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anti nav1 5 scn5a antibody  (Alomone Labs)


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    Alomone Labs anti nav1 5 scn5a antibody
    Functional screen for cardiac ion channels modulated by POPDC2 (A–D) Representative current traces of (A) HCN4, applying a voltage step from −30 mV to −120 mV within 6 s, from a holding potential of −30 mV, (B) Kv1.4, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV, (C) Kv4.3, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV or (D) <t>Nav1.5,</t> applying a voltage step from −80 mV to −20 mV within 50 ms, from a holding potential of −80 mV, expressed alone ( black ) or together with POPDC2 ( blue ) in Xenopus laevis oocytes. (E) Indicated cardiac channels or the Na + /K + ATPase (Na/K) were expressed alone or together with POPDC2 in Xenopus oocytes and relative changes in current amplitudes by POPDC2 were plotted. Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001.
    Anti Nav1 5 Scn5a Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/asc-045/Anti-NaV1%2E5+(SCN5A)+(extracellular)+Antibody/pmc11059135-288-0-4
    Average 92 stars, based on 9 article reviews
    anti nav1 5 scn5a antibody - by Bioz Stars, 2026-11
    92/100 stars

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    1) Product Images from "Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5"

    Article Title: Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5

    Journal: iScience

    doi: 10.1016/j.isci.2024.109696

    Functional screen for cardiac ion channels modulated by POPDC2 (A–D) Representative current traces of (A) HCN4, applying a voltage step from −30 mV to −120 mV within 6 s, from a holding potential of −30 mV, (B) Kv1.4, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV, (C) Kv4.3, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV or (D) Nav1.5, applying a voltage step from −80 mV to −20 mV within 50 ms, from a holding potential of −80 mV, expressed alone ( black ) or together with POPDC2 ( blue ) in Xenopus laevis oocytes. (E) Indicated cardiac channels or the Na + /K + ATPase (Na/K) were expressed alone or together with POPDC2 in Xenopus oocytes and relative changes in current amplitudes by POPDC2 were plotted. Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001.
    Figure Legend Snippet: Functional screen for cardiac ion channels modulated by POPDC2 (A–D) Representative current traces of (A) HCN4, applying a voltage step from −30 mV to −120 mV within 6 s, from a holding potential of −30 mV, (B) Kv1.4, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV, (C) Kv4.3, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV or (D) Nav1.5, applying a voltage step from −80 mV to −20 mV within 50 ms, from a holding potential of −80 mV, expressed alone ( black ) or together with POPDC2 ( blue ) in Xenopus laevis oocytes. (E) Indicated cardiac channels or the Na + /K + ATPase (Na/K) were expressed alone or together with POPDC2 in Xenopus oocytes and relative changes in current amplitudes by POPDC2 were plotted. Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001.

    Techniques Used: Functional Assay, Patch Clamp

    Interaction of POPDC proteins with the cardiac sodium channel Nav1.5 or the skeletal muscle sodium channel Nav1.4 (A) Co-immunoprecipitation of POPDC2-FLAG with Nav1.5-HA was performed in COS-7 cells using anti-HA antibodies. An empty vector served as control. The co-immunoprecipitation was subsequently detected with an anti-FLAG antibody (IB: α-Flag). (B) Co-immunoprecipitation of POPDC2 and Nav1.5 in murine heart lysates (mheart) using anti Nav1.5 antibodies (IP: α-Nav1.5). The immunoprecipitation was subsequently detected with an anti-Nav1.5 (IB: α-Nav1.5) and the co-immunoprecipitation by an anti-POPDC2 antibody (IB: α-POPDC2). HeLa cells were used as a control. (C) Oocytes were injected with cRNA for human Nav1.5 or co-injected with different murine POPDC isoforms and subsequently stored in a storage solution lacking theophylline. Currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −80 mV) and voltage-steps of 50 ms ranging from −70 to +80 mV in 10 mV increments (see inset). (D and E) (D) Relative current amplitudes analyzed at −20 mV and normalized to Nav1.5. (E) Voltage-dependence of Nav1.5 activation in the absence or presence of POPDC1, POPDC2 or POPDC3. The respective voltages of half-maximal activation (V 1/2 ) and the Boltzmann constants (k) are provided as inset. The number of technical replicates (n) is indicated in parentheses or bar graphs. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001. (F and G) (F) POPDC2 does not modulate current amplitudes of Nav1.4, analyzed at −10 mV and normalized to Nav1.4 or (G) the shape of the voltage-dependence of Nav1.4 activation. The respective voltages of half-maximal activation (V 1/2 ) and the Boltzmann constants (k) are provided as inset. The number of technical replicates (n) is indicated in parentheses or bar graphs. Oocytes were stored in a storage solution lacking theophylline. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. See also <xref ref-type=Figures S1 and . " title="Interaction of POPDC proteins with the cardiac sodium channel Nav1.5 or the skeletal muscle sodium channel Nav1.4 ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Interaction of POPDC proteins with the cardiac sodium channel Nav1.5 or the skeletal muscle sodium channel Nav1.4 (A) Co-immunoprecipitation of POPDC2-FLAG with Nav1.5-HA was performed in COS-7 cells using anti-HA antibodies. An empty vector served as control. The co-immunoprecipitation was subsequently detected with an anti-FLAG antibody (IB: α-Flag). (B) Co-immunoprecipitation of POPDC2 and Nav1.5 in murine heart lysates (mheart) using anti Nav1.5 antibodies (IP: α-Nav1.5). The immunoprecipitation was subsequently detected with an anti-Nav1.5 (IB: α-Nav1.5) and the co-immunoprecipitation by an anti-POPDC2 antibody (IB: α-POPDC2). HeLa cells were used as a control. (C) Oocytes were injected with cRNA for human Nav1.5 or co-injected with different murine POPDC isoforms and subsequently stored in a storage solution lacking theophylline. Currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −80 mV) and voltage-steps of 50 ms ranging from −70 to +80 mV in 10 mV increments (see inset). (D and E) (D) Relative current amplitudes analyzed at −20 mV and normalized to Nav1.5. (E) Voltage-dependence of Nav1.5 activation in the absence or presence of POPDC1, POPDC2 or POPDC3. The respective voltages of half-maximal activation (V 1/2 ) and the Boltzmann constants (k) are provided as inset. The number of technical replicates (n) is indicated in parentheses or bar graphs. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001. (F and G) (F) POPDC2 does not modulate current amplitudes of Nav1.4, analyzed at −10 mV and normalized to Nav1.4 or (G) the shape of the voltage-dependence of Nav1.4 activation. The respective voltages of half-maximal activation (V 1/2 ) and the Boltzmann constants (k) are provided as inset. The number of technical replicates (n) is indicated in parentheses or bar graphs. Oocytes were stored in a storage solution lacking theophylline. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. See also Figures S1 and .

