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Research Article Microarray-Based Comparisons of Ion Channel Expression Patterns: Human Keratinocytes to Reprogrammed Hipscs To
Hindawi Publishing Corporation Stem Cells International Volume 2013, Article ID 784629, 25 pages http://dx.doi.org/10.1155/2013/784629 Research Article Microarray-Based Comparisons of Ion Channel Expression Patterns: Human Keratinocytes to Reprogrammed hiPSCs to Differentiated Neuronal and Cardiac Progeny Leonhard Linta,1 Marianne Stockmann,1 Qiong Lin,2 André Lechel,3 Christian Proepper,1 Tobias M. Boeckers,1 Alexander Kleger,3 and Stefan Liebau1 1 InstituteforAnatomyCellBiology,UlmUniversity,Albert-EinsteinAllee11,89081Ulm,Germany 2 Institute for Biomedical Engineering, Department of Cell Biology, RWTH Aachen, Pauwelstrasse 30, 52074 Aachen, Germany 3 Department of Internal Medicine I, Ulm University, Albert-Einstein Allee 11, 89081 Ulm, Germany Correspondence should be addressed to Alexander Kleger; [email protected] and Stefan Liebau; [email protected] Received 31 January 2013; Accepted 6 March 2013 Academic Editor: Michael Levin Copyright © 2013 Leonhard Linta et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Ion channels are involved in a large variety of cellular processes including stem cell differentiation. Numerous families of ion channels are present in the organism which can be distinguished by means of, for example, ion selectivity, gating mechanism, composition, or cell biological function. To characterize the distinct expression of this group of ion channels we have compared the mRNA expression levels of ion channel genes between human keratinocyte-derived induced pluripotent stem cells (hiPSCs) and their somatic cell source, keratinocytes from plucked human hair. This comparison revealed that 26% of the analyzed probes showed an upregulation of ion channels in hiPSCs while just 6% were downregulated. -
Stem Cells and Ion Channels
Stem Cells International Stem Cells and Ion Channels Guest Editors: Stefan Liebau, Alexander Kleger, Michael Levin, and Shan Ping Yu Stem Cells and Ion Channels Stem Cells International Stem Cells and Ion Channels Guest Editors: Stefan Liebau, Alexander Kleger, Michael Levin, and Shan Ping Yu Copyright © 2013 Hindawi Publishing Corporation. All rights reserved. This is a special issue published in “Stem Cells International.” All articles are open access articles distributed under the Creative Com- mons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Editorial Board Nadire N. Ali, UK Joseph Itskovitz-Eldor, Israel Pranela Rameshwar, USA Anthony Atala, USA Pavla Jendelova, Czech Republic Hannele T. Ruohola-Baker, USA Nissim Benvenisty, Israel Arne Jensen, Germany D. S. Sakaguchi, USA Kenneth Boheler, USA Sue Kimber, UK Paul R. Sanberg, USA Dominique Bonnet, UK Mark D. Kirk, USA Paul T. Sharpe, UK B. Bunnell, USA Gary E. Lyons, USA Ashok Shetty, USA Kevin D. Bunting, USA Athanasios Mantalaris, UK Igor Slukvin, USA Richard K. Burt, USA Pilar Martin-Duque, Spain Ann Steele, USA Gerald A. Colvin, USA EvaMezey,USA Alexander Storch, Germany Stephen Dalton, USA Karim Nayernia, UK Marc Turner, UK Leonard M. Eisenberg, USA K. Sue O’Shea, USA Su-Chun Zhang, USA Marina Emborg, USA J. Parent, USA Weian Zhao, USA Josef Fulka, Czech Republic Bruno Peault, USA Joel C. Glover, Norway Stefan Przyborski, UK Contents Stem Cells and Ion Channels, Stefan Liebau, -
Ion Channels
UC Davis UC Davis Previously Published Works Title THE CONCISE GUIDE TO PHARMACOLOGY 2019/20: Ion channels. Permalink https://escholarship.org/uc/item/1442g5hg Journal British journal of pharmacology, 176 Suppl 1(S1) ISSN 0007-1188 Authors Alexander, Stephen PH Mathie, Alistair Peters, John A et al. Publication Date 2019-12-01 DOI 10.1111/bph.14749 License https://creativecommons.org/licenses/by/4.0/ 4.0 Peer reviewed eScholarship.org Powered by the California Digital Library University of California S.P.H. Alexander et al. The Concise Guide to PHARMACOLOGY 2019/20: Ion channels. British Journal of Pharmacology (2019) 176, S142–S228 THE CONCISE GUIDE TO PHARMACOLOGY 2019/20: Ion channels Stephen PH Alexander1 , Alistair Mathie2 ,JohnAPeters3 , Emma L Veale2 , Jörg Striessnig4 , Eamonn Kelly5, Jane F Armstrong6 , Elena Faccenda6 ,SimonDHarding6 ,AdamJPawson6 , Joanna L Sharman6 , Christopher Southan6 , Jamie A Davies6 and CGTP Collaborators 1School of Life Sciences, University of Nottingham Medical School, Nottingham, NG7 2UH, UK 2Medway School of Pharmacy, The Universities of Greenwich and Kent at Medway, Anson Building, Central Avenue, Chatham Maritime, Chatham, Kent, ME4 4TB, UK 3Neuroscience Division, Medical Education Institute, Ninewells Hospital and Medical School, University of Dundee, Dundee, DD1 9SY, UK 4Pharmacology and Toxicology, Institute of Pharmacy, University of Innsbruck, A-6020 Innsbruck, Austria 5School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, BS8 1TD, UK 6Centre for Discovery Brain Science, University of Edinburgh, Edinburgh, EH8 9XD, UK Abstract 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. -
Grid1 Regulates the Onset of Puberty in Female Rats
Grid1 Regulates the Onset of Puberty in Female Rats Jing Ye Anhui Agricultural University Ping Qin Anhui Agricultural University Hailing Li Anhui Agricultural University Tiezhu Kang Anhui Agricultural University Wenyu Si Anhui Agricultural University Zhiqiu Yao Anhui Agricultural University Ya Liu Anhui Agricultural University Tong Yu Anhui Agricultural University Yunhai Zhang Anhui Agricultural University Yinghui Ling Anhui Agricultural University Hongguo Cao Anhui Agricultural University Juhua Wang Anhui Agricultural University Yunsheng Li Anhui Agricultural University Fugui Fang ( [email protected] ) Anhui Agricultural University https://orcid.org/0000-0002-3203-6687 Research Keywords: GnRH, Grid1, puberty, rat, RFRP 3 Page 1/21 Posted Date: December 29th, 2020 DOI: https://doi.org/10.21203/rs.3.rs-134074/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 2/21 Abstract The present study aimed to investigate whether Grid1, encoding the glutamate ionotropic receptor delta type subunit 1(GluD1), inuences the onset of puberty in female rats. First, we detected the expression of Grid1 mRNA and its protein in the hypothalamus from infancy to puberty. Second, we evaluated the suppression of Grid1 expression by Lentivirus-Grid1 (LV-Grid1) in primary hypothalamus cells through measuring the expression level of Grid1. Finally, LV-Grid1 was intracerebroventricular injected (ICV) into 21-day-old rats and to investigate the effect of Grid1 suppression on puberty onset in vivo. Results showed that GluD1 immunoreactivity could be detected in the arcuate nucleus (ARC), paraventricular nucleus (PVN), and periventricular nucleus (PeN). Grid1 mRNA levels were the lowest at prepuberty. Treatment of hypothalamic neurons with LV-Grid1 decreased the mRNA expression levels of Grid1 and Rfrp-3 (encoding RFamide-related peptide 3, RFRP 3), but increased that of Gnrh (encoding gonadotropin- releasing hormone, GnRH). -
The Glutamate Receptor Ion Channels
0031-6997/99/5101-0007$03.00/0 PHARMACOLOGICAL REVIEWS Vol. 51, No. 1 Copyright © 1999 by The American Society for Pharmacology and Experimental Therapeutics Printed in U.S.A. The Glutamate Receptor Ion Channels RAYMOND DINGLEDINE,1 KARIN BORGES, DEREK BOWIE, AND STEPHEN F. TRAYNELIS Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia This paper is available online at http://www.pharmrev.org I. Introduction ............................................................................. 8 II. Gene families ............................................................................ 9 III. Receptor structure ...................................................................... 10 A. Transmembrane topology ............................................................. 10 B. Subunit stoichiometry ................................................................ 10 C. Ligand-binding sites located in a hinged clamshell-like gorge............................. 13 IV. RNA modifications that promote molecular diversity ....................................... 15 A. Alternative splicing .................................................................. 15 B. Editing of AMPA and kainate receptors ................................................ 17 V. Post-translational modifications .......................................................... 18 A. Phosphorylation of AMPA and kainate receptors ........................................ 18 B. Serine/threonine phosphorylation of NMDA receptors .................................. -
