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51. Transient Receptor Potential channels (TRP) in GtoPdb v.2021.3

Author

Blair, Nathaniel T., primary, Carvacho, Ingrid, primary, Chaudhuri, Dipayan, primary, Clapham, David E., primary, DeCaen, Paul, primary, Delling, Markus, primary, Doerner, Julia F., primary, Fan, Lu, primary, Ha, Kotdaji, primary, Jordt, Sven E., primary, Julius, David, primary, Kahle, Kristopher T, primary, Liu, Boyi, primary, McKemy, David, primary, Nilius, Bernd, primary, Oancea, Elena, primary, Owsianik, Grzegorz, primary, Riccio, Antonio, primary, Sah, Rajan, primary, Stotz, Stephanie C., primary, Tian, Jinbin, primary, Tong, Dan, primary, Van den Eynde, Charlotte, primary, Vriens, Joris, primary, Wu, Long-Jun, primary, Xu, Haoxing, primary, Yue, Lixia, primary, Zhang, Xiaoli, primary, and Zhu, Michael X., primary

Published
2021
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55. Modulation of TRPM2 by acidic pH and the underlying mechanisms for pH sensitivity

Author

Du, Jianyang, Xie, Jia, and Yue, Lixia

Subjects
Calcium channels -- Properties, Hydrogen-ion concentration -- Physiological aspects, Biological sciences, Health
Abstract

TRPM2 is a [Ca.sup.2+]-permeable nonselective cation channel that plays important roles in oxidative stress-mediated cell death and inflammation processes. However, how TRPM2 is regulated under physiological and pathological conditions is not fully understood. Here, we report that both intracellular and extracellular protons block TRPM2 by inhibiting channel gating. We demonstrate that external protons block TRPM2 with an [IC.sub.50] of p[H.sub.o] = 5.3, whereas internal protons inhibit TRPM2 with an [IC.sub.50] of p[H.sub.i] = 6.7. Extracellular protons inhibit TRPM2 by decreasing single-channel conductance. We identify three titratable residues, H958, D964, and E994, at the outer vestibule of the channel pore that are responsible for p[H.sub.o] sensitivity. Mutations of these residues reduce single-channel conductance, decrease external [Ca.sup.2+] ([[[Ca.sup.2+]].sub.o]) affinity, and inhibit [[[Ca.sup.2+]].sub.o]-mediated TRPM2 gating. These results support the following model: titration of H958, D964, and E994 by external protons inhibits TRPM2 gating by causing conformation change of the channel, and/or by decreasing local [Ca.sup.2+] concentration at the outer vestibule, therefore reducing [[[Ca.sup.2+]].sub.o] permeation and inhibiting [[[Ca.sup.2+]].sub.o]-mediated TRPM2 gating. We find that intracellular protons inhibit TRPM2 by inducing channel closure without changing channel conductance. We identify that D933 located at the C terminus of the $4-$5 linker is responsible for intracellular pH sensitivity. Replacement of [Asp.sup.933] by [Asn.sup.933] changes the [IC.sub.50] from p[H.sub.i] = 6.7 to p[H.sub.i] = 5.5. Moreover, substitution of [Asp.sup.933] with various residues produces marked changes in proton sensitivity, intracellular ADP ribose/[Ca.sup.2+] sensitivity, and gating profiles of TRPM2. These results indicate that D933 is not only essential for intracellular pH sensitivity, but it is also crucial for TRPM2 channel gating. Collectively, our findings provide a novel mechanism for TRPM2 modulation as well as molecular determinants for pH regulation of TRPM2. Inhibition of TRPM2 by acidic pH may represent an endogenous mechanism governing TRPM2 gating and its physiological/pathological functions. doi/ 10.1085/jgp.200910254

