DOCSLIB.ORG

Posttranslational Modification and Degradation

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Posttranslational Modification and Degradation Archaea Archaeal Protein Biogenesis: Posttranslational Modification and Degradation Guest Editors: Jerry Eichler, Julie Maupin-Furlow, and Joerg Soppa Archaeal Protein Biogenesis: Posttranslational Modification and Degradation Archaea Archaeal Protein Biogenesis: Posttranslational Modification and Degradation Guest Editors: Jerry Eichler, Julie Maupin-Furlow, and Joerg Soppa Copyright © 2010 Hindawi Publishing Corporation. All rights reserved. This is a special issue published in volume 2010 of “Archaea.” All articles are open access articles distributed under the Creative Com- mons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Archaea Editorial Board Maqsudul Alam, USA Dennis W. Grogan, USA Francesca M. Pisani, Italy Sonja Verena Albers, Germany Robert P. Gunsalus, USA Marina Porcelli, Italy Ricardo Amils, Spain Reinhard Hensel, Germany David Prangishvili, France Haruyuki Atomi, Japan Li Huang, China Reinhard Rachel, Germany Nils-Kare˚ Birkeland, Norway Michael Ibba, USA Anna-Louise Reysenbach, USA Paul H. Blum, USA Y. Ishino, Japan Frank T. Robb, USA E. A. Bonch-Osmolovskaya, Russia Toshio Iwasaki, Japan Francisco Rodriguez-Valera, Spain MariaJ.Bonete,Spain Zvi Kelman, USA Roberto Scandurra, Italy Giovanna Cacciapuoti, Italy S. W. M. Kengen, The Netherlands Kevin R. Sowers, USA IsaacK.O.Cann,USA Hans-Peter Klenk, Germany Stefan Spring, Germany Daniel¨ Charlier, Belgium Paola Londei, Italy Michael Thomm, Germany Antoine Danchin, France Peter A. Lund, UK Herman van Tilbeurgh, France Uwe Deppenmeier, Germany Giuseppe Manco, Italy Antonio Ventosa, Spain Nejat Duzg¨ unes,¨ USA William W. Metcalf, USA William B. Whitman, USA Jerry Eichler, Israel Marco Moracci, Italy Masafumi Yohda, Japan Harald Engelhardt, Germany Masaaki Morikawa, Japan Chuanlun Zhang, USA Michael W. Friedrich, Germany Volker Mueller, Germany ChristianW.Zwieb,USA Toshiaki Fukui, Japan Katsuhiko Murakami, USA Roger Garrett, Denmark Alla Nozhevnikova, Russia Contents Archaeal Protein Biogenesis: Posttranslational Modification and Degradation, Jerry Eichler, Julie Maupin-Furlow, and Joerg Soppa Volume 2010, Article ID 643046, 2 pages Fidelity in Archaeal Information Processing, Bart de Koning, Fabian Blombach, Stan J. J. Brouns, and John van der Oost Volume 2010, Article ID 960298, 15 pages Selenocysteine, Pyrrolysine, and the Unique Energy Metabolism of Methanogenic Archaea, Michael Rother and Joseph A. Krzycki Volume 2010, Article ID 453642, 14 pages Protein Acetylation in Archaea, Bacteria, and Eukaryotes,Jorg¨ Soppa Volume 2010, Article ID 820681, 9 pages Extensive Lysine Methylation in Hyperthermophilic Crenarchaea: Potential Implications for Protein Stability and Recombinant Enzymes, Catherine H. Botting, Paul Talbot, Sonia Paytubi, and Malcolm F. White Volume 2010, Article ID 106341, 6 pages Iron-Sulfur World in Aerobic and Hyperthermoacidophilic Archaea Sulfolobus, Toshio Iwasaki Volume 2010, Article ID 842639, 14 pages Archaeal Ubiquitin-Like Proteins: Functional Versatility and Putative Ancestral Involvement in tRNA Modification Revealed by Comparative Genomic Analysis, Kira S. Makarova and Eugene V. Koonin Volume 2010, Article ID 710303, 10 pages Phosphorylation and Methylation of Proteasomal Proteins of the Haloarcheon Haloferax volcanii, Matthew A. Humbard, Christopher J. Reuter, Kheir Zuobi-Hasona, Guangyin Zhou, and Julie A. Maupin-Furlow Volume 2010, Article ID 481725, 10 pages Archaea Signal Recognition Particle Shows the Way, Christian Zwieb and Shakhawat Bhuiyan Volume 2010, Article ID 485051, 11 pages Mutational and Bioinformatic Analysis of