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    KCNA5 potassium voltage-gated channel subfamily A member 5 [ Homo sapiens (human) ]

    Gene ID: 3741, updated on 19-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Computational Studies Show How the H463R Mutation Turns hKv1.5 into an Inactivation State.

    Computational Studies Show How the H463R Mutation Turns hKv1.5 into an Inactivation State.
    Rahman RA, Zaman B, Khan MR, Islam MS, Rashid MH.

    06/24/2024
    Novel Loss-of-Function KCNA5 Variants in Pulmonary Arterial Hypertension.

    Novel Loss-of-Function KCNA5 Variants in Pulmonary Arterial Hypertension.
    Vera-Zambrano A, Lago-Docampo M, Gallego N, Franco-Gonzalez JF, Morales-Cano D, Cruz-Utrilla A, Villegas-Esguevillas M, Fernández-Malavé E, Escribano-Subías P, Tenorio-Castaño JA, Perez-Vizcaino F, Valverde D, González T, Spanish group of Ion Channels in Pulmonary Hypertension (SICPH) investigators, Cogolludo A.

    08/2/2023
    Selective expression of KCNA5 and KCNB1 genes in gastric and colorectal carcinoma.

    Selective expression of KCNA5 and KCNB1 genes in gastric and colorectal carcinoma.
    Farah A, Kabbage M, Atafi S, Gabteni AJ, Barbirou M, Madhioub M, Hamzaoui L, Mohamed MA, Touinsi H, Kchaou AO, Chelbi E, Boubaker S, Abderrazek RB, Bouhaouala-Zahar B., Free PMC Article

    05/15/2021
    KV1.5-KVbeta1.3 Recycling Is PKC-Dependent.

    K(V)1.5-K(V)β1.3 Recycling Is PKC-Dependent.
    Macias A, de la Cruz A, Peraza DA, Benito-Bueno A, Gonzalez T, Valenzuela C., Free PMC Article

    04/17/2021
    Mechanical stretch increases Kv1.5 current through an interaction between the S1-S2 linker and N-terminus of the channel.

    Mechanical stretch increases Kv1.5 current through an interaction between the S1-S2 linker and N-terminus of the channel.
    Milton AO, Wang T, Li W, Guo J, Zhang S., Free PMC Article

    01/2/2021
    MiR-3940-5p promotes granulosa cell proliferation through targeting KCNA5 in polycystic ovarian syndrome.

    MiR-3940-5p promotes granulosa cell proliferation through targeting KCNA5 in polycystic ovarian syndrome.
    Gao L, Wu D, Wu Y, Yang Z, Sheng J, Lin X, Huang H.

    10/24/2020
    Challenges Faced with Small Molecular Modulators of Potassium Current Channel Isoform Kv1.5.

    Challenges Faced with Small Molecular Modulators of Potassium Current Channel Isoform Kv1.5.
    Zhao Z, Ruan S, Ma X, Feng Q, Xie Z, Nie Z, Fan P, Qian M, He X, Wu S, Zhang Y, Zheng X., Free PMC Article

    09/19/2020
    these results suggest that Notch activation enhances CaSR-mediated increases in [Ca(2+)]cyt by enhancing store-operated Ca(2+) entry and inhibits KCNA5/KV1.5 and KCNA2/KV1.2, ultimately leading to voltage-activated Ca(2+) entry.

    Notch enhances Ca(2+) entry by activating calcium-sensing receptors and inhibiting voltage-gated K(+) channels.
    Song S, Babicheva A, Zhao T, Ayon RJ, Rodriguez M, Rahimi S, Balistrieri F, Harrington A, Shyy JY, Thistlethwaite PA, Makino A, Yuan JX., Free PMC Article

    08/12/2020
    Kv1.5 downregulation upon PM leaves Kv1.3 as the dominant Kv1 channel expressed in dedifferentiated cells. We demonstrated that the inhibition of Kv1.3 channel function with selective blockers or by preventing Kv1.5 downregulation can represent an effective, novel strategy for the prevention of intimal hyperplasia and restenosis of the human vessels used for coronary angioplasty procedures.

    Myocardin-Dependent Kv1.5 Channel Expression Prevents Phenotypic Modulation of Human Vessels in Organ Culture.
    Arévalo-Martínez M, Cidad P, García-Mateo N, Moreno-Estar S, Serna J, Fernández M, Swärd K, Simarro M, de la Fuente MA, López-López JR, Pérez-García MT.

    04/18/2020
    Verapamil acts as an open-channel blocker of hKv1.5 channel, presumably due to direct binding to specific amino acids within pore region of hKv1.5 channel, such as Thr479, Thr480, Val505, Ile508, Val512 and Val516.

    Identification of Verapamil Binding Sites Within Human Kv1.5 Channel Using Mutagenesis and Docking Simulation.
    Ding WG, Tano A, Mi X, Kojima A, Seto T, Matsuura H.

    03/9/2019
    The N terminus and transmembrane segment S1 of Kv1.5 can co-assemble with the rest of the channel independently of the S1-S2 linkage.

    The N terminus and transmembrane segment S1 of Kv1.5 can coassemble with the rest of the channel independently of the S1-S2 linkage.
    Lamothe SM, Hogan-Cann AE, Li W, Guo J, Yang T, Tschirhart JN, Zhang S., Free PMC Article

    03/9/2019
    Molecular dynamics simulations are employed to determine the inhibitory mechanisms of three drugs, 5-(4-phenoxybutoxy)psoralen (PAP-1), vernakalant, and flecainide, on the voltage-gated K(+) channel Kv1.5, a target for the treatment of cardiac arrhythmia.

