Transcriptome Analysis of the Brain Provides Insights Into the Regulatory
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Article Evolutionary Dynamics of the OR Gene Repertoire in Teleost Fishes
bioRxiv preprint doi: https://doi.org/10.1101/2021.03.09.434524; this version posted March 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder.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. Article Evolutionary dynamics of the OR gene repertoire in teleost fishes: evidence of an association with changes in olfactory epithelium shape Maxime Policarpo1, Katherine E Bemis2, James C Tyler3, Cushla J Metcalfe4, Patrick Laurenti5, Jean-Christophe Sandoz1, Sylvie Rétaux6 and Didier Casane*,1,7 1 Université Paris-Saclay, CNRS, IRD, UMR Évolution, Génomes, Comportement et Écologie, 91198, Gif-sur-Yvette, France. 2 NOAA National Systematics Laboratory, National Museum of Natural History, Smithsonian Institution, Washington, D.C. 20560, U.S.A. 3Department of Paleobiology, National Museum of Natural History, Smithsonian Institution, Washington, D.C., 20560, U.S.A. 4 Independent Researcher, PO Box 21, Nambour QLD 4560, Australia. 5 Université de Paris, Laboratoire Interdisciplinaire des Energies de Demain, Paris, France 6 Université Paris-Saclay, CNRS, Institut des Neurosciences Paris-Saclay, 91190, Gif-sur- Yvette, France. 7 Université de Paris, UFR Sciences du Vivant, F-75013 Paris, France. * Corresponding author: e-mail: [email protected]. !1 bioRxiv preprint doi: https://doi.org/10.1101/2021.03.09.434524; this version posted March 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder.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. Abstract Teleost fishes perceive their environment through a range of sensory modalities, among which olfaction often plays an important role. -
Aquaporin Channels in the Heart—Physiology and Pathophysiology
International Journal of Molecular Sciences Review Aquaporin Channels in the Heart—Physiology and Pathophysiology Arie O. Verkerk 1,2,* , Elisabeth M. Lodder 2 and Ronald Wilders 1 1 Department of Medical Biology, Amsterdam University Medical Centers, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands; [email protected] 2 Department of Experimental Cardiology, Amsterdam University Medical Centers, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands; [email protected] * Correspondence: [email protected]; Tel.: +31-20-5664670 Received: 29 March 2019; Accepted: 23 April 2019; Published: 25 April 2019 Abstract: Mammalian aquaporins (AQPs) are transmembrane channels expressed in a large variety of cells and tissues throughout the body. They are known as water channels, but they also facilitate the transport of small solutes, gasses, and monovalent cations. To date, 13 different AQPs, encoded by the genes AQP0–AQP12, have been identified in mammals, which regulate various important biological functions in kidney, brain, lung, digestive system, eye, and skin. Consequently, dysfunction of AQPs is involved in a wide variety of disorders. AQPs are also present in the heart, even with a specific distribution pattern in cardiomyocytes, but whether their presence is essential for proper (electro)physiological cardiac function has not intensively been studied. This review summarizes recent findings and highlights the involvement of AQPs in normal and pathological cardiac function. We conclude that AQPs are at least implicated in proper cardiac water homeostasis and energy balance as well as heart failure and arsenic cardiotoxicity. However, this review also demonstrates that many effects of cardiac AQPs, especially on excitation-contraction coupling processes, are virtually unexplored. -