Haloarchaeal Lipobox-Containing Proteins, Stefanie Storf, Friedhelm Pfeiffer, Kieran Dilks, Zhong Qiang Chen, Saheed Imam, and Mechthild Pohlschroder¨ Volume 2010, Article ID 410975, 11 pages Shaping the Archaeal Cell Envelope, Albert F. Ellen, Behnam Zolghadr, Arnold M. J. Driessen, and Sonja-Verena Albers Volume 2010, Article ID 608243, 13 pages S-Layer Glycoproteins and Flagellins: Reporters of Archaeal Posttranslational Modifications, Ken F. Jarrell, Gareth M. Jones, Lina Kandiba, Divya B. Nair, and Jerry Eichler Volume 2010, Article ID 612948, 13 pages The S-Layer Glycoprotein of the Crenarchaeote Sulfolobus acidocaldarius Is Glycosylated at Multiple Sites with Chitobiose-Linked N-Glycans, Elham Peyfoon, Benjamin Meyer, Paul G. Hitchen, Maria Panico, Howard R. Morris, Stuart M. Haslam, Sonja-Verena Albers, and Anne Dell Volume 2010, Article ID 754101, 10 pages Identification of Residues Important for the Activity of Haloferax volcanii AglD, a Component of the Archaeal N-Glycosylation Pathway, Lina Kaminski and Jerry Eichler Volume 2010, Article ID 315108, 9 pages Hindawi Publishing Corporation Archaea Volume 2010, Article ID 643046, 2 pages doi:10.1155/2010/643046 Editorial Archaeal Protein Biogenesis: Posttranslational Modification and Degradation Jerry Eichler,1 Julie Maupin-Furlow,2 and Joerg Soppa3 1 Department of Life Sciences, Ben-Gurion University of the Negev, Beersheva, Israel 2 Department of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611, USA 3 Institute for Molecular Biosciences, Frankfurt University, 60325 Frankfurt, Germany Correspondence should be addressed to Jerry Eichler, [email protected] Received 1 August 2010; Accepted 1 August 2010 Copyright © 2010 Jerry Eichler et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The study of Archaea at the DNA and RNA levels has Protein degradation is the focus of two articles in this provided considerable insight into replication, transcription, special issue. Makarova and Koonin rely on comparative and other information-associated events which are either genomic analysis to reveal functional versatility of archaeal unique to this remarkable group of organisms or which ubiquitin-like proteins, while Humbard et al. report on were later found to also occur in Bacteria and/or Eukarya. the phosphorylation and methylation of Haloferax volcanii In contrast, largely due to a lack of suitable model systems proteasomal proteins. and a limited number of appropriate molecular tools, Archaeal cell surface proteins undergo a variety of post- considerably less was known about archaeal proteins in terms translational modifications. However, such proteins must of their biogenesis, modification, trafficking, or degradation. first be targeted to and traverse the plasma membrane. In recent years, however, we have witnessed major advances Accordingly, Zwieb and Bhuiyan discuss the latest findings in proteomics, successful in vitro reconstitutions, and the on the archaeal signal recognition particle targeting system. development of reporter systems compatible with extreme Storf et al. address questions related to the biogenesis of conditions. Relying on such tools, insight into different stages one class of membrane proteins, namely, lipoproteins. An in the life of archaeal proteins has begun to accumulate. article by Ellen et al. considers archaeal protein export and In this special issue of Archaea, we present a series of describes different cell surface structures, while a report articles addressing the current state of understanding of by Jarrell et al. focuses on the S-layer glycoprotein and selected facets of archaeal protein biogenesis and process- flagella as reporters of choice of different protein processing ing. events. With