DOCSLIB.ORG

Magnesium in the Central Nervous System

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

Welcome to the electronic edition of Magnesium in the Central Nervous System. The book opens with the bookmark panel and you will see the contents page. Click on this anytime to return to the contents. You can also add your own bookmarks. Each chapter heading in the contents table is clickable and will take you direct to the chapter. Return using the contents link in the bookmarks. The whole document is fully searchable. Enjoy. Magnesium in the Central Nervous System Magnesium in the Central Nervous System EDITED BY ROBERT VINK Discipline of Anatomy and Pathology & Adelaide Centre for Neuroscience Research, School of Medical Sciences, The University of Adelaide, Adelaide, South Australia, Australia MIHAI NECHIFOR Department of Pharmacology, “Gr. T. Popa” University of Medicine and Pharmacy, Iasi, Romania Published in Adelaide by University of Adelaide Press Barr Smith Library The University of Adelaide South Australia 5005 [email protected] www.adelaide.edu.au/press The University of Adelaide Press publishes externally refereed scholarly books by staff of the University of Adelaide. It aims to maximise the accessibility to its best research by publishing works through the internet as free downloads and as high quality printed volumes on demand. Electronic Index: this book is available from the website as a down‐loadable PDF with fully searchable text. Please use the electronic version to serve as the index. © 2011 The Authors This book is copyright. Apart from any fair dealing for the purposes of private study, research, criticism or review as permitted under the Copyright Act, no part may be reproduced, stored in a retrieval system, or transmitted, in any form or by any means, electronic, mechanical, photocopying, recording or otherwise without the prior written permission. Address all inquiries to the Director at the above address. For the full Cataloguing‐in‐Publication data please contact National Library of Australia Magnesium in the central nervous system / edited by Robert Vink and Mihai Nechifor. I Vink, Robert. II Nechifor, Mihai. 1 Magnesium—Physiological effect. 2 Magnesium in the body. 3 Central nervous system. ISBN (electronic) 978‐0‐9870730‐5‐1 ISBN (paperback) 978‐0‐9870730‐6‐8 Book design: Robert Vink Cover design: Emma Spoehr. Photograph with permission, istockphoto.com Paperback printed by Griffin Press, South Australia Magnesium in the Central Nervous System List of Contributors Bulent Ahishali Istanbul University, Istanbul Faculty of Medicine, Department of Physiology & Department of Histology and Embryology, Capa 34093 Istanbul, Turkey Jean-Pierre Bali Université Montpellier I, 34000 Montpellier, France Jean-Marie Billard Université Paris Descartes, Faculté de Médecine René Descartes, Centre de Psychiatrie et Neurosciences, UMR 894, Paris, 75014, France Kym Campbell Centre for Neuromuscular and Neurological Disorders, University of Western Australia & Australian Neuromuscular Research Institute, Department of Neurosurgery, Sir Charles Gairdner Hospital, Nedlands, Western Australia, Australia Yves Cazals UMR6231, Université Paul Cézanne, Marseille, France Zheng Chen Department of Psychiatry & Institute for Geriatric Clinic and Rehabilitation, Beijing Geriatric Hospital, Beijing 100095, China Dehua Chui Neuroscience Research Institute & Department of Neurobiology, Key Laboratory for Neuroscience, Ministry of Education & Ministry of Public Health, Health Science Center, Peking University, Beijing 100191, China Naomi L. Cook Discipline of Anatomy and Pathology, School of Medical Sciences & Adelaide Centre for Neuroscience Research, The University of Adelaide, Adelaide, South Australia, Australia Frances Corrigan Discipline of Anatomy and Pathology, School of Medical Sciences & Adelaide Centre for Neuroscience Research, The University of Adelaide, Adelaide, South Australia, Australia Magdalena D. Cuciureanu Department of Pharmacology, “Gr. T. Popa” University of Medicine and Pharmacy 16, Iasi, Romania Sang-Hwan Do Department of Anesthesiology and Pain medicine, Seoul National University Bundang Hospital, Seongnam, South Korea George A. Eby III George Eby Research Institute, 14909-C Fitzhugh Road, Austin, Texas, USA Karen L. Eby George Eby Research Institute, 14909-C Fitzhugh Road, Austin, Texas, USA Mounir N. Ghabriel Discipline of Anatomy and Pathology, School of Medical Sciences & Adelaide Centre for Neuroscience Research, The University of Adelaide, Adelaide, South Australia, Australia Tomoyo Hashimoto Department of Internal Medicine (Neurology and Rheumatology), Shinshu University School of Medicine, Nagano, Japan Michael R. Hoane Restorative Neuroscience Laboratory, Brain and Cognitive Science Program, Department of Psychology Southern Illinois University, Carbondale, Illinois, USA Xavier Holy