| Roles of KCNA2 in Neurological Diseases: from Physiology to Pathology. | Roles of KCNA2 in Neurological Diseases: from Physiology to Pathology.
Xie C, Kessi M, Yin F, Peng J. | 10/30/2024 |
| KCNA2 IgG autoimmunity in neuropsychiatric diseases. | KCNA2 IgG autoimmunity in neuropsychiatric diseases.
Arlt FA, Miske R, Machule ML, Broegger Christensen P, Mindorf S, Teegen B, Borowski K, Buthut M, Rößling R, Sánchez-Sendín E, van Hoof S, Cordero-Gómez C, Bünger I, Radbruch H, Kraft A, Ayzenberg I, Klausewitz J, Hansen N, Timäus C, Körtvelyessy P, Postert T, Baur-Seack K, Rost C, Brunkhorst R, Doppler K, Haigis N, Hamann G, Kunze A, Stützer A, Maschke M, Melzer N, Rosenow F, Siebenbrodt K, Stenør C, Dichgans M, Georgakis MK, Fang R, Petzold GC, Görtler M, Zerr I, Wunderlich S, Mihaljevic I, Turko P, Schmidt Ettrup M, Buchholz E, Foverskov Rasmussen H, Nasouti M, Talucci I, Maric HM, Heinemann SH, Endres M, DEMDAS study group, Komorowski L, Prüss H. | 03/5/2024 |
| Two epilepsy-associated variants in KCNA2 (KV 1.2) at position H310 oppositely affect channel functional expression. | Two epilepsy-associated variants in KCNA2 (K(V) 1.2) at position H310 oppositely affect channel functional expression.
Mínguez-Viñas T, Prakash V, Wang K, Lindström SH, Pozzi S, Scott SA, Spiteri E, Stevenson DA, Ashley EA, Gunnarsson C, Pantazis A. | 12/5/2023 |
| An epilepsy-associated KV1.2 charge-transfer-center mutation impairs KV1.2 and KV1.4 trafficking. | An epilepsy-associated K(V)1.2 charge-transfer-center mutation impairs K(V)1.2 and K(V)1.4 trafficking.
Nilsson M, Lindström SH, Kaneko M, Wang K, Minguez-Viñas T, Angelini M, Steccanella F, Holder D, Ottolia M, Olcese R, Pantazis A., Free PMC Article | 06/18/2022 |
| Deep phenotyping unstructured data mining in an extensive pediatric database to unravel a common KCNA2 variant in neurodevelopmental syndromes. | Deep phenotyping unstructured data mining in an extensive pediatric database to unravel a common KCNA2 variant in neurodevelopmental syndromes.
Hully M, Lo Barco T, Kaminska A, Barcia G, Cances C, Mignot C, Desguerre I, Garcelon N, Kabashi E, Nabbout R., Free PMC Article | 07/10/2021 |
| Refining Genotypes and Phenotypes in KCNA2-Related Neurological Disorders. | Refining Genotypes and Phenotypes in KCNA2-Related Neurological Disorders.
Döring JH, Schröter J, Jüngling J, Biskup S, Klotz KA, Bast T, Dietel T, Korenke GC, Christoph S, Brennenstuhl H, Rubboli G, Møller RS, Lesca G, Chaix Y, Kölker S, Hoffmann GF, Lemke JR, Syrbe S., Free PMC Article | 04/24/2021 |
| 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 |
| recurrent de novo variants in the paralogous PVP motif of KCNA2 have previously been shown to abolish channel function and also cause early-onset epileptic encephalopathy. Importantly, this report extends the range of phenotypes associated with KCNA1 variants to include epileptic encephalopathy when the PVP motif is involved. | De novo KCNA1 variants in the PVP motif cause infantile epileptic encephalopathy and cognitive impairment similar to recurrent KCNA2 variants.
Rogers A, Golumbek P, Cellini E, Doccini V, Guerrini R, Wallgren-Pettersson C, Thuresson AC, Gurnett CA. | 08/24/2019 |
| We identified 3 patients with KCNA2 mutations with novel characteristics | Novel clinical manifestations in patients with KCNA2 mutations.
Sachdev M, Gaínza-Lein M, Tchapyjnikov D, Jiang YH, Loddenkemper T, Mikati MA. | 06/16/2018 |
| study indicates well represented genotype-phenotype associations between three subgroups of patients with KCNA2 encephalopathy according to the electrophysiological features of the mutations. | Clinical spectrum and genotype-phenotype associations of KCNA2-related encephalopathies.