this in mind, Peyfoon and colleagues describe An article by De Koning et al. discussing how fidelity the N-linked glycan decorating the S-layer glycoprotein in archaeal information processing at the DNA, RNA, and of Sulfolobus acidocaldarius. Finally, Kaminski and Eichler protein levels is achieved begins this special issue. Rother consider the workings of AglD, one of the enzymes which and Krzycki then address proteins containing the unusual is involved in Haloferax volcanii S-layer glycoprotein N- animo acids, selenocysteine, and pyrrolysine, as related to the glycosylation. unique energy metabolism of methanogenic archaea. Soppa In this, the first special issue of Archaea dedicated to compares one specific posttranslational modification, acety- archaeal protein biogenesis, we have tried to give the reader lation, across evolutionary lines, while Botting et al. discuss a sampling of the current research scene. It is our sincere the importance of lysine methylation in hyperthermophilic hope that the community will find interest in the articles crenarchaeota. Questions related to protein assembly are included here. More importantly, it is our intention that the considered when Iwasaki addresses the iron-sulfur world in work presented will stimulate other laboratories to begin hyperthermoacidophilic archaea. studying questions related to archaeal protein biogenesis, 2 Archaea hopefully in time for the next installment of this special issue. Jerry Eichler Julie Maupin-Furlow Joerg Soppa Hindawi Publishing Corporation Archaea Volume 2010, Article ID 960298, 15 pages doi:10.1155/2010/960298 Review Article Fidelity in Archaeal Information Processing Bart de Koning, Fabian Blombach, Stan J. J. Brouns, and John van der Oost Laboratory of Microbiology, Wageningen University, Dreijenplein 10, 6703 HB Wageningen, The Netherlands Correspondence should be addressed to Bart de Koning, [email protected] Received 15 May 2010; Accepted 12 July 2010 Academic Editor:
Load more

Recommended publications
  • The Deiodination of Thyroid Hormone in Rat Liver
    The deiodination of thyroid hormone in rat liver De dejodering van schildklierhormoon in de lever van de rat PROEFSCHRIFT T er verkrijging van de graad van doctor in de geneeskunde aan de Erasmus Universiteit Rotterdam op gezag van de rector magnificus prof. dr. M. W. van Hof en vo1gens bes1uit van het college van dekanen. De openbare verdediging zal p1aatsvinden op woensdag 12 juni 1985 te 15.45 uur door Jan Adrianus Mol geboren te Dordrecht BEGELEIDINGSCOMMISSIE PROMOTOR PROF. DR. G. HENNEMANN OVERIGE LEDEN PROF. DR. W.C. HuLSMANN PROF. DR. H.J. VANDER MOLEN PROF. DR. H.J. VAN EIJK The studies in this thesis were carried out under the direction of Dr. T.J. Visser in the laboratory of the Thyroid Hormone Research Unit (head Prof. Dr. G. Hennemann) at the Department of Internal Medicine III and Clinical ·Endocrinology (head Prof. Dr. J.c. Birkenhager), Erasmus University Medical School, Rotterdam, The Netherlands. The investigations were supported by grant 13-34-108 from the Foundation for Medical Research FUNGO. Kennis, zij zal afgedaan hebben •... zo blijven dan: Geloof, hoop en liefde •.•. (I Korintiers 13) aan mijn Ouders aan Ellen, Gerben en Jurjan CONTENTS List of abbreviations. 7 Chapter I General introduction. 9 Chapter II The liver, a central organ for iodothyronine 17 metabolism? Chapter III Synthesis and some properties of sulfate 45 esters and sulfamates o_f iodothyronines. Chapter IV Rapid and selective inner ring deiodination 61 of T4 sulfate by rat liver deiodinase. Chapter V Modification of rat liver iodothyronine 75 5'-deiodinase activity with diethylpyrocarbo­ nate and Rose Bengal: evidence for an active site histidine residue.
