The Disposition of Morphine and Its 3- and 6-Glucuronide Metabolites in Humans
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Phthalates: Toxicology and Food Safety – a Review
Czech J. Food Sci. Vol. 23, No. 6: 217–223 Phthalates: Toxicology and Food Safety – a Review PŘEMYSL MIKULA1, ZDEŇKA SVOBODOVÁ1 and MIRIAM SMUTNÁ2 1Department of Veterinary Public Health and Toxicology and 2Department of Biochemistry and Biophysics, Faculty of Veterinary Hygiene and Ecology, University of Veterinary and Pharmaceutical Sciences, Brno, Czech Republic Abstract MIKULA P., SVOBODOVÁ Z., SMUTNÁ M. (2005): Phthalates: toxicology and food safety – a review. Czech J. Food Sci., 23: 217–223. Phthalates are organic substances used mainly as plasticisers in the manufacture of plastics. They are ubiquitous in the environment. Although tests in rodents have demonstrated numerous negative effects of phthalates, it is still unclear whether the exposure to phthalates may also damage human health. This paper describes phthalate toxicity and toxicokinetics, explains the mechanisms of phthalate action, and outlines the issues relating to the presence of phthalates in foods. Keywords: di(2-ethylhexyl)phthalate; dibutyl phthalate; peroxisome proliferators; reproductive toxicity Phthalic acid esters, often also called phtha- air, soil, food, etc.). People as well as animals lates, are organic substances frequently used can be exposed to these compounds through in many industries. They are usually colourless ingestion, inhalation or dermal exposure, and or slightly yellowish oily and odourless liquids iatrogenic exposure to phthalates from blood only very slightly soluble in water. Phthalates are bags, injection syringes, intravenous canyllas much more readily soluble in organic solvents, and catheters, and from plastic parts of dialysers and the longer their side chain, the higher their is also a possibility (VELÍŠEK 1999; ČERNÁ 2000; liposolubility and the boiling point. Phthalates LOVEKAMP-SWAN & DAVIS 2003). -
Problems of Drug Dependence 1980 Proceedings of the 42Nd Annual Scientific Meeting the Committee on Problems of Drug Dependence
National Institute on Drug Abuse MONOGRAPH SERIES Problems of Drug Dependence 1980 Proceedings of the 42nd Annual Scientific Meeting The Committee on Problems of Drug Dependence, Inc. U.S. DEPARTMENT OF HEALTH AND HUMAN SERVICES • Public Health Service • Alcohol, Drug Abuse, and Mental Health Administration Problems of Drug Dependence, 1980 Proceedings of the 42nd Annual Scientific Meeting, The Committee on Problems of Drug Dependence, Inc. Editor: Louis S. Harris, Ph.D. NIDA Research Monograph 34 February 1981 DEPARTMENT OF HEALTH AND HUMAN SERVICES Public Health Service Alcohol, Drug Abuse, and Mental Health Administration National Institute on Drug Abuse Division of Research 5600 Fishers Lane Rockville, Maryland 20857 For sale by the Superintendent of Documents, U.S. Government Printing Office Washington, D.C. 20402 The NIDA Research Monograph series is prepared by the Division of Research of the National Institute on Drug Abuse. Its primary objective is to provide critical reviews of research problem areas and techniques, the content of state-of-the-art conferences, integrative research reviews and significant original research. Its dual publication emphasis is rapid and targeted dissemination to the scientific and professional community. Editorial Advisory Board Avram Goldstein, M.D. Addiction Research Foundation Palo Alto, California Jerome Jaffe, M.D. College of Physicians and Surgeons Columbia University, New York Reese T. Jones, M.D. Langley Porter Neuropsychiatric Institute University of California San Francisco, California William McGlothlin, Ph.D. Deportment of Psychology, UCLA Los Angeles, California Jack Mendelson, M.D. Alcohol and Drug Abuse Research Center Harvard Medical School McLean Hospital Belmont, Massachusetts Helen Nowlis, Ph.D. Office of Drug Education, DHHS Washington, D.C Lee Robins, Ph.D. -
Safety Evaluation of Certain Food Additives and Contaminants. WHO Food Additives Series, No
WHO FOOD Safety evaluation of ADDITIVES certain food additives SERIES: 64 and contaminants Prepared by the Seventy-third meeting of the Joint FAO/ WHO Expert Committee on Food Additives (JECFA) World Health Organization, Geneva, 2011 WHO Library Cataloguing-in-Publication Data Safety evaluation of certain food additives and contaminants / prepared by the seventy-third meeting of the Joint FAO/WHO Expert Committee on Food Additives (JECFA). (WHO food additives series ; 64) 1.Food additives - toxicity. 2.Food contamination. 3.Flavoring agents - analysis. 4.Flavoring agents - toxicity. 