DOCSLIB.ORG

In the IUPHAR/BPS Guide to Pharmacology Database

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
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. Table 1: Class A orphan GPCRs with putative endogenous ligands GPR3 GPR4 GPR6 GPR12 GPR15 GPR17 GPR20 GPR22 GPR26 GPR31 GPR34 GPR35 GPR37 GPR39 GPR50 GPR63 GRP65 GPR68 GPR75 GPR84 GPR87 GPR88 GPR132 GPR149 GPR161 GPR183 LGR4 LGR5 1 LGR6 MAS1 MRGPRD MRGPRX1 MRGPRX2 P2RY10 TAAR2 In addition the orphan receptors GPR18, GPR55 and GPR119 which are reported to respond to endogenous agents analogous to the endogenous cannabinoid ligands have been grouped together (GPR18, GPR55 and GPR119). Contents This is a citation summary for Class A Orphans in the Guide to Pharmacology database (GtoPdb). It exists purely as an adjunct to the database to facilitate the recognition of citations to and from the database by citation analyzers. Readers will almost certainly want to visit the relevant sections of the database which are given here under database links. GtoPdb is an expert-driven guide to pharmacological targets and the substances that act on them. GtoPdb is a reference work which is most usefully represented as an on-line database. As in any publication this work should be appropriately cited, and the papers it cites should also be recognized. This document provides a citation for the relevant parts of the database, and also provides a reference list for the research cited by those parts. Please note that the database version for the citations given in GtoPdb are to the most recent preceding version in which the family or its subfamilies and targets were substantially changed. The links below are to the current version. If you need to consult the cited version, rather than the most recent version, please contact the GtoPdb curators. Database links Class A Orphans http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=16 Introduction to Class A Orphans http://www.guidetopharmacology.org/GRAC/FamilyIntroductionForward?familyId=16 Receptors BB3 receptor http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=40 GPR3 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=83 GPR4 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=84 GPR6 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=85 GPR42 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=228 GPR12 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=86 GPR15 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=87 GPR17 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=88 GPR18 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=89 GPR19 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=90 GPR20 2 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=91 GPR21 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=92 GPR22 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=93 GPR25 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=95 GPR26 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=96 GPR27 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=97 GPR31 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=98 GPR32 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=99 GPR33 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=100 GPR34 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=101 GPR35 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=102 GPR37 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=103 GPR37L1 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=104 GPR39 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=105 GPR45 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=106 GPR50 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=107 GPR52 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=108 GPR55 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=109 GPR61 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=110 GPR62 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=111 GPR63 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=112 GPR65 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=113 GPR68 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=114 GPR75 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=115 GPR78 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=116 GPR79 3 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=117 GPR82 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=118 GPR83 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=119 GPR84 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=120 GPR85 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=121 GPR87 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=122 GPR88 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=123 GPR101 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=125 GPR119 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=126 GPR132 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=128 GPR135 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=129 GPR139 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=130 GPR141 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=131 GPR142 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=132 GPR146 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=133 GPR148 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=134 GPR149 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=135 GPR150 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=136 GPR151 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=137 GPR152 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=138 GPR153 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=139 GPR160 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=140 GPR161 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=141 GPR162 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=142 GPR171 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=143 GPR173 4 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=144 GPR174 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=145 GPR176 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=637 GPR182 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=146 GPR183 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=81 LGR4 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=147 LGR5 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=148 LGR6 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=149 MAS1 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=150 MAS1L http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=151 MRGPRD http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=152 MRGPRE http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=153 MRGPRF http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=154 MRGPRG http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=155 MRGPRX1 http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=156
Load more

Recommended publications
  • Strategies to Increase ß-Cell Mass Expansion
    This electronic thesis or dissertation has been downloaded from the King’s Research Portal at https://kclpure.kcl.ac.uk/portal/ Strategies to increase -cell mass expansion Drynda, Robert Lech Awarding institution: King's College London The copyright of this thesis rests with the author and no quotation from it or information derived from it may be published without proper acknowledgement. END USER LICENCE AGREEMENT Unless another licence is stated on the immediately following page this work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International licence. https://creativecommons.org/licenses/by-nc-nd/4.0/ You are free to copy, distribute and transmit the work Under the following conditions: Attribution: You must attribute the work in the manner specified by the author (but not in any way that suggests that they endorse you or your use of the work). Non Commercial: You may not use this work for commercial purposes. No Derivative Works - You may not alter, transform, or build upon this work. Any of these conditions can be waived if you receive permission from the author. Your fair dealings and other rights are in no way affected by the above. Take down policy If you believe that this document 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 Strategies to increase β-cell mass expansion A thesis submitted by Robert Drynda For the degree of Doctor of Philosophy from King’s College London Diabetes Research Group Division of Diabetes & Nutritional Sciences Faculty of Life Sciences & Medicine King’s College London 2017 Table of contents Table of contents .................................................................................................
