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Journal articles on the topic 'HERG'

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Author: Grafiati

Published: 4 June 2021

Last updated: 6 July 2024

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1

Trudeau, Matthew C., Jeffrey W. Warmke, Barry Ganetzky, and Gail A. Robertson. "HERG Sequence Correction." Science 272, no. 5265 (May 24, 1996): 1087. http://dx.doi.org/10.1126/science.272.5265.1087.c.

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2

LIAN, JIANGFANG, JIAN GUO, XIAOYAN HUANG, XI YANG, GUOCHANG HUANG, HAIYAN MAO, HUAN HUAN SUN, YANNA BA, and JIANQING ZHOU. "miRNAs Regulate hERG." Journal of Cardiovascular Electrophysiology 27, no. 12 (September 26, 2016): 1472–82. http://dx.doi.org/10.1111/jce.13084.

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3

Trudeau, M. C., J. W. Warmke, B. Ganetzky, and G. A. Robertson. "HERG Sequence Correction." Science 272, no. 5265 (May 24, 1996): 1083j—1087. http://dx.doi.org/10.1126/science.272.5265.1083j.

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4

Trudeau, M. C., J. W. Warmke, B. Ganetzky, and G. A. Robertson. "HERG Sequence Correction." Science 272, no. 5265 (May 24, 1996): 1087c. http://dx.doi.org/10.1126/science.272.5265.1087c.

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5

Czodrowski, Paul. "hERG Me Out." Journal of Chemical Information and Modeling 53, no. 9 (August 21, 2013): 2240–51. http://dx.doi.org/10.1021/ci400308z.

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6

Zhou, Qinlian, Agnieszka Lis, and G. Bett. "Modeling HERG Isoforms." Biophysical Journal 104, no. 2 (January 2013): 264a. http://dx.doi.org/10.1016/j.bpj.2012.11.1485.

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7

Inanobe, Atsushi, Kazuharu Furutani, and Yoshihisa Kurachi⁎. "Facilitation of hERG Current Occurs in Various hERG Channel Blockers." Journal of Molecular and Cellular Cardiology 45, no. 4 (October 2008): S13. http://dx.doi.org/10.1016/j.yjmcc.2008.09.632.

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8

Kim, Ki-Suk, Sang-Joon Park, Hankwang Na, Hae-Sung Park, and Eun-Joo Kim. "EFFECT OF HERG CURRENT BY DRUGS IN hERG TRAFFICKING MUTANTS." Journal of Pharmacological and Toxicological Methods 56, no. 2 (September 2007): e5. http://dx.doi.org/10.1016/j.vascn.2007.02.010.

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9

Friederich, P., A. Solth, S. Schillemeit, and D. Isbrandt. "Local anaesthetic sensitivities of cloned HERG channels from human heart: comparison with HERG/MiRP1 and HERG/MiRP1 T8A." British Journal of Anaesthesia 92, no. 1 (January 2004): 93–101. http://dx.doi.org/10.1093/bja/aeh026.

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10

El Harchi, Aziza, Dario Melgari, and Jules C. Hancox. "Investigation of the Influence of hERG 1b on hERG Channel Pharmacology." Biophysical Journal 104, no. 2 (January 2013): 297a. http://dx.doi.org/10.1016/j.bpj.2012.11.1655.

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11

Aromolaran, Kelly A., Donald D. Chang, R. Suzanne Zukin, Henry M. Colecraft, Mohamed Chahine, Mohamed Boutjdir, and Ademuyiwa Aromolaran. "Modulation of hERG 1a Trafficking by hERG 1b Subunits in Heart." Biophysical Journal 110, no. 3 (February 2016): 273a. http://dx.doi.org/10.1016/j.bpj.2015.11.1483.

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12

Kiehn, Johann, Antonio E. Lacerda, and Arthur M. Brown. "Pathways of HERG inactivation." American Journal of Physiology-Heart and Circulatory Physiology 277, no. 1 (July 1, 1999): H199—H210. http://dx.doi.org/10.1152/ajpheart.1999.277.1.h199.