TAS1R1 (NM 138697) Human Tagged ORF Clone Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for RG219286 TAS1R1 (NM_138697) Human Tagged ORF Clone Product data: Product Type: Expression Plasmids Product Name: TAS1R1 (NM_138697) Human Tagged ORF Clone Tag: TurboGFP Symbol: TAS1R1 Synonyms: GM148; GPR70; T1R1; TR1 Vector: pCMV6-AC-GFP (PS100010) E. coli Selection: Ampicillin (100 ug/mL) Cell Selection: Neomycin This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 6 TAS1R1 (NM_138697) Human Tagged ORF Clone – RG219286 ORF Nucleotide >RG219286 representing NM_138697 Sequence: Red=Cloning site Blue=ORF Green=Tags(s) TTTTGTAATACGACTCACTATAGGGCGGCCGGGAATTCGTCGACTGGATCCGGTACCGAGGAGATCTGCC GCCGCGATCGCC ATGCTGCTCTGCACGGCTCGCCTGGTCGGCCTGCAGCTTCTCATTTCCTGCTGCTGGGCCTTTGCCTGCC ATAGCACGGAGTCTTCTCCTGACTTCACCCTCCCCGGAGATTACCTCCTGGCAGGCCTGTTCCCTCTCCA TTCTGGCTGTCTGCAGGTGAGGCACAGACCCGAGGTGACCCTGTGTGACAGGTCTTGTAGCTTCAATGAG CATGGCTACCACCTCTTCCAGGCTATGCGGCTTGGGGTTGAGGAGATAAACAACTCCACGGCCCTGCTGC CCAACATCACCCTGGGGTACCAGCTGTATGATGTGTGTTCTGACTCTGCCAATGTGTATGCCACGCTGAG AGTGCTCTCCCTGCCAGGGCAACACCACATAGAGCTCCAAGGAGACCTTCTCCACTATTCCCCTACGGTG CTGGCAGTGATTGGGCCTGACAGCACCAACCGTGCTGCCACCACAGCCGCCCTGCTGAGCCCTTTCCTGG TGCCCATGATTAGCTATGCGGCCAGCAGCGAGACGCTCAGCGTGAAGCGGCAGTATCCCTCTTTCCTGCG CACCATCCCCAATGACAAGTACCAGGTGGAGACCATGGTGCTGCTGCTGCAGAAGTTCGGGTGGACCTGG -
Mismatches Between Feeding Ecology and Taste Receptor Evolution
satisfactory explanation exists (2). Furthermore, Tas1r2 is absent LETTER in all bird genomes sequenced thus far (2), irrespective of their diet. Mismatches between feeding ecology Jiang et al. (1) further contended that sea lions and dolphins and taste receptor evolution: An need not sense the umami taste because they swallow food whole. Although it is true that Tas1r1 is pseudogenized in these inconvenient truth two species, the authors ignore the previous finding that Tas1r1 is also pseudogenized or missing in all bats examined, regardless Comparative and evolutionary biology can not only verify labo- of their diet (fruits, insects, or blood) (3). Although the pseu- ratory findings of gene functions but also provide insights into dogenization of Tas1r1 in the giant panda (4) occurred at ap- their physiological roles in nature that are sometimes difficult to proximately the same time as it switched from being a meat-eater discern in the laboratory. Specifically, if our understanding of the to a plant-eater (5), and thus may be related to the feeding physiological function of a gene is complete and accurate, the ecology, herbivorous mammals, such as the horse and cow, still gene should be inactivated or pseudogenized in and only in carry an intact Tas1r1 (5). organisms in which the presumed function of the gene has be- Clearly, the presence/absence of intact Tas1r2 and Tas1r1 in come useless or harmful. On the basis of multiple independent mammals and other vertebrates is sometimes inconsistent with pseudogenizations of the sweet taste receptor gene Tas1r2 in the known functions of these genes and the involved tastes. -
Activation Mechanism of the G Protein-Coupled Sweet Receptor Heterodimer with Sweeteners and Allosteric Agonists
Supporting Information Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists Soo-Kyung Kim, *† Yalu Chen, † Ravinder Abrol, †, ‡ William A. Goddard III,*† and Brian Guthrie§ †Materials and Process Simulation Center (MC 139-74), California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125; ‡Current address, Departments of Chemistry and Biochemistry, California State University, Northridge, CA 91330; §Cargill Global Food Research, 2301 Crosby Road, Wayzata, MN 55391 * CORRESPONDING AUTHOR Prof. William A. Goddard III California Institute of Technology MC 139-74, 1200 E. California Blvd., Pasadena, CA 91125; phone: 1-626-395-2731, e-mail: [email protected] Dr. Soo-Kyung Kim phone: 1-626-395-2724, e-mail: [email protected] 1 RESULTS Structures for Allosteric ligand bound at the TMD of all three TAS1Rs As described in the METHODS section, the DarwinDock procedure (1) involves sampling ~50,000 poses for each of ~10 diverse ligand conformations from which, we select finally two energetically