    Techniques Used: Co-Immunoprecipitation Assay, Plasmid Preparation, Control, Immunoprecipitation, Injection, Activation Assay, Patch Clamp

    POPDC2 does not alter the current kinetics of Nav1.5 (A) Current traces of human Nav1.5 expressed alone or co-expressed with human POPDC2. Representative traces are depicted at −30 mV, −20 mV and −10 mV. (B) Voltage-dependence of activation and inactivation curves fitted to a Boltzmann equation. The respective voltages of half-maximal activation (V 1/2 ) together with the Boltzmann constants (k), as well as the window currents, are provided as inset. For the V 1/2 of activation measurements, the currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −80 mV) and voltage-steps of 50 ms ranging from −70 to +80 mV in 10 mV increments (see inset activation protocol). For the V 1/2 of inactivation measurements, the currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −100 mV) and voltage-steps of 50 ms ranging from −120 to −10 mV in 10 mV increments with a final step to −30 mV for 50 ms (see inset inactivation protocol). The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. (C) Representative current traces of the kinetics of inactivation recorded with a single-step protocol from −100 mV to −30 mV for 65 ms (inset illustrates voltage protocol). (D) Representative recordings of the recovery from inactivation (inset illustrates voltage protocol). (E) Time-course of the recovery from inactivation recorded with a two-pulse protocol, first step to −10 mV for 50 ms and the second test pulse stepped to −10 mV with increasing interpulse intervals. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. (F) Time constants of the fast and slow component of the recovery from inactivation (lower panel) and the relative contribution of the fast and slow component (upper panel). Values were obtained by a bi-exponential fit from the data in (E). Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. See also <xref ref-type=Figure S3 . " title="POPDC2 does not alter the current kinetics of Nav1.5 (A) Current traces of human Nav1.5 expressed alone ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: POPDC2 does not alter the current kinetics of Nav1.5 (A) Current traces of human Nav1.5 expressed alone or co-expressed with human POPDC2. Representative traces are depicted at −30 mV, −20 mV and −10 mV. (B) Voltage-dependence of activation and inactivation curves fitted to a Boltzmann equation. The respective voltages of half-maximal activation (V 1/2 ) together with the Boltzmann constants (k), as well as the window currents, are provided as inset. For the V 1/2 of activation measurements, the currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −80 mV) and voltage-steps of 50 ms ranging from −70 to +80 mV in 10 mV increments (see inset activation protocol). For the V 1/2 of inactivation measurements, the currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −100 mV) and voltage-steps of 50 ms ranging from −120 to −10 mV in 10 mV increments with a final step to −30 mV for 50 ms (see inset inactivation protocol). The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. (C) Representative current traces of the kinetics of inactivation recorded with a single-step protocol from −100 mV to −30 mV for 65 ms (inset illustrates voltage protocol). (D) Representative recordings of the recovery from inactivation (inset illustrates voltage protocol). (E) Time-course of the recovery from inactivation recorded with a two-pulse protocol, first step to −10 mV for 50 ms and the second test pulse stepped to −10 mV with increasing interpulse intervals. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. (F) Time constants of the fast and slow component of the recovery from inactivation (lower panel) and the relative contribution of the fast and slow component (upper panel). Values were obtained by a bi-exponential fit from the data in (E). Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. See also Figure S3 .

    Techniques Used: Activation Assay, Inactivation, Patch Clamp

    POPDC2 reduces Nav1.5 current amplitudes in a cAMP-dependent manner (A) POPDC2 modulation of Nav1.5 is cAMP-dependent. Representative current traces recorded by voltage steps to −20 mV. Oocytes were injected with 10 ng Nav1.5 alone or 10 ng Nav1.5 together with 5 ng POPDC2 (50%) or 10 ng POPDC2 (100%), and stored in ND96 solution with or without theophylline before voltage-clamp measurements in oocytes. Inset illustrates the applied voltage protocol. (B) Analyses of peak current amplitudes from experiments performed in (A), analyzed at −20 mV and normalized to Nav1.5. The number of technical replicates (n) is indicated in bar graphs. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗, p < 0.05; ∗∗∗, p < 0.001. (C) Oocytes were injected as in (A-B) but incubated in a storage solution containing theophylline. Relative current amplitudes were analyzed at −20 mV and normalized to Nav1.5. The number of technical replicates is indicated in bar graphs. Data are presented as mean ± s.e.m. See also <xref ref-type=Figure S4 . " title="POPDC2 reduces Nav1.5 current amplitudes in a cAMP-dependent manner (A) ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: POPDC2 reduces Nav1.5 current amplitudes in a cAMP-dependent manner (A) POPDC2 modulation of Nav1.5 is cAMP-dependent. Representative current traces recorded by voltage steps to −20 mV. Oocytes were injected with 10 ng Nav1.5 alone or 10 ng Nav1.5 together with 5 ng POPDC2 (50%) or 10 ng POPDC2 (100%), and stored in ND96 solution with or without theophylline before voltage-clamp measurements in oocytes. Inset illustrates the applied voltage protocol. (B) Analyses of peak current amplitudes from experiments performed in (A), analyzed at −20 mV and normalized to Nav1.5. The number of technical replicates (n) is indicated in bar graphs. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗, p < 0.05; ∗∗∗, p < 0.001. (C) Oocytes were injected as in (A-B) but incubated in a storage solution containing theophylline. Relative current amplitudes were analyzed at −20 mV and normalized to Nav1.5. The number of technical replicates is indicated in bar graphs. Data are presented as mean ± s.e.m. See also Figure S4 .

    Techniques Used: Injection, Incubation, Patch Clamp

    POPDC2 co-localizes with Nav1.5 at the plasma membrane and intracellular compartments and regulates the surface expression of Nav1.5 in a cAMP-dependent manner (A and C) HeLa cells were transfected exclusively with Nav1.5-HA or (B and D) in combination with POPDC2-YFP. 24 h after transfection the cells were fixed, non-permeabilized (A-B) or permeabilized (C-D) and immunostained with anti HA antibody and Alexa 647 conjugated secondary antibody. The cells were then analyzed by confocal microscopy. Nuclear counterstaining with Hoechst 33342 is depicted in blue and nuclei of non-transfected cells are indicated by asterisk. Arrows point to either (A) Nav1.5- or (B) Nav1.5- plus POPDC2-YFP-stained membrane protrusions; PM, plasma membrane. Arrowheads in (D) depict Nav1.5-positive intracellular structures co-labelled by POPDC2-YFP, which are also designated by arrows in the single fluorescence images shown on the left. Scale bars, 10 μm. (E) Cartoon of the chemiluminescence-based ELISA-assay performed in HeLa cells transiently transfected with Nav1.5 HA to quantify the changes in Nav1.5 surface expression by co-transfection with POPDC2. In fixed cells, the primary antibody detects extracellularly HA-tagged Nav1.5 channels (Nav1.5 HA ) at the surface membrane while the peroxidase-enzyme (POD) which is linked to the secondary antibody catalyzes the oxidation of a luminol-substrate which is accompanied by the emission of light. Subsequently, the light emission can be quantified as relative light units (RLUs) as a measure of the surface expression of the channel. (F) Chemiluminescence assay of extracellularly HA-tagged Nav1.5 to determine the relative changes in surface expression by co-expressed POPDC2. The number of biological replicates (N) is indicated in the bar graphs. Data are expressed as relative light units (RLUs). Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗, p < 0.05. (G) Chemiluminescence assay of extracellularly HA-tagged Nav1.5 to determine the relative changes in surface expression by co-expressed POPDC2 in the presence of theophylline. The number of biological replicates (N) is indicated in the bar graphs. Data are expressed as relative light units (RLUs). Data are presented as mean ± s.e.m.
    Figure Legend Snippet: POPDC2 co-localizes with Nav1.5 at the plasma membrane and intracellular compartments and regulates the surface expression of Nav1.5 in a cAMP-dependent manner (A and C) HeLa cells were transfected exclusively with Nav1.5-HA or (B and D) in combination with POPDC2-YFP. 24 h after transfection the cells were fixed, non-permeabilized (A-B) or permeabilized (C-D) and immunostained with anti HA antibody and Alexa 647 conjugated secondary antibody. The cells were then analyzed by confocal microscopy. Nuclear counterstaining with Hoechst 33342 is depicted in blue and nuclei of non-transfected cells are indicated by asterisk. Arrows point to either (A) Nav1.5- or (B) Nav1.5- plus POPDC2-YFP-stained membrane protrusions; PM, plasma membrane. Arrowheads in (D) depict Nav1.5-positive intracellular structures co-labelled by POPDC2-YFP, which are also designated by arrows in the single fluorescence images shown on the left. Scale bars, 10 μm. (E) Cartoon of the chemiluminescence-based ELISA-assay performed in HeLa cells transiently transfected with Nav1.5 HA to quantify the changes in Nav1.5 surface expression by co-transfection with POPDC2. In fixed cells, the primary antibody detects extracellularly HA-tagged Nav1.5 channels (Nav1.5 HA ) at the surface membrane while the peroxidase-enzyme (POD) which is linked to the secondary antibody catalyzes the oxidation of a luminol-substrate which is accompanied by the emission of light. Subsequently, the light emission can be quantified as relative light units (RLUs) as a measure of the surface expression of the channel. (F) Chemiluminescence assay of extracellularly HA-tagged Nav1.5 to determine the relative changes in surface expression by co-expressed POPDC2. The number of biological replicates (N) is indicated in the bar graphs. Data are expressed as relative light units (RLUs). Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗, p < 0.05. (G) Chemiluminescence assay of extracellularly HA-tagged Nav1.5 to determine the relative changes in surface expression by co-expressed POPDC2 in the presence of theophylline. The number of biological replicates (N) is indicated in the bar graphs. Data are expressed as relative light units (RLUs). Data are presented as mean ± s.e.m.

