نتایج جستجو برای: kcnq1

تعداد نتایج: 1121  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2017
Dazhi Xiong Tian Li Hui Dai Anthony F Arena Leigh D Plant Steve A N Goldstein

IKs channels open in response to depolarization of the membrane voltage during the cardiac action potential, passing potassium ions outward to repolarize ventricular myocytes and end each beat. Here, we show that the voltage required to activate IKs channels depends on their covalent modification by small ubiquitin-like modifier (SUMO) proteins. IKs channels are comprised of four KCNQ1 pore-for...

2017
Hsiang-Chun Lee Yoram Rudy Hongwu Liang Chih-Chieh Chen Ching-Hsing Luo Sheng-Hsiung Sheu Jianmin Cui

Gain-of-function mutations in the pore-forming subunit of IKs channels, KCNQ1, lead to short QT syndrome (SQTS) and lethal arrhythmias. However, how mutant IKs channels cause SQTS and the possibility of IKs-specific pharmacological treatment remain unclear. V141M KCNQ1 is a SQTS associated mutation. We studied its effect on IKs gating properties and changes in the action potentials (AP) of huma...

Journal: :Cardiovascular research 2005
Kui Hong David R Piper Aurora Diaz-Valdecantos Josep Brugada Antonio Oliva Elena Burashnikov José Santos-de-Soto Josefina Grueso-Montero Ernesto Diaz-Enfante Pedro Brugada Frank Sachse Michael C Sanguinetti Ramon Brugada

OBJECTIVE We describe a genetic basis for atrial fibrillation and short QT syndrome in utero. Heterologous expression of the mutant channel was used to define the physiological consequences of the mutation. METHODS A baby girl was born at 38 weeks after induction of delivery that was prompted by bradycardia and irregular rythm. ECG revealed atrial fibrillation with slow ventricular response a...

Journal: :Biophysical journal 2016
Jianmin Cui

Gating of voltage-dependent cation channels involves three general molecular processes: voltage sensor activation, sensor-pore coupling, and pore opening. KCNQ1 is a voltage-gated potassium (Kv) channel whose distinctive properties have provided novel insights on fundamental principles of voltage-dependent gating. 1) Similar to other Kv channels, KCNQ1 voltage sensor activation undergoes two re...

2012
Jana V. van Vliet-Ostaptchouk Timon W. van Haeften Gijs W. D. Landman Erwin Reiling Nanne Kleefstra Henk J. G. Bilo Olaf H. Klungel Anthonius de Boer Cleo C. van Diemen Cisca Wijmenga H. Marike Boezen Jacqueline M. Dekker Esther van 't Riet Giel Nijpels Laura M. C. Welschen Hata Zavrelova Elinda J. Bruin Clara C. Elbers Florianne Bauer N. Charlotte Onland-Moret Yvonne T. van der Schouw Diederick E. Grobbee Annemieke M. W. Spijkerman Daphne L. van der A Annemarie M. Simonis-Bik Elisabeth M. W. Eekhoff Michaela Diamant Mark H. H. Kramer Dorret I. Boomsma Eco J. de Geus Gonneke Willemsen P. Eline Slagboom Marten H. Hofker Leen M. 't Hart

BACKGROUND Genome-wide association studies in Japanese populations recently identified common variants in the KCNQ1 gene to be associated with type 2 diabetes. We examined the association of these variants within KCNQ1 with type 2 diabetes in a Dutch population, investigated their effects on insulin secretion and metabolic traits and on the risk of developing complications in type 2 diabetes pa...

Journal: :The Journal of General Physiology 2004
Steven D. Gage William R. Kobertz

The five KCNE genes encode a family of type I transmembrane peptides that assemble with KCNQ1 and other voltage-gated K(+) channels, resulting in potassium conducting complexes with varied channel-gating properties. It has been recently proposed that a triplet of amino acids within the transmembrane domain of KCNE1 and KCNE3 confers modulation specificity to the peptide, since swapping of these...

Journal: :Cardiovascular research 2008
Céline S Nicolas Kyu-Ho Park Aziza El Harchi Jacques Camonis Robert S Kass Denis Escande Jean Mérot Gildas Loussouarn Françoise Le Bouffant Isabelle Baró

AIMS KCNQ1 (alias KvLQT1 or Kv7.1) and KCNE1 (alias IsK or minK) co-assemble to form the voltage-activated K(+) channel responsible for I(Ks)-a major repolarizing current in the human heart-and their dysfunction promotes cardiac arrhythmias. The channel is a component of larger macromolecular complexes containing known and undefined regulatory proteins. Thus, identification of proteins that mod...

2014
He Zhang Michael J. Zeitz Hong Wang Beibei Niu Shengfang Ge Wei Li Jiuwei Cui Guanjun Wang Guanxiang Qian Michael J. Higgins Xianqun Fan Andrew R. Hoffman Ji-Fan Hu

Kcnq1ot1 is a long noncoding ribonucleic acid (RNA; lncRNA) that participates in the regulation of genes within the Kcnq1 imprinting domain. Using a novel RNA-guided chromatin conformation capture method, we demonstrate that the 5' region of Kcnq1ot1 RNA orchestrates a long-range intrachromosomal loop between KvDMR1 and the Kcnq1 promoter that is required for maintenance of imprinting. PRC2 (po...

2011
Ewa Moric-Janiszewska Joanna Głogowska-Ligus Monika Paul-Samojedny Ludmiła Węglarz Grażyna Markiewicz-Łoskot Lesław Szydłowski

INTRODUCTION The main goal of this study was to examine the patient age and sex dependent expression of KCNQ1 and HERG genes that encode potassium channels responsible for the occurrence of long QT syndrome (LQTS). MATERIAL AND METHODS The study enrolled 43 families whose members suffered from LQTS type 1 (LQTS1) or 2 (LQTS2) or were healthy. The study attempted to prove that β-actin is a goo...

2018
Hui Huang Georg Kuenze Jarrod A Smith Keenan C Taylor Amanda M Duran Arina Hadziselimovic Jens Meiler Carlos G Vanoye Alfred L George Charles R Sanders

Mutations that induce loss of function (LOF) or dysfunction of the human KCNQ1 channel are responsible for susceptibility to a life-threatening heart rhythm disorder, the congenital long QT syndrome (LQTS). Hundreds of KCNQ1 mutations have been identified, but the molecular mechanisms responsible for impaired function are poorly understood. We investigated the impact of 51 KCNQ1 variants with m...

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