5.Risk assessment. I.Joint FAO/WHO Expert Committee on Food Additives. Meeting (73rd : 2010: Geneva, Switzerland). II.World Health Organization. III.Series. ISBN 978 924 166064 8 (NLM classification: WA 712) ISSN 0300-0923 © World Health Organization 2011 All rights reserved. Publications of the World Health Organization can be obtained from WHO Press, World Health Organization, 20 Avenue Appia, 1211 Geneva 27, Switzerland (tel.: +41 22 791 3264; fax: +41 22 791 4857; e-mail: [email protected]). Requests for permission to reproduce or translate WHO publications—whether for sale or for non- commercial distribution—should be addressed to WHO Press at the above address (fax: +41 22 791 4806; e-mail: [email protected]). The designations employed and the presentation of the material in this publication do not imply the expression of any opinion whatsoever on the part of the World Health Organization concerning the legal status of any country, territory, city or area or of its authorities, or concerning the delimitation of its frontiers or boundaries. Dotted lines on maps represent approximate border lines for which there may not yet be full agreement. -
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Glucuronic Acid Derivatives in Enzymatic Biomass Degradation: Synthesis and Evaluation of Enzymatic Activity
Downloaded from orbit.dtu.dk on: Oct 08, 2021 Glucuronic Acid Derivatives in Enzymatic Biomass Degradation: Synthesis and Evaluation of Enzymatic Activity d'Errico, Clotilde Publication date: 2016 Document Version Publisher's PDF, also known as Version of record Link back to DTU Orbit Citation (APA): d'Errico, C. (2016). Glucuronic Acid Derivatives in Enzymatic Biomass Degradation: Synthesis and Evaluation of Enzymatic Activity. DTU Chemistry. General rights Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights. Users may download and print one copy of any publication from the public portal for the purpose of private study or research. You may not further distribute the material or use it for any profit-making activity or commercial gain You may freely distribute the URL identifying the publication in the public portal If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. GLUCURONIC ACID DERIVATIVES IN ENZYMATIC BIOMASS DEGRADATION: SYNTHESIS AND EVALUATION OF ENZYMATIC ACTIVITY PHD THESIS – MAY 2016 CLOTILDE D’ERRICO DEPARTMENT OF CHEMISTRY TECHNICAL UNIVERSITY OF DENMARK ACKNOWLEDGEMENTS This dissertation describes the work produced during my PhD studies. The work was primarily conducted at the DTU Chemistry in the period between November 2012 and January 2016 with an external stay at Novozymes A/S between September 2013 and March 2014. -
Hydrolytic Enzymes Targeting to Prodrug/Drug Metabolism for Translational Application in Cancer
Journal of Clinical Science & Translational Medicine Hydrolytic Enzymes Targeting to Prodrug/Drug Metabolism for Translational Application in Cancer Prabha M* Review Article Department of Biotechnology, Ramaiah Institute of Technology, India Volume 1 Issue 1 Received Date: April 04, 2019 *Corresponding author: Prabha M, Department of Biotechnology, Ramaiah Institute of Published Date: June 20, 2019 Technology, Bangalore-560054, India, Tel: 080-23588236; Email: [email protected] Abstract A variety of approaches are under development to improve the effectiveness and specificity of enzyme activation for drug metabolism on tumour cell targeting for cancer treatment. Many such methods involve conjugates like monoclonal antibodies, substrate specificity and offer attractive means of directing to tumour toxic agents such as drugs, radioisotopes, protein cytotoxins, cytokines, effector cells of the immune system, gene therapy, stem cell therapy and enzyme therapy for therapeutic use. Hydrolytic enzymes belong to class III of enzyme classification and play an important role in the drug metabolism towards the treatment of cancer. Hydrolases helps drugs for metabolic efficiency to target on cancer cell since it is involved in the hydrolytic reaction of various biomolecules and compounds. The prodrug is designed to be a substrate for the chosen enzyme activity. A number of prodrugs have been developed that can be transformed into an active anticancerous drugs by enzymes of both mammalian and non mammalian origin. The basic molecular biochemistry, biotechnological processes and other information related to enzyme catalysis, has a major impact for the production of efficient drugs. In the current review some of the Hydrolases has been discussed which play a significant role towards prodrug to drug metabolism for cancer treatment. -
In Vitroo and in Vivo Pharmacology of 4-Substituted