    Inhibition of Voltage-Gated K(+) Channel Kv1.5 by Antiarrhythmic Drugs.
    Chen R, Chung SH.

    09/15/2018
    This study adds insights to the functional impact of KCNA5 mutations in modulating atrial contractile functions.

    In-silico investigations of the functional impact of KCNA5 mutations on atrial mechanical dynamics.
    Ni H, Adeniran I, Zhang H.

    05/19/2018
    In addition, as IKur is an atrial-specific channel and a number of IKur-selective blockers have been developed as anti-AF agents, this study also helps to understand some contradictory results on both pro- and anti-arrhythmic effects of blocking IKur.

    In silico assessment of genetic variation in KCNA5 reveals multiple mechanisms of human atrial arrhythmogenesis.
    Colman MA, Ni H, Liang B, Schmitt N, Zhang H., Free PMC Article

    08/19/2017
    our finding indicated that KCNA5 protein may interact with Cav-1, thereby contributing to the proliferation and early transformation of mammary cells.

    Expression of KCNA5 Protein in Human Mammary Epithelial Cell Line Associated with Caveolin-1.
    Liu J, Qu C, Li H, Zhang Y, Sun J, Yang S, Liu J, An L, Zou W.

    07/29/2017
    Putative binding sites for arachidonic acid on the human cardiac Kv 1.5 channel

    Putative binding sites for arachidonic acid on the human cardiac Kv 1.5 channel.
    Bai JY, Ding WG, Kojima A, Seto T, Matsuura H., Free PMC Article

    10/29/2016
    Studies demonstrate that DNA hypermethylation contributes to epigenetic repression of the KCNA5 locus and that the resulting suppression of the Kv1.5 ion channel supports cancer cell proliferation.

    Promoter Methylation Analysis Reveals That KCNA5 Ion Channel Silencing Supports Ewing Sarcoma Cell Proliferation.
    Ryland KE, Hawkins AG, Weisenberger DJ, Punj V, Borinstein SC, Laird PW, Martens JR, Lawlor ER., Free PMC Article

    10/22/2016
    Kv1.5 expression is increased in osteosarcoma cells and tissues and shRNA mediated silencing of Kv1.5 results in cell proliferation inhibition, cell cycle arrest, and induces cell apoptosis.

    Silencing of Kv1.5 Gene Inhibits Proliferation and Induces Apoptosis of Osteosarcoma Cells.
    Wu J, Chen Z, Liu Q, Zeng W, Wu X, Lin B., Free PMC Article

    08/27/2016
    Direct interaction with specific amino acids underlies the blocking action of propofol on voltage-gated hKv1.5 channel.

    Interaction of propofol with voltage-gated human Kv1.5 channel through specific amino acids within the pore region.
    Kojima A, Ito Y, Ding WG, Kitagawa H, Matsuura H.

    07/30/2016
    demonstrate that PK treatment cleaved mature membrane-bound (75kDa) Kv1.5 channels at a single locus in the S1-S2 linker, producing 42-kDa N-terminal fragments and 33-kDa C-terminal fragments

    Proteolytic cleavage in the S1-S2 linker of the Kv1.5 channel does not affect channel function.
    Hogan-Cann A, Li W, Guo J, Yang T, Zhang S.

    07/16/2016
    These results indicate that CHIP decreases the Kv1.5 protein level and functional channel by facilitating its degradation in concert with chaperone Hsc70

    E3 ligase CHIP and Hsc70 regulate Kv1.5 protein expression and function in mammalian cells.
    Li P, Kurata Y, Maharani N, Mahati E, Higaki K, Hasegawa A, Shirayoshi Y, Yoshida A, Kondo T, Kurozawa Y, Yamamoto K, Ninomiya H, Hisatome I.

    05/28/2016
    The expression of Kv1.5 channel protein changes with atrial fibrillation but not with age, rheumatic heart diseases, and sex in atrial fibrillation.

    Remodeling of Kv1.5 channel in right atria from Han Chinese patients with atrial fibrillation.
    Ou XH, Li ML, Liu R, Fan XR, Mao L, Fan XH, Yang Y, Zeng XR., Free PMC Article

    04/23/2016
    One KCNA5 variant, H463R, was a novel mutation; the histidine at codon 463 is located in the S5-pore loop, in the vicinity of the pore of KV1.5 subunit. The other variant, T527M, showed a gain-of-function effect with an enhanced steady-state activation.

    Functional Characterization of Rare Variants Implicated in Susceptibility to Lone Atrial Fibrillation.
    Hayashi K, Konno T, Tada H, Tani S, Liu L, Fujino N, Nohara A, Hodatsu A, Tsuda T, Tanaka Y, Kawashiri MA, Ino H, Makita N, Yamagishi M.

    02/6/2016
    The KCNA5 promoter is marked in cancer cells with PcG-dependent chromatin repressive modifications that increase in hypoxia.

    Polycomb-dependent repression of the potassium channel-encoding gene KCNA5 promotes cancer cell survival under conditions of stress.
    Ryland KE, Svoboda LK, Vesely ED, McIntyre JC, Zhang L, Martens JR, Lawlor ER., Free PMC Article

    11/28/2015
    Mutations in KCNA5 gene is not associated with pulmonary arterial hypertension.

    Novel mutations in BMPR2, ACVRL1 and KCNA5 genes and hemodynamic parameters in patients with pulmonary arterial hypertension.
    Pousada G, Baloira A, Vilariño C, Cifrian JM, Valverde D., Free PMC Article

    10/31/2015
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