    Techniques Used: Clinical Proteomics, Membrane, Expressing, Transfection, Confocal, Microscopy, Staining, Fluorescence, Enzyme-linked Immunosorbent Assay, Cotransfection, Chemiluminescence Immunoassay, Immunofluorescence


    Figure Legend Snippet:

    Techniques Used:

    Related Articles

    Western Blot:

    Article Title: Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5
    Article Snippet: For CoIP Dynabeads protein A magnetic beads (Thermo Fisher Scientific) were used following manufacturer’s instructions. .. Anti-Nav1.5 (SCN5A) antibody (493-511, Alomone) was used for precipitation and Western Blots were stained with anti-Nav1.5 (SCN5A) (493-511, Alomone, 1:1000) or anti-POPDC2 (Sigma, HPA 024255, 1:500) antibodies and peroxidase-conjugated anti-rabbit secondary antibody (Thermo, 31460, 1:8000). ..

    Staining:

    Article Title: Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5
    Article Snippet: For CoIP Dynabeads protein A magnetic beads (Thermo Fisher Scientific) were used following manufacturer’s instructions. .. Anti-Nav1.5 (SCN5A) antibody (493-511, Alomone) was used for precipitation and Western Blots were stained with anti-Nav1.5 (SCN5A) (493-511, Alomone, 1:1000) or anti-POPDC2 (Sigma, HPA 024255, 1:500) antibodies and peroxidase-conjugated anti-rabbit secondary antibody (Thermo, 31460, 1:8000). ..

    Incubation:

    Article Title: Candesartan Cilexetil Attenuates Arrhythmogenicity Following Pressure Overload in Rats via the Modulation of Cardiac Electrical and Structural Remodeling and Calcium Handling Dysfunction
    Article Snippet: Protein samples (30– 100 μg) were separated on 4% to 20% gradient gel (Mini- Protean Precast gels; Bio- Rad Laboratories) or 8% to 10% SDS- PAGE and transferred onto polyvinylidene difluoride (PVDF) membranes (PerkinElmer Life Sciences, Boston, MA). .. Membranes were blocked and then incubated overnight at 4 °C with primary antibody against ryanodine receptor Ca2+ release channel 2 (RyR2) (1:1000; ThermoFisher Scientific, Waltham, MA), Ser2808- phosphorylated RyR2 (pSer2808- RyR2) (1:5000; Badrilla, Leeds, United Kingdom), pSer2814- RyR2 (1:500; Badrilla), SERCA2a (sarco[endo]plasmic reticulum Ca2+ATPase) (1:5000; Badrilla), phospholamban (1:2000; Badrilla), pSer16- phospholamban (1:2000; Millipore, Temecula, CA), pThr17- phospholamban (1:2000; Badrilla), Na+- Ca2+ exchanger 1 (NCX1) (1:500; Santa Cruz Biotechnology, Santa Cruz, CA), voltage- gated L- type calcium 1.2a channel subunit (CaV1.2a) (1:400; Millipore), voltage- gated sodium 1.5 channel subunit (NaV1.5) (1:500; Alomone, Jerusalem, Israel), voltagegated potassium 4.2 channel subunit (Kv4.2) (1:200; Millipore), voltage- gated potassium 4.3 channel subunit (Kv4.3) (1:200; Alomone), voltage- gated potassium 1.4 channel subunit (Kv1.4) (1:200; Alomone), Kv- channel interacting protein 2 (KChIP2) (1:500; ThermoFisher Scientific), voltage- gated potassium 2.1 channel subunit (Kv2.1) (1:500; Alomone), and inwardly rectifying potassium 2.1 channel subunit (Kir2.1) (1:600; Alomone). .. The blot was also probed by a glyceraldehyde 3- phosphate dehydrogenase (GAPDH) antibody (1:1000; Santa Cruz) or a β- actin antibody (1:1000; Abcam, Cambridge, MA) as an internal control.

    Article Title: Candesartan Cilexetil Attenuates Arrhythmogenicity Following Pressure Overload in Rats via the Modulation of Cardiac Electrical and Structural Remodeling and Calcium Handling Dysfunction
    Article Snippet: Protein samples (30–100 μg) were separated on 4% to 20% gradient gel (Mini‐Protean Precast gels; Bio‐Rad Laboratories) or 8% to 10% SDS‐PAGE and transferred onto polyvinylidene difluoride (PVDF) membranes (PerkinElmer Life Sciences, Boston, MA). .. Membranes were blocked and then incubated overnight at 4 °C with primary antibody against ryanodine receptor Ca 2+ release channel 2 (RyR2) (1:1000; ThermoFisher Scientific, Waltham, MA), Ser 2808 ‐phosphorylated RyR2 (pSer 2808 ‐RyR2) (1:5000; Badrilla, Leeds, United Kingdom), pSer 2814 ‐RyR2 (1:500; Badrilla), SERCA2a (sarco[endo]plasmic reticulum Ca 2+ ‐ATPase) (1:5000; Badrilla), phospholamban (1:2000; Badrilla), pSer 16 ‐phospholamban (1:2000; Millipore, Temecula, CA), pThr 17 ‐phospholamban (1:2000; Badrilla), Na + ‐Ca 2+ exchanger 1 (NCX1) (1:500; Santa Cruz Biotechnology, Santa Cruz, CA), voltage‐gated L‐type calcium 1.2a channel subunit (Ca V 1.2a) (1:400; Millipore), voltage‐gated sodium 1.5 channel subunit (Na V 1.5) (1:500; Alomone, Jerusalem, Israel), voltage‐gated potassium 4.2 channel subunit (Kv4.2) (1:200; Millipore), voltage‐gated potassium 4.3 channel subunit (Kv4.3) (1:200; Alomone), voltage‐gated potassium 1.4 channel subunit (Kv1.4) (1:200; Alomone), Kv‐channel interacting protein 2 (KChIP2) (1:500; ThermoFisher Scientific), voltage‐gated potassium 2.1 channel subunit (Kv2.1) (1:500; Alomone), and inwardly rectifying potassium 2.1 channel subunit (Kir2.1) (1:600; Alomone). .. The blot was also probed by a glyceraldehyde 3‐phosphate dehydrogenase (GAPDH) antibody (1:1000; Santa Cruz) or a β‐actin antibody (1:1000; Abcam, Cambridge, MA) as an internal control.

