The sodium channel beta-subunit SCN3b modulates the kinetics of SCN5a and is expressed heterogeneously in sheep heart

Fahmi, Ahmed I.; Patel, Manoj K.; Stevens, Edward B.; Fowden, Abigail L.; John, J. Edward; Lee, Kevin; Pinnock, R.D.; Morgan, Kevin; Jackson, Antony P.; Vandenberg, Jamie I.

doi:10.1111/j.1469-7793.2001.00693.x

Cited by 69 publications

(61 citation statements)

References 27 publications

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“…The association of Na v 1.5 with ␤1 or ␤3 may produce a depolarizing shift in voltage dependence of inactivation (33,51,52) and in recovery from inactivation (51). Several inherited mutations linked to Long QT syndrome and Brugada syndrome have been reported in the acidic-rich domain in the C terminus of the cardiac Na v 1.5 channel, which overlaps with CR1, i.e.…”

Section: Discussionmentioning

confidence: 99%

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Modulation of the Cardiac Sodium Channel Nav1.5 by Fibroblast Growth Factor Homologous Factor 1B

Liu

Dib‐Hajj

Renganathan

et al. 2003

Journal of Biological Chemistry

146

147

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We have previously shown that fibroblast growth factor homologous factor 1B (FHF1B), a cytosolic member of the fibroblast growth factor family, associates with the sensory neuron-specific channel Na v 1.9 but not with the other sodium channels present in adult rat dorsal root ganglia neurons. We show in this study that FHF1B binds to the C terminus of the cardiac voltage-gated sodium channel Na v 1.5 and modulates the properties of the channel. The N-terminal 41 amino acid residues of FHF1B are essential for binding to Na v 1.5, and the conserved acidic rich domain (amino acids 1773-1832) in the C terminus of Na v 1.5 is sufficient for association with this factor. Binding of the growth factor to recombinant wild type human Na v 1.5 in human embryonic kidney 293 cells produces a significant hyperpolarizing shift in the voltage dependence of channel inactivation. An aspartic acid to glycine substitution at position 1790 of the channel, which underlies one of the LQT-3 phenotypes of cardiac arrythmias, abolishes the interaction of the Na v 1.5 channel with FHF1B. This is the first report showing that interaction with a growth factor can modulate properties of a voltage-gated sodium channel.

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Section: Discussionmentioning

confidence: 99%

“…Sodium channels Na v 1.1 and Na v 1.5 and the auxiliary subunits ␤1, ␤2, and ␤3 are present in cardiac myocytes (39,51,52). The association of Na v 1.5 with ␤1 or ␤3 may produce a depolarizing shift in voltage dependence of inactivation (33,51,52) and in recovery from inactivation (51).…”

Section: Discussionmentioning

confidence: 99%

Modulation of the Cardiac Sodium Channel Nav1.5 by Fibroblast Growth Factor Homologous Factor 1B

Liu

Dib‐Hajj

Renganathan

et al. 2003

Journal of Biological Chemistry

146

147

View full text Add to dashboard Cite

show abstract

“…Briefly, the coding exons of genes were amplified using primers as previously reported. 17,23, 24 HRM analyses were performed using the LightCycler ® 480 (Roche Applied Science, USA). Melting curves were generated by ramping between 64°C and 98°C at 0.02°C/s.…”

Section: Gene Scanningmentioning

confidence: 99%

L-Type Calcium Channel Mutations in Japanese Patients With Inherited Arrhythmias

Fukuyama

Ohno

Wang

et al. 2013

Circ J

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“…[11][12][13] VGSCbs can affect VGSC functioning via multiple mechanisms, including modification of voltage-dependent gating, activation and inactivation. 7,[14][15][16][17] These subunits can also increase the amplitude of VGSC currents by (i) modulating the intracellular trafficking of VGSCa protein (thereby incorporating more VGSCs into the cell's plasma membrane) and (ii) increasing their cell surface stability via association with cytoskeletal molecules such as ankyrin. 7,8,18,19 VGSCbs are unique among voltage-gated ion channel auxillary subunits in that they can also function independently of pore-forming VGSCas, in cell adhesion, cell migration and in neurite outgrowth.…”

Section: Introductionmentioning

confidence: 99%

β-Subunits of voltage-gated sodium channels in human prostate cancer: quantitative in vitro and in vivo analyses of mRNA expression

Diss

Fraser

Walker

et al. 2007

Prostate Cancer Prostatic Dis

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We previously identified high levels of Na v 1.7 voltage-gated sodium channel a-subunit (VGSCa) mRNA and protein in human prostate cancer cells and tissues. Here, we investigated auxillary b-subunit (VGSCbs) expression. In vitro, the combined expression of all four VGSCbs was significantly (B4.5-fold) higher in strongly compared to weakly metastatic cells. This was mainly due to increased b1-expression, which was under androgenic control. In vivo, b1-b4 mRNAs were detectable and their expression in CaP vs non-CaP tissues generally reflected the in vitro levels in relation to metastatic potential. The possible role(s) of VGSCbs (VGSCa-associated and VGSCaindependent) in prostate cancer are discussed.

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The sodium channel beta-subunit SCN3b modulates the kinetics of SCN5a and is expressed heterogeneously in sheep heart

Cited by 69 publications

References 27 publications

Modulation of the Cardiac Sodium Channel Nav1.5 by Fibroblast Growth Factor Homologous Factor 1B

Modulation of the Cardiac Sodium Channel Nav1.5 by Fibroblast Growth Factor Homologous Factor 1B

L-Type Calcium Channel Mutations in Japanese Patients With Inherited Arrhythmias

β-Subunits of voltage-gated sodium channels in human prostate cancer: quantitative in vitro and in vivo analyses of mRNA expression

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