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Edinburgh Research Explorer
Edinburgh Research Explorer International Union of Basic and Clinical Pharmacology. LXXXVIII. G protein-coupled receptor list Citation for published version: Davenport, AP, Alexander, SPH, Sharman, JL, Pawson, AJ, Benson, HE, Monaghan, AE, Liew, WC, Mpamhanga, CP, Bonner, TI, Neubig, RR, Pin, JP, Spedding, M & Harmar, AJ 2013, 'International Union of Basic and Clinical Pharmacology. LXXXVIII. G protein-coupled receptor list: recommendations for new pairings with cognate ligands', Pharmacological reviews, vol. 65, no. 3, pp. 967-86. https://doi.org/10.1124/pr.112.007179 Digital Object Identifier (DOI): 10.1124/pr.112.007179 Link: Link to publication record in Edinburgh Research Explorer Document Version: Publisher's PDF, also known as Version of record Published In: Pharmacological reviews Publisher Rights Statement: U.S. Government work not protected by U.S. copyright 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: 02. Oct. 2021 1521-0081/65/3/967–986$25.00 http://dx.doi.org/10.1124/pr.112.007179 PHARMACOLOGICAL REVIEWS Pharmacol Rev 65:967–986, July 2013 U.S. -
Angiotensin-II and Arginine Vasopressin Regulate Body Fluid
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Apollo 1 Angiotensin II type 1 receptor dependent GLP-1 and PYY secretion in mice and 2 humans 3 4 Ramona Pais, Juraj Rievaj, Pierre Larraufie, Fiona Gribble and Frank Reimann 5 6 Wellcome Trust-MRC Institute of Metabolic Science, Metabolic Research Laboratories, 7 University of Cambridge, Addenbrooke’s Hospital, Box 289, Hills Road, Cambridge, CB2 8 0QQ, United Kingdom 9 10 Abbreviated Title: Control of L-cells by Angiotensin II 11 12 Key terms: Renin-Angiotensin System (RAS); Angiotensin II; glucagon-like peptide-1 (GLP- 13 1); L-cells; Peptide YY (PYY) 14 15 Word count: 4652 16 17 No of figures and tables: 6 figures, 0 tables 18 19 Correspondence and reprint requests should be addressed to: 20 Dr. Frank Reimann and Prof. Fiona Gribble 21 Wellcome Trust-MRC Institute of Metabolic Science, Metabolic Research Laboratories 22 Addenbrooke’s Hospital, Box 289 23 University of Cambridge 24 Hills Road, Cambridge, CB2 0QQ, United Kingdom 25 Phone: +44 (0)1223 336746 26 Fax: + 44 (0)1223 330598 27 Email: [email protected], [email protected] 28 29 Disclosure statement: The authors have nothing to disclose. 30 Abstract 31 Angiotensin II (Ang II) is the key hormone mediator of the renin angiotensin system which 32 regulates blood pressure and fluid and electrolyte balance in the body. Here we report that in 33 colonic epithelium the Ang II type 1 receptor (AT1R) is highly and exclusively expressed in 34 enteroendocrine L-cells which produce the gut hormones glucagon-like peptide-1 (GLP-1) 35 and peptide YY (PYY). -
Supplementary Material
Supplementary Material Table S1: Significant downregulated KEGGs pathways identified by DAVID following exposure to five cinnamon- based phenylpropanoids (p < 0.05). p-value Term: Genes (Benjamini) Cytokine-cytokine receptor interaction: FASLG, TNFSF14, CXCL11, IL11, FLT3LG, CCL3L1, CCL3L3, CXCR6, XCR1, 2.43 × 105 RTEL1, CSF2RA, TNFRSF17, TNFRSF14, CCNL2, VEGFB, AMH, TNFRSF10B, INHBE, IFNB1, CCR3, VEGFA, CCR2, IL12A, CCL1, CCL3, CXCL5, TNFRSF25, CCR1, CSF1, CX3CL1, CCL7, CCL24, TNFRSF1B, IL12RB1, CCL21, FIGF, EPO, IL4, IL18R1, FLT1, TGFBR1, EDA2R, HGF, TNFSF8, KDR, LEP, GH2, CCL13, EPOR, XCL1, IFNA16, XCL2 Neuroactive ligand-receptor interaction: OPRM1, THRA, GRIK1, DRD2, GRIK2, TACR2, TACR1, GABRB1, LPAR4, 9.68 × 105 GRIK5, FPR1, PRSS1, GNRHR, FPR2, EDNRA, AGTR2, LTB4R, PRSS2, CNR1, S1PR4, CALCRL, TAAR5, GABRE, PTGER1, GABRG3, C5AR1, PTGER3, PTGER4, GABRA6, GABRA5, GRM1, PLG, LEP, CRHR1, GH2, GRM3, SSTR2, Chlorogenic acid Chlorogenic CHRM3, GRIA1, MC2R, P2RX2, TBXA2R, GHSR, HTR2C, TSHR, LHB, GLP1R, OPRD1 Hematopoietic cell lineage: IL4, CR1, CD8B, CSF1, FCER2, GYPA, ITGA2, IL11, GP9, FLT3LG, CD38, CD19, DNTT, 9.29 × 104 GP1BB, CD22, EPOR, CSF2RA, CD14, THPO, EPO, HLA-DRA, ITGA2B Cytokine-cytokine receptor interaction: IL6ST, IL21R, IL19, TNFSF15, CXCR3, IL15, CXCL11, TGFB1, IL11, FLT3LG, CXCL10, CCR10, XCR1, RTEL1, CSF2RA, IL21, CCNL2, VEGFB, CCR8, AMH, TNFRSF10C, IFNB1, PDGFRA, EDA, CXCL5, TNFRSF25, CSF1, IFNW1, CNTFR, CX3CL1, CCL5, TNFRSF4, CCL4, CCL27, CCL24, CCL25, CCL23, IFNA6, IFNA5, FIGF, EPO, AMHR2, IL2RA, FLT4, TGFBR2, EDA2R, -
