Neural Stem Cell–Specific ITPA Deficiency Causes Neural Depolarization and Epilepsy
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A Disease Spectrum for ITPA Variation: Advances in Biochemical and Clinical Research Nicholas E
Burgis Journal of Biomedical Science (2016) 23:73 DOI 10.1186/s12929-016-0291-y REVIEW Open Access A disease spectrum for ITPA variation: advances in biochemical and clinical research Nicholas E. Burgis Abstract Human ITPase (encoded by the ITPA gene) is a protective enzyme which acts to exclude noncanonical (deoxy) nucleoside triphosphates ((d)NTPs) such as (deoxy)inosine 5′-triphosphate ((d)ITP), from (d)NTP pools. Until the last few years, the importance of ITPase in human health and disease has been enigmatic. In 2009, an article was published demonstrating that ITPase deficiency in mice is lethal. All homozygous null offspring died before weaning as a result of cardiomyopathy due to a defect in the maintenance of quality ATP pools. More recently, a whole exome sequencing project revealed that very rare, severe human ITPA mutation results in early infantile encephalopathy and death. It has been estimated that nearly one third of the human population has an ITPA status which is associated with decreased ITPase activity. ITPA status has been linked to altered outcomes for patients undergoing thiopurine or ribavirin therapy. Thiopurine therapy can be toxic for patients with ITPA polymorphism, however, ITPA polymorphism is associated with improved outcomes for patients undergoing ribavirin treatment. ITPA polymorphism has also been linked to early-onset tuberculosis susceptibility. These data suggest a spectrum of ITPA-related disease exists in human populations. Potentially, ITPA status may affect a large number of patient outcomes, suggesting that modulation of ITPase activity is an important emerging avenue for reducing the number of negative outcomes for ITPA-related disease. -
The Nutrition and Food Web Archive Medical Terminology Book
The Nutrition and Food Web Archive Medical Terminology Book www.nafwa. -
A Comparative Study of Purinoceptors in Some Invertebrates and Vertebrates
A COMPARATIVE STUDY OF PURINOCEPTORS IN SOME INVERTEBRATES AND VERTEBRATES by Gillian Elizabeth Knight G.l.Biol Department Of Anatomy and Centre for Neuroscience, University College London, Gower Street, London WCIE 6BT Thesis submitted for the degree of Doctor of Philosophy University of London ProQuest Number: 10017490 All rights reserved INFORMATION TO ALL USERS The quality of this reproduction is dependent upon the quality of the copy submitted. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. Also, if material had to be removed, a note will indicate the deletion. uest. ProQuest 10017490 Published by ProQuest LLC(2016). Copyright of the Dissertation is held by the Author. All rights reserved. This work is protected against unauthorized copying under Title 17, United States Code. Microform Edition © ProQuest LLC. ProQuest LLC 789 East Eisenhower Parkway P.O. Box 1346 Ann Arbor, Ml 48106-1346 ABSTRACT The main objective of this thesis has been to identify and characterise responses to purine compounds in a variety of invertebrates and lower vertebrates, and to examine whether they act on receptors that resemble the purinoceptor subtypes established in mammals. Tissues were chosen largely from the gastrointestinal or cardiovascular systems. In mammalian systems adenosine and adenosine 5 ’-triphosphate (ATP) activate separate classes of purinoceptors; this also appears to be true for tissues in most invertebrate groups, but there are exceptions, for instance the hearts of the snail Helix aspeTsa, and slug Avion atev, and the snail rectum all possess purinoceptors that do not appear to distinguish the purine nucleosides from nucleotides. -
Variations in Bacterial Adenosine Triphosphate Values Due to Genus and Environmental Conditions
VARIATIONS IN BACTERIAL ADENOSINE TRIPHOSPHATE VALUES DUE TO GENUS AND ENVIRONMENTAL CONDITIONS by Ruann Knox Hampson Thesis submitted to the Faculty of the Virginia Polytechnic Institute and State University in partial fulfillment of the requirements for the degree of Master of Science in Food Science and Technology APPROVED: M. D. Pierson, Chairman J. K. Palmer A. A. Yousten December, 1986 Blacksburg, Virginia VARIATIONS IN BACTERIAL ADENOSINE TRIPOSPHATE VALUES DUE TO GENUS AND ENVIRONMENTAL CONDITIONS by Ruann Knox Hampson Committee Chairman: Merle D. Pierson Food Science and Technology (ABSTRACT) Variations in ATP content in three ground beef spoilage bacteria, Lactobacillus brevis, Lactobacillus jensenii, and Pseudomonas sp. were investigated using the bioluminescence (luciferin-luciferase) assay. Environmental factors (temperature, atmosphere, pH, aeration, and phase of growth), as well as differences among genera and species, were