The Concise Guide to PHARMACOLOGY 2015/16
Edinburgh Research Explorer The Concise Guide to PHARMACOLOGY 2015/16 Citation for published version: CGTP Collaborators, Alexander, SP, Peters, JA, Kelly, E, Marrion, N, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C & Davies, JA 2015, 'The Concise Guide to PHARMACOLOGY 2015/16: Ligand-gated ion channels', British Journal of Pharmacology, vol. 172, no. 24, pp. 5870-5903. https://doi.org/10.1111/bph.13350 Digital Object Identifier (DOI): 10.1111/bph.13350 Link: Link to publication record in Edinburgh Research Explorer Document Version: Publisher's PDF, also known as Version of record Published In: British Journal of Pharmacology General rights Copyright for the publications made accessible via the Edinburgh Research Explorer is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Take down policy The University of Edinburgh has made every reasonable effort to ensure that Edinburgh Research Explorer content complies with UK legislation. If you believe that the public display of this file breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim. Download date: 05. Oct. 2021 S.P.H. Alexander et al. The Concise Guide to PHARMACOLOGY 2015/16: Ligand-gated ion channels. British Journal of Pharmacology (2015) 172, 5870–5903 THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Ligand-gated ion channels Stephen -
The Identification and Functional Implications of Human-Specific
BMC Evolutionary Biology BioMed Central Research article Open Access The identification and functional implications of human- specific "fixed" amino acid substitutions in the glutamate receptor family Hiroki Goto1, Kazunori Watanabe1, Naozumi Araragi1, Rui Kageyama1, Kunika Tanaka1, Yoko Kuroki3, Atsushi Toyoda4, Masahira Hattori5, Yoshiyuki Sakaki2, Asao Fujiyama2,6, Yasuyuki Fukumaki*1 and Hiroki Shibata1 Address: 1Division of Human Moelcular Genetics, Research Center for Genetic Information, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan, 2RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan, 3RIKEN Advanced Science Institute (ASI), Advanced Computational Sciences Department, Computational Systems Biology Research Group, Synthetic Biology Team, Suehiro-cho 1-7-22, Tsurumi-ku, Yokohama, Kanagawa, Japan, 4Comparative Genomics Laboratory, National Institute of Genetics, Yata 1111, Mishima, Shizuoka 411-8540, Japan, 5Graduate School of Frontier Sciences, University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8561, Japan and 6National Institute of Informatics, 2-1-2 Hitotsubashi, Chiyoda-ku, Tokyo, 101-8430, Japan Email: Hiroki Goto - [email protected]; Kazunori Watanabe - [email protected]; Naozumi Araragi - naozumi.araragi@uni- wuerzburg.de; Rui Kageyama - [email protected]; Kunika Tanaka - [email protected]; Yoko Kuroki - [email protected]; Atsushi Toyoda - [email protected]; Masahira Hattori - [email protected]; Yoshiyuki Sakaki - [email protected]; Asao Fujiyama - [email protected]; Yasuyuki Fukumaki* - [email protected]; Hiroki Shibata - [email protected] * Corresponding author Published: 8 September 2009 Received: 14 November 2008 Accepted: 8 September 2009 BMC Evolutionary Biology 2009, 9:224 doi:10.1186/1471-2148-9-224 This article is available from: http://www.biomedcentral.com/1471-2148/9/224 © 2009 Goto et al; licensee BioMed Central Ltd. -
1 Probing the Ionotropic Activity of the Orphan Glutamate Delta 2 Receptor With