Published
2009

56. THE CONCISE GUIDE TO PHARMACOLOGY 2019/20: G protein-coupled receptors

Author

Alexander, Stephen PH, Christopoulos, Arthur, Davenport, Anthony P, Kelly, Eamonn, Mathie, Alistair, Peters, John A, Veale, Emma L, Armstrong, Jane F, Faccenda, Elena, Harding, Simon D, Pawson, Adam J, Sharman, Joanna L, Southan, Christopher, Davies, Jamie A, Arumugam, Thiruma V, Bennett, Andrew, Sjogren, Benita, Sobey, Christopher, Wong, Szu Shen, Abbracchio, Maria P, Alexander, Wayne, Al-hosaini, Khaled, Back, Magnus, Beaulieu, Jean-Martin, Bernstein, Kenneth E, Bettler, Bernhard, Birdsall, Nigel JM, Blaho, Victoria, Bousquet, Corinne, Brauner-Osborne, Hans, Burnstock, Geoffrey, Calo, Girolamo, Castano, Justo P, Catt, Kevin J, Ceruti, Stefania, Chazot, Paul, Chiang, Nan, Chun, Jerold, Cianciulli, Antonia, Clapp, Lucie H, Couture, Rejean, Csaba, Zsolt, Dent, Gordon, Singh, Khuraijam Dhanachandra, Douglas, Steven D, Dournaud, Pascal, Eguchi, Satoru, Escher, Emanuel, Filardo, Edward, Fong, Tung M, Fumagalli, Marta, Gainetdinov, Raul R, de Gasparo, Marc, Gershengorn, Marvin, Gobeil, Fernand, Goodfriend, Theodore L, Goudet, Cyril, Gregory, Karen J, Gundlach, Andrew L, Hamann, Jorg, Hanson, Julien, Hauger, Richard L, Hay, Debbie, Heinemann, Akos, Hollenberg, Morley D, Holliday, Nicholas D, Horiuchi, Mastgugu, Hoyer, Daniel, Hunyady, Laszlo, Husain, Ahsan, Ijzerman, Adriaan P, Inagami, Tadashi, Jacobson, Kenneth A, Jensen, Robert T, Jockers, Ralf, Jonnalagadda, Deepa, Karnik, Sadashiva, Kaupmann, Klemens, Kemp, Jacqueline, Kennedy, Charles, Kihara, Yasuyuki, Kozielewicz, Pawel, Kreienkamp, Hans-Juergen, Kukkonen, Jyrki P, Langenhan, Tobias, Leach, Katie, Lecca, Davide, Lee, John D, Leeman, Susan E, Leprince, Jerome, Lolait, Stephen J, Lupp, Amelie, Macrae, Robyn, Maguire, Janet, Mazella, Jean, McArdle, Craig A, Melmed, Shlomo, Michel, Martin C, Miller, Laurence, Mitolo, Vincenzo, Mouillac, Bernard, Murphy, Philip M, Nahon, Jean-Louis, Norel, Xavier, Nyimanu, Duuamene, O'Carroll, Anne-Marie, Offermanns, Stefan, Panaro, Maria A, Pertwee, Roger G, Pin, Jean-Philippe, Prossnitz, Eric, Ramachandran, Rithwik, Reinscheid, Rainer K, Rondard, Philippe, Rovati, G Enrico, Ruzza, Chiara, Sanger, Gareth, Schoeneberg, Torsten, Schulte, Gunnar, Schulz, Stefan, Segaloff, Deborah L, Serhan, Charles N, Stoddart, Leigh A, Sugimoto, Yukihiko, Summers, Roger, Tan, Valerie, Thomas, Walter, Timmermans, Pieter BMWM, Tirupula, Kalyan, Tulipano, Giovanni, Unal, Hamiyet, Unger, Thomas, Vanderheyden, Patrick, Vaudry, David, Vaudry, Hubert, Vilardaga, Jean-Pierre, Walker, Christopher S, Ward, Donald T, Wester, Hans-Juergen, Willars, Gary B, Williams, Tom Lloyd, Woodruff, Trent M, Yao, Chengcan, Aldrich, Richard W, Becirovic, Elvir, Biel, Martin, Catterall, William A, Conner, Alex C, Davies, Paul, Delling, Markus, Di Virgilio, Francesco, Falzoni, Simonetta, George, Chandy, Goldstein, Steve AN, Grissmer, Stephan, Ha, Kotdaji, Hammelmann, Verena, Hanukoglu, Israel, Jarvis, Mike, Jensen, Anders A, Kaczmarek, Leonard K, Kellenberger, Stephan, King, Brian, Lynch, Joseph W, Perez-Reyes, Edward, Plant, Leigh D, Rash, Lachlan D, Ren, Dejian, Sivilotti, Lucia G, Smart, Trevor G, Snutch, Terrance P, Tian, Jinbin, Van den Eynde, Charlotte, Vriens, Joris, Wei, Aguan D, Winn, Brenda T, Wulff, Heike, Xu, Haoxing, Yue, Lixia, Zhang, Xiaoli, Zhu, Michael, Coons, Laurel, Fuller, Peter, Korach, Kenneth