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The rapid, repolarizing K+ current in cardiomyocytes ( I Kr) has unique inwardly rectifying properties that contribute importantly to the downstroke of the cardiac action potential. The human ether-à-go-go-related gene ( HERG) expresses a macroscopic current virtually identical to I Kr, but a description of the single-channel properties that cause rectification is lacking. For this reason we measured single-channel and macropatch currents heterologously expressed by HERG in Xenopus oocytes. Our experiments had two main findings. First, the single-channel current-voltage relation showed inward rectification, and conductance was 9.7 pS at −100 mV and 3.9 pS at 100 mV when measured in symmetrical 100 mM K+ solutions. Second, single channels frequently showed no openings during depolarization but nevertheless revealed bursts of openings during repolarization. This type of gating may explain the inward rectification of HERG currents. To test this hypothesis, we used a three-closed state kinetics model and obtained rate constants from fits to macropatch data. Results from the model are consistent with rapid inactivation from closed states as a significant source of HERG rectification.

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13

Berthet, Myriam, Isabelle Denjoy, Claire Donger, Laurence Demay, Hicham Hammoude, Didier Klug, Eric Schulze-Bahr, et al. "C-terminal HERG Mutations." Circulation 99, no. 11 (March 23, 1999): 1464–70. http://dx.doi.org/10.1161/01.cir.99.11.1464.

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14

Zhou, QinLian, and Glenna C. L. Bett. "Modeling HERG Gating Transitions." Biophysical Journal 100, no. 3 (February 2011): 426a. http://dx.doi.org/10.1016/j.bpj.2010.12.2521.

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15

Bett, Glenna C. L., Qinlian Zhou, and Randall L. Rasmusson. "Models of HERG Gating." Biophysical Journal 101, no. 3 (August 2011): 631–42. http://dx.doi.org/10.1016/j.bpj.2011.06.050.

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16

Franks, Brandon, Glenna C. L. Bett, and Randall Rasmusson. "Models of hERG Block." Biophysical Journal 114, no. 3 (February 2018): 292a—293a. http://dx.doi.org/10.1016/j.bpj.2017.11.1672.

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17

Tseng, Gea-Ny. "IKr: The hERG Channel." Journal of Molecular and Cellular Cardiology 33, no. 5 (May 2001): 835–49. http://dx.doi.org/10.1006/jmcc.2000.1317.

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18

Leishman, Derek J., Matthew M. Abernathy, and Evan B. Wang. "Revisiting the hERG safety margin after 20 years of routine hERG screening." Journal of Pharmacological and Toxicological Methods 105 (September 2020): 106900. http://dx.doi.org/10.1016/j.vascn.2020.106900.

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19

Lee, Hong Joon, Bok Hee Choi, Jin-Sung Choi, and Sang June Hahn. "Effects of cariprazine on hERG 1A and hERG 1A/3.1 potassium channels." European Journal of Pharmacology 854 (July 2019): 92–100. http://dx.doi.org/10.1016/j.ejphar.2019.04.006.

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20

Kim, Hyunho, and Hojung Nam. "hERG-Att: Self-attention-based deep neural network for predicting hERG blockers." Computational Biology and Chemistry 87 (August 2020): 107286. http://dx.doi.org/10.1016/j.compbiolchem.2020.107286.

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21

Sugimoto, Shintaro, Fumiya Tamura, Nanami Iwasaki, Masaki Ieda, Kazuho Sakamoto, and Junko Kurokawa. "Reciprocal action of a synthetic estrogen and hERG blockers on the hERG channel." Proceedings for Annual Meeting of The Japanese Pharmacological Society 92 (2019): 1—SS—80. http://dx.doi.org/10.1254/jpssuppl.92.0_1-ss-80.

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22

Hancox, Jules C., Mark J. McPate, Aziza El Harchi, and Yi hong Zhang. "The hERG potassium channel and hERG screening for drug-induced torsades de pointes." Pharmacology & Therapeutics 119, no. 2 (August 2008): 118–32. http://dx.doi.org/10.1016/j.pharmthera.2008.05.009.

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23

Schmidtke, Peter, Marine Ciantar, Isabelle Theret, and Pierre Ducrot. "Dynamics of hERG Closure Allow Novel Insights into hERG Blocking by Small Molecules." Journal of Chemical Information and Modeling 54, no. 8 (July 18, 2014): 2320–33. http://dx.doi.org/10.1021/ci5001373.