Institut de Recherche Biomédicale des Armées, Antenne de Brétigny, Brétigny-sur-Orge, France Stefano Iotti Dipartimento di Medicina Interna, dell’Invecchiamento e Malattie Nefrologiche, Università di Bologna, Italy and Istituto Nazionale di Biostrutture e Biosistemi, Roma, Italy v Magnesium in the Central Nervous System Mehmet Kaya Istanbul University, Istanbul Faculty of Medicine, Department of Physiology & Department of Histology and Embryology, Capa 34093 Istanbul, Turkey Neville W. Knuckey Centre for Neuromuscular and Neurological Disorders, University of Western Australia, & Australian Neuromuscular Research Institute, Department of Neurosurgery, Sir Charles Gairdner Hospital, Nedlands, Western Australia, Australia Marzia Leidi Università di Milano, Dipartimento di Scienze Cliniche Luigi Sacco, Via G.B. Grassi 74, 20157 Milano, Italy Yi Liu Neuroscience Research Institute & Department of Neurobiology, Key Laboratory for Neuroscience, Ministry of Education & Ministry of Public Health, Health Science Center, Peking University, Beijing 100191, China Jeanette A.M. Maier Università di Milano, Dipartimento di Scienze Cliniche Luigi Sacco, Via G.B. Grassi 74, 20157 Milano, Italy Emil Malucelli Dipartimento di Medicina Interna, dell’Invecchiamento e Malattie Nefrologiche, Università di Bologna, Italy Lucia Mastrototaro Istituto di Patologia Generale e Centro di Ricerche Oncologiche Giovanni XXIII, Università Cattolica del Sacro Cuore, Rome, Italy Alexander Mauskop The New York Headache Center, 30 East 76th Street, New York, NY, USA Bruno P. Meloni Centre for Neuromuscular and Neurological Disorders, University of Western Australia, & Australian Neuromuscular Research Institute, Department of Neurosurgery, Sir Charles Gairdner Hospital, Nedlands, Western Australia, Australia Marianne Mousain-Bosc Ecole de l’ADN, Museum d’Histoire Naturelle de Nîmes, 19, Grand’rue, 30000 Nimes, France Harald Murck Clinic of Psychiatry and Psychotherapy, University of Marburg, Marburg, Germany Hyo-Seok Na Department of Anesthesiology and Pain medicine, Seoul National University Bundang Hospital, Seongnam, South Korea Mihai Nechifor Department of Pharmacology, “Gr. T. Popa” University of Medicine and Pharmacy, Iasi, Romania Kiyomitsu Oyanagi Department of Brain Disease Research, Shinshu University School of Medicine, Nagano Japan Victoria Papadopol Regional Centre of Public Health Iaşi, Romania Florent Raffin Institut de Recherche Biomédicale des Armées, Antenne de la Tronche, La Tronche, France Andrea M.P. Romani Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, Ohio USA Harry Rubin Department of Molecular and Cell Biology, Life Sciences Addition, University of California, Berkeley, CA, USA Jung-Hee Ryu Department of Anesthesiology and Pain medicine, Seoul National University Bundang Hospital, Seongnam, South Korea vi Magnesium in the Central Nervous System Jeffrey L. Saver UCLA Stroke Center, Geffen School of Medicine of the University of California, Los Angeles, CA, USA Isabelle Sendowski Institut de Recherche Biomédicale des Armées, Antenne de la Tronche, La Tronche, France Christian Siatka Ecole de l’ADN, Museum d’Histoire Naturelle de Nîmes, 19, grand’rue, 30000 Nimes, France Yuetao Song Department of Psychiatry & Institute for Geriatric Clinic and Rehabilitation, Beijing Geriatric Hospital, Beijing 100095, China Sidney Starkman UCLA Stroke Center, Geffen School of Medicine of the University of California, Los Angeles, CA, USA Valentina Trapani Istituto di Patologia Generale e Centro di Ricerche Oncologiche Giovanni XXIII, Università Cattolica del Sacro Cuore, Rome, Italy Walter M. van den Bergh Department of Intensive Care, Academic Medical Center, 1100 DD Amsterdam, The Netherlands Corinna van den Heuvel Discipline of Anatomy and Pathology, School of Medical Sciences & Adelaide Centre for Neuroscience Research, The University of Adelaide, Adelaide, South Australia, Australia Robert Vink Discipline of Anatomy and Pathology, School of Medical Sciences & Adelaide Centre for Neuroscience Research, The University of Adelaide, Adelaide, South Australia, Australia Weishan Wang Department of Psychiatry & Institute for Geriatric Clinic and Rehabilitation, Beijing Geriatric Hospital, Beijing 100095, China Federica I. Wolf Istituto di Patologia Generale e Centro di Ricerche Oncologiche Giovanni XXIII, Università Cattolica del Sacro Cuore, Rome, Italy Lisa A. Yablon The New York Headache Center, 30 East 76th Street, New York, NY, USA Huan Yang Neuroscience Research Institute & Department of Neurobiology, Key Laboratory for Neuroscience, Ministry of Education & Ministry of Public Health, Health Science Center, Peking University, Beijing 100191, China Jia Yu Department of Psychiatry
Recommended publications
  • Bioinformatic Analyses of Integral Membrane Transport Proteins Encoded Within the Genome of the Planctomycetes Species, Rhodopirellula Baltica