    [Show full text]
  • Biochemical Mechanisms of Thyroid Hormone Deiodination
    THYROID Volume 15, Number 8, 2005 © Mary Ann Liebert, Inc. Biochemical Mechanisms of Thyroid Hormone Deiodination George G.J.M. Kuiper, Monique H.A. Kester, Robin P. Peeters, and Theo J. Visser Deiodination is the foremost pathway of thyroid hormone metabolism not only in quantitative terms but also because thyroxine (T4) is activated by outer ring deiodination (ORD) to 3,3’,5-triiodothyronine (T3), whereas both T4 and T3 are inactivated by inner ring deiodination (IRD) to 3,3’,5-triiodothyronine and 3,3’- diiodothyronine, respectively. These reactions are catalyzed by three iodothyronine deiodinases, D1-3. Although they are homologous selenoproteins, they differ in important respects such as catalysis of ORD and/or IRD, deiodination of sulfated iodothyronines, inhibition by the thyrostatic drug propylthiouracil, and regulation during fetal and neonatal development, by thyroid state, and during illness. In this review we will briefly discuss recent developments in these different areas. These have resulted in the emerging view that the biological activity of thyroid hormone is regulated locally by tissue-specific regulation of the different deiodinases. HYROID HORMONE is essential for growth, development, thyrostatic drug 6-propyl-2-thiouracil (PTU). D1 activity is Tand regulation of energy metabolism (1–3). Amphibian positively regulated by T3, reflecting regulation of D1 ex- metamorphosis is an important example of thyroid hormone pression by T3 at the pretranslational level. actions on development (4). Equally well known is the crit- In humans, D2 activity is found in brain, anterior pitu- ical role of thyroid hormone in development and function itary, placenta, thyroid and skeletal muscle, and D2 mRNA of the human central nervous system (5,6).
    [Show full text]
  • Thyroid-Modulating Activities of Olive and Its Polyphenols: a Systematic Review
    nutrients Review Thyroid-Modulating Activities of Olive and Its Polyphenols: A Systematic Review Kok-Lun Pang 1,† , Johanna Nathania Lumintang 2,† and Kok-Yong Chin 1,* 1 Department of Pharmacology, Faculty of Medicine, Universiti Kebangsaan Malaysia, Jalan Yaacob Latif, Bandar Tun Razak, Cheras 56000, Kuala Lumpur, Malaysia; [email protected] 2 Faculty of Applied Sciences, UCSI University Kuala Lumpur Campus, Jalan Menara Gading, Taman Connaught, Cheras 56000, Kuala Lumpur, Malaysia; [email protected] * Correspondence: [email protected]; Tel.: +60-3-91459573 † These authors contributed equally to this work. Abstract: Olive oil, which is commonly used in the Mediterranean diet, is known for its health benefits related to the reduction of the risks of cancer, coronary heart disease, hypertension, and neurodegenerative disease. These unique properties are attributed to the phytochemicals with potent antioxidant activities in olive oil. Olive leaf also harbours similar bioactive compounds. Several studies have reported the effects of olive phenolics, olive oil, and leaf extract in the modulation of thyroid activities. A systematic review of the literature was conducted to identify relevant studies on the effects of olive derivatives on thyroid function. A comprehensive search was conducted in October 2020 using the PubMed, Scopus, and Web of Science databases. Cellular, animal, and human studies reporting the effects of olive derivatives, including olive phenolics, olive oil, and leaf extracts on thyroid function were considered. The literature search found 445 articles on this topic, but only nine articles were included based on the inclusion and exclusion criteria. All included articles were animal studies involving the administration of olive oil, olive leaf extract, or olive pomace residues orally.