bioRxiv preprint doi: https://doi.org/10.1101/2020.05.14.093419; this version posted May 15, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 Probing the ionotropic activity of the orphan glutamate delta 2 receptor with 2 genetically-engineered photopharmacology. 3 4 5 6 Damien Lemoine1, Sarah Mondoloni1, Jérôme Tange1, Bertrand Lambolez1, Philippe 7 Faure1, Antoine Taly2,3*, Ludovic Tricoire1* and Alexandre Mourot1*. 8 9 10 1 Neuroscience Paris Seine - Institut de Biologie Paris Seine (NPS - IBPS), CNRS, 11 INSERM, Sorbonne Université, Paris, France 12 2 CNRS, Université de Paris, UPR 9080, Laboratoire de Biochimie Théorique, UPR 13 9080, 13 rue Pierre et Marie Curie, F-75005, Paris, France 14 3 Institut de Biologie Physico-Chimique-Fondation Edmond de Rothschild, PSL 15 Research University, Paris, France 16 * Equal contribution 17 18 19 Correspondence to: [email protected] ; [email protected] 20 21 22 23 Keywords: optogenetics, photopharmacology, Glutamate receptors, tethered ligands, 24 ion channels, azobenzene 25 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.05.14.093419; this version posted May 15, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 26 Abstract 27 Glutamate delta (GluD) receptors belong to the ionotropic glutamate receptor family, 28 yet whether they actually form functional and physiologically-relevant ion channels in 29 neurons remains a debated question. Here we used a chemo-genetic approach to 30 engineer specific and photo-reversible pharmacology in the orphan GluD2 receptor. -
Detection of H3k4me3 Identifies Neurohiv Signatures, Genomic
viruses Article Detection of H3K4me3 Identifies NeuroHIV Signatures, Genomic Effects of Methamphetamine and Addiction Pathways in Postmortem HIV+ Brain Specimens that Are Not Amenable to Transcriptome Analysis Liana Basova 1, Alexander Lindsey 1, Anne Marie McGovern 1, Ronald J. Ellis 2 and Maria Cecilia Garibaldi Marcondes 1,* 1 San Diego Biomedical Research Institute, San Diego, CA 92121, USA; [email protected] (L.B.); [email protected] (A.L.); [email protected] (A.M.M.) 2 Departments of Neurosciences and Psychiatry, University of California San Diego, San Diego, CA 92103, USA; [email protected] * Correspondence: [email protected] Abstract: Human postmortem specimens are extremely valuable resources for investigating trans- lational hypotheses. Tissue repositories collect clinically assessed specimens from people with and without HIV, including age, viral load, treatments, substance use patterns and cognitive functions. One challenge is the limited number of specimens suitable for transcriptional studies, mainly due to poor RNA quality resulting from long postmortem intervals. We hypothesized that epigenomic Citation: Basova, L.; Lindsey, A.; signatures would be more stable than RNA for assessing global changes associated with outcomes McGovern, A.M.; Ellis, R.J.; of interest. We found that H3K27Ac or RNA Polymerase (Pol) were not consistently detected by Marcondes, M.C.G. Detection of H3K4me3 Identifies NeuroHIV Chromatin Immunoprecipitation (ChIP), while the enhancer H3K4me3 histone modification was Signatures, Genomic Effects of abundant and stable up to the 72 h postmortem. We tested our ability to use H3K4me3 in human Methamphetamine and Addiction prefrontal cortex from HIV+ individuals meeting criteria for methamphetamine use disorder or not Pathways in Postmortem HIV+ Brain (Meth +/−) which exhibited poor RNA quality and were not suitable for transcriptional profiling. -
Genome-Wide Gene Expression Profiling of Randall's Plaques In
CLINICAL RESEARCH www.jasn.org Genome-Wide Gene Expression Profiling of Randall’s Plaques in Calcium Oxalate Stone Formers † † Kazumi Taguchi,* Shuzo Hamamoto,* Atsushi Okada,* Rei Unno,* Hideyuki Kamisawa,* Taku Naiki,* Ryosuke Ando,* Kentaro Mizuno,* Noriyasu Kawai,* Keiichi Tozawa,* Kenjiro Kohri,* and Takahiro Yasui* *Department of Nephro-urology, Nagoya City University Graduate School of Medical Sciences, Nagoya, Japan; and †Department of Urology, Social Medical Corporation Kojunkai Daido Hospital, Daido Clinic, Nagoya, Japan ABSTRACT Randall plaques (RPs) can contribute to the formation of idiopathic calcium oxalate (CaOx) kidney stones; however, genes related to RP formation have not been identified. We previously reported the potential therapeutic role of osteopontin (OPN) and macrophages in CaOx kidney stone formation, discovered using genome-recombined mice and genome-wide analyses. Here, to characterize the genetic patho- genesis of RPs, we used microarrays and immunohistology to compare gene expression among renal papillary RP and non-RP tissues of 23 CaOx stone