    Bioinformatic Analyses of Integral Membrane Transport Proteins Encoded Within the Genome of the Planctomycetes Species, Rhodopirellula Baltica

    UC San Diego UC San Diego Previously Published Works Title Bioinformatic analyses of integral membrane transport proteins encoded within the genome of the planctomycetes species, Rhodopirellula baltica. Permalink https://escholarship.org/uc/item/0f85q1z7 Journal Biochimica et biophysica acta, 1838(1 Pt B) ISSN 0006-3002 Authors Paparoditis, Philipp Västermark, Ake Le, Andrew J et al. Publication Date 2014 DOI 10.1016/j.bbamem.2013.08.007 Peer reviewed eScholarship.org Powered by the California Digital Library University of California Biochimica et Biophysica Acta 1838 (2014) 193–215 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbamem Bioinformatic analyses of integral membrane transport proteins encoded within the genome of the planctomycetes species, Rhodopirellula baltica Philipp Paparoditis a, Åke Västermark a,AndrewJ.Lea, John A. Fuerst b, Milton H. Saier Jr. a,⁎ a Department of Molecular Biology, Division of Biological Sciences, University of California at San Diego, La Jolla, CA, 92093–0116, USA b School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland, 9072, Australia article info abstract Article history: Rhodopirellula baltica (R. baltica) is a Planctomycete, known to have intracellular membranes. Because of its un- Received 12 April 2013 usual cell structure and ecological significance, we have conducted comprehensive analyses of its transmembrane Received in revised form 8 August 2013 transport proteins. The complete proteome of R. baltica was screened against the Transporter Classification Data- Accepted 9 August 2013 base (TCDB) to identify recognizable integral membrane transport proteins. 342 proteins were identified with a Available online 19 August 2013 high degree of confidence, and these fell into several different classes.
  • Some Drugs Are Excluded from Medicare Part D, but Are Covered by Your Medicaid Benefits Under the Healthpartners® MSHO Plan (HMO)

    Some Drugs Are Excluded from Medicare Part D, but Are Covered by Your Medicaid Benefits Under the Healthpartners® MSHO Plan (HMO)