studied in relation to their effect on cellular ATP. Variations for each of the environmental factors and bacteria were shown statistically to be significantly different at the 0.05 level. The mean ATP/cell for each of the bacteria was 2.71 fg/cell (1..:_ brevis), 2.20 fg/cell (1..:_ jensenii), and 1.36 fg/cell (Pseudomonas sp.). For all three bacteria, ATP/cell was lower and more stable throughout the culture's growth cycle at 3°c or in N2 . In general, ATP/cell increases from a lowest value in lag phase to a highest value in stationary phase. The effect of sonication on ATP/cell was tested for each bacterium at one set of factors. Sonication studies showed that L. brevis cells were clumping, especially in aged cultures. -
Probing the Base Stacking Contributions During
PROBING THE BASE STACKING CONTRIBUTIONS DURING TRANSLESION DNA SYNTHESIS by BABHO DEVADOSS Submitted in partial fulfillment of the requirements For the degree of Doctor of Philosophy Thesis Adviser: Dr. Irene Lee Department of Chemistry CASE WESTERN RESERVE UNIVERSITY January, 2009 CASE WESTERN RESERVE UNIVERSITY SCHOOL OF GRADUATE STUDIES We hereby approve the thesis/dissertation of _____________________________________________________ candidate for the ______________________degree *. (signed)_______________________________________________ (chair of the committee) ________________________________________________ ________________________________________________ ________________________________________________ ________________________________________________ ________________________________________________ (date) _______________________ *We also certify that written approval has been obtained for any proprietary material contained therein. ii TABLE OF CONTENTS Title Page…………………………………………………………………………………..i Committee Sign-off Sheet………………………………………………………………...ii Table of Contents…………………………………………………………………………iii List of Tables…………………………………………………………………………….vii List of Figures…………………………………………………………………….………ix Acknowledgements…………………………………………………………….………..xiv List of Abbreviations…………………………………………………………….………xv Abstract………………………………………………………………………………….xix CHAPTER 1 Introduction…………………………………………………………………1 1.1 The Chemistry and Biology of DNA…………………………………………2 1.2 DNA Synthesis……………………………………………………………….6 1.3 Structural Features of DNA Polymerases…………………………………...11 -
Original Article Identification of B Cells Participated in the Mechanism of Postmenopausal Women Osteoporosis Using Microarray Analysis
Int J Clin Exp Med 2015;8(1):1027-1034 www.ijcem.com /ISSN:1940-5901/IJCEM0003564 Original Article Identification of B cells participated in the mechanism of postmenopausal women osteoporosis using microarray analysis Bing Yan*, Jie Li*, Li Zhang Department of Orthopedics, Shandong Provincial Traditional Chinise Medical Hospital, Jinan 250014, Shandong Province, China. *Equal contributors. Received November 3, 2014; Accepted January 7, 2015; Epub January 15, 2015; Published January 30, 2015 Abstract: To further understand the molecular mechanism of lymphocytes B cells in postmenopausal women os- teoporosis. Microarray data (GSE7429) were downloaded from Gene Expression Omnibus, in which B cells were separated from the whole blood of postmenopausal women, including 10 with high bone mineral density (BMD) and 10 with low BMD. Differentially expressed genes (DEGs) between high and low BMD women were identified by Student’s t-test, and P < 0.01 was used as the significant criterion. Functional enrichment analysis was performed for up- and down-regulated DEGs using KEGG, REACTOME, and Gene Ontology (GO) databases. Protein-protein inter- action network (PPI) of up- and down-regulated DEGs was respectively constructed by Cytoscape software using the STRING data. Total of 169 up-regulated and 69 down-regulated DEGs were identified. Functional enrichment analy- sis indicated that the genes (ITPA, ATIC, UMPS, HPRT1, COX10 and COX15) might participate in metabolic pathways, MAP3K10 and MAP3K9 might participate in the activation of JNKK activity, COX10 and COX15 might involve in mitochondrial electron transport, and ATIC, UMPS and HPRT1 might involve in transferase activity. MAPK3, ITPA, ATIC, UMPS and HPRT1 with a higher degree in PPI network were identified. -
Sheep Gene Mapping by Somatic Cell Hybridization