    Article Title: Cardiac electrical abnormalities in a mouse model of left ventricular non-compaction cardiomyopathy
    Article Snippet: .. Cells were rinsed repeatedly and incubated overnight at 4°C with the primary antibodies anti-K V 4.2 (1:200, Alomone labs, Israel), anti-K V 4.3 (1:200, Alomone labs, Israel), anti-Na V 1.5 (1:200, Alomone labs, Israel), and anti-α-actinin (1:200, Sigma). .. Cells were rinsed repeatedly and incubated overnight at 4°C with the primary antibodies anti-K V 4.2 (1:200, Alomone labs, Israel), anti-K V 4.3 (1:200, Alomone labs, Israel), anti-Na V 1.5 (1:200, Alomone labs, Israel), and anti-α-actinin (1:200, Sigma).

    Immunostaining:

    Article Title: Gene therapy targeting protein trafficking regulator MOG1 in mouse models of Brugada syndrome, arrhythmias, and mild cardiomyopathy.
    Article Snippet: Brugada syndrome (BrS) is a fatal arrhythmia that causes an estimated 4% of all sudden death in high-incidence areas.. SCN5A encodes cardiac sodium channel NaV1.5 and causes 25 to 30% of BrS cases.. Here, we report generation of a knock-in (KI) mouse model of BrS (Scn5aG1746R/+).

    Control:

    Article Title: Gene therapy targeting protein trafficking regulator MOG1 in mouse models of Brugada syndrome, arrhythmias, and mild cardiomyopathy.
    Article Snippet: Brugada syndrome (BrS) is a fatal arrhythmia that causes an estimated 4% of all sudden death in high-incidence areas.. SCN5A encodes cardiac sodium channel NaV1.5 and causes 25 to 30% of BrS cases.. Here, we report generation of a knock-in (KI) mouse model of BrS (Scn5aG1746R/+).

    Article Title: Knockout of interleukin-17A diminishes ventricular arrhythmia susceptibility in diabetic mice via inhibiting NF-κB-mediated electrical remodeling.
    Article Snippet: .. Interleukin-17A (IL-17), a potent proinflammatory cytokine, has been shown to participate in cardiac electrical disorders.. Diabetes mellitus is an independent risk factor for ventricular arrhythmia.. In this study, we investigated the role of IL-17 in ventricular arrhythmia of diabetic mice. .. Interleukin-17A (IL-17), a potent proinflammatory cytokine, has been shown to participate in cardiac electrical disorders.. Diabetes mellitus is an independent risk factor for ventricular arrhythmia.. In this study, we investigated the role of IL-17 in ventricular arrhythmia of diabetic mice.

    Membrane:

    Article Title: Single-Molecule Localization of the Cardiac Voltage-Gated Sodium Channel Reveals Different Modes of Reorganization at Cardiomyocyte Membrane Domains
    Article Snippet: Secondary antibodies were rabbit AlexaFluor 568 (Life Technologies, Carlsbad, California; SMLM: 1:10,000; confocal: 1:200), mouse AlexaFluor 647 (Life Technologies; SMLM: 1:5000), and mouse AlexaFluor 488 (Life Technologies; confocal: 1:200). .. Our group has shown a similar reduction of Nav1.5 at the lateral membrane of mdx mice using the aforementioned Alomone antibody9. .. Firstly, the confocal image in Figure 1 shows that the staining pattern of the Pineda antibody is highly similar to that of the widely used Alomone ASC-005 antibody2.