    Some drugs are excluded from Medicare Part D, but are covered by your Medicaid benefits under the HealthPartners® MSHO Plan (HMO). These drugs include some over‐the‐counter (OTC) items, vitamins, and cough and cold medicines. If covered, these drugs will have no copay and will not count toward your total drug cost. For questions, please call Member Services at 952‐967‐7029 or 1‐888‐820‐4285. TTY members should call 952‐883‐6060 or 1‐800‐443‐0156. From October 1 through February 14, we take calls from 8 a.m. to 8 p.m., seven days a week. You’ll speak with a representative. From February 15 to September 30, call us 8 a.m. to 8 p.m. Monday through Friday to speak with a representative. On Saturdays, Sundays and holidays, you can leave a message and we’ll get back to you within one business day. Drug Description Strength 3 DAY VAGINAL 4% 5‐HYDROXYTRYPTOPHAN 50 MG ABSORBASE ACETAMINOPHEN 500 MG ACETAMINOPHEN 120MG ACETAMINOPHEN 325 MG ACETAMINOPHEN 650MG ACETAMINOPHEN 80 MG ACETAMINOPHEN 650 MG ACETAMINOPHEN 160 MG/5ML ACETAMINOPHEN 500 MG/5ML ACETAMINOPHEN 160 MG/5ML ACETAMINOPHEN 500MG/15ML ACETAMINOPHEN 100 MG/ML ACETAMINOPHEN 500 MG ACETAMINOPHEN 325 MG ACETAMINOPHEN 500 MG ACETAMINOPHEN 80 MG ACETAMINOPHEN 100.00% ACETAMINOPHEN 80 MG ACETAMINOPHEN 160 MG ACETAMINOPHEN 80MG/0.8ML ACETAMINOPHEN‐BUTALBITAL 50MG‐325MG ACNE CLEANSING PADS 2% ACNE TREATMENT,EXTRA STRENGTH 10% ACT ANTI‐CAVITY MOUTH RINSE 0.05% Updated 12/01/2012 ACTICAL ACTIDOSE‐AQUA 50G/240ML ACTIDOSE‐AQUA 15G/72ML ACTIDOSE‐AQUA 25G/120ML ACTIVATED CHARCOAL 25 G ADEKS 7.5 MG
  • Slc1a3-2A-Creert2 Mice Reveal Unique Features of Bergmann Glia and Augment a Growing Collection of Cre Drivers and Effectors In

    Slc1a3-2A-Creert2 Mice Reveal Unique Features of Bergmann Glia and Augment a Growing Collection of Cre Drivers and Effectors In

    www.nature.com/scientificreports OPEN Slc1a3‑2A‑CreERT2 mice reveal unique features of Bergmann glia and augment a growing collection of Cre drivers and efectors in the 129S4 genetic background Lech Kaczmarczyk1,2, Nicole Reichenbach2, Nelli Blank2, Maria Jonson1, Lars Dittrich2, Gabor C. Petzold2,3 & Walker S. Jackson1,2* Genetic variation is a primary determinant of phenotypic diversity. In laboratory mice, genetic variation can be a serious experimental confounder, and thus minimized through inbreeding. However, generalizations of results obtained with inbred strains must be made with caution, especially when working with complex phenotypes and disease models. Here we compared behavioral characteristics of C57Bl/6—the strain most widely used in biomedical research—with those of 129S4. In contrast to 129S4, C57Bl/6 demonstrated high within‑strain and intra‑litter behavioral hyperactivity. Although high consistency would be advantageous, the majority of disease models and transgenic tools are in C57Bl/6. We recently established six Cre driver lines and two Cre efector lines in 129S4. To augment this collection, we genetically engineered a Cre line to study astrocytes in 129S4. It was validated with two Cre efector lines: calcium indicator gCaMP5g‑tdTomato and RiboTag—a tool widely used to study cell type‑specifc translatomes. These reporters are in diferent genomic loci, and in both the Cre was functional and astrocyte‑specifc. We found that calcium signals lasted longer and had a higher amplitude in cortical compared to hippocampal astrocytes, genes linked to a single neurodegenerative disease have highly divergent expression patterns, and that ribosome proteins are non‑uniformly expressed across brain regions and cell types.
  • Cellular and Molecular Signatures in the Disease Tissue of Early