    [Show full text]
  • REVIEW Iodothyronine Deiodinase Structure and Function
    189 REVIEW Iodothyronine deiodinase structure and function: from ascidians to humans Veerle M Darras and Stijn L J Van Herck Animal Physiology and Neurobiology Section, Department of Biology, Laboratory of Comparative Endocrinology, KU Leuven, Naamsestraat 61, PO Box 2464, B-3000 Leuven, Belgium (Correspondence should be addressed to V M Darras; Email: [email protected]) Abstract Iodothyronine deiodinases are important mediators of thyroid of each of them, however, varies amongst species, develop- hormone (TH) action. They are present in tissues throughout mental stages and tissues. This is especially true for 0 the body where they catalyse 3,5,3 -triiodothyronine (T3) amphibians, where the impact of D1 may be minimal. D2 production and degradation via, respectively, outer and inner and D3 expression and activity respond to thyroid status in ring deiodination. Three different types of iodothyronine an opposite and conserved way, while the response of D1 is deiodinases (D1, D2 and D3) have been identified in variable, especially in fish. Recently, a number of deiodinases vertebrates from fish to mammals. They share several have been cloned from lower chordates. Both urochordates common characteristics, including a selenocysteine residue and cephalochordates possess selenodeiodinases, although in their catalytic centre, but show also some type-specific they cannot be classified in one of the three vertebrate types. differences. These specific characteristics seem very well In addition, the cephalochordate amphioxus also expresses conserved for D2 and D3, while D1 shows more evolutionary a non-selenodeiodinase. Finally, deiodinase-like sequences diversity related to its Km, 6-n-propyl-2-thiouracil sensitivity have been identified in the genome of non-deuterostome and dependence on dithiothreitol as a cofactor in vitro.
    [Show full text]
  • Selenium Vs. Sulfur: Investigating the Substrate Specificity of a Selenocysteine Lyase
    University of Central Florida STARS Electronic Theses and Dissertations, 2004-2019 2019 Selenium vs. Sulfur: Investigating the Substrate Specificity of a Selenocysteine Lyase Michael Johnstone University of Central Florida Part of the Biotechnology Commons Find similar works at: https://stars.library.ucf.edu/etd University of Central Florida Libraries http://library.ucf.edu This Masters Thesis (Open Access) is brought to you for free and open access by STARS. It has been accepted for inclusion in Electronic Theses and Dissertations, 2004-2019 by an authorized administrator of STARS. For more information, please contact [email protected]. STARS Citation Johnstone, Michael, "Selenium vs. Sulfur: Investigating the Substrate Specificity of a Selenocysteine Lyase" (2019). Electronic Theses and Dissertations, 2004-2019. 6511. https://stars.library.ucf.edu/etd/6511 SELENIUM VS. SULFUR: INVESTIGATING THE SUBSTRATE SPECIFICITY OF A SELENOCYSTEINE LYASE by MICHAEL ALAN JOHNSTONE B.S. University of Central Florida, 2017 A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science in the Burnett School of Biomedical Sciences in the College of Medicine at the University of Central Florida Orlando, Florida Summer Term 2019 Major Professor: William T. Self © 2019 Michael Alan Johnstone ii ABSTRACT Selenium is a vital micronutrient in many organisms. While traces are required for survival, excess amounts are toxic; thus, selenium can be regarded as a biological “double-edged sword”. Selenium is chemically similar to the essential element sulfur, but curiously, evolution has selected the former over the latter for a subset of oxidoreductases. Enzymes involved in sulfur metabolism are less discriminate in terms of preventing selenium incorporation; however, its specific incorporation into selenoproteins reveals a highly discriminate process that is not completely understood.
    [Show full text]
  • Association of Antiepileptic Drug Usage, Trace Elements and Thyroid Hormone Status
    C Zevenbergen, Trace elements and thyroid 174:4 425–432 Clinical Study T I M Korevaar, hormones A Schuette and others Association of antiepileptic drug usage, trace elements and thyroid hormone status Chantal Zevenbergen1,2,*, Tim I M Korevaar1,2,*, Andrea Schuette3,*, Robin P Peeters1,2, Marco Medici1,2, Theo J Visser1,2, Lutz Schomburg3 and W Edward Visser1,2 1Department of Internal Medicine and 2Rotterdam Thyroid Center, Erasmus Medical Center, Wytemaweg 80, 3015 Correspondence CN Rotterdam, The Netherlands and 3Institut fu¨ r Experimentelle Endokrinologie, Charite´ -Universita¨ tsmedizin should be addressed Berlin, Augustenburger Platz 1, D-13353 Berlin, Germany to W E Visser *(C Zevenbergen, T I M Korevaar, A Schuette contributed equally to this work) Email [email protected] Abstract Background: Levels of thyroid hormone (TH) and trace elements (copper (Cu) and selenium (Se)) are important for development and function of the brain. Anti-epileptic drugs (AEDs) can influence serum TH and trace element levels. As the relationship between AEDs, THs, and trace elements has not yet been studied directly, we explored these interactions. Method: In total 898 participants, from the Thyroid Origin of Psychomotor Retardation study designed to investigate thyroid parameters in subjects with intellectual disability (ID), had data available on serum Se, Cu, thyroid stimulating hormone (TSH), free thyroxine (FT4), tri-iodothyronine (T3), reverse T3,T4, and thyroxine-binding globulin (TBG); 401 subjects were on AED treatment. Differences in trace elements according to medication usage was investigated using ANOVA, and associations between trace elements and thyroid parameters were analysed using (non-) linear regression models. Results: Study participants were not deficient in any of the trace elements analyzed.