formers (SFs) (age- and sex-matched) and normal papillary tissue of seven controls. Transmission electron microscopy showed OPN and collagen expression inside and around RPs, respectively. Cluster analysis revealed that the papillary gene expression of CaOx SFs differed significantly from that of controls. Disease and function analysis of gene expression revealed activation of cellular hyperpolarization, reproductive development, and molecular transport in papillary tissue from RPs and non-RP regions of CaOx SFs. Compared with non-RP tissue, RP tissue showed upregulation (˃2-fold) of LCN2, IL11, PTGS1, GPX3,andMMD and downregulation (0.5-fold) of SLC12A1 and NALCN (P,0.01). In network and toxicity analyses, these genes associated with activated mitogen- activated protein kinase, the Akt/phosphatidylinositol 3-kinase pathway, and proinflammatory cytokines that cause renal injury and oxidative stress. -
Table S1. 103 Ferroptosis-Related Genes Retrieved from the Genecards
Table S1. 103 ferroptosis-related genes retrieved from the GeneCards. Gene Symbol Description Category GPX4 Glutathione Peroxidase 4 Protein Coding AIFM2 Apoptosis Inducing Factor Mitochondria Associated 2 Protein Coding TP53 Tumor Protein P53 Protein Coding ACSL4 Acyl-CoA Synthetase Long Chain Family Member 4 Protein Coding SLC7A11 Solute Carrier Family 7 Member 11 Protein Coding VDAC2 Voltage Dependent Anion Channel 2 Protein Coding VDAC3 Voltage Dependent Anion Channel 3 Protein Coding ATG5 Autophagy Related 5 Protein Coding ATG7 Autophagy Related 7 Protein Coding NCOA4 Nuclear Receptor Coactivator 4 Protein Coding HMOX1 Heme Oxygenase 1 Protein Coding SLC3A2 Solute Carrier Family 3 Member 2 Protein Coding ALOX15 Arachidonate 15-Lipoxygenase Protein Coding BECN1 Beclin 1 Protein Coding PRKAA1 Protein Kinase AMP-Activated Catalytic Subunit Alpha 1 Protein Coding SAT1 Spermidine/Spermine N1-Acetyltransferase 1 Protein Coding NF2 Neurofibromin 2 Protein Coding YAP1 Yes1 Associated Transcriptional Regulator Protein Coding FTH1 Ferritin Heavy Chain 1 Protein Coding TF Transferrin Protein Coding TFRC Transferrin Receptor Protein Coding FTL Ferritin Light Chain Protein Coding CYBB Cytochrome B-245 Beta Chain Protein Coding GSS Glutathione Synthetase Protein Coding CP Ceruloplasmin Protein Coding PRNP Prion Protein Protein Coding SLC11A2 Solute Carrier Family 11 Member 2 Protein Coding SLC40A1 Solute Carrier Family 40 Member 1 Protein Coding STEAP3 STEAP3 Metalloreductase Protein Coding ACSL1 Acyl-CoA Synthetase Long Chain Family Member 1 Protein -
ION CHANNEL RECEPTORS TÁMOP-4.1.2-08/1/A-2009-0011 Ion Channel Receptors
Manifestation of Novel Social Challenges of the European Union in the Teaching Material of Medical Biotechnology Master’s Programmes at the University of Pécs and at the University of Debrecen Identification number: TÁMOP-4.1.2-08/1/A-2009-0011 Manifestation of Novel Social Challenges of the European Union in the Teaching Material of Medical Biotechnology Master’s Programmes at the University of Pécs and at the University of Debrecen Identification number: TÁMOP-4.1.2-08/1/A-2009-0011 Tímea Berki and Ferenc Boldizsár Signal transduction ION CHANNEL RECEPTORS TÁMOP-4.1.2-08/1/A-2009-0011 Ion channel receptors 1 Cys-loop receptors: pentameric structure, 4 transmembrane (TM) regions/subunit – Acetylcholin (Ach) Nicotinic R – Na+ channel - – GABAA, GABAC, Glycine – Cl channels (inhibitory role in CNS) 2 Glutamate-activated cationic channels: (excitatory role in CNS), tetrameric stucture, 3 TM regions/subunit – eg. iGlu 3 ATP-gated channels: 3 homologous subunits, 2 TM regions/subunit – eg. P2X purinoreceptor TÁMOP-4.1.2-08/1/A-2009-0011 Cys-loop ion-channel receptors N Pore C C C N N N N C C TM TM TM TM 1 2 3 4 Receptor type GABAA GABAC Glycine g a b p2 p1 b a Subunit diversity a1-6, b1-3, g1-3, d,e,k, and q p1-3 a1-4, b TÁMOP-4.1.2-08/1/A-2009-0011 Vertebrate anionic Cys-loop receptors Type Class Protein name Gene Previous names a1 GABRA1 a2 GABRA2 a3 GABRA3 EJM, ECA4 alpha a4 GABRA4 a5 GABRA5 a6 GABRA6 b1 GABRB1 beta b2 GABRB2 ECA5 b3 GABRB3 g1 GABRG1 GABAA gamma g2 GABRG2 CAE2, ECA2, GEFSP3 g3 GABRG3 delta d GABRD epsilon e GABRE pi p GABRP