Mismatches Between Feeding Ecology and Taste Receptor Evolution
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Cellular Mechanisms in Taste Buds
Bull Tokyo Dent Coll (2007) 48(4): 151–161 151 Review Article Cellular Mechanisms in Taste Buds Takashi Suzuki Professor (retired), Department of Physiology, Tokyo Dental College, 1-2-2 Masago, Mihama-ku, Chiba 261-8502, Japan Received 23 May, 2007/Accepted for publication 10 October, 2007 Abstract In the soft palate, tongue, pharynx and larynx surrounding the oral region, taste buds are present, allowing the sensation of taste. On the tongue surface, 3 kinds of papillae are present: fungiform, foliate, and circumvallate. Approximately 5,000 taste buds cover the surface of the human tongue, with about 30% fungiform, 30% foliate and 40% circumvallate papillae. Each taste bud comprises 4 kinds of cells, namely high dark (type I), low light (type II), and intermediate (type III) cells in electron density and Merkel-like taste basal cells (type IV) located at a distance from taste pores. Type II cells sense taste stimuli and type III cells transmit taste signals to sensory afferent nerve fibers. However, type I and type IV cells are not considered to possess obvious taste functions. Synaptic interactions that mediate communication in taste cells provide signal outputs to primary afferent fibers. In the study of taste bud cells, molecular functional techniques using single cells have recently been applied. Serotonin (5-HT) plays a role in cell-to-cell transmission of taste signals. ATP fills the criterion of a neurotransmitter that activates receptors of taste nerve fibers. Findings on 5-HT and ATP suggest that various different transmitters and receptors are present in taste buds. However, no firm evidence for taste- evoked release from type III cells has been identified, except for 5-HT and ATP. -
Food, Food Chemistry and Gustatory Sense
Food, Food Chemistry and Gustatory Sense COOH N H María González Esguevillas MacMillan Group Meeting May 12th, 2020 Food and Food Chemistry Introduction Concepts Food any nourishing substance eaten or drunk to sustain life, provide energy and promote growth any substance containing nutrients that can be ingested by a living organism and metabolized into energy and body tissue country social act culture age pleasure election It is fundamental for our life Food and Food Chemistry Introduction Concepts Food any nourishing substance eaten or drunk to sustain life, provide energy and promote growth any substance containing nutrients that can be ingested by a living organism and metabolized into energy and body tissue OH O HO O O HO OH O O O limonin OH O O orange taste HO O O O 5-caffeoylquinic acid Coffee taste OH H iPr N O Me O O 2-decanal Capsaicinoids Coriander taste Chilli burning sensation Astray, G. EJEAFChe. 2007, 6, 1742-1763 Food and Food Chemistry Introduction Concepts Food Chemistry the study of chemical processes and interactions of all biological and non-biological components of foods biological substances areas food processing techniques de Man, J. M. Principles of Food Chemistry 1999, Springer Science Fennema, O. R. Food Chemistry. 1985, 2nd edition New York: Marcel Dekker, Inc Food and Food Chemistry Introduction Concepts Food Chemistry the study of chemical processes and interactions of all biological and non-biological components of foods biological substances areas food processing techniques carbo- hydrates water minerals lipids flavors vitamins protein food enzymes colors additive Fennema, O. R. Food Chemistry. -
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 -
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. -
Dimers of Serotonin Receptors: Impact on Ligand Affinity and Signaling
Dimers of serotonin receptors: impact on ligand affinity and signaling Luc Maroteaux, Catherine Béchade, Anne Roumier To cite this version: Luc Maroteaux, Catherine Béchade, Anne Roumier. Dimers of serotonin receptors: impact on ligand affinity and signaling. Biochimie, Elsevier, 2019, 161, pp.23-33. 10.1016/j.biochi.2019.01.009. hal- 01996206 HAL Id: hal-01996206 https://hal.archives-ouvertes.fr/hal-01996206 Submitted on 28 Jan 2019 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Maroteaux et al., 1 Dimers of serotonin receptors: impact on ligand affinity and signaling. Luc Maroteaux1,2,3, Catherine Béchade1,2,3, and Anne Roumier1,2,3 Affiliations: 1: INSERM UMR-S839, S1270, Paris, 75005, France; 2Sorbonne Université, Paris, 75005, France; 3Institut du Fer à Moulin, Paris, 75005, France. Running title: Dimers of serotonin receptors Correspondence should be addressed to: Luc Maroteaux INSERM UMR-S839, S1270, 17 rue du Fer a Moulin Paris, 75005, France; E-mail : [email protected] Abstract Membrane receptors often form complexes with other membrane proteins that directly interact with different effectors of the signal transduction machinery. G-protein-coupled receptors (GPCRs) were for long time considered as single pharmacological entities. -
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. -
Characterization of Gonadotropin Receptors Fshr And