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24

Doherty, Colleen, Arek Raczynski, Hong Zang, Suresh Balani, Scott Coleman, Carl Alden, Peter Smith, and Vivek J. Kadambi. "EXPANDING THE SCOPE OF THE hERG BINDING ASSAY: hERG TRAFFICKING AND METABOLITE TESTING." Journal of Pharmacological and Toxicological Methods 56, no. 2 (September 2007): e55. http://dx.doi.org/10.1016/j.vascn.2007.02.110.

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25

Raschi, Emanuel, Luisa Ceccarini, Fabrizio De Ponti, and Maurizio Recanatini. "hERG-related drug toxicity and models for predicting hERG liability and QT prolongation." Expert Opinion on Drug Metabolism & Toxicology 5, no. 9 (July 3, 2009): 1005–21. http://dx.doi.org/10.1517/17425250903055070.

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26

Franks, Brandon, Mark Nowak, Brian Panama, Randall Rasmusson, and Glenna Bett. "Modeling Trapping Block of HERG for CiPA: Does the Basal HERG Mode Matter?" Biophysical Journal 116, no. 3 (February 2019): 246a—247a. http://dx.doi.org/10.1016/j.bpj.2018.11.1349.

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27

Gang, Hongying, and Shetuan Zhang. "Na+ Permeation and Block of hERG Potassium Channels." Journal of General Physiology 128, no. 1 (June 12, 2006): 55–71. http://dx.doi.org/10.1085/jgp.200609500.

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The inactivation gating of hERG channels is important for the channel function and drug–channel interaction. Whereas hERG channels are highly selective for K+, we have found that inactivated hERG channels allow Na+ to permeate in the absence of K+. This provides a new way to directly monitor and investigate hERG inactivation. By using whole cell patch clamp method with an internal solution containing 135 mM Na+ and an external solution containing 135 mM NMG+, we recorded a robust Na+ current through hERG channels expressed in HEK 293 cells. Kinetic analyses of the hERG Na+ and K+ currents indicate that the channel experiences at least two states during the inactivation process, an initial fast, less stable state followed by a slow, more stable state. The Na+ current reflects Na+ ions permeating through the fast inactivated state but not through the slow inactivated state or open state. Thus the hERG Na+ current displayed a slow inactivation as the channels travel from the less stable, fast inactivated state into the more stable, slow inactivated state. Removal of fast inactivation by the S631A mutation abolished the Na+ current. Moreover, acceleration of fast inactivation by mutations T623A, F627Y, and S641A did not affect the hERG Na+ current, but greatly diminished the hERG K+ current. We also found that external Na+ potently blocked the hERG outward Na+ current with an IC50 of 3.5 mM. Mutations in the channel pore and S6 regions, such as S624A, F627Y, and S641A, abolished the inhibitory effects of external Na+ on the hERG Na+ current. Na+ permeation and blockade of hERG channels provide novel ways to extend our understanding of the hERG gating mechanisms.

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28

Shi, Yuan-Qi, Meng Yan, Li-Rong Liu, Xiao Zhang, Xue Wang, Huai-Ze Geng, Xin Zhao, and Bao-Xin Li. "High Glucose Represses hERG K+ Channel Expression through Trafficking Inhibition." Cellular Physiology and Biochemistry 37, no. 1 (2015): 284–96. http://dx.doi.org/10.1159/000430353.