IN VITROO AND IN VIVO PHARMACOLOGY OF 4-SUBSTITUTED METHOXYBENZOYL-ARYL-THIAZOLES (SMART) AND 2- ARYLTHIAZOLIDINE-4-CARBOXYLIC ACID AMIDES (ATCAA) Dissertation Presented in Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy in the Graduate School of The Ohio State University By Chien-Ming Li, M.S. Graduate Program in Pharmacy The Ohio State University 2010 Dissertation Committee: Dr. James T. Dalton, Advisor Dr. Robert W. Brueggemeier Dr. Thomas D. Schmittgen Dr. Mitch A. Phelps Copyright by Chien-Ming Li 2010 ABSTRACT Formation of microtubules is a dynamic process that involves polymerization and depolymerization of the αβ-tubulin heterodimers. Drugs that enhance or inhibit tubulin polymerization can destroy this dynamic process, arresting cells in the G2/M phase of the cell cycle. Although drugs that target tubulin generally demonstrate cytotoxic potency in sub-nanomolar range, resistance due to drug efflux is a common phenomenon among the antitubulin agents. We recently reported a class of 4-Substituted Methoxybenzoyl-Aryl- Thiazoles (SMART), which exhibited great in vitro and in vivo potency. SMART compounds effectively inhibited tubulin polymerization in dose dependent manner, suggesting that SMART compounds may bind to tubulin and subsequently hamper the polymerization. To date the only method to determine the binding of inhibitor to tubulin has been competitive radioligand binding assays. We developed a novel non-radioactive mass spectrometry (MS) binding assay to study the tubulin binding of colchicine, vinblastine and paclitaxel. The method involves a very simple step of separating the unbound ligand from macromolecules using ultrafiltration. The unbound ligand in the filtrate can be accurately determined using a highly sensitive and specific LC-MS/MS method. -
Properties and Kinetic Analysis of UDP-Glucose Dehydrogenase from Group a Streptococci IRREVERSIBLE INHIBITION by UDP-CHLOROACETOL*
THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 272, No. 6, Issue of February 7, pp. 3416–3422, 1997 © 1997 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Properties and Kinetic Analysis of UDP-glucose Dehydrogenase from Group A Streptococci IRREVERSIBLE INHIBITION BY UDP-CHLOROACETOL* (Received for publication, September 19, 1996, and in revised form, November 6, 1996) Robert E. Campbell‡§, Rafael F. Sala‡, Ivo van de Rijn¶, and Martin E. Tanner‡i From the ‡Department of Chemistry, University of British Columbia, Vancouver, British Columbia V6T 1Z1, Canada and ¶Wake Forest University Medical Center, Winston-Salem, North Carolina 27157 UDP-glucuronic acid is used by many pathogenic bac- the capsule enables the bacteria to evade the host’s immune teria in the construction of an antiphagocytic capsule system (7, 8). Group A and C streptococci are mammalian that is required for virulence. The enzyme UDP-glucose pathogens that use UDPGDH in the synthesis of a capsule dehydrogenase catalyzes the NAD1-dependent 2-fold ox- composed of hyaluronic acid (a polysaccharide consisting of idation of UDP-glucose and provides a source of the alternating glucuronic acid and N-acetylglucosamine residues) acid. In the present study the recombinant dehydrogen- (9, 10). Many of the known strains of Streptococcus pneumoniae ase from group A streptococci has been purified and also use UDP-glucuronic acid in the construction of their po- found to be active as a monomer. The enzyme contains lysaccharide capsule (11), and it has recently been shown that no chromophoric cofactors, and its activity is unaffected UDPGDH is required for capsule production in S. -
Comparison of Opioid Agonists in Maintaining Responding and in Suppressing Morphine Withdrawal in Rhesus Monkeys
Psychopharmacology Psychopharmacology (1981) 74:329 - 335 Springer-Verlag 1981 Comparison of Opioid Agonists in Maintaining Responding and in Suppressing Morphine Withdrawal in Rhesus Monkeys Alice M. Young*, Henry H. Swain, and James H. Woods Department of Pharmacology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA Abstract. Sixteen opioid agonists were studied for their 1976; Deneau et al. 1969; Downs and Woods 1974; Goldberg capacity both to maintain responding previously reinforced et al. 1976; Harrigan and Downs 1978; Hoffmeister 1979b; by codeine and to suppress the withdrawal syndrome induced Hoffmeister et al. 1980; Hoffmeister and Goldberg 1973; by morphine deprivation in rhesus monkeys. All compounds, Hoffmeister and Schlichting 1972; Hoffmeister and Wuttke which included examples from each of the major chemical 1974; Jones and Prada 1977; Schuster and Balster 1973; families of opioids, maintained responding at rates above Smith et al. 1976; Stretch and Gerber 1977; Wurster et al. those maintained by saline. There were differences among the 1977; Young and Woods 1980). compounds in the maximal response rates maintained, and The present study describes the self-administration of a large differences in their potencies in maintaining responding. number of compounds, from various chemical families, that In morphine-dependent monkeys, the abstinence signs that suppress the signs of morphine withdrawal in the rhesus developed 14 h after the last morphine dose were suppressed monkey. The ability of these compounds to maintain be- completely by all of the compounds except codeine. There was havior was studied under a rapid substitution procedure in a strong positive correlation (r = 0.92) between the potency rhesus monkeys experienced in self-injecting codeine (Woods of a compound in maintaining drug-reinforced responding 1980). -