S, Young, Morag, Bryant, Clare, Farndale, Richard W, Hobbs, Adrian, Jarvis, Gavin E, MacEwan, David, Monie, Tom P, Waldman, Scott, Beuve, Annie, Boison, Detlev, Brouckaert, Peter, Burnett, John C, Burns, Kathryn, Dessauer, Carmen, Friebe, Andreas, Garthwaite, John, Gertsch, Jurg, Helsby, Nuala, Izzo, Angelo A, Koesling, Doris, Kuhn, Michaela, Ostrom, Rennolds, Papapetropoulos, Andreas, Potter, Lincoln R, Pyne, Nigel J, Pyne, Susan, Russwurm, Michael, Schmidt, Harald HHW, Seifert, Roland, Stasch, Johannes-Peter, Szabo, Csaba, van der Stelt, Mario, van der Vliet, Albert, Watts, Val, Anderson, Catriona MH, Broer, Stefan, Dawson, Paul, Hagenbuch, Bruno, Hammond, James R, Hancox, Jules, Inui, Ken-ichi, Kanai, Yoshikatsu, Kemp, Stephan, Thwaites, David T, Verri, Tiziano, University of Nottingham, UK (UON), Monash university, University of Cambridge [UK] (CAM), University of Bristol [Bristol], University of Greenwich, Ninewells Hospital and Medical School [Dundee], University of Edinburgh, Institut de Génomique Fonctionnelle (IGF), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier), Institut de médecine moléculaire de Rangueil (I2MR), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Drug Design and Pharmacology [Copenhagen] (ILF), Faculty of Health and Medical Sciences, University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), University of Córdoba [Córdoba], Neuroprotection du Cerveau en Développement / Promoting Research Oriented Towards Early Cns Therapies (PROTECT), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Robert Debré-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Novartis Institutes for BioMedical Research (NIBR), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Différenciation et communication neuronale et neuroendocrine (DC2N), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), ARVALIS - Institut du végétal [Paris], Laboratoire de Recherche Vasculaire Translationnelle (LVTS (UMR_S_1148 / U1148)), Université Paris 13 (UP13)-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Max Planck Institute for Heart and Lung Research (MPI-HLR), Max-Planck-Gesellschaft, Glaxo Smith Kline [Harlow], University of Antwerp (UA), Neuroendocrinologie cellulaire et moléculaire, European Synchrotron Radiation Facility (ESRF), Experimental Medicine and Immunotherapeutics [Cambridge, UK], Department of Pharmacology and Toxicology, College of Pharmacy, King Saud University [Riyadh] (KSU), Department of Cardiology, Karolinska University Hospital, Karolinska Institutet [Stockholm], Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Department of Medical Sciences, Università degli Studi di Ferrara (UniFE), Department of Pharmacological Sciences and Biomolecular, University of Milan, Department of Molecular Biology Helen L. Dorris, The Scripps Research Institute, Département de Physiologie, Université de Montréal (UdeM), Department of Pharmacology, Université de Sherbrooke (UdeS), Departments of Physiology & Pharmacology, and Medicine [Calgary, Canada] (School of Medicine), University of Calgary, Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Université Côte d'Azur (UCA), Université Paris Diderot - Paris 7 (UPD7)-Université Paris 13 (UP13)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institute of Biochemistry, Medical Faculty, University of Leipzig, Department of Molecular and Biochemical Pharmacology, and Pleinlaan 2