University of Groningen on the Mechanism of Cationic Lipid
University of Groningen On the mechanism of cationic lipid-mediated delivery of oligonucleotides Shi, Fuxin IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2004 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Shi, F. (2004). On the mechanism of cationic lipid-mediated delivery of oligonucleotides: towards an antisense therapy. s.n. Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 25-09-2021 Chapter 4 Antisense oligonucleotides reach mRNA targets via the RNA matrix: downregulation of the 5-HT1A receptor Fuxin Shia, Willy H. Vissera, Natasja M. J. de Jongb, Robert S. B. Liemc, Eric Ronkenb and Dick Hoekstraa a Department of Membrane Cell Biology, Faculty of Medical Sciences, University of Groningen, Antonius Deusinglaan 1,9713 AV, Groningen, The Netherlands b Solvay Pharmaceuticals, Research Laboratories, Weesp, The Netherlands c Department of Electron Microscopy, Faculty of Medical Sciences, Groningen, The Netherlands Published in Experimental Cell Research, 291(2003): 313-325 65 Chapter 4 Abstract Successful application of antisense oligonucleotides (ODNs) in cell biology and therapy will depend on the ease of design, efficiency of (intra)cellular delivery, ODN stability, and target specificity. -
In the IUPHAR/BPS Guide to Pharmacology Database
IUPHAR/BPS Guide to Pharmacology CITE https://doi.org/10.2218/gtopdb/F16/2019.4 Class A Orphans (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database Stephen P.H. Alexander1, Jim Battey2, Helen E. Benson3, Richard V. Benya4, Tom I. Bonner5, Anthony P. Davenport6, Satoru Eguchi7, Anthony Harmar3, Nick Holliday1, Robert T. Jensen2, Sadashiva Karnik8, Evi Kostenis9, Wen Chiy Liew3, Amy E. Monaghan3, Chido Mpamhanga10, Richard Neubig11, Adam J. Pawson3, Jean-Philippe Pin12, Joanna L. Sharman3, Michael Spedding13, Eliot Spindel14, Leigh Stoddart15, Laura Storjohann16, Walter G. Thomas17, Kalyan Tirupula8 and Patrick Vanderheyden18 1. University of Nottingham, UK 2. National Institutes of Health, USA 3. University of Edinburgh, UK 4. University of Illinois at Chicago, USA 5. National Institute of Mental Health, USA 6. University of Cambridge, UK 7. Temple University, USA 8. Cleveland Clinic Lerner Research Institute, USA 9. University of Bonn, Germany 10. LifeArc, UK 11. Michigan State University, USA 12. Université de Montpellier, France 13. Spedding Research Solutions SARL, France 14. Oregon Health & Science University, USA 15. University of Glasgow, UK 16. University of Utah, USA 17. University of Queensland, Australia 18. Vrije Universiteit Brussel, Belgium Abstract Table 1 lists a number of putative GPCRs identified by NC-IUPHAR [191], for which preliminary evidence for an endogenous ligand has been published, or for which there exists a potential link to a disease, or disorder. These GPCRs have recently been reviewed in detail [148]. The GPCRs in Table 1 are all Class A, rhodopsin-like GPCRs. Class A orphan GPCRs not listed in Table 1 are putative GPCRs with as-yet unidentified endogenous ligands. -
G Protein-Coupled Receptors