Masnada S, Hedrich UBS, Gardella E, Schubert J, Kaiwar C, Klee EW, Lanpher BC, Gavrilova RH, Synofzik M, Bast T, Gorman K, King MD, Allen NM, Conroy J, Ben Zeev B, Tzadok M, Korff C, Dubois F, Ramsey K, Narayanan V, Serratosa JM, Giraldez BG, Helbig I, Marsh E, O'Brien M, Bergqvist CA, Binelli A, Porter B, Zaeyen E, Horovitz DD, Wolff M, Marjanovic D, Caglayan HS, Arslan M, Pena SDJ, Sisodiya SM, Balestrini S, Syrbe S, Veggiotti P, Lemke JR, Møller RS, Lerche H, Rubboli G. | 11/4/2017 |
| Pharmacogenetic and case-control study evaluated the role of the variants of KCNA1, KCNA2, and KCNV2 in the susceptibility and drug resistance of genetic generalized epilepsies and revealed no significant association between 8 variants of KCNA1, KCNA2, and KCNV2 genes and risk or drug resistance of genetic generalized epilepsies after a Bonferroni correction for multiple comparisons. | Pharmacogenetic and case-control study on potassium channel related gene variants and genetic generalized epilepsy.
Qu J, Lu SH, Lu ZL, Xu P, Xiang DX, Qu Q., Free PMC Article | 07/22/2017 |
| In the asymptomatic mother, the mutated copy of the CDKL5 gene was inactivated in 90% of blood cells. We also identified a premature stop codon (p.Arg926*) in IQSEC2 in a patient with a Rett-like phenotype. Finally, exome sequencing enabled us to characterize a heterozygous de novo missense (p.Val408Ala) in KCNA2 in a girl with infantile-onset seizures variant of Rett syndrome (RTT) | Rett-like phenotypes: expanding the genetic heterogeneity to the KCNA2 gene and first familial case of CDKL5-related disease.
Allou L, Julia S, Amsallem D, El Chehadeh S, Lambert L, Thevenon J, Duffourd Y, Saunier A, Bouquet P, Pere S, Moustaïne A, Ruaud L, Roth V, Jonveaux P, Philippe C. | 07/1/2017 |
| Novel recurrent missense mutation within the Kv1.2 voltage sensor associated with variable phenotypes, including hereditary spastic paraplegia, ataxia, and intellectual disability. | A recurrent mutation in KCNA2 as a novel cause of hereditary spastic paraplegia and ataxia.
Helbig KL, Hedrich UB, Shinde DN, Krey I, Teichmann AC, Hentschel J, Schubert J, Chamberlin AC, Huether R, Lu HM, Alcaraz WA, Tang S, Jungbluth C, Dugan SL, Vainionpää L, Karle KN, Synofzik M, Schöls L, Schüle R, Lehesjoki AE, Helbig I, Lerche H, Lemke JR., Free PMC Article | 06/10/2017 |
| This study demonstrated that KCNA2 mutation causes episodic ataxia and pharmacoresponsive epilepsy. | Dominant KCNA2 mutation causes episodic ataxia and pharmacoresponsive epilepsy.
Corbett MA, Bellows ST, Li M, Carroll R, Micallef S, Carvill GL, Myers CT, Howell KB, Maljevic S, Lerche H, Gazina EV, Mefford HC, Bahlo M, Berkovic SF, Petrou S, Scheffer IE, Gecz J., Free PMC Article | 05/20/2017 |
| Use-dependent activation of Kv1.2 channels is mediated by an extrinsic regulator that binds preferentially to the channel closed state, with Thr252 being necessary but not sufficient for this interaction to alter channel function. | Determinants of frequency-dependent regulation of Kv1.2-containing potassium channels.
Baronas VA, Yang R, Vilin YY, Kurata HT., Free PMC Article | 12/17/2016 |
| This gene has not been previously described as a cause of disease in humans, but mutations of the orthologous gene in mice (Kcna2) are known to cause both ataxia and convulsions | Ataxia and myoclonic epilepsy due to a heterozygous new mutation in KCNA2: proposal for a new channelopathy.
Pena SD, Coimbra RL. | 09/26/2015 |
| KCNA2 is a new gene involved in human neurodevelopmental disorders through two different mechanisms, predicting either hyperexcitability or electrical silencing of KV1.2-expressing neurons. | De novo loss- or gain-of-function mutations in KCNA2 cause epileptic encephalopathy.
