressing, Transfection, Incubation

    Effect of cholesterol depletion on outward current parameters resulting from Kv1.5 subunit overexpression in neonatal cardiomyocytes Current density–voltage relationships ( A ) and voltage dependence ( B ) of I Kur activation under control conditions (•) and following 7 min MCD application (^). In A and B , each point represents average data from 5 cells.

    Journal: The Journal of Physiology

    Article Title: Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes

    doi: 10.1113/jphysiol.2007.134809

    Figure Lengend Snippet: Effect of cholesterol depletion on outward current parameters resulting from Kv1.5 subunit overexpression in neonatal cardiomyocytes Current density–voltage relationships ( A ) and voltage dependence ( B ) of I Kur activation under control conditions (•) and following 7 min MCD application (^). In A and B , each point represents average data from 5 cells.

    Article Snippet: Then slides were incubated with rabbit anti-Kv1.5 polyclonal antibodies (pAbs) (1: 20), with mouse anti-caveolin-3 monoclonal antibodies (mAbs) (1: 50), with a mixture of mouse anti-caveolin-3 and rabbit anti-connexin-43 (1: 50) antibodies, or with a mixture of mouse anti-α-actinin sarcomeric and rabbit anti-Kv1.5 antibodies for 1 h at RT.

    Techniques: Over Expression, Activation Assay