Subjects
0301 basic medicine, RM, Databases, Pharmaceutical, Computer science, Drug classification, Pharmacology, Ligands, Receptors, G-Protein-Coupled, NO, law.invention, 03 medical and health sciences, Databases, G-Protein-Coupled, 0302 clinical medicine, law, Summary information, Receptors, Animals, Humans, Pharmacology & Pharmacy, The Concise Guide to Pharmacology 2019/20, ComputingMilieux_MISCELLANEOUS, G protein-coupled receptor, Clinical pharmacology, Science & Technology, Extramural, POTENT, Pharmaceutical Preparations, 3. Good health, 030104 developmental biology, Pharmaceutical, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Catalytic receptors, Life Sciences & Biomedicine, 030217 neurology & neurosurgery
Abstract

© 2019 The Authors. British Journal of Pharmacology published by John Wiley & Sons Ltd on behalf of The British Pharmacological Society. The Concise Guide to PHARMACOLOGY 2019/20 is the fourth in this series of biennial publications. The Concise Guide provides concise overviews of the key properties of nearly 1800 human drug targets with an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide represents approximately 400 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.14748. G protein-coupled receptors are one of the six major pharmacological targets into which the Guide is divided, with the others being: ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2019, and supersedes data presented in the 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the International Union of Basic and Clinical Pharmacology Committee on Receptor Nomenclature and Drug Classification (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.

Published
2019

58. Functional characterization of homo- and heteromeric channel kinases TRPM6 and TRPM7

Author

Li, Mingjiang, Jiang, Jianmin, and Yue, Lixia

Subjects
Homeostasis -- Research, Ion channels -- Research, Biological sciences, Health
Abstract

TRPM6 and TRPM7 are two known channel kinases that play important roles in various physiological processes, including [Mg.sup.2+] homeostasis. Mutations in TRPM6 cause hereditary hypomagnesemia and secondary hypocalcemia (HSH). However, whether TRPM6 encodes functional channels is controversial. Here we demonstrate several signature features of TRPM6 that distinguish TRPM6 from TRPM7 and TRPM6/7 channels. We show that heterologous expression of TRPM6 but not the mutant TRPM[6.sup.S141L] produces functional channels with divalent cation permeability profile and pH sensitivity distinctive from those of TRPM7 channels and TRPM6/7 complexes. TRPM6 exhibits unique unitary conductance that is 2- and 1.5-fold bigger than that of TRPM7 and TRPM6/7. Moreover, micromolar levels of 2-aminoethoxydiphenyl borate (2-APB) maximally increase TRPM6 but significantly inhibit TRPM7 channel activities; whereas millimolar concentrations of 2-APB potentiate TRPM6/7 and TRPM7 channel activities. Furthermore, [Mg.sup.2+] and [Ca.sup.2+] entry through TRPM6 is enhanced three- to fourfold by 2-APB. Collectively, these results indicate that TRPM6 forms functional homomeric channels as well as heteromeric TRPM6/7 complexes. The unique characteristics of these three channel types, TRPM6, TRPM7, and TRPM6/7, suggest that they may play different roles in vivo.

Published
2006

59. Potentiation of TRPM7 inward currents by protons

Author

Jiang, Jianmin, Li, Mingjiang, and Yue, Lixia

Subjects
Physiology -- Research, Protein kinases -- Research, Protein kinases -- Physiological aspects, Ion channels -- Research, Ion channels -- Physiological aspects, Biological sciences, Health
Abstract