S.P.H. Alexander et al. The Concise Guide to PHARMACOLOGY 2015/16: G protein-coupled receptors. British Journal of Pharmacology (2015) 172, 5744–5869 THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: G protein-coupled receptors Stephen PH Alexander1, Anthony P Davenport2, Eamonn Kelly3, Neil Marrion3, John A Peters4, Helen E Benson5, Elena Faccenda5, Adam J Pawson5, Joanna L Sharman5, Christopher Southan5, Jamie A Davies5 and CGTP Collaborators 1School of Biomedical Sciences, University of Nottingham Medical School, Nottingham, NG7 2UH, UK, 2Clinical Pharmacology Unit, University of Cambridge, Cambridge, CB2 0QQ, UK, 3School of Physiology and Pharmacology, University of Bristol, Bristol, BS8 1TD, UK, 4Neuroscience Division, Medical Education Institute, Ninewells Hospital and Medical School, University of Dundee, Dundee, DD1 9SY, UK, 5Centre for Integrative Physiology, University of Edinburgh, Edinburgh, EH8 9XD, UK Abstract The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/ 10.1111/bph.13348/full. G protein-coupled receptors are one of the eight major pharmacological targets into which the Guide is divided, with the others being: ligand-gated ion channels, voltage-gated ion channels, other 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. -
G Protein‐Coupled Receptors
S.P.H. Alexander et al. The Concise Guide to PHARMACOLOGY 2019/20: G protein-coupled receptors. British Journal of Pharmacology (2019) 176, S21–S141 THE CONCISE GUIDE TO PHARMACOLOGY 2019/20: G protein-coupled receptors Stephen PH Alexander1 , Arthur Christopoulos2 , Anthony P Davenport3 , Eamonn Kelly4, Alistair Mathie5 , John A Peters6 , Emma L Veale5 ,JaneFArmstrong7 , Elena Faccenda7 ,SimonDHarding7 ,AdamJPawson7 , Joanna L Sharman7 , Christopher Southan7 , Jamie A Davies7 and CGTP Collaborators 1School of Life Sciences, University of Nottingham Medical School, Nottingham, NG7 2UH, UK 2Monash Institute of Pharmaceutical Sciences and Department of Pharmacology, Monash University, Parkville, Victoria 3052, Australia 3Clinical Pharmacology Unit, University of Cambridge, Cambridge, CB2 0QQ, UK 4School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, BS8 1TD, UK 5Medway School of Pharmacy, The Universities of Greenwich and Kent at Medway, Anson Building, Central Avenue, Chatham Maritime, Chatham, Kent, ME4 4TB, UK 6Neuroscience Division, Medical Education Institute, Ninewells Hospital and Medical School, University of Dundee, Dundee, DD1 9SY, UK 7Centre for Discovery Brain Sciences, 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. Although the Concise Guide represents approximately 400 pages, the material presented is substantially reduced compared to information and links presented on the website. -
Diverse Immunoregulatory Roles of Oxysterols— the Oxidized Cholesterol Metabolites
H OH metabolites OH Review Diverse Immunoregulatory Roles of Oxysterols— The Oxidized Cholesterol Metabolites Chloe Choi 1,* and David K. Finlay 1,2,* 1 School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Pearse Street 152-160, Dublin 2, Ireland 2 School of Pharmacy and Pharmaceutical Sciences, Trinity Biomedical Sciences Institute, Trinity College Dublin, Pearse Street 152-160, Dublin 2, Ireland * Correspondence: [email protected] (C.C.); fi[email protected] (D.K.F.); Tel.: +353-1-896-3564 (D.K.F.) Received: 13 August 2020; Accepted: 24 September 2020; Published: 28 September 2020 Abstract: Intermediates of both cholesterol synthesis and cholesterol metabolism can have diverse roles in the control of cellular processes that go beyond the control of cholesterol homeostasis. For example, oxidized forms of cholesterol, called oxysterols have functions ranging from the control of gene expression, signal transduction and cell migration. This is of particular interest in the context of immunology and immunometabolism where we now know that metabolic processes are key towards shaping the nature of immune responses. Equally, aberrant metabolic processes including altered cholesterol homeostasis contribute to immune dysregulation and dysfunction in pathological situations. This review article brings together our current understanding of how oxysterols affect the control of immune responses in diverse immunological settings. Keywords: oxysterols; cholesterol; SREBP; LXR; GPR183; ROR; SERM; Ch25h; Cyp27a1; inflammation; cancer; infection; obesity; autoimmunity; endometriosis; immunometabolism 1. Introduction Cholesterol is a vital component of our cells and our bodies. It is a structural component of cellular membranes, plays a role in regulating intracellular signal transduction and is a precursor for the generation of other important molecules such as bile acids and steroid hormones. -