Species Differences in the Conjugation of 4-Hydroxy-3-Methoxyphenylethanol with Glucuronic Acid and Sulphuric Acid
Biochem. J. (1976) 158, 33-37 33 Printed in Great Britain Species Differences in the Conjugation of 4-Hydroxy-3-methoxyphenylethanol with Glucuronic Acid and Sulphuric Acid By KIM PING WONG Department ofBiochemistry, University ofSingapore, Singapore 3 (Received 24 September 1975) The biosynthesis of the glucuronide and sulphate conjugates of 4-hydroxy-3-methoxy- phenylethanol was demonstrated in vitro by using the high-speed supernatant and micro- somal fractions ofliver respectively. These two conjugates were also produced simultane- ously byusingthe post-mitochondrial fraction ofrat, rabbit or guinea-pig liver. In contrast only the glucuronide was synthesized by human liver and only the sulphate by mouse and cat livers. Neither of these conjugates was formed by the kidney or the small or large intestine of the rat. A high sulphate-conjugating activity was observed in mouse kidney; therate ofsulphation of4-hydroxy-3-methoxyphenylethanol with kidney homogenate and high-speed supematant preparations was 1.8 times greater than with liver preparations. The sulpho-conjugates of4-hydroxy-3-methoxyphenylethanol and 4-hydroxy-3-methoxy- phenylglycol were also formed by enzyme preparations ofrabbit adrenal andrat brain; the glycol was the better substrate in the latter system. Mouse brain did not possess any sulphotransferase activity. For the conjugation of 4-hydroxy-3-methoxyphenylethanol by rabbit liver, the Km for UDP-glucuronic acid was 0.22mM and that for Na2SO4 was 3.45mM. The sulphotransferase has a greater affinity for 4-hydroxy-3-methoxyphenyl- ethanol than has glucuronyltransferase, as indicated by their respective Km values of 0.036 and 1.3mM. It was concluded that sulphate conjugation of 4-hydroxy-3- methoxyphenylethanol predominates in most species of animals. -
BMJ Open Is Committed to Open Peer Review. As Part of This Commitment We Make the Peer Review History of Every Article We Publish Publicly Available
BMJ Open: first published as 10.1136/bmjopen-2018-027935 on 5 May 2019. Downloaded from BMJ Open is committed to open peer review. As part of this commitment we make the peer review history of every article we publish publicly available. When an article is published we post the peer reviewers’ comments and the authors’ responses online. We also post the versions of the paper that were used during peer review. These are the versions that the peer review comments apply to. The versions of the paper that follow are the versions that were submitted during the peer review process. They are not the versions of record or the final published versions. They should not be cited or distributed as the published version of this manuscript. BMJ Open is an open access journal and the full, final, typeset and author-corrected version of record of the manuscript is available on our site with no access controls, subscription charges or pay-per-view fees (http://bmjopen.bmj.com). If you have any questions on BMJ Open’s open peer review process please email [email protected] http://bmjopen.bmj.com/ on September 26, 2021 by guest. Protected copyright. BMJ Open BMJ Open: first published as 10.1136/bmjopen-2018-027935 on 5 May 2019. Downloaded from Treatment of stable chronic obstructive pulmonary disease: a protocol for a systematic review and evidence map Journal: BMJ Open ManuscriptFor ID peerbmjopen-2018-027935 review only Article Type: Protocol Date Submitted by the 15-Nov-2018 Author: Complete List of Authors: Dobler, Claudia; Mayo Clinic, Evidence-Based Practice Center, Robert D. -
WO 2014/085719 Al 5 June 2014 (05.06.2014) P O P C T
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2014/085719 Al 5 June 2014 (05.06.2014) P O P C T (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every A61M 15/00 (2006.01) A24F 47/00 (2006.01) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, (21) International Application Number: BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, PCT/US20 13/072426 DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (22) International Filing Date: HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KN, KP, KR, 27 November 2013 (27.1 1.2013) KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, (25) Filing Language: English OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, (26) Publication Language: English SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, (30) Priority Data: ZW. 61/730,738 28 November 2012 (28. 11.2012) US 61/794,601 15 March 2013 (15.03.2013) US (84) Designated States (unless otherwise indicated, for every 61/83 1,992 6 June 2013 (06.06.2013) us kind of regional protection available): ARIPO (BW, GH, 61/887,045 4 October 201 3 (04.