    [Show full text]
  • Ligand-Gated Chloride Channels Are Receptors for Biogenic Amines in C
    Ligand-Gated Chloride Channels Are Receptors for Biogenic Amines in C. elegans The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Ringstad, N., N. Abe, and H. R. Horvitz. “Ligand-Gated Chloride Channels Are Receptors for Biogenic Amines in C. elegans.” Science 325, no. 5936 (July 2, 2009): 96-100. As Published http://dx.doi.org/10.1126/science.1169243 Publisher American Association for the Advancement of Science (AAAS) Version Author's final manuscript Citable link http://hdl.handle.net/1721.1/84506 Terms of Use Creative Commons Attribution-Noncommercial-Share Alike 3.0 Detailed Terms http://creativecommons.org/licenses/by-nc-sa/3.0/ NIH Public Access Author Manuscript Science. Author manuscript; available in PMC 2010 October 25. NIH-PA Author ManuscriptPublished NIH-PA Author Manuscript in final edited NIH-PA Author Manuscript form as: Science. 2009 July 3; 325(5936): 96±100. doi:10.1126/science.1169243. Ligand-gated chloride channels are receptors for biogenic amines in C. elegans Niels Ringstad1,2, Namiko Abe1,2,3, and H. Robert Horvitz1 1HHMI, Department of Biology and McGovern Institute for Brain Research, MIT, Cambridge MA 02139 Abstract Biogenic amines such as serotonin and dopamine are intercellular signaling molecules that function widely as neurotransmitters and neuromodulators. We have identified in the nematode Caenorhabditis elegans three ligand-gated chloride channels that are receptors for biogenic amines: LGC-53 is a high-affinity dopamine receptor, LGC-55 is a high-affinity tyramine receptor, and LGC-40 is a low-affinity serotonin receptor that is also gated by choline and acetylcholine.
    [Show full text]
  • 4695389.Pdf (3.200Mb)
    Non-classical amine recognition evolved in a large clade of olfactory receptors The Harvard community has made this article openly available. Please share how this access benefits you. Your story matters Citation Li, Qian, Yaw Tachie-Baffour, Zhikai Liu, Maude W Baldwin, Andrew C Kruse, and Stephen D Liberles. 2015. “Non-classical amine recognition evolved in a large clade of olfactory receptors.” eLife 4 (1): e10441. doi:10.7554/eLife.10441. http://dx.doi.org/10.7554/ eLife.10441. Published Version doi:10.7554/eLife.10441 Citable link http://nrs.harvard.edu/urn-3:HUL.InstRepos:23993622 Terms of Use This article was downloaded from Harvard University’s DASH repository, and is made available under the terms and conditions applicable to Other Posted Material, as set forth at http:// nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of- use#LAA RESEARCH ARTICLE Non-classical amine recognition evolved in a large clade of olfactory receptors Qian Li1, Yaw Tachie-Baffour1, Zhikai Liu1, Maude W Baldwin2, Andrew C Kruse3, Stephen D Liberles1* 1Department of Cell Biology, Harvard Medical School, Boston, United States; 2Department of Organismic and Evolutionary Biology, Museum of Comparative Zoology, Harvard University, Cambridge, United States; 3Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, United States Abstract Biogenic amines are important signaling molecules, and the structural basis for their recognition by G Protein-Coupled Receptors (GPCRs) is well understood. Amines are also potent odors, with some activating olfactory trace amine-associated receptors (TAARs). Here, we report that teleost TAARs evolved a new way to recognize amines in a non-classical orientation.
