Identification of Nutritional Components in Black Sesame
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Endogenous Metabolites: JHU NIMH Center Page 1
S. No. Amino Acids (AA) 24 L-Homocysteic acid 1 Glutaric acid 25 L-Kynurenine 2 Glycine 26 N-Acetyl-Aspartic acid 3 L-arginine 27 N-Acetyl-L-alanine 4 L-Aspartic acid 28 N-Acetyl-L-phenylalanine 5 L-Glutamine 29 N-Acetylneuraminic acid 6 L-Histidine 30 N-Methyl-L-lysine 7 L-Isoleucine 31 N-Methyl-L-proline 8 L-Leucine 32 NN-Dimethyl Arginine 9 L-Lysine 33 Norepinephrine 10 L-Methionine 34 Phenylacetyl-L-glutamine 11 L-Phenylalanine 35 Pyroglutamic acid 12 L-Proline 36 Sarcosine 13 L-Serine 37 Serotonin 14 L-Tryptophan 38 Stachydrine 15 L-Tyrosine 39 Taurine 40 Urea S. No. AA Metabolites and Conjugates 1 1-Methyl-L-histidine S. No. Carnitine conjugates 2 2-Methyl-N-(4-Methylphenyl)alanine 1 Acetyl-L-carnitine 3 3-Methylindole 2 Butyrylcarnitine 4 3-Methyl-L-histidine 3 Decanoyl-L-carnitine 5 4-Aminohippuric acid 4 Isovalerylcarnitine 6 5-Hydroxylysine 5 Lauroyl-L-carnitine 7 5-Hydroxymethyluracil 6 L-Glutarylcarnitine 8 Alpha-Aspartyl-lysine 7 Linoleoylcarnitine 9 Argininosuccinic acid 8 L-Propionylcarnitine 10 Betaine 9 Myristoyl-L-carnitine 11 Betonicine 10 Octanoylcarnitine 12 Carnitine 11 Oleoyl-L-carnitine 13 Creatine 12 Palmitoyl-L-carnitine 14 Creatinine 13 Stearoyl-L-carnitine 15 Dimethylglycine 16 Dopamine S. No. Krebs Cycle 17 Epinephrine 1 Aconitate 18 Hippuric acid 2 Citrate 19 Homo-L-arginine 3 Ketoglutarate 20 Hydroxykynurenine 4 Malate 21 Indolelactic acid 5 Oxalo acetate 22 L-Alloisoleucine 6 Succinate 23 L-Citrulline 24 L-Cysteine-glutathione disulfide Semi-quantitative analysis of endogenous metabolites: JHU NIMH Center Page 1 25 L-Glutathione, reduced Table 1: Semi-quantitative analysis of endogenous molecules and their derivatives by Liquid Chromatography- Mass Spectrometry (LC-TripleTOF “or” LC-QTRAP). -
2'-Deoxyguanosine Toxicity for B and Mature T Lymphoid Cell Lines Is Mediated by Guanine Ribonucleotide Accumulation
2'-deoxyguanosine toxicity for B and mature T lymphoid cell lines is mediated by guanine ribonucleotide accumulation. Y Sidi, B S Mitchell J Clin Invest. 1984;74(5):1640-1648. https://doi.org/10.1172/JCI111580. Research Article Inherited deficiency of the enzyme purine nucleoside phosphorylase (PNP) results in selective and severe T lymphocyte depletion which is mediated by its substrate, 2'-deoxyguanosine. This observation provides a rationale for the use of PNP inhibitors as selective T cell immunosuppressive agents. We have studied the relative effects of the PNP inhibitor 8- aminoguanosine on the metabolism and growth of lymphoid cell lines of T and B cell origin. We have found that 2'- deoxyguanosine toxicity for T lymphoblasts is markedly potentiated by 8-aminoguanosine and is mediated by the accumulation of deoxyguanosine triphosphate. In contrast, the growth of T4+ mature T cell lines and B lymphoblast cell lines is inhibited by somewhat higher concentrations of 2'-deoxyguanosine (ID50 20 and 18 microM, respectively) in the presence of 8-aminoguanosine without an increase in deoxyguanosine triphosphate levels. Cytotoxicity correlates instead with a three- to fivefold increase in guanosine triphosphate (GTP) levels after 24 h. Accumulation of GTP and growth inhibition also result from exposure to guanosine, but not to guanine at equimolar concentrations. B lymphoblasts which are deficient in the purine salvage enzyme hypoxanthine guanine phosphoribosyltransferase are completely resistant to 2'-deoxyguanosine or guanosine concentrations up to 800 microM and do not demonstrate an increase in GTP levels. Growth inhibition and GTP accumulation are prevented by hypoxanthine or adenine, but not by 2'-deoxycytidine. -