favorable binding poses based on two scoring methods: UCav E: unified cavity energy for which we consider that interactions of the best 100 poses with the union of all residues involve in their separate binding sites (providing a uniform comparison) BE: snap binding energy considering all interactions of ligand with protein As a first validation of the predicted structures for the 7 helix TMD, we used DarwinDock to predict the binding site for the allosteric ligands to each TAS1R TMD in Table S10. Here we find, S819 [1-((1H-pyrrol-2-yl)methyl)-3-(4-isopropoxyphenyl)thiourea] is a sweet compound that interacts with the TAS1R2 TMD.(2) and Lactisole is a competitive inhibitor of the sweet taste receptor that binds to TAS1R3 TMD.(3, 4) These structures were further relaxed through annealing. -
Allosteric Mechanism of Water Channel Gating by Ca2+–Calmodulin
Portland State University PDXScholar Chemistry Faculty Publications and Presentations Chemistry 9-2013 Allosteric Mechanism of Water Channel Gating by Ca2+–calmodulin Steve Reichow [email protected] Daniel M. Clemens University of California, Irvine J. Alfredo Freites University of California, Irvine Karin L. Németh-Cahalan University of California, Irvine Matthias Heyden University of California, Irvine See next page for additional authors Let us know how access to this document benefits ouy . Follow this and additional works at: https://pdxscholar.library.pdx.edu/chem_fac Part of the Biochemistry Commons, and the Structural Biology Commons Citation Details Reichow, S. L., Clemens, D. M., Freites, J. A., Németh-Cahalan, K. L., Heyden, M., Tobias, D. J., ... & Gonen, T. (2013). Allosteric mechanism of water-channel gating by Ca2+–calmodulin. Nature structural & molecular biology, 20(9), 1085-1092. This Post-Print is brought to you for free and open access. It has been accepted for inclusion in Chemistry Faculty Publications and Presentations by an authorized administrator of PDXScholar. For more information, please contact [email protected]. Authors Steve Reichow, Daniel M. Clemens, J. Alfredo Freites, Karin L. Németh-Cahalan, Matthias Heyden, Douglas J. Tobias, James E. Hall, and Tamir Gonen This post-print is available at PDXScholar: https://pdxscholar.library.pdx.edu/chem_fac/198 HHS Public Access Author manuscript Author Manuscript Author ManuscriptNat Struct Author Manuscript Mol Biol. Author Author Manuscript manuscript; available in PMC 2014 March 01. Published in final edited form as: Nat Struct Mol Biol. 2013 September ; 20(9): 1085–1092. doi:10.1038/nsmb.2630. Allosteric mechanism of water channel gating by Ca2+– calmodulin Steve L. -
Renal Aquaporins
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Kidney International, Vol. 49 (1996), pp.1712—1717 Renal aquaporins MARK A. KNEPPER, JAMES B. WADE, JAMES TERRIS, CAROLYN A. ECELBARGER, DAVID MARPLES, BEATRICE MANDON, CHUNG-LIN CHOU, B.K. KISHORE, and SØREN NIELSEN Laborato,y of Kidney and Electrolyte Metabolism, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Matyland, USA; Department of Cell Biology, Institute of Anatomy, University of Aarhus, Aarhus, Denmark; and Department of Physiology, University of Maiyland College of Medicine, Baltimore, and Department of Physiology, Unifornied Services University of the Health Sciences, Bethesda, Maiyland, USA Renal aquaporins. Aquaporins (AQPs) are a newly recognized family of gate the localization and regulation of the four renal aquaporins transmembrane proteins that function as molecular water channels. At (AQP1, AQP2, AQP3 and AQP4). least four aquaporins are expressed in the kidney where they mediate Urine is concentrated as a result of the combined function of rapid water transport across water-permeable epithelia and play critical roles in urinary concentrating and diluting processes. AQP1 is constitu- the loop of Henle, which generates a high osmolality in the renal tively expressed at extremely high levels in the proximal tubule and medulla by countercurrent multiplication, and the collecting duct, descending limb of Henle's loop. AQP2, -3 and -4 are expressed predom- which, in the presence of the antidiuretic hormone vasopressin, inantly in the collecting duct system. AQP2 is the predominant water permits osmotic equilibration between the urine and the hyper- channel in the apical plasma membrane and AQP3 and -4arefound in the basolateral plasma membrane. -