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    Functional screen for cardiac ion channels modulated by POPDC2 (A–D) Representative current traces of (A) HCN4, applying a voltage step from −30 mV to −120 mV within 6 s, from a holding potential of −30 mV, (B) Kv1.4, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV, (C) Kv4.3, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV or (D) <t>Nav1.5,</t> applying a voltage step from −80 mV to −20 mV within 50 ms, from a holding potential of −80 mV, expressed alone ( black ) or together with POPDC2 ( blue ) in Xenopus laevis oocytes. (E) Indicated cardiac channels or the Na + /K + ATPase (Na/K) were expressed alone or together with POPDC2 in Xenopus oocytes and relative changes in current amplitudes by POPDC2 were plotted. Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001.
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    Ion channel protein expression of the ventricular tissue of the PM2.5 group (n = 6) and the control group (n = 5). Panel A showed the relative protein levels of Cav1.2, SERCA2, RYR, NCX, <t>Nav1.5,</t> Kv11.1, KvLQ1 and Kir2.1. Panel B showed the western blot analysis of the ion channel protein expression. * Indicate p < 0.05 comparison of CaV1.2 was performed with Mann–Whitney U Test, while the remaining were performed with Student’s t-test. CaV1.2 = cardiac calcium channels, SERCA2 = SR-calcium-ATPase2, RYR = ryanodine receptor, NCX = sodium/calcium-exchanger, Nav1.5 = cardiac sodium channels Nav1.5, Kv11.1 = voltage-gated potassium channel Kv11.1, KvLQT1 = voltage-gated potassium channel KvLQT1, Kir2.1 = inward-rectifier potassium ion channel.
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    Ion channel protein expression of the ventricular tissue of the PM2.5 group (n = 6) and the control group (n = 5). Panel A showed the relative protein levels of Cav1.2, SERCA2, RYR, NCX, <t>Nav1.5,</t> Kv11.1, KvLQ1 and Kir2.1. Panel B showed the western blot analysis of the ion channel protein expression. * Indicate p < 0.05 comparison of CaV1.2 was performed with Mann–Whitney U Test, while the remaining were performed with Student’s t-test. CaV1.2 = cardiac calcium channels, SERCA2 = SR-calcium-ATPase2, RYR = ryanodine receptor, NCX = sodium/calcium-exchanger, Nav1.5 = cardiac sodium channels Nav1.5, Kv11.1 = voltage-gated potassium channel Kv11.1, KvLQT1 = voltage-gated potassium channel KvLQT1, Kir2.1 = inward-rectifier potassium ion channel.
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    Ion channel protein expression of the ventricular tissue of the PM2.5 group (n = 6) and the control group (n = 5). Panel A showed the relative protein levels of Cav1.2, SERCA2, RYR, NCX, <t>Nav1.5,</t> Kv11.1, KvLQ1 and Kir2.1. Panel B showed the western blot analysis of the ion channel protein expression. * Indicate p < 0.05 comparison of CaV1.2 was performed with Mann–Whitney U Test, while the remaining were performed with Student’s t-test. CaV1.2 = cardiac calcium channels, SERCA2 = SR-calcium-ATPase2, RYR = ryanodine receptor, NCX = sodium/calcium-exchanger, Nav1.5 = cardiac sodium channels Nav1.5, Kv11.1 = voltage-gated potassium channel Kv11.1, KvLQT1 = voltage-gated potassium channel KvLQT1, Kir2.1 = inward-rectifier potassium ion channel.
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    Ion channel protein expression of the ventricular tissue of the PM2.5 group (n = 6) and the control group (n = 5). Panel A showed the relative protein levels of Cav1.2, SERCA2, RYR, NCX, <t>Nav1.5,</t> Kv11.1, KvLQ1 and Kir2.1. Panel B showed the western blot analysis of the ion channel protein expression. * Indicate p < 0.05 comparison of CaV1.2 was performed with Mann–Whitney U Test, while the remaining were performed with Student’s t-test. CaV1.2 = cardiac calcium channels, SERCA2 = SR-calcium-ATPase2, RYR = ryanodine receptor, NCX = sodium/calcium-exchanger, Nav1.5 = cardiac sodium channels Nav1.5, Kv11.1 = voltage-gated potassium channel Kv11.1, KvLQT1 = voltage-gated potassium channel KvLQT1, Kir2.1 = inward-rectifier potassium ion channel.
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    Ion channel protein expression of the ventricular tissue of the PM2.5 group (n = 6) and the control group (n = 5). Panel A showed the relative protein levels of Cav1.2, SERCA2, RYR, NCX, <t>Nav1.5,</t> Kv11.1, KvLQ1 and Kir2.1. Panel B showed the western blot analysis of the ion channel protein expression. * Indicate p < 0.05 comparison of CaV1.2 was performed with Mann–Whitney U Test, while the remaining were performed with Student’s t-test. CaV1.2 = cardiac calcium channels, SERCA2 = SR-calcium-ATPase2, RYR = ryanodine receptor, NCX = sodium/calcium-exchanger, Nav1.5 = cardiac sodium channels Nav1.5, Kv11.1 = voltage-gated potassium channel Kv11.1, KvLQT1 = voltage-gated potassium channel KvLQT1, Kir2.1 = inward-rectifier potassium ion channel.
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    Ion channel protein expression of the ventricular tissue of the PM2.5 group (n = 6) and the control group (n = 5). Panel A showed the relative protein levels of Cav1.2, SERCA2, RYR, NCX, <t>Nav1.5,</t> Kv11.1, KvLQ1 and Kir2.1. Panel B showed the western blot analysis of the ion channel protein expression. * Indicate p < 0.05 comparison of CaV1.2 was performed with Mann–Whitney U Test, while the remaining were performed with Student’s t-test. CaV1.2 = cardiac calcium channels, SERCA2 = SR-calcium-ATPase2, RYR = ryanodine receptor, NCX = sodium/calcium-exchanger, Nav1.5 = cardiac sodium channels Nav1.5, Kv11.1 = voltage-gated potassium channel Kv11.1, KvLQT1 = voltage-gated potassium channel KvLQT1, Kir2.1 = inward-rectifier potassium ion channel.
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    Figure 1. The intracellular level of NADH is increased by A280V GPD1-L and is reversed by incubation with [NAD]o. Data from 3 to 4 samples are normalized to the <t>SCN5A</t> cell group. ***P0.001 vs all other groups.
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    Image Search Results


    Functional screen for cardiac ion channels modulated by POPDC2 (A–D) Representative current traces of (A) HCN4, applying a voltage step from −30 mV to −120 mV within 6 s, from a holding potential of −30 mV, (B) Kv1.4, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV, (C) Kv4.3, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV or (D) Nav1.5, applying a voltage step from −80 mV to −20 mV within 50 ms, from a holding potential of −80 mV, expressed alone ( black ) or together with POPDC2 ( blue ) in Xenopus laevis oocytes. (E) Indicated cardiac channels or the Na + /K + ATPase (Na/K) were expressed alone or together with POPDC2 in Xenopus oocytes and relative changes in current amplitudes by POPDC2 were plotted. Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001.

    Journal: iScience

    Article Title: Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5

    doi: 10.1016/j.isci.2024.109696

    Figure Lengend Snippet: Functional screen for cardiac ion channels modulated by POPDC2 (A–D) Representative current traces of (A) HCN4, applying a voltage step from −30 mV to −120 mV within 6 s, from a holding potential of −30 mV, (B) Kv1.4, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV, (C) Kv4.3, applying a voltage step from −80 mV to +40 mV within 2 s, from a holding potential of −80 mV or (D) Nav1.5, applying a voltage step from −80 mV to −20 mV within 50 ms, from a holding potential of −80 mV, expressed alone ( black ) or together with POPDC2 ( blue ) in Xenopus laevis oocytes. (E) Indicated cardiac channels or the Na + /K + ATPase (Na/K) were expressed alone or together with POPDC2 in Xenopus oocytes and relative changes in current amplitudes by POPDC2 were plotted. Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001.

    Article Snippet: Anti-Nav1.5 (SCN5A) antibody (493-511, Alomone) was used for precipitation and Western Blots were stained with anti-Nav1.5 (SCN5A) (493-511, Alomone, 1:1000) or anti-POPDC2 (Sigma, HPA 024255, 1:500) antibodies and peroxidase-conjugated anti-rabbit secondary antibody (Thermo, 31460, 1:8000).

    Techniques: Functional Assay, Patch Clamp

    Interaction of POPDC proteins with the cardiac sodium channel Nav1.5 or the skeletal muscle sodium channel Nav1.4 (A) Co-immunoprecipitation of POPDC2-FLAG with Nav1.5-HA was performed in COS-7 cells using anti-HA antibodies. An empty vector served as control. The co-immunoprecipitation was subsequently detected with an anti-FLAG antibody (IB: α-Flag). (B) Co-immunoprecipitation of POPDC2 and Nav1.5 in murine heart lysates (mheart) using anti Nav1.5 antibodies (IP: α-Nav1.5). The immunoprecipitation was subsequently detected with an anti-Nav1.5 (IB: α-Nav1.5) and the co-immunoprecipitation by an anti-POPDC2 antibody (IB: α-POPDC2). HeLa cells were used as a control. (C) Oocytes were injected with cRNA for human Nav1.5 or co-injected with different murine POPDC isoforms and subsequently stored in a storage solution lacking theophylline. Currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −80 mV) and voltage-steps of 50 ms ranging from −70 to +80 mV in 10 mV increments (see inset). (D and E) (D) Relative current amplitudes analyzed at −20 mV and normalized to Nav1.5. (E) Voltage-dependence of Nav1.5 activation in the absence or presence of POPDC1, POPDC2 or POPDC3. The respective voltages of half-maximal activation (V 1/2 ) and the Boltzmann constants (k) are provided as inset. The number of technical replicates (n) is indicated in parentheses or bar graphs. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001. (F and G) (F) POPDC2 does not modulate current amplitudes of Nav1.4, analyzed at −10 mV and normalized to Nav1.4 or (G) the shape of the voltage-dependence of Nav1.4 activation. The respective voltages of half-maximal activation (V 1/2 ) and the Boltzmann constants (k) are provided as inset. The number of technical replicates (n) is indicated in parentheses or bar graphs. Oocytes were stored in a storage solution lacking theophylline. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. See also <xref ref-type=Figures S1 and . " width="100%" height="100%">