TRPM7 is unique in being both an ion channel and a protein kinase. It conducts a large outward current at + 100 mV but a small inward current at voltages ranging from--100 to -40 mV under physiological ionic conditions. Here we show that the small inward current of TRPM7 was dramatically enhanced by a decrease in extracellular pH, with an ~10-fold increase at pH 4.0 and 1-2-fold increase at pH 6.0. Several lines of evidence suggest that protons enhance TRPM7 inward currents by competing with [Ca.sup.2+] and [Mg.sup.2+] for binding sites, thereby releasing blockade of divalent cations on inward monovalent currents. First, extracellular protons significantly increased monovalent cation permeability. Second, higher proton concentrations were required to induce 50% of maximal increase in TRPM7 currents when the external [Ca.sup.2+] and [Mg.sup.2+ concentrations were increased. Third, the apparent] affinity for [Ca.sup.2+] and [Mg.sup.2+] was significantly diminished at elevated external [H.sup.+] concentrations. Fourth, the anomalous-mole fraction behavior of [H.sup.+] permeation further suggests that protons compete with divalent cations for binding sites in the TRPM7 pore. Taken together, it appears that at physiological pH (7.4), [Ca.sup.2+] and [Mg.sup.2+] bind to TRPM7 and inhibit the monovalent cationic currents; whereas at high [H.sup.+] concentrations, the affinity of TRPM7 for [Ca.sup.2+] and [Mg.sup.2+] is decreased, thereby allowing monovalent cations to pass through TRPM7. Furthermore, we showed that the endogenous TRPM7-like current, which is known as [Mg.sup.2+]-inhibitable cation current (MIC) or Mg nucleotide--regulated metal ion current (MagNuM) in rat basophilic leukemia (RBL) cells was also significantly potentiated by acidic pH, suggesting that MIC/MagNuM is encoded by TRPM7. The pH sensitivity represents a novel feature of TRPM7 and implies that TRPM7 may play a role under acidic pathological conditions.

Published
2005

61. The cation selectivity filter of the bacterial sodium channel, NaChBac

Author

Yue, Lixia, Navarro, Betsy, Ren, Dejian, Ramos, Arnolt, and Clapham, David E.

Subjects
Cations -- Physiological aspects, Sodium channels -- Physiological aspects, Bacillus (Bacteria) -- Physiological aspects, Biological sciences, Health
Abstract

The Bacillus halodurans voltage-gated sodium-selective channel (NaChBac) (Ren, D., B. Navarro, H. Xu, L. Yue, Q. Shi, and D.E. Clapham. 200lb. Science. 294:2372-2375), is an ideal candidate for high resolution structural studies because it can be expressed in mammalian cells and its functional properties studied in detail. It has the added advantage of being a single six transmembrane (6TM) orthologue of a single repeat of mammalian voltage-gated [Ca.sup.2+] (Cav) and [Na.sub.+] (Nav) channels. Here we report that six amino acids in the pore domain (LESWAS) participate in the selectivity filter. Replacing the amino acid residues adjacent to glutamatic acid (E) by a negatively charged aspartate (D; LEDWAS) converted the [Na.sub.+]-selective NaChBac to a [Ca.sup.2+]- and [Na.sub.+]-permeant channel. When additional aspartates were incorporated (LDDWAD), the mutant channel resulted in a highly expressing voltage-gated [Ca.sup.2+]-selective conductance. KEY WORDS: bacterial channels * calcium channels * sodium channels * ion/membrane channel

Published
2002

62. CaT1 manifests the pore properties of the calcium-release-activated calcium channel

Author

Yue, Lixia, Peng, Ji-Bin, Hediger, Matthias A., and Clapham, David E.

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Lixia Yue [1]; Ji-Bin Peng [2]; Matthias A. Hediger [2]; David E. Clapham (corresponding author) [1, 3] The calcium-release-activated Ca[sup.2+] channel, I [sub.CRAC] [1, 2, 3], is a highly [...]