University of Florida Thesis Or Dissertation Formatting
NOVEL GENOME ENGINEERING STRATEGIES TO MODEL REPEAT EXPANSION DISEASES By RUAN OLIVEIRA A DISSERTATION PRESENTED TO THE GRADUATE SCHOOL OF THE UNIVERSITY OF FLORIDA IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY UNIVERSITY OF FLORIDA 2018 © 2018 Ruan Oliveira To my parents, whose hard work and continuous support allowed me to obtain a doctoral degree ACKNOWLEDGMENTS First, I would like to thank my parents, Rosane and Rudimar Oliveira, for their unconditional love and uninterrupted support over the last 26 years. Their commitment to my education makes me prouder than my own graduate degree. Next, I would like to express my deepest gratitude to Andriel Fenner, whose ears endured my daily complaints about graduate school. His continued support kept me sane and his company eased the process of transitioning into adulthood (in progress). Also, I would like to thank Maria Seabra for crossing my path in 2010, when my sophomore version went to a conference in São Paulo and met this loud and contagious woman who was unable to stop talking about her experiences as a Ph.D. student at the University of Florida. If I did not meet Maria, I would have never heard of Gainesville. I would like to thank my Ph.D. mentor, Dr. Maurice Swanson, for giving me freedom to pursue my own ideas and trusting me. I also thank Maury for teaching me how to be a scientist and for his patience with my learning curve. I am grateful to Myrna Stenberg, who taught me discipline and offered me psychological support in the moments I needed the most. -
The Association of Bovine T1R Family of Receptors Polymorphisms with Cattle Growth Traits ⇑ C.L
Research in Veterinary Science xxx (2012) xxx–xxx Contents lists available at SciVerse ScienceDirect Research in Veterinary Science journal homepage: www.elsevier.com/locate/rvsc The association of bovine T1R family of receptors polymorphisms with cattle growth traits ⇑ C.L. Zhang a, J. Yuan a, Q. Wang a, Y.H. Wang a, X.T. Fang a, C.Z. Lei b, D.Y. Yang c, H. Chen a, a Institute of Cellular and Molecular Biology, Xuzhou Normal University, Xuzhou, Jiangsu, PR China b College of Animal Science and Technology, Northwest Agriculture and Forestry University, Shaanxi Key Laboratory of Molecular Biology for Agriculture, Yangling, Shaanxi, PR China c College of Life Science, Dezhou University, Dezhou, Shandong 253023, PR China article info abstract Article history: The three members of the T1R class of taste-specific G protein-coupled receptors have been proven to Received 12 August 2011 function in combination with heterodimeric sweet and umami taste receptors in many mammals that Accepted 20 January 2012 affect food intake. This may in turn affect growth traits of livestock. We performed a comprehensive eval- Available online xxxx uation of single-nucleotide polymorphisms (SNPs) in the bovine TAS1R gene family, which encodes receptors for umami and sweet tastes. Complete DNA sequences of TAS1R1-, TAS1R2-, and TAS1R3-cod- Keywords: ing regions, obtained from 436 unrelated female cattle, representing three breeds (Qinchuan, Jiaxian Red, Taste receptors Luxi), revealed substantial coding and noncoding diversity. A total of nine SNPs in the TAS1R1 gene were SNP identified, among which seven SNPs were in the coding region, and two SNPs were in the introns. -
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. -