    [Show full text]
  • Genome-Wide Prediction of Small Molecule Binding to Remote
    bioRxiv preprint doi: https://doi.org/10.1101/2020.08.04.236729; this version posted August 5, 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 Genome-wide Prediction of Small Molecule Binding 2 to Remote Orphan Proteins Using Distilled Sequence 3 Alignment Embedding 1 2 3 4 4 Tian Cai , Hansaim Lim , Kyra Alyssa Abbu , Yue Qiu , 5,6 1,2,3,4,7,* 5 Ruth Nussinov , and Lei Xie 1 6 Ph.D. Program in Computer Science, The Graduate Center, The City University of New York, New York, 10016, USA 2 7 Ph.D. Program in Biochemistry, The Graduate Center, The City University of New York, New York, 10016, USA 3 8 Department of Computer Science, Hunter College, The City University of New York, New York, 10065, USA 4 9 Ph.D. Program in Biology, The Graduate Center, The City University of New York, New York, 10016, USA 5 10 Computational Structural Biology Section, Basic Science Program, Frederick National Laboratory for Cancer Research, 11 Frederick, MD 21702, USA 6 12 Department of Human Molecular Genetics and Biochemistry, Sackler School of Medicine, Tel Aviv University, Tel 13 Aviv, Israel 7 14 Helen and Robert Appel Alzheimer’s Disease Research Institute, Feil Family Brain & Mind Research Institute, Weill 15 Cornell Medicine, Cornell University, New York, 10021, USA * 16 [email protected] 17 July 27, 2020 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.08.04.236729; this version posted August 5, 2020.
    [Show full text]
  • 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.
    [Show full text]
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
    [Show full text]
  • 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).
    [Show full text]
  • Bombesin Receptors in Distinct Tissue Compartments of Human Pancreatic Diseases Achim Fleischmann, Ursula Läderach, Helmut Friess, Markus W
    0023-6837/00/8012-1807$03.00/0 LABORATORY INVESTIGATION Vol. 80, No. 12, p. 1807, 2000 Copyright © 2000 by The United States and Canadian Academy of Pathology, Inc. Printed in U.S.A. Bombesin Receptors in Distinct Tissue Compartments of Human Pancreatic Diseases Achim Fleischmann, Ursula Läderach, Helmut Friess, Markus W. Buechler, and Jean Claude Reubi Division of Cell Biology and Experimental Cancer Research (AF, UL, JCR), Institute of Pathology, University of Berne, and Department of Visceral and Transplantation Surgery (HF, MWB), Inselspital, University of Berne, Berne, Switzerland SUMMARY: Overexpression of receptors for regulatory peptides in various human diseases is reportedly of clinical interest. Among these peptides, bombesin and gastrin-releasing peptide (GRP) have been shown to play a physiological and pathophysiological role in pancreatic tissues. Our aim has been to localize bombesin receptors in the human diseased pancreas to identify potential clinical applications of bombesin analogs in this tissue. The presence of bombesin receptor subtypes has been evaluated in specimens of human pancreatic tissues with chronic pancreatitis (n ϭ 23) and ductal pancreatic carcinoma (n ϭ 29) with in vitro receptor autoradiography on tissue sections incubated with 125I-[Tyr4]-bombesin or the universal ligand 125I-[D-Tyr6, ␤-Ala11, Phe13, Nle14]-bombesin(6–14) as radioligands and displaced by subtype-selective bombesin receptor agonists and antagonists. GRP receptors were identified in the pancreatic exocrine parenchyma in 17 of 20 cases with chronic pancreatitis. No measurable bombesin receptors were found in the tumor tissue of ductal pancreatic carcinomas, however, GRP receptors were detected in a subset of peritumoral small veins in 19 of 29 samples.
    [Show full text]
  • 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,
    [Show full text]
  • UNITED STATES SECURITIES and EXCHANGE COMMISSION Washington, DC 20549
    UNITED STATES SECURITIES AND EXCHANGE COMMISSION Washington, DC 20549 FORM 8-K CURRENT REPORT Pursuant to Section 13 or 15(d) of the Securities Exchange Act of 1934 Date of Report (Date of earliest event reported): May 10, 2012 OMEROS CORPORATION (Exact name of registrant as specified in its charter) Washington 001-34475 91-1663741 (State or other jurisdiction of (Commission (IRS Employer incorporation) File Number) Identification No.) 1420 Fifth Avenue, Suite 2600 Seattle, Washington 98101 (Address of principal executive offices, including zip code) (206) 676-5000 (Registrant’s telephone number, including area code) (Former name or former address, if changed since last report) Check the appropriate box below if the Form 8-K filing is intended to simultaneously satisfy the filing obligation of the registrant under any of the following provisions (see General Instruction A.2. below): ¨ Written communications pursuant to Rule 425 under the Securities Act (17 CFR 230.425) ¨ Soliciting material pursuant to Rule 14a-12 under the Exchange Act (17 CFR 240.14a-12) ¨ Pre-commencement communications pursuant to Rule 14d-2(b) under the Exchange Act (17 CFR 240.14d-2(b)) ¨ Pre-commencement communications pursuant to Rule 13e-4(c) under the Exchange Act (17 CFR 240.13e-4(c)) Item 2.02 Results of Operation and Financial Condition. On May 10, 2012, Omeros Corporation issued a press release announcing financial results for the three months ended March 31, 2012. A copy of such press release is furnished herewith as Exhibit 99.1 and is incorporated herein by reference. The information in this Current Report on Form 8-K, including the exhibit hereto, shall not be deemed to be “filed” for purposes of Section 18 of the Securities Exchange Act of 1934, as amended, or otherwise subject to the liabilities of that Section or Sections 11 and 12(a)(2) of the Securities Act of 1933, as amended.