    Journal: iScience

    Article Title: Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5

    doi: 10.1016/j.isci.2024.109696

    Figure Lengend Snippet: Interaction of POPDC proteins with the cardiac sodium channel Nav1.5 or the skeletal muscle sodium channel Nav1.4 (A) Co-immunoprecipitation of POPDC2-FLAG with Nav1.5-HA was performed in COS-7 cells using anti-HA antibodies. An empty vector served as control. The co-immunoprecipitation was subsequently detected with an anti-FLAG antibody (IB: α-Flag). (B) Co-immunoprecipitation of POPDC2 and Nav1.5 in murine heart lysates (mheart) using anti Nav1.5 antibodies (IP: α-Nav1.5). The immunoprecipitation was subsequently detected with an anti-Nav1.5 (IB: α-Nav1.5) and the co-immunoprecipitation by an anti-POPDC2 antibody (IB: α-POPDC2). HeLa cells were used as a control. (C) Oocytes were injected with cRNA for human Nav1.5 or co-injected with different murine POPDC isoforms and subsequently stored in a storage solution lacking theophylline. Currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −80 mV) and voltage-steps of 50 ms ranging from −70 to +80 mV in 10 mV increments (see inset). (D and E) (D) Relative current amplitudes analyzed at −20 mV and normalized to Nav1.5. (E) Voltage-dependence of Nav1.5 activation in the absence or presence of POPDC1, POPDC2 or POPDC3. The respective voltages of half-maximal activation (V 1/2 ) and the Boltzmann constants (k) are provided as inset. The number of technical replicates (n) is indicated in parentheses or bar graphs. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗∗∗, p < 0.001. (F and G) (F) POPDC2 does not modulate current amplitudes of Nav1.4, analyzed at −10 mV and normalized to Nav1.4 or (G) the shape of the voltage-dependence of Nav1.4 activation. The respective voltages of half-maximal activation (V 1/2 ) and the Boltzmann constants (k) are provided as inset. The number of technical replicates (n) is indicated in parentheses or bar graphs. Oocytes were stored in a storage solution lacking theophylline. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. See also Figures S1 and .

    Article Snippet: Anti-Nav1.5 (SCN5A) antibody (493-511, Alomone) was used for precipitation and Western Blots were stained with anti-Nav1.5 (SCN5A) (493-511, Alomone, 1:1000) or anti-POPDC2 (Sigma, HPA 024255, 1:500) antibodies and peroxidase-conjugated anti-rabbit secondary antibody (Thermo, 31460, 1:8000).

    Techniques: Co-Immunoprecipitation Assay, Plasmid Preparation, Control, Immunoprecipitation, Injection, Activation Assay, Patch Clamp

    POPDC2 does not alter the current kinetics of Nav1.5 (A) Current traces of human Nav1.5 expressed alone or co-expressed with human POPDC2. Representative traces are depicted at −30 mV, −20 mV and −10 mV. (B) Voltage-dependence of activation and inactivation curves fitted to a Boltzmann equation. The respective voltages of half-maximal activation (V 1/2 ) together with the Boltzmann constants (k), as well as the window currents, are provided as inset. For the V 1/2 of activation measurements, the currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −80 mV) and voltage-steps of 50 ms ranging from −70 to +80 mV in 10 mV increments (see inset activation protocol). For the V 1/2 of inactivation measurements, the currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −100 mV) and voltage-steps of 50 ms ranging from −120 to −10 mV in 10 mV increments with a final step to −30 mV for 50 ms (see inset inactivation protocol). The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. (C) Representative current traces of the kinetics of inactivation recorded with a single-step protocol from −100 mV to −30 mV for 65 ms (inset illustrates voltage protocol). (D) Representative recordings of the recovery from inactivation (inset illustrates voltage protocol). (E) Time-course of the recovery from inactivation recorded with a two-pulse protocol, first step to −10 mV for 50 ms and the second test pulse stepped to −10 mV with increasing interpulse intervals. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. (F) Time constants of the fast and slow component of the recovery from inactivation (lower panel) and the relative contribution of the fast and slow component (upper panel). Values were obtained by a bi-exponential fit from the data in (E). Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. See also <xref ref-type=Figure S3 . " width="100%" height="100%">

    Journal: iScience

    Article Title: Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5

    doi: 10.1016/j.isci.2024.109696

    Figure Lengend Snippet: POPDC2 does not alter the current kinetics of Nav1.5 (A) Current traces of human Nav1.5 expressed alone or co-expressed with human POPDC2. Representative traces are depicted at −30 mV, −20 mV and −10 mV. (B) Voltage-dependence of activation and inactivation curves fitted to a Boltzmann equation. The respective voltages of half-maximal activation (V 1/2 ) together with the Boltzmann constants (k), as well as the window currents, are provided as inset. For the V 1/2 of activation measurements, the currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −80 mV) and voltage-steps of 50 ms ranging from −70 to +80 mV in 10 mV increments (see inset activation protocol). For the V 1/2 of inactivation measurements, the currents were recorded with a P/N ( N = 4) voltage-step protocol (holding potential −100 mV) and voltage-steps of 50 ms ranging from −120 to −10 mV in 10 mV increments with a final step to −30 mV for 50 ms (see inset inactivation protocol). The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. (C) Representative current traces of the kinetics of inactivation recorded with a single-step protocol from −100 mV to −30 mV for 65 ms (inset illustrates voltage protocol). (D) Representative recordings of the recovery from inactivation (inset illustrates voltage protocol). (E) Time-course of the recovery from inactivation recorded with a two-pulse protocol, first step to −10 mV for 50 ms and the second test pulse stepped to −10 mV with increasing interpulse intervals. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. (F) Time constants of the fast and slow component of the recovery from inactivation (lower panel) and the relative contribution of the fast and slow component (upper panel). Values were obtained by a bi-exponential fit from the data in (E). Oocytes were stored in a storage solution lacking theophylline. The number of technical replicates (n) is indicated in parentheses. Data are presented as mean ± s.e.m. See also Figure S3 .

    Article Snippet: Anti-Nav1.5 (SCN5A) antibody (493-511, Alomone) was used for precipitation and Western Blots were stained with anti-Nav1.5 (SCN5A) (493-511, Alomone, 1:1000) or anti-POPDC2 (Sigma, HPA 024255, 1:500) antibodies and peroxidase-conjugated anti-rabbit secondary antibody (Thermo, 31460, 1:8000).