    [Show full text]
  • Ata Grant Recipients: Publications
    American Thyroid Association Grant Recipients: PUBLICATIONS 2003 KNAUF, J. “Tyrosine kinase receptor oncogenes and prostanoid biosynthesis: Role of RET/PTC-induced activation of PGE2 synthase in thyroid tumorigenesis” 1. Puxeddu E, Mitsutake N, Knauf JA, Moretti S, Kim HW, Seta KA, Brockman D, Myatt L, Millhorn DE, Fagin JA 2003. Microsomal prostaglandin E2 synthase-1 is induced by conditional expression of RET/PTC in thyroid PCCL3 cells through the activation of the MEK-ERK pathway. J Biol Chem 278:52131- 52138. 2. Knauf JA, Ouyang B, Croyle M, Kimura E, Fagin JA 2003. Acute expression of RET/PTC induces isozyme-specific activation and subsequent downregulation of PKCepsilon in PCCL3 thyroid cells. Oncogene 22:6830-6838. 3. Knauf JA, Kuroda H, Basu S, Fagin JA 2003. RET/PTC-induced dedifferentiation of thyroid cells is mediated through Y1062 signaling through SHC-RAS-MAP kinase. Oncogene 22:4406-4412. 4. Wang J, Knauf JA, Basu S, Puxeddu E, Kuroda H, Santoro M, Fusco A, Fagin JA 2003. Conditional expression of RET/PTC induces a weak oncogenic drive in thyroid PCCL3 cells and inhibits thyrotropin action at multiple levels. Mol Endocrinol 17:1425-1436. JACOBSON, E. “Molecular determinants of the presentation of immunogenic thyroglobulin peptides by HLA-DR3” New to the thyroid field; no prior thyroid publications XU, XIULONG* “BRAF gene mutation and oncogenesis of papillary thyroid carcinomas” * ThyCa award 1. Xu X, Quiros RM, Maxhimer JB, Jiang P, Marcinek R, Ain KB, Platt JL, Shen J, Gattuso P, Prinz RA 2003. Inverse correlation between heparan sulfate composition and heparanase-1 gene expression in thyroid papillary carcinomas: a potential role in tumor metastasis.
    [Show full text]
  • Iodotyrosine Deiodinase from Selected Phyla Engineered for Bacterial Expression
    ABSTRACT Title of Document: IODOTYROSINE DEIODINASE FROM SELECTED PHYLA ENGINEERED FOR BACTERIAL EXPRESSION Jennifer Marilyn Buss Doctor of Philosophy, 2012 Directed By: Professor Steven E. Rokita Department of Chemistry and Biochemistry Iodide is a well known halogen necessary for development. The majority of iodide processing in biological systems occurs in the thyroid gland. Iodide salvage is essential to thyroid hormone metabolism and metabolic regulation. The DEHAL1 gene product iodotyrosine deiodinase (IYD) is responsible for deiodination of the mono- and diiodotyrosine byproducts of thyroid hormone synthesis (triiodothyronine and thyroxine, T3 and T4, respectively). IYD is a membrane-bound flavoprotein comprised of three domains with the catalytic domain belonging to the NADPH oxidase/flavin reductase structural superfamily. This enzyme required engineering for expression of soluble protein in E. coli and was characterized using CD spectra, kinetic rate constants, binding constants of substrates, and crystal structure. Analysis of the crystal structure of IYD indicates a dimer with an active site comprising of both monomers and orienting the C-I bond of iodotyrosine substrate stacking above the N5 of the flavin mononucleotide (FMN) required for activity. The crystal structure also identifies an active site lid that distinguishes IYD from other proteins in the NADPH oxidase/flavin reductase superfamily. Three amino acids (E153, Y157, and K178) on the active site lid form hydrogen bonding and electrostatic contacts with the zwitterionic portion of the substrate. Mutation to any of these three amino acids significantly decreases substrate-binding affinity and enzymatic activity. Homologous sequences of IYD were identified in other organisms and four sequences as representatives from their phyla were expressed in E.