    [Show full text]
  • Comprehensive, Structurally-Curated Alignment and Phylogeny of Vertebrate Biogenic Amine Receptors
    A peer-reviewed version of this preprint was published in PeerJ on 17 February 2015. View the peer-reviewed version (peerj.com/articles/773), which is the preferred citable publication unless you specifically need to cite this preprint. Spielman SJ, Kumar K, Wilke CO. 2015. Comprehensive, structurally-informed alignment and phylogeny of vertebrate biogenic amine receptors. PeerJ 3:e773 https://doi.org/10.7717/peerj.773 Comprehensive, structurally-curated alignment and phylogeny of vertebrate biogenic amine receptors Stephanie J. Spielman1,2,3, Keerthana Kumar1,2,3, and Claus O. Wilke1,2,3 1Department of Integrative Biology, The University of Texas at Austin, Austin, U.S.A. 2Institute of Cellular and Molecular Biology, The University of Texas at Austin, Austin, U.S.A. 3Center for Computational Biology and Bioinformatics, The University of Texas at Austin, Austin, U.S.A. ABSTRACT Biogenic amine receptors play critical roles in regulating behavior and physiology, particularly within the central nervous system, in both vertebrates and invertebrates. These receptors belong to the G-protein coupled receptor (GPCR) family and interact with endogenous bioamine ligands, such as dopamine, serotonin, and epinephrine, and they are targeted by a wide array of pharmaceuticals. Despite these receptors’ clear clinical and biological importance, their evolutionary history remains poorly characterized. In particular, the relationships among biogenic amine receptors and any specific evolutionary constraints acting within distinct receptor subtypes are largely unknown. To advance and facilitate studies in this receptor family, we have constructed a comprehensive, high-quality, structurally-curated sequence alignment of vertebrate biogenic PrePrints amine receptors. We demonstrate that aligning GPCR sequences without considering structure produces an alignment with substantial error, whereas a structurally-aware approach greatly improves alignment accuracy.
    [Show full text]
  • BBC Program 2016.Pages
    March 5-6, 2016 La Quinta Inn & Suites Medical Center San Antonio, TX Behavior, Biology, and Chemistry: Translational Research in Addiction BBC 2016 BBC Publications BBC 2011 Stockton Jr SD and Devi LA (2012) Functional relevance of μ–δ opioid receptor heteromerization: A Role in novel signaling and implications for the treatment of addiction disorders: From a symposium on new concepts in mu-opioid pharmacology. Drug and Alcohol Dependence Mar 1;121(3):167-72. doi: 10.1016/j.drugalcdep.2011.10.025. Epub 2011 Nov 23 Traynor J (2012) μ-Opioid receptors and regulators of G protein signaling (RGS) proteins: From a sym- posium on new concepts in mu-opioid pharmacology. Drug and Alcohol Dependence Mar 1;121(3): 173-80. doi: 10.1016/j.drugalcdep.2011.10.027. Epub 2011 Nov 29 Lamb K, Tidgewell K, Simpson DS, Bohn LM and Prisinzano TE (2012) Antinociceptive effects of herkinorin, a MOP receptor agonist derived from salvinorin A in the formalin test in rats: New concepts in mu opioid receptor pharmacology: From a symposium on new concepts in mu-opioid pharma- cology. Drug and Alcohol Dependence Mar 1;121(3):181-8. doi: 10.1016/j.drugalcdep.2011.10.026. Epub 2011 Nov 26 Whistler JL (2012) Examining the role of mu opioid receptor endocytosis in the beneficial and side-ef- fects of prolonged opioid use: From a symposium on new concepts in mu-opioid pharmacology. Drug and Alcohol Dependence Mar 1;121(3):189-204. doi: 10.1016/j.drugalcdep.2011.10.031. Epub 2012 Jan 9 BBC 2012 Zorrilla EP, Heilig M, de Wit, H and Shaham Y (2013) Behavioral, biological, and chemical perspectives on targeting CRF1 receptor antagonists to treat alcoholism.
    [Show full text]