Initial, Transient, and Specific Interaction Between G Protein
Sato T. et al. Medical Research Archives, vol. 6, issue 9, September 2018 Page 1 of 25 ARTICLE Initial, transient, and specific interaction between G protein-coupled receptor and target G protein in parallel signal processing: a case of olfactory discrimination of cancer-induced odors Takaaki Sato1, Mutsumi Matsukawa2, Yoichi Mizutani3, Toshio Iijima4, Hiroyoshi Matsumura5 Authors’ affiliations: 1 Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Osaka, Japan 2 Division of Anatomical Science, Department of Functional Morphology, Nihon University School of Medicine, Tokyo, Japan 3 Department of Medical Engineering, Faculty of Health Science, Aino University, Osaka, Japan 4 Graduate School of Life Sciences, Tohoku University, Sendai, Japan 5 College of Life Sciences, Ritsumeikan University, Kusatsu, Japan * Corresponding author: Takaaki Sato, Biomedical Research Institute, National Institute of Ad- vanced Industrial Science and Technology, 1-8-31 Midorioka, Ikeda, Osaka 563-8577, Japan, E-mail: [email protected] Abstract: G protein-coupled receptors (GPCRs) detect and distinguish between various subtypes of extracellular sig- nals, such as neurotransmitters, hormones, light, and odorous chemicals. As determinants for robust and appropriate cellular responses, common and unique features of interactions between GPCRs and their target G proteins provide insights into structure-based drug design for treatment of GPCR-related diseases. Re- cently, we found that the hydrophobic core buried between GPCR helix 8 and TM1–2 is essential for acti- vation of both specific and nonspecific G proteins. Furthermore, the 2nd residue of helix 8 is responsible for initial, transient, and specific interaction with a target G protein. Analysis of human and murine olfactory receptors (ORs) and other class-A GPCRs revealed that several amino acids, such as Glu, Gln, and Asp, are conserved at this position. -
Supplementary Materials
Supplementary Materials Supplemental Figure S1. Distinct difference in expression of 576 sensome genes comparing cortex versus microglia. (A) This heatmap shows all 576 sensome candidate genes ordered by DE and with the left column shows if the gene is present in the “Hickman et al. sensome” Supplemental Figure S2. Mouse sensome and human sensome genes categorized by group. (A) Bar graph showing the number of mouse and human sensome genes per group (Cell-Cell Interactions, Chemokine and related receptors, Cytokine receptors, ECM receptors, Endogenous ligands receptors, sensors and transporters, Fc receptors, Pattern recognition and related receptors, Potential sensors but no known ligands and Purinergic and related receptors). Supplementary Figure S3. Overlap of ligands recognized by microglia sensome (A) Overlap between the ligands of the receptors from respectively human and mouse core sensome was shown using Venn Diagrams. (B) Ligands of human and mouse receptors categorized in groups (Glycoproteins, Cytokines, Immunoglobulin, Amino acids, Carbohydrates, Electrolytes, Lipopeptides, Chemokines, Neuraminic acids, Nucleic acids, Receptors, Lipids, Fatty acids, Leukotrienes, Hormones, Steroids and Phospholipids) and spread of different groups shown as parts of whole again highlighting that the distribution of ligands what the human and mouse sensome genes can sense (Categorization of ligands in Supplementary Table S1). Supplementary Figure S4. Microglia core sensome expression during aging. (A) Two-log fold change of microglia core sensome genes in aging mice derived from Holtman et al. [12]. (B) Accelerated aging model (ERCC1), with impaired DNA repair mechanism, shows changes of microglia core sensome expression [12]. (C) Microglia core sensome expression during aging in human derived from Olah et al. -