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Background/Aims: Abnormal QT prolongation is the most prominent cardiac electrical disturbance in patients with diabetes mellitus (DM). It is well known that the human ether-ago-go-related gene (hERG) controls the rapid delayed rectifier K+ current (IKr) in cardiac cells. The expression of the hERG channel is severely down-regulated in diabetic hearts, and this down-regulation is a critical contributor to the slowing of repolarization and QT prolongation. However, the intracellular mechanisms underlying the diabetes-induced hERG deficiency remain unknown. Methods: The expression of the hERG channel was assessed via western blot analysis, and the hERG current was detected with a patch-clamp technique. Results: The results of our study revealed that the expression of the hERG protein and the hERG current were substantially decreased in high-glucose-treated hERG-HEK cells. Moreover, we demonstrated that the high-glucose-mediated damage to the hERG channel depended on the down-regulation of protein levels but not the alteration of channel kinetics. These discoveries indicated that high glucose likely disrupted hERG channel trafficking. From the western blot and immunoprecipitation analyses, we found that high glucose induced trafficking inhibition through an effect on the expression of Hsp90 and its interaction with hERG. Furthermore, the high-glucose-induced inhibition of hERG channel trafficking could activate the unfolded protein response (UPR) by up-regulating the expression levels of activating transcription factor-6 (ATF-6) and the ER chaperone protein calnexin. In addition, we demonstrated that 100 nM insulin up-regulated the expression of the hERG channel and rescued the hERG channel repression caused by high glucose. Conclusion: The results of our study provide the first evidence of a high-glucose-induced hERG channel deficiency resulting from the inhibition of channel trafficking. Furthermore, insulin promotes the expression of the hERG channel and ameliorates the high-glucose-induced inhibition of the hERG channel.

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29

Witchel, H. J., J. C. Hancox, D. J. Nutt, and S. Wilson. "Antipsychotics, HERG and sudden death." British Journal of Psychiatry 182, no. 2 (February 2003): 171–72. http://dx.doi.org/10.1192/bjp.182.2.171-a.

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30

Yao, Y. "Aminoglycosides restore truncated HERG channels." European Heart Journal 34, suppl 1 (August 2, 2013): P2294. http://dx.doi.org/10.1093/eurheartj/eht308.p2294.

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31

Lee, Seung Ho, Hyang Mi Lee, and Bok Hee Choi. "Alprenolol Inhibits Herg Potassium Channels." Biophysical Journal 98, no. 3 (January 2010): 115a—116a. http://dx.doi.org/10.1016/j.bpj.2009.12.631.

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32

Islas, León D. "The electric heart of hERG." Journal of General Physiology 141, no. 4 (March 11, 2013): 409–11. http://dx.doi.org/10.1085/jgp.201310973.

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33

Pakladok, Tatsiana, Ahmad Almilaji, Carlos Munoz, Ioana Alesutan, and Florian Lang. "PIKfyve Sensitivity of hERG Channels." Cellular Physiology and Biochemistry 31, no. 6 (2013): 785–94. http://dx.doi.org/10.1159/000350096.

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34

Alper, Kenneth, Rong Bai, Nian Liu, Steven J. Fowler, Xi-Ping Huang, Silvia G. Priori, and Yanfei Ruan. "hERG Blockade by Iboga Alkaloids." Cardiovascular Toxicology 16, no. 1 (January 31, 2015): 14–22. http://dx.doi.org/10.1007/s12012-015-9311-5.

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35

Wang, Zhi, Hamse Y. Mussa, Robert Lowe, Robert C. Glen, and Aixia Yan. "Probability Based hERG Blocker Classifiers." Molecular Informatics 31, no. 9 (September 2012): 679–85. http://dx.doi.org/10.1002/minf.201200011.

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36

Brown, A. M. "Drugs, hERG and sudden death." Cell Calcium 35, no. 6 (June 2004): 543–47. http://dx.doi.org/10.1016/j.ceca.2004.01.008.

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37

Qiu, Hai-Yan, Sha-Sha Yuan, Fang-Yuan Yang, Ting-Ting Shi, and Jin-Kui Yang. "HERG Protein Plays a Role in Moxifloxacin-Induced Hypoglycemia." Journal of Diabetes Research 2016 (2016): 1–6. http://dx.doi.org/10.1155/2016/6741745.