Multi-Functionality of Proteins Involved in GPCR and G Protein Signaling: Making Sense of Structure–Function Continuum with In
Cellular and Molecular Life Sciences (2019) 76:4461–4492 https://doi.org/10.1007/s00018-019-03276-1 Cellular andMolecular Life Sciences REVIEW Multi‑functionality of proteins involved in GPCR and G protein signaling: making sense of structure–function continuum with intrinsic disorder‑based proteoforms Alexander V. Fonin1 · April L. Darling2 · Irina M. Kuznetsova1 · Konstantin K. Turoverov1,3 · Vladimir N. Uversky2,4 Received: 5 August 2019 / Revised: 5 August 2019 / Accepted: 12 August 2019 / Published online: 19 August 2019 © Springer Nature Switzerland AG 2019 Abstract GPCR–G protein signaling system recognizes a multitude of extracellular ligands and triggers a variety of intracellular signal- ing cascades in response. In humans, this system includes more than 800 various GPCRs and a large set of heterotrimeric G proteins. Complexity of this system goes far beyond a multitude of pair-wise ligand–GPCR and GPCR–G protein interactions. In fact, one GPCR can recognize more than one extracellular signal and interact with more than one G protein. Furthermore, one ligand can activate more than one GPCR, and multiple GPCRs can couple to the same G protein. This defnes an intricate multifunctionality of this important signaling system. Here, we show that the multifunctionality of GPCR–G protein system represents an illustrative example of the protein structure–function continuum, where structures of the involved proteins represent a complex mosaic of diferently folded regions (foldons, non-foldons, unfoldons, semi-foldons, and inducible foldons). The functionality of resulting highly dynamic conformational ensembles is fne-tuned by various post-translational modifcations and alternative splicing, and such ensembles can undergo dramatic changes at interaction with their specifc partners. -
PKD1 Haploinsufficiency Causes a Syndrome of Inappropriate Antidiuresis in Mice
JASN Express. Published on May 2, 2007 as doi: 10.1681/ASN.2006010052 PKD1 Haploinsufficiency Causes a Syndrome of Inappropriate Antidiuresis in Mice Ali K. Ahrabi,* Sara Terryn,† Giovanna Valenti,‡ Nathalie Caron,§ ʈ ʈ Claudine Serradeil-Le Gal, Danielle Raufaste, Soren Nielsen,¶ Shigeo Horie,** Jean-Marc Verbavatz,†† and Olivier Devuyst* *Division of Nephrology, Universite´catholique de Louvain Medical School, Brussels, Belgium; †Laboratory of Cell Physiology, Center for Environmental Sciences, Hasselt University, Diepenbeek, Belgium; ‡Department of Physiology, University of Bari, Bari, Italy; §Department of Physiology and Pharmacology, University of Mons-Hainaut, Mons, ʈ Belgium; Sanofi-Aventis, Toulouse, France; ¶The Water and Salt Research Center, University of Aarhus, Aarhus, Denmark; **Department of Urology, Teikyo University, Tokyo, Japan; and ††Cell and Molecular Imaging, CEA/Saclay, Gif-sur-Yvette, France Mutations in PKD1 are associated with autosomal dominant polycystic kidney disease. Studies in mouse models suggest that the vasopressin (AVP) V2 receptor (V2R) pathway is involved in renal cyst progression, but potential changes before cystogenesis are unknown. This study used a noncystic mouse model to investigate the effect of Pkd1 haploinsufficiency on water handling and AVP signaling in the collecting duct (CD). In comparison with wild-type littermates, Pkd1ϩ/Ϫ mice showed inappropriate antidiuresis with higher urine osmolality and lower plasma osmolality at baseline, despite similar renal function and water intake. The Pkd1ϩ/Ϫ mice had a decreased aquaretic response to both a water load and a selective V2R antagonist, despite similar V2R distribution and affinity. They showed an inappropriate expression of AVP in brain, irrespective of the hypo-osmolality. The cAMP levels in kidney and urine were unchanged, as were the mRNA levels of aquaporin-2 (AQP2), V2R, and cAMP-dependent mediators in kidney.