GPCR Expression Profiles Were Determined Using
Supplemental Figures and Tables for Tischner et al., 2017 Supplemental Figure 1: GPCR expression profiles were determined using the NanoString nCounter System in 250 ng of pooled cell RNA obtained from freshly isolated CD4 T cells from naïve lymph nodes (CD4ln), spinal cord infiltrating CD4 T cells at peak EAE disease (CD4sc), and primary lung endothelial cells (luEC). Supplemental Figure 2: Array design and quality controls. A, Sorted leukocytes or endothelial cells were subjected to single‐cell expression analysis and re‐evaluated based on the expression of various identity‐defining genes. B, Expression of identity‐defining and quality control genes after deletion of contaminating or reference gene‐negative cells. Expression data are calculated as 2(Limit of detection(LoD) Ct – sample Ct) ; LoD Ct was set to 24. Supplemental Figure 3: Overview over GPCR expression frequencies in different freshly isolated immune cell populations and spinal cord endothelial cells as determined by single cell RT‐PCR. Abbreviations: CD4ln‐Tcon/CD4ln‐Treg, conventional (con) and regulatory (reg) CD4 T cells from lymph nodes (CD4ln) of naïve mice; CD4dr/CD4sc, CD4 T cells from draining lymph nodes (dr) or spinal cord (sc) at peak EAE disease; CD4spn2D/ CD4spn2DTh1/ CD4spn2DTh17, splenic CD4 T cells from 2D2 T cell receptor transgenic mice before (2D) and after in vitro differentiation towards Th1 (2DTh1) or Th17 (2DTh17); MonoSpn, splenic monocytes; CD11b_sc, spinal cord infiltrating CD11b‐ positive cells; sc_microglia, Ccr2neg,Cx3cr1pos microglia from spinal cord at peak disease; sc_macrophages, CCr2pos;Cx3cr1lo/neg macrophages from spinal cord at peak disease; BMDM_M1/BMDM_M2, bone marrow‐derived macrophages differentiated towards M1 or M2; ECscN and ECscEAE, spinal cord endothelial cells from naïve mice (N) and at peak EAE disease (EAE); SMC, smooth muscle cells from various vessel types (included as positive control to ascertain primer functionality). -
Expression Map of 78 Brain-Expressed Mouse Orphan Gpcrs Provides a Translational Resource for Neuropsychiatric Research
ARTICLE DOI: 10.1038/s42003-018-0106-7 OPEN Expression map of 78 brain-expressed mouse orphan GPCRs provides a translational resource for neuropsychiatric research Aliza T. Ehrlich1,2, Grégoire Maroteaux2,5, Anne Robe1, Lydie Venteo3, Md. Taufiq Nasseef2, 1234567890():,; Leon C. van Kempen4,6, Naguib Mechawar2, Gustavo Turecki2, Emmanuel Darcq2 & Brigitte L. Kieffer 1,2 Orphan G-protein-coupled receptors (oGPCRs) possess untapped potential for drug dis- covery. In the brain, oGPCRs are generally expressed at low abundance and their function is understudied. Expression profiling is an essential step to position oGPCRs in brain function and disease, however public databases provide only partial information. Here, we fine-map expression of 78 brain-oGPCRs in the mouse, using customized probes in both standard and supersensitive in situ hybridization. Images are available at http://ogpcr-neuromap.douglas. qc.ca. This searchable database contains over 8000 coronal brain sections across 1350 slides, providing the first public mapping resource dedicated to oGPCRs. Analysis with public mouse (60 oGPCRs) and human (56 oGPCRs) genome-wide datasets identifies 25 oGPCRs with potential to address emotional and/or cognitive dimensions of psychiatric conditions. We probe their expression in postmortem human brains using nanoString, and included data in the resource. Correlating human with mouse datasets reveals excellent suitability of mouse models for oGPCRs in neuropsychiatric research. 1 IGBMC, Institut Génétique Biologie Moléculaire Cellulaire, Illkirch, France. 2 Douglas Mental Health University Institute and McGill University, Department of Psychiatry, Montreal, Canada. 3 Label Histologie, 51100 Reims, France. 4 Lady Davis Institute for Medical Research, Jewish General Hospital and McGill University, Department of Pathology, Montreal, Canada.