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The purpose of this study was to investigate the effect of moxifloxacin on HERG channel protein and glucose metabolism. HERG expression was investigated using immunohistochemistry. The whole-cell patch clamp method was used to examine the effect of moxifloxacin on HERG channel currents. A glucose tolerance test was used to analyze the effects of moxifloxacin on blood glucose and insulin concentrations in mice. Results show that HERG protein was expressed in human pancreatic β-cells. Moxifloxacin inhibited HERG time-dependent and tail currents in HEK293 cells in a concentration-dependent manner. The IC50 of moxifloxacin inhibition was 36.65 μmol/L. Moxifloxacin (200 mg/kg) reduced blood glucose levels and increased insulin secretion in wild-type mice at 60 min after the start of the glucose tolerance test. In contrast, moxifloxacin did not significantly alter blood glucose and insulin levels in HERG knockout mice. Serum glucose levels increased and insulin concentrations decreased in HERG knockout mice when compared to wild-type mice. The moxifloxacin-induced decrease in blood glucose and increase in insulin secretion occurred via the HERG protein; thus, HERG protein plays a role in insulin secretion.

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38

Wible, Barbara A., Peter Hawryluk, Eckhard Ficker, Yuri A. Kuryshev, Glenn Kirsch, and Arthur M. Brown. "HERG-Lite®: A novel comprehensive high-throughput screen for drug-induced hERG risk." Journal of Pharmacological and Toxicological Methods 52, no. 1 (July 2005): 136–45. http://dx.doi.org/10.1016/j.vascn.2005.03.008.

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39

Puckerin, Akil, Kelly A. Aromolaran, Donald D. Chang, R. Suzanne Zukin, Henry M. Colecraft, Mohamed Boutjdir, and Ademuyiwa S. Aromolaran. "hERG 1a LQT2 C-terminus truncation mutants display hERG 1b-dependent dominant negative mechanisms." Heart Rhythm 13, no. 5 (May 2016): 1121–30. http://dx.doi.org/10.1016/j.hrthm.2016.01.012.

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40

Cortes, D. Marien, and Luis G. Cuello. "A KcsA-hERG Chimera Provides Structural Insights into the Unusual hERG Inactivation Gating Mechanism." Biophysical Journal 104, no. 2 (January 2013): 122a. http://dx.doi.org/10.1016/j.bpj.2012.11.704.

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41

Bian, Jin-Song, Anna Kagan, and Thomas V. McDonald. "Molecular analysis of PIP2 regulation of HERG and IKr." American Journal of Physiology-Heart and Circulatory Physiology 287, no. 5 (November 2004): H2154—H2163. http://dx.doi.org/10.1152/ajpheart.00120.2004.

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We previously reported that cloned human ether-à-go-go-related gene (HERG) K+ channels are regulated by changes in phosphatidylinositol 4,5-bisphosphate (PIP2) concentration. Here we investigated the molecular determinants of PIP2 interactions with HERG channel protein. To establish the molecular nature of the PIP2-HERG interaction, we examined a segment of the HERG COOH terminus with a high concentration of positively charged amino acids (nos. 883–894) as a possible site of interaction with negatively charged PIP2. When we excised deletion-HERG (D-HERG) or mutated methionine-substituted-HERG (M-HERG) this segment of HERG to neutralize the amino acid charge, the mutant channels produced current that was indistinguishable from wild-type HERG. Elevating internal PIP2, however, no longer accelerated the activation kinetics of the mutant HERG. Moreover, PIP2-dependent hyperpolarizing shifts in the voltage dependence of activation were abolished with both mutants. PIP2 effects on channel-inactivation kinetics remained intact, which suggests an uncoupling of inactivation and activation regulation by PIP2. The specific binding of radiolabeled PIP2 to both mutant channel proteins was nearly abolished. Stimulation of α1A-adrenergic receptors produced a reduction in current amplitude of the rapidly activating delayed rectifier K+ current (the current carried by ERG protein) from rabbit ventricular myocytes. The α-adrenergic-induced current reduction was accentuated by PKC blockers and also unmasked a depolarizing shift in the voltage dependence of activation, which supports the conclusion that receptor activation of PLC results in PIP2 consumption that alters channel activity. These results support a physiological role for PIP2 regulation of the rapidly activating delayed rectifier K+ current during autonomic stimulation and localize a site of interaction to the COOH-terminal tail of the HERG K+ channel.

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42

Jeon, Eul-Hye, Ji-Hyeon Park, Jin-Hee Jeong, and Sung-Kwang Lee. "2D-QSAR analysis for hERG ion channel inhibitors." Analytical Science and Technology 24, no. 6 (December 25, 2011): 533–43. http://dx.doi.org/10.5806/ast.2011.24.6.533.