    Cellular and Molecular Signatures in the Disease Tissue of Early

    Cellular and Molecular Signatures in the Disease Tissue of Early Rheumatoid Arthritis Stratify Clinical Response to csDMARD-Therapy and Predict Radiographic Progression Frances Humby1,* Myles Lewis1,* Nandhini Ramamoorthi2, Jason Hackney3, Michael Barnes1, Michele Bombardieri1, Francesca Setiadi2, Stephen Kelly1, Fabiola Bene1, Maria di Cicco1, Sudeh Riahi1, Vidalba Rocher-Ros1, Nora Ng1, Ilias Lazorou1, Rebecca E. Hands1, Desiree van der Heijde4, Robert Landewé5, Annette van der Helm-van Mil4, Alberto Cauli6, Iain B. McInnes7, Christopher D. Buckley8, Ernest Choy9, Peter Taylor10, Michael J. Townsend2 & Costantino Pitzalis1 1Centre for Experimental Medicine and Rheumatology, William Harvey Research Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK. Departments of 2Biomarker Discovery OMNI, 3Bioinformatics and Computational Biology, Genentech Research and Early Development, South San Francisco, California 94080 USA 4Department of Rheumatology, Leiden University Medical Center, The Netherlands 5Department of Clinical Immunology & Rheumatology, Amsterdam Rheumatology & Immunology Center, Amsterdam, The Netherlands 6Rheumatology Unit, Department of Medical Sciences, Policlinico of the University of Cagliari, Cagliari, Italy 7Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow G12 8TA, UK 8Rheumatology Research Group, Institute of Inflammation and Ageing (IIA), University of Birmingham, Birmingham B15 2WB, UK 9Institute of
  • Magnesium Is a Key Player in Neuronal Maturation and Neuropathology

    Magnesium Is a Key Player in Neuronal Maturation and Neuropathology

    International Journal of Molecular Sciences Review Magnesium Is a Key Player in Neuronal Maturation and Neuropathology Ryu Yamanaka 1,2 , Yutaka Shindo 1 and Kotaro Oka 1,3,4,* 1 Center for Biosciences and Informatics, School of Fundamental Science and Technology Graduate School of Science and Technology, Keio University, Yokohama, Kanagawa 223-8522, Japan 2 Faculty of Pharmaceutical Sciences, Sanyo-Onoda City University, Sanyo-Onoda, Yamaguchi 756-0884, Japan 3 Graduate Institute of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung City 80708, Taiwan 4 Waseda Research Institute for Science and Engineering, Waseda University, 2-2 Wakamatsucho, Shinjuku, Tokyo 162-8480, Japan * Correspondence: [email protected]; Tel.: +81-045-566-1789 Received: 16 June 2019; Accepted: 9 July 2019; Published: 12 July 2019 Abstract: Magnesium (Mg) is the second most abundant cation in mammalian cells, and it is essential for numerous cellular processes including enzymatic reactions, ion channel functions, metabolic cycles, cellular signaling, and DNA/RNA stabilities. Because of the versatile and universal nature of Mg2+, the homeostasis of intracellular Mg2+ is physiologically linked to growth, proliferation, differentiation, energy metabolism, and death of cells. On the cellular and tissue levels, maintaining Mg2+ within optimal levels according to the biological context, such as cell types, developmental stages, extracellular environments, and pathophysiological conditions, is crucial for development, normal functions, and diseases. Hence, Mg2+ is pathologically involved in cancers, diabetes, and neurodegenerative diseases, such as Parkinson’s disease, Alzheimer’s disease, and demyelination. In the research field regarding the roles and mechanisms of Mg2+ regulation, numerous controversies caused by its versatility and complexity still exist.
  • Supplementary Table S4. FGA Co-Expressed Gene List in LUAD