General and Comparative Endocrinology 285 (2020) 113276 Contents lists available at ScienceDirect General and Comparative Endocrinology journal homepage: www.elsevier.com/locate/ygcen Characterization of gonadotropin receptors Fshr and Lhr in Japanese T medaka, Oryzias latipes Susann Burowa, Naama Mizrahib,1, Gersende Maugarsa,1, Kristine von Krogha, Rasoul Nourizadeh-Lillabadia, Lian Hollander-Cohenb, Michal Shpilmanb, Ishwar Atreb, ⁎ ⁎ Finn-Arne Weltziena, , Berta Levavi-Sivanb, a Department of Basic Sciences and Aquatic Medicine, Faculty of Veterinary Medicine, Norwegian University of Life Sciences, 0454 Oslo, Norway b Department of Animal Sciences, Faculty of Agriculture, Food and Environment, The Hebrew University, Rehovot 76100, Israel ARTICLE INFO ABSTRACT Keywords: Reproduction in vertebrates is controlled by the brain-pituitary-gonad axis, where the two gonadotropins fol- Follicle-stimulating hormone licle-stimulating hormone (Fsh) and luteinizing hormone (Lh) play vital parts by activating their cognate re- Follicle-stimulating hormone receptor ceptors in the gonads. The main purpose of this work was to study intra- and interspecies ligand promiscuity of Luteinizing hormone teleost gonadotropin receptors, since teleost receptor specificity is unclear, in contrast to mammalian receptors. Luteinizing hormone receptor Receptor activation was investigated by transfecting COS-7 cells with either Fsh receptor (mdFshr, tiFshr) or Lh Protein structure receptor (mdLhr, tiLhr), and tested for activation by recombinant homologous and heterologous ligands Receptor-ligand interaction Transactivation assay (mdFshβα, mdLhβα, tiFshβα, tiLhβα) from two representative fish orders, Japanese medaka (Oryzias latipes, Beloniformes) and Nile tilapia (Oreochromis niloticus, Cichliformes). Results showed that each gonadotropin preferentially activates its own cognate receptor. Cross-reactivity was detected to some extent as mdFshβα was able to activate the mdLhr, and mdLhβα the mdFshr. -
Human Taste Thresholds Are Modulated by Serotonin and Noradrenaline
12664 • The Journal of Neuroscience, December 6, 2006 • 26(49):12664–12671 Behavioral/Systems/Cognitive Human Taste Thresholds Are Modulated by Serotonin and Noradrenaline Tom P. Heath,1 Jan K. Melichar,2 David J. Nutt,2 and Lucy F. Donaldson1 1Department of Physiology and 2Psychopharmacology Unit, University of Bristol, Bristol BS8 1TD, United Kingdom Circumstances in which serotonin (5-HT) and noradrenaline (NA) are altered, such as in anxiety or depression, are associated with taste disturbances, indicating the importance of these transmitters in the determination of taste thresholds in health and disease. In this study, we show for the first time that human taste thresholds are plastic and are lowered by modulation of systemic monoamines. Measurement of taste function in healthy humans before and after a 5-HT reuptake inhibitor, NA reuptake inhibitor, or placebo showed that enhancing 5-HT significantly reduced the sucrose taste threshold by 27% and the quinine taste threshold by 53%. In contrast, enhancing NA significantly reduced bitter taste threshold by 39% and sour threshold by 22%. In addition, the anxiety level was positively correlated with bitter and salt taste thresholds. We show that 5-HT and NA participate in setting taste thresholds, that human taste in normal healthy subjects is plastic, and that modulation of these neurotransmitters has distinct effects on different taste modalities. We present a model to explain these findings. In addition, we show that the general anxiety level is directly related to taste perception, suggesting that altered taste and appetite seen in affective disorders may reflect an actual change in the gustatory system. -
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. -
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. -
Chemosensory Signalling Pathways Involved in Sensing of Amino Acids by the Ghrelin Cell L
Chemosensory signalling pathways involved in sensing of amino acids by the ghrelin cell L. Vancleef, T. van den Broeck, T. Thijs, S. Steensels, Loïc Briand, J. Tack, I. Depoortere To cite this version: L. Vancleef, T. van den Broeck, T. Thijs, S. Steensels, Loïc Briand, et al.. Chemosensory signalling pathways involved in sensing of amino acids by the ghrelin cell. Scientific Reports, Nature Publishing Group, 2015, 5, pp.15725. 10.1038/srep15725. hal-01233907 HAL Id: hal-01233907 https://hal.archives-ouvertes.fr/hal-01233907 Submitted on 27 May 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution| 4.0 International License www.nature.com/scientificreports OPEN Chemosensory signalling pathways involved in sensing of amino acids by the ghrelin cell Received: 05 May 2015 1 1 1 1 2 1 1 Accepted: 01 October 2015 L. Vancleef , T. Van Den Broeck , T. Thijs , S. Steensels , L. Briand , J. Tack & I. Depoortere Published: 29 October 2015 Taste receptors on enteroendocrine cells sense nutrients and transmit signals that control gut hormone release. This study aimed to investigate the amino acid (AA) sensing mechanisms of the ghrelin cell in a gastric ghrelinoma cell line, tissue segments and mice.