    [Show full text]
  • Food Sources of Selenium and Its Relationship with Chronic Diseases
    nutrients Review Food Sources of Selenium and Its Relationship with Chronic Diseases Wenli Hu , Chong Zhao, Hongbo Hu and Shutao Yin * College of Food Science and Nutritional Engineering, China Agricultural University, 17 Qinghua East Road, Haidian District, Beijing 100083, China; [email protected] (W.H.); [email protected] (C.Z.); [email protected] (H.H.) * Correspondence: [email protected] Abstract: Selenium (Se) is an essential micronutrient for mammals, and its deficiency seriously threatens human health. A series of biofortification strategies have been developed to produce Se-enriched foods for combating Se deficiency. Although there have been some inconsistent results, extensive evidence has suggested that Se supplementation is beneficial for preventing and treating several chronic diseases. Understanding the association between Se and chronic diseases is essential for guiding clinical practice, developing effective public health policies, and ultimately counteracting health issues associated with Se deficiency. The current review will discuss the food sources of Se, biofortification strategies, metabolism and biological activities, clinical disorders and dietary reference intakes, as well as the relationship between Se and health outcomes, especially cardiovascular disease, diabetes, chronic inflammation, cancer, and fertility. Additionally, some concepts were proposed, there is a non-linear U-shaped dose-responsive relationship between Se status and health effects: subjects with a low baseline Se status can benefit from Se supplementation, while Se supplementation in populations with an adequate or high status may potentially increase the risk of some diseases. In addition, at supra-nutritional levels, methylated Se compounds exerted more promising cancer Citation: Hu, W.; Zhao, C.; Hu, H.; chemo-preventive efficacy in preclinical trials.
    [Show full text]
  • Comparative Kinetic Characterization of Rat Thyroid Iodotyrosine Dehalogenase and Iodothyronine Deiodinase Type 1
    385 Comparative kinetic characterization of rat thyroid iodotyrosine dehalogenase and iodothyronine deiodinase type 1 J C Solís-S, P Villalobos, A Orozco and C Valverde-R Department of Cellular and Molecular Neurobiology, Institute of Neurobiology, UNAM, Campus UNAM-UAQ Juriquilla, Queretaro, Qro 76230, Mexico (Requests for offprints should be addressed to J C Solís-S; Email: [email protected]) Abstract The initial characterization of a thyroid iodotyrosine of the two different dehalogenating enzymes has not yet dehalogenase (tDh), which deiodinates mono-iodotyrosine been clearly defined. This work compares and contrasts and di-iodotyrosine, was made almost 50 years ago, but the kinetic properties of tDh and ID1 in the rat thyroid little is known about its catalytic and kinetic properties. gland. Differential affinities for substrates, cofactors and A distinct group of dehalogenases, the so-called iodo- inhibitors distinguish the two activities, and a reaction thyronine deiodinases (IDs), that specifically remove mechanism for tDh is proposed. The results reported here iodine atoms from iodothyronines were subsequently support the view that the rat thyroid gland has a distinctive discovered and have been extensively characterized. set of dehalogenases specialized in iodine metabolism. Iodothyronine deiodinase type 1 (ID1) is highly expressed Journal of Endocrinology (2004) 181, 385–392 in the rat thyroid gland, but the co-expression in this tissue Introduction inactive intracellular THs in practically all vertebrate tissues (Köhrle 2000, Bianco et al. 2002). There seems to Iodine, the rate-limiting trace element in the biosynthesis be important species-specific differences regarding the of iodothyronines or thyroid hormones (THs), is actively expression of IDs in the thyroid gland.