    Supplementary Table S4. FGA Co-Expressed Gene List in LUAD

    Supplementary Table S4. FGA co-expressed gene list in LUAD tumors Symbol R Locus Description FGG 0.919 4q28 fibrinogen gamma chain FGL1 0.635 8p22 fibrinogen-like 1 SLC7A2 0.536 8p22 solute carrier family 7 (cationic amino acid transporter, y+ system), member 2 DUSP4 0.521 8p12-p11 dual specificity phosphatase 4 HAL 0.51 12q22-q24.1histidine ammonia-lyase PDE4D 0.499 5q12 phosphodiesterase 4D, cAMP-specific FURIN 0.497 15q26.1 furin (paired basic amino acid cleaving enzyme) CPS1 0.49 2q35 carbamoyl-phosphate synthase 1, mitochondrial TESC 0.478 12q24.22 tescalcin INHA 0.465 2q35 inhibin, alpha S100P 0.461 4p16 S100 calcium binding protein P VPS37A 0.447 8p22 vacuolar protein sorting 37 homolog A (S. cerevisiae) SLC16A14 0.447 2q36.3 solute carrier family 16, member 14 PPARGC1A 0.443 4p15.1 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha SIK1 0.435 21q22.3 salt-inducible kinase 1 IRS2 0.434 13q34 insulin receptor substrate 2 RND1 0.433 12q12 Rho family GTPase 1 HGD 0.433 3q13.33 homogentisate 1,2-dioxygenase PTP4A1 0.432 6q12 protein tyrosine phosphatase type IVA, member 1 C8orf4 0.428 8p11.2 chromosome 8 open reading frame 4 DDC 0.427 7p12.2 dopa decarboxylase (aromatic L-amino acid decarboxylase) TACC2 0.427 10q26 transforming, acidic coiled-coil containing protein 2 MUC13 0.422 3q21.2 mucin 13, cell surface associated C5 0.412 9q33-q34 complement component 5 NR4A2 0.412 2q22-q23 nuclear receptor subfamily 4, group A, member 2 EYS 0.411 6q12 eyes shut homolog (Drosophila) GPX2 0.406 14q24.1 glutathione peroxidase
  • Low Acyl Gellan Gum for Inclusion on the National List of Substances Allowed in Organic Production and Handling (7 CFR 205.605 (B)

    Low Acyl Gellan Gum for Inclusion on the National List of Substances Allowed in Organic Production and Handling (7 CFR 205.605 (B)

    Petition for Evaluation of Low Acyl Gellan Gum for Inclusion on the National List of Substances Allowed in Organic Production and Handling (7 CFR 205.605 (b) Submitted by: CP Kelco U.S., Inc. 3100 Cumberland Blvd., Suite 600 Atlanta, GA 30339 Date: 08 August 2019 CP Kelco U.S., Inc. 08 August 2019 National Organic List Petiion Low Acyl Gellan Gum Table of Contents Item A.1 — Section of National List ........................................................................................................... 4 Item A.2 — OFPA Category - Crop and Livestock Materials .................................................................... 4 Item A.3 — Inert Ingredients ....................................................................................................................... 4 1. Substance Name ................................................................................................................................... 5 2. Petitioner and Manufacturer Information ............................................................................................. 5 2.1. Corporate Headquarters ................................................................................................................5 2.2. Manufacturing/Processing Facility ...............................................................................................5 2.3. Contact for USDA Correspondence .............................................................................................5 3. Intended or Current Use .......................................................................................................................5
  • Figure S1. HAEC ROS Production and ML090 NOX5-Inhibition

    Figure S1. HAEC ROS Production and ML090 NOX5-Inhibition

    Figure S1. HAEC ROS production and ML090 NOX5-inhibition. (a) Extracellular H2O2 production in HAEC treated with ML090 at different concentrations and 24 h after being infected with GFP and NOX5-β adenoviruses (MOI 100). **p< 0.01, and ****p< 0.0001 vs control NOX5-β-infected cells (ML090, 0 nM). Results expressed as mean ± SEM. Fold increase vs GFP-infected cells with 0 nM of ML090. n= 6. (b) NOX5-β overexpression and DHE oxidation in HAEC. Representative images from three experiments are shown. Intracellular superoxide anion production of HAEC 24 h after infection with GFP and NOX5-β adenoviruses at different MOIs treated or not with ML090 (10 nM). MOI: Multiplicity of infection. Figure S2. Ontology analysis of HAEC infected with NOX5-β. Ontology analysis shows that the response to unfolded protein is the most relevant. Figure S3. UPR mRNA expression in heart of infarcted transgenic mice. n= 12-13. Results expressed as mean ± SEM. Table S1: Altered gene expression due to NOX5-β expression at 12 h (bold, highlighted in yellow). N12hvsG12h N18hvsG18h N24hvsG24h GeneName GeneDescription TranscriptID logFC p-value logFC p-value logFC p-value family with sequence similarity NM_052966 1.45 1.20E-17 2.44 3.27E-19 2.96 6.24E-21 FAM129A 129. member A DnaJ (Hsp40) homolog. NM_001130182 2.19 9.83E-20 2.94 2.90E-19 3.01 1.68E-19 DNAJA4 subfamily A. member 4 phorbol-12-myristate-13-acetate- NM_021127 0.93 1.84E-12 2.41 1.32E-17 2.69 1.43E-18 PMAIP1 induced protein 1 E2F7 E2F transcription factor 7 NM_203394 0.71 8.35E-11 2.20 2.21E-17 2.48 1.84E-18 DnaJ (Hsp40) homolog.
  • Dietary Supplements Compendium Volume 1