    Techniques: Activation Assay, Inactivation, Patch Clamp

    POPDC2 reduces Nav1.5 current amplitudes in a cAMP-dependent manner (A) POPDC2 modulation of Nav1.5 is cAMP-dependent. Representative current traces recorded by voltage steps to −20 mV. Oocytes were injected with 10 ng Nav1.5 alone or 10 ng Nav1.5 together with 5 ng POPDC2 (50%) or 10 ng POPDC2 (100%), and stored in ND96 solution with or without theophylline before voltage-clamp measurements in oocytes. Inset illustrates the applied voltage protocol. (B) Analyses of peak current amplitudes from experiments performed in (A), analyzed at −20 mV and normalized to Nav1.5. The number of technical replicates (n) is indicated in bar graphs. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗, p < 0.05; ∗∗∗, p < 0.001. (C) Oocytes were injected as in (A-B) but incubated in a storage solution containing theophylline. Relative current amplitudes were analyzed at −20 mV and normalized to Nav1.5. The number of technical replicates is indicated in bar graphs. Data are presented as mean ± s.e.m. See also <xref ref-type=Figure S4 . " width="100%" height="100%">

    Journal: iScience

    Article Title: Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5

    doi: 10.1016/j.isci.2024.109696

    Figure Lengend Snippet: POPDC2 reduces Nav1.5 current amplitudes in a cAMP-dependent manner (A) POPDC2 modulation of Nav1.5 is cAMP-dependent. Representative current traces recorded by voltage steps to −20 mV. Oocytes were injected with 10 ng Nav1.5 alone or 10 ng Nav1.5 together with 5 ng POPDC2 (50%) or 10 ng POPDC2 (100%), and stored in ND96 solution with or without theophylline before voltage-clamp measurements in oocytes. Inset illustrates the applied voltage protocol. (B) Analyses of peak current amplitudes from experiments performed in (A), analyzed at −20 mV and normalized to Nav1.5. The number of technical replicates (n) is indicated in bar graphs. Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗, p < 0.05; ∗∗∗, p < 0.001. (C) Oocytes were injected as in (A-B) but incubated in a storage solution containing theophylline. Relative current amplitudes were analyzed at −20 mV and normalized to Nav1.5. The number of technical replicates is indicated in bar graphs. Data are presented as mean ± s.e.m. See also Figure S4 .

    Article Snippet: Anti-Nav1.5 (SCN5A) antibody (493-511, Alomone) was used for precipitation and Western Blots were stained with anti-Nav1.5 (SCN5A) (493-511, Alomone, 1:1000) or anti-POPDC2 (Sigma, HPA 024255, 1:500) antibodies and peroxidase-conjugated anti-rabbit secondary antibody (Thermo, 31460, 1:8000).

    Techniques: Injection, Incubation, Patch Clamp

    POPDC2 co-localizes with Nav1.5 at the plasma membrane and intracellular compartments and regulates the surface expression of Nav1.5 in a cAMP-dependent manner (A and C) HeLa cells were transfected exclusively with Nav1.5-HA or (B and D) in combination with POPDC2-YFP. 24 h after transfection the cells were fixed, non-permeabilized (A-B) or permeabilized (C-D) and immunostained with anti HA antibody and Alexa 647 conjugated secondary antibody. The cells were then analyzed by confocal microscopy. Nuclear counterstaining with Hoechst 33342 is depicted in blue and nuclei of non-transfected cells are indicated by asterisk. Arrows point to either (A) Nav1.5- or (B) Nav1.5- plus POPDC2-YFP-stained membrane protrusions; PM, plasma membrane. Arrowheads in (D) depict Nav1.5-positive intracellular structures co-labelled by POPDC2-YFP, which are also designated by arrows in the single fluorescence images shown on the left. Scale bars, 10 μm. (E) Cartoon of the chemiluminescence-based ELISA-assay performed in HeLa cells transiently transfected with Nav1.5 HA to quantify the changes in Nav1.5 surface expression by co-transfection with POPDC2. In fixed cells, the primary antibody detects extracellularly HA-tagged Nav1.5 channels (Nav1.5 HA ) at the surface membrane while the peroxidase-enzyme (POD) which is linked to the secondary antibody catalyzes the oxidation of a luminol-substrate which is accompanied by the emission of light. Subsequently, the light emission can be quantified as relative light units (RLUs) as a measure of the surface expression of the channel. (F) Chemiluminescence assay of extracellularly HA-tagged Nav1.5 to determine the relative changes in surface expression by co-expressed POPDC2. The number of biological replicates (N) is indicated in the bar graphs. Data are expressed as relative light units (RLUs). Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗, p < 0.05. (G) Chemiluminescence assay of extracellularly HA-tagged Nav1.5 to determine the relative changes in surface expression by co-expressed POPDC2 in the presence of theophylline. The number of biological replicates (N) is indicated in the bar graphs. Data are expressed as relative light units (RLUs). Data are presented as mean ± s.e.m.

    Journal: iScience

    Article Title: Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5

    doi: 10.1016/j.isci.2024.109696

    Figure Lengend Snippet: POPDC2 co-localizes with Nav1.5 at the plasma membrane and intracellular compartments and regulates the surface expression of Nav1.5 in a cAMP-dependent manner (A and C) HeLa cells were transfected exclusively with Nav1.5-HA or (B and D) in combination with POPDC2-YFP. 24 h after transfection the cells were fixed, non-permeabilized (A-B) or permeabilized (C-D) and immunostained with anti HA antibody and Alexa 647 conjugated secondary antibody. The cells were then analyzed by confocal microscopy. Nuclear counterstaining with Hoechst 33342 is depicted in blue and nuclei of non-transfected cells are indicated by asterisk. Arrows point to either (A) Nav1.5- or (B) Nav1.5- plus POPDC2-YFP-stained membrane protrusions; PM, plasma membrane. Arrowheads in (D) depict Nav1.5-positive intracellular structures co-labelled by POPDC2-YFP, which are also designated by arrows in the single fluorescence images shown on the left. Scale bars, 10 μm. (E) Cartoon of the chemiluminescence-based ELISA-assay performed in HeLa cells transiently transfected with Nav1.5 HA to quantify the changes in Nav1.5 surface expression by co-transfection with POPDC2. In fixed cells, the primary antibody detects extracellularly HA-tagged Nav1.5 channels (Nav1.5 HA ) at the surface membrane while the peroxidase-enzyme (POD) which is linked to the secondary antibody catalyzes the oxidation of a luminol-substrate which is accompanied by the emission of light. Subsequently, the light emission can be quantified as relative light units (RLUs) as a measure of the surface expression of the channel. (F) Chemiluminescence assay of extracellularly HA-tagged Nav1.5 to determine the relative changes in surface expression by co-expressed POPDC2. The number of biological replicates (N) is indicated in the bar graphs. Data are expressed as relative light units (RLUs). Data are presented as mean ± s.e.m. Significance was probed using a two-sided Student’s t-test. ∗, p < 0.05. (G) Chemiluminescence assay of extracellularly HA-tagged Nav1.5 to determine the relative changes in surface expression by co-expressed POPDC2 in the presence of theophylline. The number of biological replicates (N) is indicated in the bar graphs. Data are expressed as relative light units (RLUs). Data are presented as mean ± s.e.m.

    Article Snippet: Anti-Nav1.5 (SCN5A) antibody (493-511, Alomone) was used for precipitation and Western Blots were stained with anti-Nav1.5 (SCN5A) (493-511, Alomone, 1:1000) or anti-POPDC2 (Sigma, HPA 024255, 1:500) antibodies and peroxidase-conjugated anti-rabbit secondary antibody (Thermo, 31460, 1:8000).

    Techniques: Clinical Proteomics, Membrane, Expressing, Transfection, Confocal, Microscopy, Staining, Fluorescence, Enzyme-linked Immunosorbent Assay, Cotransfection, Chemiluminescence Immunoassay, Immunofluorescence

    Journal: iScience

    Article Title: Popeye domain containing proteins modulate the voltage-gated cardiac sodium channel Nav1.5

    doi: 10.1016/j.isci.2024.109696

    Figure Lengend Snippet:

    Article Snippet: Anti-Nav1.5 (SCN5A) antibody (493-511, Alomone) was used for precipitation and Western Blots were stained with anti-Nav1.5 (SCN5A) (493-511, Alomone, 1:1000) or anti-POPDC2 (Sigma, HPA 024255, 1:500) antibodies and peroxidase-conjugated anti-rabbit secondary antibody (Thermo, 31460, 1:8000).