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43

Zhou, Wei, Francisco S. Cayabyab, Peter S. Pennefather, Lyanne C. Schlichter, and Thomas E. DeCoursey. "HERG-like K+ Channels in Microglia." Journal of General Physiology 111, no. 6 (June 1, 1998): 781–94. http://dx.doi.org/10.1085/jgp.111.6.781.

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A voltage-gated K+ conductance resembling that of the human ether-à-go-go-related gene product (HERG) was studied using whole-cell voltage-clamp recording, and found to be the predominant conductance at hyperpolarized potentials in a cell line (MLS-9) derived from primary cultures of rat microglia. Its behavior differed markedly from the classical inward rectifier K+ currents described previously in microglia, but closely resembled HERG currents in cardiac muscle and neuronal tissue. The HERG-like channels opened rapidly on hyperpolarization from 0 mV, and then decayed slowly into an absorbing closed state. The peak K+ conductance–voltage relation was half maximal at −59 mV with a slope factor of 18.6 mV. Availability, assessed by a hyperpolarizing test pulse from different holding potentials, was more steeply voltage dependent, and the midpoint was more positive (−14 vs. −39 mV) when determined by making the holding potential progressively more positive than more negative. The origin of this hysteresis is explored in a companion paper (Pennefather, P.S., W. Zhou, and T.E. DeCoursey. 1998. J. Gen. Physiol. 111:795–805). The pharmacological profile of the current differed from classical inward rectifier but closely resembled HERG. Block by Cs+ or Ba2+ occurred only at millimolar concentrations, La3+ blocked with Ki = ∼40 μM, and the HERG-selective blocker, E-4031, blocked with Ki = 37 nM. Implications of the presence of HERG-like K+ channels for the ontogeny of microglia are discussed.

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44

Luo, Ling, Peijing Hu, Changqing Miao, Aiqun Ma, and Tingzhong Wang. "Clenbuterol Attenuates hERG Channel by Promoting the Mature Channel Degradation." International Journal of Toxicology 36, no. 4 (May 24, 2017): 314–24. http://dx.doi.org/10.1177/1091581817710786.

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Clenbuterol, a β2-selective adrenergic receptor agonist, is illicitly used in weight loss and performance enhancement and animal production. Increasing evidence demonstrates that clenbuterol induces various kinds of arrhythmias and QTc interval prolongation. However, little is known about the underlying mechanism. Most drugs are associated with QTc prolongation through interfering with human ether-a-go-go-related gene (hERG) K+ channels. The present study aims to investigate the effects and underlying mechanisms of clenbuterol on the hERG channel. HEK 293 cells were transfected with wild type and Y652A or F656A mutants of the hERG channel and treated with clenbuterol. The hERG current was recorded using whole-cell patch-clamp technique, and protein level was evaluated by Western blot. We found that clenbuterol decreases the mature form of the hERG protein at the cell membrane in a concentration- and time-dependent manner, without affecting the immature form. Correspondingly, clenbuterol chronic treatment reduced hERG current to a greater extent compared to acute treatment. In the presence of Brefeldin A (BFA), which was used to block hERG channel trafficking to cell membrane, clenbuterol reduced hERG on plasma membrane to a greater extent than BFA alone. In addition, the hERG channel’s drug binding sites mutant Y652A and F656A abolished clenbuterol-mediated hERG reduction and current blockade. In conclusion, clenbuterol reduces hERG channel expression and current by promoting the channel degradation. The effect of clenbuterol on the hERG channel is related to the drug-binding sites, Tyr-652 and Phe-656, located on the S6 domain. This biophysical mechanism may underlie clenbuterol-induced QTc prolongation or arrhythmia.

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45

Wang, Ying, Xiaoyan Huang, Jianqing Zhou, Xi Yang, Di Li, Haiyan Mao, Huan Huan Sun, Ningsheng Liu, and Jiangfang Lian. "Trafficking-Deficient G572R-hERG and E637K-hERG Activate Stress and Clearance Pathways in Endoplasmic Reticulum." PLoS ONE 7, no. 1 (January 5, 2012): e29885. http://dx.doi.org/10.1371/journal.pone.0029885.