    Dietary Supplements Compendium Volume 1

    2015 Dietary Supplements Compendium DSC Volume 1 General Notices and Requirements USP–NF General Chapters USP–NF Dietary Supplement Monographs USP–NF Excipient Monographs FCC General Provisions FCC Monographs FCC Identity Standards FCC Appendices Reagents, Indicators, and Solutions Reference Tables DSC217M_DSCVol1_Title_2015-01_V3.indd 1 2/2/15 12:18 PM 2 Notice and Warning Concerning U.S. Patent or Trademark Rights The inclusion in the USP Dietary Supplements Compendium of a monograph on any dietary supplement in respect to which patent or trademark rights may exist shall not be deemed, and is not intended as, a grant of, or authority to exercise, any right or privilege protected by such patent or trademark. All such rights and privileges are vested in the patent or trademark owner, and no other person may exercise the same without express permission, authority, or license secured from such patent or trademark owner. Concerning Use of the USP Dietary Supplements Compendium Attention is called to the fact that USP Dietary Supplements Compendium text is fully copyrighted. Authors and others wishing to use portions of the text should request permission to do so from the Legal Department of the United States Pharmacopeial Convention. Copyright © 2015 The United States Pharmacopeial Convention ISBN: 978-1-936424-41-2 12601 Twinbrook Parkway, Rockville, MD 20852 All rights reserved. DSC Contents iii Contents USP Dietary Supplements Compendium Volume 1 Volume 2 Members . v. Preface . v Mission and Preface . 1 Dietary Supplements Admission Evaluations . 1. General Notices and Requirements . 9 USP Dietary Supplement Verification Program . .205 USP–NF General Chapters . 25 Dietary Supplements Regulatory USP–NF Dietary Supplement Monographs .
  • How Do Bacterial Cells Ensure That Metalloproteins Get the Correct Metal?

    How Do Bacterial Cells Ensure That Metalloproteins Get the Correct Metal?

    REVIEWS How do bacterial cells ensure that metalloproteins get the correct metal? Kevin J. Waldron and Nigel J. Robinson Abstract | Protein metal-coordination sites are richly varied and exquisitely attuned to their inorganic partners, yet many metalloproteins still select the wrong metals when presented with mixtures of elements. Cells have evolved elaborate mechanisms to scavenge for sufficient metal atoms to meet their needs and to adjust their needs to match supply. Metal sensors, transporters and stores have often been discovered as metal-resistance determinants, but it is emerging that they perform a broader role in microbial physiology: they allow cells to overcome inadequate protein metal affinities to populate large numbers of metalloproteins with the right metals. It has been estimated that one-quarter to one-third of all Both monovalent (cuprous) copper, which is expected proteins require metals, although the exploitation of ele- to predominate in a reducing cytosol, and trivalent ments varies from cell to cell and has probably altered over (ferric) iron, which is expected to predominate in an the aeons to match geochemistry1–3 (BOX 1). The propor- oxidizing periplasm, are also highly competitive, as are tions have been inferred from the numbers of homologues several non-essential metals, such as cadmium, mercury of known metalloproteins, and other deduced metal- and silver6 (BOX 2). How can a cell simultaneously contain binding motifs, encoded within sequenced genomes. A some proteins that require copper or zinc and others that large experimental estimate was generated using native require uncompetitive metals, such as magnesium or polyacrylamide-gel electrophoresis of extracts from iron- manganese? In a most simplistic model in which pro- rich Ferroplasma acidiphilum followed by the detection of teins pick elements from a cytosol in which all divalent metal in protein spots using inductively coupled plasma metals are present and abundant, all proteins would bind mass spectrometry4.
  • Glucono Delta-Lactone Processing