Syrbe S, Hedrich UBS, Riesch E, Djémié T, Müller S, Møller RS, Maher B, Hernandez-Hernandez L, Synofzik M, Caglayan HS, Arslan M, Serratosa JM, Nothnagel M, May P, Krause R, Löffler H, Detert K, Dorn T, Vogt H, Krämer G, Schöls L, Mullis PE, Linnankivi T, Lehesjoki AE, Sterbova K, Craiu DC, Hoffman-Zacharska D, Korff CM, Weber YG, Steinlin M, Gallati S, Bertsche A, Bernhard MK, Merkenschlager A, Kiess W, EuroEPINOMICS RES consortium, Gonzalez M, Züchner S, Palotie A, Suls A, De Jonghe P, Helbig I, Biskup S, Wolff M, Maljevic S, Schüle R, Sisodiya SM, Weckhuysen S, Lerche H, Lemke JR., Free PMC Article | 06/20/2015 |
| the inhibition of two K(+) channel isoforms, Kv1.2 and KCa3.1, by two drug molecules, lidocaine and TRAM-34, is examined in atomic detail using molecular dynamics simulations. | Mechanisms and energetics of potassium channel block by local anesthetics and antifungal agents.
Chen R, Gryn'ova G, Wu Y, Coote ML, Chung SH. | 01/3/2015 |
| isoform betaII plays a central role in the PKC-dependent regulation of Kv1.5/Kvbeta1.2 channels. | Isoenzyme-specific regulation of cardiac Kv1.5/Kvβ1.2 ion channel complex by protein kinase C: central role of PKCβII.
Fischer F, Vonderlin N, Seyler C, Zitron E, Korkmaz S, Szabó G, Thomas D, Katus HA, Scholz EP. | 01/3/2015 |
| Using mutagenesis and analysis of gating currents from gating pore mutations in the Shaker Kv channel, we identified statistically highly significant correlations between VSD function and physicochemical properties of gating pore residues. | Moving gating charges through the gating pore in a Kv channel voltage sensor.
Lacroix JJ, Hyde HC, Campos FV, Bezanilla F., Free PMC Article | 07/12/2014 |
| This study indicated that the T2DM condition leads to potassium channel-mediated peripheral nerve hyperexcitability , thus identifying them as a potential drug target to treat some of the DPN related symptoms. | Altered distribution of juxtaparanodal kv1.2 subunits mediates peripheral nerve hyperexcitability in type 2 diabetes mellitus.
Zenker J, Poirot O, de Preux Charles AS, Arnaud E, Médard JJ, Lacroix C, Kuntzer T, Chrast R., Free PMC Article | 08/11/2012 |
| The immunoreactivity of potassium channels (Kv1.2) was markedly reduced in the ventral roots, but normal in the dorsal roots of all the amyotrophic lateral sclerosis patients. | Markedly reduced axonal potassium channel expression in human sporadic amyotrophic lateral sclerosis: an immunohistochemical study.
Shibuya K, Misawa S, Arai K, Nakata M, Kanai K, Yoshiyama Y, Ito K, Isose S, Noto Y, Nasu S, Sekiguchi Y, Fujimaki Y, Ohmori S, Kitamura H, Sato Y, Kuwabara S. | 12/24/2011 |
| Using fluorimetry and gating currents, study of the Kv1.2 voltage sensor domain revealed at least two independent conformational changes in this region in response to depolarization. | Fast and slow voltage sensor rearrangements during activation gating in Kv1.2 channels detected using tetramethylrhodamine fluorescence.
Horne AJ, Peters CJ, Claydon TW, Fedida D., Free PMC Article | 03/19/2011 |
| in addition to its known effect on pore stability, V370 of Kv1.2 is also crucial in controlling ion selectivity. | Control of ionic selectivity by a pore helix residue in the Kv1.2 channel.
Chao CC, Huang CC, Kuo CS, Leung YM., Free PMC Article | 02/5/2011 |
| observe for both the open and closed conformations of the Kv1.2 that specific mutations of S4 gating-charge residues destabilize the electrostatic network between helices of the voltage sensor domain | Effect of sensor domain mutations on the properties of voltage-gated ion channels: molecular dynamics studies of the potassium channel Kv1.2.
Delemotte L, Treptow W, Klein ML, Tarek M., Free PMC Article | 01/29/2011 |