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46

Huo, Jianhua, Aifeng Zhang, Xueyan Guo, Hua Qiang, Ping Liu, Ling Bai, and Aiqun Ma. "Pharmacological rescue of hERG currents carried out by G604S and wide type hERG co-expression." Clinical and Experimental Pharmacology and Physiology 43, no. 9 (July 26, 2016): 851–61. http://dx.doi.org/10.1111/1440-1681.12593.

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47

Huang, Na, Jiang‑Fang Lian, Jian‑Hua Huo, Li‑Ying Liu, Lei Ni, Xi Yang, Jian‑Qing Zhou, Zong‑Fang Li, Tu‑Sheng Song, and Chen Huang. "The EGFP/hERG fusion protein alter the electrophysiological properties of hERG channels in HEK293 cells." Cell Biology International 35, no. 3 (January 26, 2011): 193–99. http://dx.doi.org/10.1042/cbi20100022.

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48

Crumb, William J., Slavica Milosavljev, and Sean Ekins. "Can more be done with hERG data? The correlation of hERG block and QT prolongation." Journal of Pharmacological and Toxicological Methods 66, no. 2 (September 2012): 170. http://dx.doi.org/10.1016/j.vascn.2012.08.038.

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49

Lin, Jijin, Shuguang Lin, Patrick C. Choy, Xiuzhang Shen, Chunyu Deng, Sujuan Kuang, Jun Wu, and Wencan Xu. "The regulation of the cardiac potassium channel (HERG) by caveolin-1." Biochemistry and Cell Biology 86, no. 5 (October 2008): 405–15. http://dx.doi.org/10.1139/o08-118.

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Protein–protein interaction plays a key role in the regulation of biological processes. The human potassium (HERG) channel is encoded by the ether-à-go-go-related gene (herg), and its activity may be regulated by association with other cellular proteins. To identify cellular proteins that might play a role in the regulation of the HERG channel, we screened a human heart cDNA library with the N terminus of HERG using a yeast 2-hybrid system, and identified caveolin-1 as a potential HERG partner. The interaction between these 2 proteins was confirmed by coimmunoprecipitation assay, and their overlapping subcellular localization was demonstrated by fluorescence immunocytochemistry. The physiologic implication of the protein–protein interaction was studied in whole-cell patch-clamp electrophysiology experiments. A significant increase in HERG current amplitude and a faster deactivation of tail current were observed in HEK293/HERG cells in a membrane lipid rafts disruption model and caveolin-1 knocked down cells by RNA interference. Alternatively, when caveolin-1 was overexpressed, the HERG current amplitude was significantly reduced and the tail current was deactivated more slowly. Taken together, these data indicate that HERG channels interact with caveolin-1 and are negatively regulated by this interaction. The finding from this study clearly demonstrates the regulatory role of caveolin-1 on HERG channels, and may help to understand biochemical events leading to arrhythmogenesis in the long QT syndrome in cardiac patients.

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Dennis, A., L. Wang, X. Wan, and E. Ficker. "hERG channel trafficking: novel targets in drug-induced long QT syndrome." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 1060–63. http://dx.doi.org/10.1042/bst0351060.

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Abstract:

The cardiac potassium channel hERG (human ether-a-go-go-related gene) encodes the α-subunit of the rapid delayed rectifier current IKr in the heart, which contributes to terminal repolarization in human cardiomyocytes. Direct block of hERG/IKr channels by a large number of therapeutic compounds produces acLQTS [acquired LQTS (long QT syndrome)] characterized by drug-induced QT prolongation and torsades de pointes arrhythmias. The cardiotoxicity associated with unintended hERG block has prompted pharmaceutical companies to screen developmental compounds for hERG blockade and made hERG a major target in drug safety programmes. More recently, a novel form of acLQTS has been discovered that may go undetected in most conventional safety assays. Several therapeutic compounds have been identified that reduce hERG/IKr currents not by direct block but by inhibition of hERG/IKr trafficking to the cell surface. Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant. Increased awareness of drug-induced hERG trafficking defects will help to further reduce the potentially lethal adverse cardiac events associated with acLQTS.

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