Sheep gene mapping by somatic cell hybridization N Saïdi-Mehtar M Imam-Ghali1 S Heuertz2 MC Hors-Cayla2 1 Université d’Oran Es-Sénia, Laboratoire de Biologie M oléculaire et Génétique, Unite de Recherches de Biologie, Algeria; z 2 INSERM U12, Unit6 de Recherches de Genetique M6dicale, Paris, France (Proceedings of the 9th European Colloquium on Cytogenetics of Domestic Animals; Toulouse-Auzeville, 10-13 July 1990) sheep / ovine / gene mapping / synteny / cell hybrid INTRODUCTION Twenty-five hamster x sheep hybrid cell lines were previously obtained (Saidi- Mehtar et al, 1981b). Analysis of these hybrids has already enabled the identification of 5 syntenic groups and 10 independent markers (Saidi-Mehtar et al, 1981a, b, 1987; Millot et al, 1981; Imam-Ghali et al, 1987). In this paper, we report results obtained with 3 other enzyme markers: aconitase 1 (AC01), inosine triphosphatase (ITPA) and glyceraldehyde-3-phosphate dehydrogenase (GAPD); and 6 DNA markers: ornithine transcarbamylase (OTC), color vision red pigment (RCB), raf oncogene (ARAF1) and /3-gene locus DR of human lymphocyte antigen region (HLA-DR!). ENZYME MARKERS AC01, ITPA and GAPD were studied by cellulose acetate electrophoresis using modified versions of the methods described by Womack and Moll (1986). The cytoplasmic (AC01) and mitochondrial (AC02) forms of aconitase were identified by successive freezing and thawing of cells followed by electrophoresis of the supernatants. AC01 was obtained first and corresponded to the most anodal band. A different electrophoretic migration between sheep and hamster was only observed for ACO1. Ovine ITPA migrated more anodally than hamster ITPA. Ovine GAPD is a trimeric enzyme: positive hybrids for sheep GAPD showed 2 intermediate bands (fig 1). -
Inosine Triphosphate Pyrophosphatase (ITPA) (NM 181493) 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 RC215516L4 Inosine triphosphate pyrophosphatase (ITPA) (NM_181493) Human Tagged ORF Clone Product data: Product Type: Expression Plasmids Product Name: Inosine triphosphate pyrophosphatase (ITPA) (NM_181493) Human Tagged ORF Clone Tag: mGFP Symbol: ITPA Synonyms: C20orf37; DEE35; dJ794I6.3; HLC14-06-P; ITPase; My049; NTPase Vector: pLenti-C-mGFP-P2A-Puro (PS100093) E. coli Selection: Chloramphenicol (34 ug/mL) Cell Selection: Puromycin ORF Nucleotide The ORF insert of this clone is exactly the same as(RC215516). Sequence: Restriction Sites: SgfI-MluI Cloning Scheme: ACCN: NM_181493 ORF Size: 531 bp 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 / 2 Inosine triphosphate pyrophosphatase (ITPA) (NM_181493) Human Tagged ORF Clone – RC215516L4 OTI Disclaimer: The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info OTI Annotation: This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. RefSeq: NM_181493.1 RefSeq Size: 1155 bp RefSeq ORF: 534 bp Locus ID: 3704 UniProt ID: Q9BY32 Protein Families: Druggable Genome Protein Pathways: Drug metabolism - other enzymes, Metabolic pathways, Purine metabolism, Pyrimidine metabolism MW: 19.4 kDa Gene Summary: This gene encodes an inosine triphosphate pyrophosphohydrolase. -
A Realtime and Handson Research Course in Protein
Q 2011 by The International Union of Biochemistry and Molecular Biology BIOCHEMISTRY AND MOLECULAR BIOLOGY EDUCATION Vol. 39, No. 1, pp. 28–37, 2011 Special Section: Innovative Laboratory Exercises A Real-time and Hands-on Research Course in Protein Purification and Characterization*,y,‡ PURIFICATION AND CRYSTAL GROWTH OF HUMAN INOSINE TRIPHOSPHATE PYROPHOSPHATASE Received for publication, March 19, 2010, and in revised form, June 7, 2010 Jodi L. Kreiling§**, Kerry Brader¶, Carol Kolar¶, and Gloria E. O. Borgstahl¶ From the §Department of Chemistry, University of Nebraska at Omaha, Omaha, Nebraska 68182, ¶Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198 A new lecture/laboratory course to offer advanced biochemical training for undergraduate and early graduate students has been developed in the Department of Chemistry at the University of Nebraska at Omaha. This unique course offers students an opportunity to work hands-on with modern instrumentation not normally found in a predominately undergraduate institution, and to complete an entire research project in a realistic timeframe via a time-intensive curriculum as a special summer session. The course content gives a strong background in protein structure/chemistry, purification principles, protocol development, optimization strategies, use and pro- gramming of an automated chromatography instrument, and characterization strategies with an emphasis on X-ray crystallography. The laboratory portion offers students the chance to purify a protein (human inosine tri- phosphate pyrophosphatase) from start to finish, program and use an A¨ KTA fast protein liquid chromatography instrument, and to grow and analyze their own protein crystals using their purified protein. -
Pharmacogenomics of Ventricular Conduction in Multi-Ethnic Populations Amanda Seyerle Dissertation Committee