    [Show full text]
  • Type 1 and Type 2 Iodothyronine Deiodinases in the Thyroid Gland of Patients with Huge Goitrous Hashimoto’S Thyroiditis
    Endocrine (2019) 64:584–590 https://doi.org/10.1007/s12020-019-01855-7 ORIGINAL ARTICLE Type 1 and type 2 iodothyronine deiodinases in the thyroid gland of patients with huge goitrous Hashimoto’s thyroiditis 1 1 1 2 2 2 Azusa Harada ● Emiko Nomura ● Kumiko Nishimura ● Mitsuru Ito ● Hiroshi Yoshida ● Akira Miyauchi ● 2 1 1 Mitsushige Nishikawa ● Ichiro Shiojima ● Nagaoki Toyoda Received: 10 November 2018 / Accepted: 28 January 2019 / Published online: 8 February 2019 © Springer Science+Business Media, LLC, part of Springer Nature 2019 Abstract Purpose The serum free triiodothyronine (FT3)/free thyroxine (FT4) ratio in patients with huge goitrous Hashimoto’s thyroiditis (HG-HT) is relatively high. We investigated the cause of high FT3/FT4 ratios. Methods We measured the serum FT3,FT4, and thyrotropin (TSH) levels of seven patients with HG-HT who had undergone a total thyroidectomy. Eleven patients with papillary thyroid carcinoma served as controls. The activities and mRNA levels of type 1 and type 2 iodothyronine deiodinases (D1 and D2, respectively) were measured in the thyroid tissues of HG-HT and perinodular thyroid tissues of papillary thyroid carcinoma. fi 1234567890();,: 1234567890();,: Results The TSH levels in the HG-HT group were not signi cantly different from those of the controls. The FT4 levels in the HG-HT group were significantly lower than those of the controls, whereas the FT3 levels and FT3/FT4 ratios were sig- nificantly higher in the HG-HT group. The FT3/FT4 ratios in the HG-HT group who had undergone total thyroidectomy and received levothyroxine therapy decreased significantly to normal values.
    [Show full text]
  • Thermogenesis in Adipose Tissue Activated by Thyroid Hormone
    International Journal of Molecular Sciences Review Thermogenesis in Adipose Tissue Activated by Thyroid Hormone Winifred W. Yau 1 and Paul M. Yen 1,2,* 1 Laboratory of Hormonal Regulation, Cardiovascular and Metabolic Disorders Program, Duke NUS Medical School, Singapore 169857, Singapore; [email protected] 2 Duke Molecular Physiology Institute, Duke University, Durham, NC 27708, USA * Correspondence: [email protected]; Tel.: +65-6516-7666 Received: 23 March 2020; Accepted: 22 April 2020; Published: 24 April 2020 Abstract: Thermogenesis is the production of heat that occurs in all warm-blooded animals. During cold exposure, there is obligatory thermogenesis derived from body metabolism as well as adaptive thermogenesis through shivering and non-shivering mechanisms. The latter mainly occurs in brown adipose tissue (BAT) and muscle; however, white adipose tissue (WAT) also can undergo browning via adrenergic stimulation to acquire thermogenic potential. Thyroid hormone (TH) also exerts profound effects on thermoregulation, as decreased body temperature and increased body temperature occur during hypothyroidism and hyperthyroidism, respectively. We have termed the TH-mediated thermogenesis under thermoneutral conditions “activated” thermogenesis. TH acts on the brown and/or white adipose tissues to induce uncoupled respiration through the induction of the uncoupling protein (Ucp1) to generate heat. TH acts centrally to activate the BAT and browning through the sympathetic nervous system. However, recent studies also show that TH acts peripherally on the BAT to directly stimulate Ucp1 expression and thermogenesis through an autophagy-dependent mechanism. Additionally, THs can exert Ucp1-independent effects on thermogenesis, most likely through activation of exothermic metabolic pathways. This review summarizes thermogenic effects of THs on adipose tissues.
    [Show full text]