Published
2001
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65. Biodegradable nanofiber-based piezoelectric transducer

Author

Curry, Eli J., primary, Le, Thinh T., additional, Das, Ritopa, additional, Ke, Kai, additional, Santorella, Elise M., additional, Paul, Debayon, additional, Chorsi, Meysam T., additional, Tran, Khanh T. M., additional, Baroody, Jeffrey, additional, Borges, Emily R., additional, Ko, Brian, additional, Golabchi, Asiyeh, additional, Xin, Xiaonan, additional, Rowe, David, additional, Yue, Lixia, additional, Feng, Jianlin, additional, Morales-Acosta, M. Daniela, additional, Wu, Qian, additional, Chen, I-Ping, additional, Cui, X. Tracy, additional, Pachter, Joel, additional, and Nguyen, Thanh D., additional

Published
2019
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67. Transient Receptor Potential channels (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

Author

Blair, Nathaniel T., primary, Carvacho, Ingrid, primary, Chaudhuri, Dipayan, primary, Clapham, David E., primary, DeCaen, Paul, primary, Delling, Markus, primary, Doerner, Julia F., primary, Fan, Lu, primary, Ha, Kotdaji, primary, Jordt, Sven E., primary, Julius, David, primary, Kahle, Kristopher T, primary, Liu, Boyi, primary, McKemy, David, primary, Nilius, Bernd, primary, Oancea, Elena, primary, Owsianik, Grzegorz, primary, Riccio, Antonio, primary, Sah, Rajan, primary, Stotz, Stephanie C., primary, Tian, Jinbin, primary, Tong, Dan, primary, Van den Eynde, Charlotte, primary, Vriens, Joris, primary, Wu, Long-Jun, primary, Xu, Haoxing, primary, Yue, Lixia, primary, Zhang, Xiaoli, primary, and Zhu, Michael X., primary

Published
2019
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68. Transmural heterogeneity of action potentials and I(sub to1) in myocytes isolated from the human right ventricle

Author

Li, Gui-Rong, Feng, Jianlin, Yue, Lixia, and Carrier, Michel

Subjects
Heart ventricle, Right -- Research, Heart cells -- Research, Muscle cells -- Research, Biological sciences
Abstract

Research was conducted to examine the transmural heterogeneity of action potentials and I(sub to1) in myocytes isolated from the human right ventricle. Results reveal that M cells are present in the right ventricle in humans and that a gradient of I(sub to1) is present in cells across the human right ventricular wall from the endocardium to the epicardium. Findings show important transmural heterogeneity in the action potential and I(sub to1) properties pointing to an important clinical implication in human cardiac electrophysiology.

Published
1998

69. Transient outward and delayed rectifier currents in canine atrium: properties and role of isolation methods

Author

Yue, Lixia, Feng, Jianlin, Li, Gui-Rong, and Nattel, Stanley

Subjects
Potassium channels -- Observations, Chloride channels -- Observations, Atriums -- Research, Electrophysiology -- Analysis, Dogs as laboratory animals -- Usage, Biological sciences
Abstract

Isolation of cells by chunk and perfusion methods reveals that the transient outward K+ current, (Ito1), Ca2+ dependent Cl- current, (Ito2), and the delayed rectifier K+ current, (Ik), are found in the dog atrium. Ik is more sensitive to the isolation method than Ito1 or Ito2. The properties of Ito1 and Ik repolarizing currents of the dog atrium are similar to those in the human atrium. These studies help in the in vivo and in vitro analysis of canine atrial electrophysiology.

Published
1996

76. Recapitulating and Correcting Marfan Syndrome in a Cellular Model

Author

Park, Jung Woo, primary, Yan, Li, additional, Stoddard, Chris, additional, Wang, Xiaofang, additional, Yue, Zhichao, additional, Crandall, Leann, additional, Robinson, Tiwanna, additional, Chang, Yuxiao, additional, Denton, Kyle, additional, Li, Enqin, additional, Jiang, Bin, additional, Zhang, Zhenwu, additional, Martins-Taylor, Kristen, additional, Yee, Siu-Pok, additional, Nie, Hong, additional, Gu, Feng, additional, Si, Wei, additional, Xie, Ting, additional, Yue, Lixia, additional, and Xu, Ren-He, additional

Published
2017
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77. An Isogenic Human ESC Platform for Functional Evaluation of Genome-wide-Association-Study-Identified Diabetes Genes and Drug Discovery