Pharmacogenomics of Ventricular Conduction in Multi-Ethnic Populations Amanda Seyerle Dissertation Committee: Christy Avery (chair) Kari North Eric Whitsel Til Stürmer Craig Lee 1 TABLE OF CONTENTS Page LIST OF TABLES ...................................................................................................................................... v LIST OF FIGURES ..................................................................................................................................... vi LIST OF ABBREVIATIONS ..................................................................................................................... vii LIST OF GENE NAMES ............................................................................................................................ ix 1. Overview .............................................................................................................................................. 1 2. Specific Aims ....................................................................................................................................... 3 3. Background and Significance ............................................................................................................ 4 A. Ventricular Conduction ......................................................................................................................... 4 A.1. Electrical Conduction of the Heart ................................................................................................ 4 A.1.1. Sodium Channels.................................................................................................................. -
ASM Abbreviations
The words, abbreviations, and designations that follow are commonly encountered in ASM manuscripts. An asterisk (*) indicates that the abbreviation may be used (without introduction) with or without a numeral; however, the term should always be abbreviated in the bodies of tables. A double asterisk (**) indicates that the abbreviation must be used without introduction. “Need not be defined” means that the abbreviation does not have to be introduced, but it may be. “Hyphenated as unit modifier” means that the phrase is hyphenated when it is used adjectivally and precedes the noun it modifies; when it follows the noun, it should not be hyphenated: Gram-positive cells, BUT the cells were Gram positive. “Follow au.” means that ASM copy editors follow the author if one of the alternative forms is used consistently throughout the manuscript; otherwise, the copy editor will choose one form and be consistent. At times, your definition for an abbreviation may vary significantly from the one given here. Generally, ASM copy editors will follow the author, especially if the term is a chemical name that can be verified. If the variation is slight, however (e.g., hyphens, spacing), the copy editor will follow this manual. You may find helpful medical acronym websites like https://www.medindia.net/medical-abbreviations-and- acronyms/index.asp and https://www.medilexicon.com/abbreviations. As a general rule, use the specific abbreviations given in this list: PFU, NOT pfu; i.p., NOT IP; cpm, NOT CPM; IFN, NOT IF. For abbreviations that do not appear in this manual, periods and all-lowercase abbreviations should be avoided. -
New Insights Into Marine Group III Euryarchaeota, from Dark to Light
The ISME Journal (2017), 1–16 © 2017 International Society for Microbial Ecology All rights reserved 1751-7362/17 www.nature.com/ismej ORIGINAL ARTICLE New insights into marine group III Euryarchaeota, from dark to light Jose M Haro-Moreno1,3, Francisco Rodriguez-Valera1, Purificación López-García2, David Moreira2 and Ana-Belen Martin-Cuadrado1,3 1Evolutionary Genomics Group, Departamento de Producción Vegetal y Microbiología, Universidad Miguel Hernández, Alicante, Spain and 2Unité d’Ecologie, Systématique et Evolution, UMR CNRS 8079, Université Paris-Sud, Orsay Cedex, France Marine Euryarchaeota remain among the least understood major components of marine microbial communities. Marine group II Euryarchaeota (MG-II) are more abundant in surface waters (4–20% of the total prokaryotic community), whereas marine group III Euryarchaeota (MG-III) are generally considered low-abundance members of deep mesopelagic and bathypelagic communities. Using genome assembly from direct metagenome reads and metagenomic fosmid clones, we have identified six novel MG-III genome sequence bins from the photic zone (Epi1–6) and two novel bins from deep-sea samples (Bathy1–2). Genome completeness in those genome bins varies from 44% to 85%. Photic-zone MG-III bins corresponded to novel groups with no similarity, and significantly lower GC content, when compared with previously described deep-MG-III genome bins. As found in many other epipelagic microorganisms, photic-zone MG-III bins contained numerous photolyase and rhodopsin genes, as well as genes for peptide and lipid uptake and degradation, suggesting a photoheterotrophic lifestyle. Phylogenetic analysis of these photolyases and rhodopsins as well as their genomic context suggests that these genes are of bacterial origin, supporting the hypothesis of an MG-III ancestor that lived in the dark ocean.