    Techniques:

    Ion channel protein expression of the ventricular tissue of the PM2.5 group (n = 6) and the control group (n = 5). Panel A showed the relative protein levels of Cav1.2, SERCA2, RYR, NCX, Nav1.5, Kv11.1, KvLQ1 and Kir2.1. Panel B showed the western blot analysis of the ion channel protein expression. * Indicate p < 0.05 comparison of CaV1.2 was performed with Mann–Whitney U Test, while the remaining were performed with Student’s t-test. CaV1.2 = cardiac calcium channels, SERCA2 = SR-calcium-ATPase2, RYR = ryanodine receptor, NCX = sodium/calcium-exchanger, Nav1.5 = cardiac sodium channels Nav1.5, Kv11.1 = voltage-gated potassium channel Kv11.1, KvLQT1 = voltage-gated potassium channel KvLQT1, Kir2.1 = inward-rectifier potassium ion channel.

    Journal: Scientific Reports

    Article Title: Neural mechanism facilitating PM2.5-related cardiac arrhythmias through cardiovascular autonomic and calcium dysregulation in a rat model

    doi: 10.1038/s41598-023-41148-8

    Figure Lengend Snippet: Ion channel protein expression of the ventricular tissue of the PM2.5 group (n = 6) and the control group (n = 5). Panel A showed the relative protein levels of Cav1.2, SERCA2, RYR, NCX, Nav1.5, Kv11.1, KvLQ1 and Kir2.1. Panel B showed the western blot analysis of the ion channel protein expression. * Indicate p < 0.05 comparison of CaV1.2 was performed with Mann–Whitney U Test, while the remaining were performed with Student’s t-test. CaV1.2 = cardiac calcium channels, SERCA2 = SR-calcium-ATPase2, RYR = ryanodine receptor, NCX = sodium/calcium-exchanger, Nav1.5 = cardiac sodium channels Nav1.5, Kv11.1 = voltage-gated potassium channel Kv11.1, KvLQT1 = voltage-gated potassium channel KvLQT1, Kir2.1 = inward-rectifier potassium ion channel.

    Article Snippet: The ionic channel proteins included cardiac calcium channels CaV1.2 (Thermo Scientific, Waltham, MA, USA), SR-calcium-ATPase2 (SERCA2, Thermo Scientific, Waltham, MA, USA), ryanodine receptor (RyR) 2 (Abcam, Cambridge, CB2 0AX, UK), and sodium/calcium-exchanger (NCX, Swant, Bellinzona, Switzerland), cardiac sodium channels Nav1.5 (Alomone Labs, Jerusalem, Israel), voltage-gated potassium channel Kv11.1 (Alomone Labs, Jerusalem, Israel), and KvLQT1 (Merck Millipore, Darmstadt, Germany in USA), inward-rectifier potassium ion channel Kir2.1 (Santa Cruz, CA, USA).

    Techniques: Expressing, Tissue, Control, Western Blot, Analysis, Comparison, MANN-WHITNEY

    Figure 1. The intracellular level of NADH is increased by A280V GPD1-L and is reversed by incubation with [NAD]o. Data from 3 to 4 samples are normalized to the SCN5A cell group. ***P0.001 vs all other groups.

    Journal: Circulation Research

    Article Title: Cardiac Na + Current Regulation by Pyridine Nucleotides

    doi: 10.1161/circresaha.109.197277

    Figure Lengend Snippet: Figure 1. The intracellular level of NADH is increased by A280V GPD1-L and is reversed by incubation with [NAD]o. Data from 3 to 4 samples are normalized to the SCN5A cell group. ***P0.001 vs all other groups.

    Article Snippet: For biotin labeling, SCN5A cells were incubated as above for 2-10 min. Biotinylation of cell surface proteins was performed with the Pinpoint Cell Surface Protein Isolation Kit (Pierce, Rockford, IL) as previously described.3 For detection of SCN5A, the primary antibody (rabbit anti- SCN5A, Alomone Labs, Jerusalem, Israel) was diluted 1:100.

    Techniques: Incubation

    Figure 5. The effects of altering NAD(H) on arrhythmic risk. Representative MAP recordings with PES during Krebs–Henseleit buffer per- fusion (A), after 20 minutes perfusion with lactate:pyruvate (10:1) buffer to increase [NADH]i (B), and after reintroduction of Krebs–H- enseleit buffer (C). D, Representative traces of MAPs from left ventricular epicardium of Langendorff-perfused SCN5A/ heart during standard pacing at a basic cycle length of 125 ms in the control condition. Vertical lines below the MAPs represent the times when electric stimulations were delivered. E, Action potentials recorded with the patch-clamp technique in single ventricular myocytes and with the MAP electrode on whole heart. F, MAPs after 20 minutes of perfusion with 100 mol/L [NAD]o. G, Histogram of APD90 in control condition and with 100 mol/L [NAD]o. H, Representative MAPs recorded during PES showing PES-induced VT in SCN5A/

    Journal: Circulation Research

    Article Title: Cardiac Na + Current Regulation by Pyridine Nucleotides

    doi: 10.1161/circresaha.109.197277

    Figure Lengend Snippet: Figure 5. The effects of altering NAD(H) on arrhythmic risk. Representative MAP recordings with PES during Krebs–Henseleit buffer per- fusion (A), after 20 minutes perfusion with lactate:pyruvate (10:1) buffer to increase [NADH]i (B), and after reintroduction of Krebs–H- enseleit buffer (C). D, Representative traces of MAPs from left ventricular epicardium of Langendorff-perfused SCN5A/ heart during standard pacing at a basic cycle length of 125 ms in the control condition. Vertical lines below the MAPs represent the times when electric stimulations were delivered. E, Action potentials recorded with the patch-clamp technique in single ventricular myocytes and with the MAP electrode on whole heart. F, MAPs after 20 minutes of perfusion with 100 mol/L [NAD]o. G, Histogram of APD90 in control condition and with 100 mol/L [NAD]o. H, Representative MAPs recorded during PES showing PES-induced VT in SCN5A/

    Article Snippet: For biotin labeling, SCN5A cells were incubated as above for 2-10 min. Biotinylation of cell surface proteins was performed with the Pinpoint Cell Surface Protein Isolation Kit (Pierce, Rockford, IL) as previously described.3 For detection of SCN5A, the primary antibody (rabbit anti- SCN5A, Alomone Labs, Jerusalem, Israel) was diluted 1:100.

    Techniques: Control, Patch Clamp

    Figure 6. Possible signaling pathways for the effects of A280V GPD1-L, [NADH]i and NAD to regulate the Nav1.5.

    Journal: Circulation Research

    Article Title: Cardiac Na + Current Regulation by Pyridine Nucleotides

    doi: 10.1161/circresaha.109.197277

    Figure Lengend Snippet: Figure 6. Possible signaling pathways for the effects of A280V GPD1-L, [NADH]i and NAD to regulate the Nav1.5.

    Article Snippet: For biotin labeling, SCN5A cells were incubated as above for 2-10 min. Biotinylation of cell surface proteins was performed with the Pinpoint Cell Surface Protein Isolation Kit (Pierce, Rockford, IL) as previously described.3 For detection of SCN5A, the primary antibody (rabbit anti- SCN5A, Alomone Labs, Jerusalem, Israel) was diluted 1:100.

    Techniques: Protein-Protein interactions