Author

Zeng, Hui, primary, Guo, Min, additional, Zhou, Ting, additional, Tan, Lei, additional, Chong, Chi Nok, additional, Zhang, Tuo, additional, Dong, Xue, additional, Xiang, Jenny Zhaoying, additional, Yu, Albert S., additional, Yue, Lixia, additional, Qi, Qibin, additional, Evans, Todd, additional, Graumann, Johannes, additional, and Chen, Shuibing, additional

Published
2016
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78. Caspase‐1 P20 Fragment, a Marker for Inflammasome Activation, is Elevated in Serum of Patients during Myocardial Infarction

Author

Morgan, Andrew, primary, Liang, Bruce, additional, Chen, Kai, additional, Na, Doohwan, additional, Gold, Courtney, additional, Azrin, Michael, additional, Lee, JuYong, additional, Schumacher, Jayne, additional, Yue, Lixia, additional, Aguila, Hector Leonardo, additional, Shapiro, Linda, additional, Tate, Janet, additional, and Protas, Matthew, additional

Published
2016
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87. Modeling Supravalvular Aortic Stenosis Syndrome With Human Induced Pluripotent Stem Cells

Author

Ge, Xin, primary, Ren, Yongming, additional, Bartulos, Oscar, additional, Lee, Min Young, additional, Yue, Zhichao, additional, Kim, Kun-Yong, additional, Li, Wei, additional, Amos, Peter J., additional, Bozkulak, Esra Cagavi, additional, Iyer, Amulya, additional, Zheng, Wei, additional, Zhao, Hongyu, additional, Martin, Kathleen A., additional, Kotton, Darrell N., additional, Tellides, George, additional, Park, In-Hyun, additional, Yue, Lixia, additional, and Qyang, Yibing, additional

Published
2012
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94. American Heart Association Atrial Fibrillation Research Summit

Author

Estes, N.A. Mark, primary, Sacco, Ralph L., additional, Al-Khatib, Sana M., additional, Ellinor, Patrick T., additional, Bezanson, Judy, additional, Alonso, Alvaro, additional, Antzelevitch, Charles, additional, Brockman, Randall G., additional, Chen, Peng-Sheng, additional, Chugh, Sumeet S., additional, Curtis, Anne B., additional, DiMarco, John P., additional, Ellenbogen, Kenneth A., additional, Epstein, Andrew E., additional, Ezekowitz, Michael D., additional, Fayad, Pierre, additional, Gage, Brian F., additional, Go, Alan S., additional, Hlatky, Mark A., additional, Hylek, Elaine M., additional, Jerosch-Herold, Michael, additional, Konstam, Marvin A., additional, Lee, Richard, additional, Packer, Douglas L., additional, Po, Sunny S., additional, Prystowsky, Eric N., additional, Redline, Susan, additional, Rosenberg, Yves, additional, Van Wagoner, David R., additional, Wood, Kathryn A., additional, Yue, Lixia, additional, and Benjamin, Emelia J., additional

Published
2011
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95. Specification of Region-Specific Neurons Including Forebrain Glutamatergic Neurons from Human Induced Pluripotent Stem Cells

Author

Zeng, Hui, primary, Guo, Min, additional, Martins-Taylor, Kristen, additional, Wang, Xiaofang, additional, Zhang, Zheng, additional, Park, Jung Woo, additional, Zhan, Shuning, additional, Kronenberg, Mark S., additional, Lichtler, Alexander, additional, Liu, Hui-Xia, additional, Chen, Fang-Ping, additional, Yue, Lixia, additional, Li, Xue-Jun, additional, and Xu, Ren-He, additional

Published
2010
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100. A Novel TRPC6 Mutation That Causes Childhood FSGS

Author

Heeringa, Saskia F., primary, Möller, Clemens C., additional, Du, Jianyang, additional, Yue, Lixia, additional, Hinkes, Bernward, additional, Chernin, Gil, additional, Vlangos, Christopher N., additional, Hoyer, Peter F., additional, Reiser, Jochen, additional, and Hildebrandt, Friedhelm, additional

Published
2009
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