    Glucono Delta-Lactone Processing

    Glucono Delta-Lactone Processing Executive Summary Glucono delta-lactone (GDL) was petitioned to be added to the National List as a tofu coagulant. It is produced by the oxidation of gluconic acid by a number of various methods. In addition to coagulation, GDL is used as an acidulant, leavening agent, and sequestrant. The NOSB was petitioned for this substance in 1995, and declined to refer it to the Technical Advisory Panel. The reviewers all considered it possible to make GDL from non-synthetic sources, although one considered certain sources and processes synthetic. All considered it to be non-agricultural. Two recommended that it be added to the National List with an annotation; one recommended that it remain off the National List. All three recommended that it be allowed for use in a made with organic (specified ingredients) claim. Of these, two supported with annotations, and one recommended no annotations for this use. Further investigation may be required to determine if sources are produced by the use of genetic engineering. Summary of Advised Recommendation 95% organic Synthetic / Non-Synthetic: Allowed or Prohibited: Suggested Annotation: Either synthetic Allowed (1) (Reviewer 1) None. or non-synthetic Prohibited (1) (Reviewer 2) Produced by microbial depending on the fermentation of carbohydrate substances source and or by enzymatic oxidation of organic manufacturing glucose process (1) (Reviewer 3).Must be produced by Non-synthetic (2) fermentation of glucose by naturally occurring microorganisms or enzymes Made with organic (70% or more organic ingredients) Agricultural / Non-Agricultural Allowed or Prohibited: Suggested Annotation: Non-agricultural (3) Allowed (3) (Reviewer 1) For tofu production only.
  • Calcium Chloride

    Calcium Chloride

    Electrolytes Livestock 1 2 Identification of Petitioned Substance 3 4 Chemical Names (Compiled from commercial 44 Calcium propionate, propanoic acid, calcium salt 5 electrolyte formulations): 45 Ca(CH3.CH2.COO)2 6 Calcium chloride (10043-52-4) 46 Calcium oxide, lime CaO 7 Calcium borogluconate (5743-34-0) 47 Calcium sulfate, gypsum CaSO4 8 Calcium gluconate (299-28-5) 48 9 Calcium hypophosphite (7789-79-9) 49 Magnesium diborogluconate, Mg[(HO.CH2CH 10 Calcium lactate (814-80-2) 50 (HBO3)CH(CH.OH)2 COO]2 11 Calcium phosphate tribasic (7758-87-4) 51 Magnesium citrate, Mg3(C6H5O7)2 12 Calcium phosphate dibasic (7757-93-9) 52 Magnesium hypophosphite Mg(H2PO2)2 13 Calcium phosphate monobasic (10031-30-8) 53 Magnesium sulfate, Epsom salts MgSO4 14 Calcium propionate (4075-81-4) 54 Potassium chloride KCl 15 Calcium oxide (1305-78-8) 55 Potassium citrate, K3(C6H5O7) 16 Calcium sulfate (7778-18-19) 56 Tripotassium phosphate K3(PO4) 17 Magnesium borogluconate (not available) 57 Dipotassium hydrogen phosphate K2HPO4 18 Magnesium citrate, tribasic (3344-18-1) 58 Potassium dihydrogen phosphate KH2PO4 19 Magnesium hypophosphite (10377-57-8) 59 Sodium acetate Na(CH3COO) 20 Magnesium sulfate (7487-88-9) 60 Sodium bicarbonate, baking soda NaHCO3 21 Potassium chloride (7447-40-7) 61 Sodium chloride, table salt, NaCl 22 Potassium citrate (866-84-2) 62 Sodium citrate, trisodium citrate Na3(C6H5O7) 23 Potassium phosphate, tribasic (7778-53-2) 63 Trisodium phosphate Na3(PO4) 24 Potassium phosphate, dibasic (7758-11-4) 64 Disodium hydrogen phosphate Na2HPO4 25 Potassium phosphate, monobasic (7778-77-0) 65 Sodium dihydrogen phosphate NaH2PO4 26 Sodium acetate (127-09-3) 66 27 Sodium bicarbonate (144-55-8) 67 Trade Names: 28 Sodium chloride (7647-14-5) 68 These individual electrolyte salts are not sold 29 Sodium citrate (68-04-2) 69 with Trade Names.