Identification of Compounds That Rescue Otic and Myelination
RESEARCH ARTICLE Identification of compounds that rescue otic and myelination defects in the zebrafish adgrg6 (gpr126) mutant Elvira Diamantopoulou1†, Sarah Baxendale1†, Antonio de la Vega de Leo´ n2, Anzar Asad1, Celia J Holdsworth1, Leila Abbas1, Valerie J Gillet2, Giselle R Wiggin3, Tanya T Whitfield1* 1Bateson Centre and Department of Biomedical Science, University of Sheffield, Sheffield, United Kingdom; 2Information School, University of Sheffield, Sheffield, United Kingdom; 3Sosei Heptares, Cambridge, United Kingdom Abstract Adgrg6 (Gpr126) is an adhesion class G protein-coupled receptor with a conserved role in myelination of the peripheral nervous system. In the zebrafish, mutation of adgrg6 also results in defects in the inner ear: otic tissue fails to down-regulate versican gene expression and morphogenesis is disrupted. We have designed a whole-animal screen that tests for rescue of both up- and down-regulated gene expression in mutant embryos, together with analysis of weak and strong alleles. From a screen of 3120 structurally diverse compounds, we have identified 68 that reduce versican b expression in the adgrg6 mutant ear, 41 of which also restore myelin basic protein gene expression in Schwann cells of mutant embryos. Nineteen compounds unable to rescue a strong adgrg6 allele provide candidates for molecules that may interact directly with the Adgrg6 receptor. Our pipeline provides a powerful approach for identifying compounds that modulate GPCR activity, with potential impact for future drug design. DOI: https://doi.org/10.7554/eLife.44889.001 *For correspondence: [email protected] †These authors contributed Introduction equally to this work Adgrg6 (Gpr126) is an adhesion (B2) class G protein-coupled receptor (aGPCR) with conserved roles in myelination of the vertebrate peripheral nervous system (PNS) (reviewed in Langenhan et al., Competing interest: See 2016; Patra et al., 2014). -
Amino Acid Analysis in Biological Fluids by GC-MS
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by University of Regensburg Publication Server Amino acid analysis in biological fluids by GC-MS Dissertation zur Erlangung des Doktorgrades der Naturwissenschaften (Dr. rer. nat.) an der Fakultät für Chemie und Pharmazie der Universität Regensburg vorgelegt von Hannelore Kaspar aus Fürstenfeldbruck Juni 2009 Diese Doktorarbeit entstand in der Zeit von Oktober 2005 bis Juni 2009 am Institut für Funktionelle Genomik der Universität Regensburg. Die Arbeit wurde angeleitet von Prof. Dr. Peter J. Oefner. Promotionsgesuch eingereicht im Juni 2009 Kolloquiumstermin: 17.07.2009 Prüfungsausschuß: Vorsitzender: Prof. Dr. Manfred Scheer Erstgutachter: Prof. Dr. Frank-Michael Matysik Zweitgutachter: Prof. Dr. Peter J. Oefner Drittprüfer: Prof. Dr. Jörg Heilmann Für meine Eltern Danksagung Diese Doktorarbeit ist ein großer Meilensteil in meinem bisherigen Leben, den ich durch großartige Unterstützung von vielen lieben Leuten meistern konnte. Den allerwichtigsten Menschen möchte ich hier danken. Als erstes bedanke ich mich bei Prof. PJ. Oefner dafür in seinem Institut promovieren zu dürfen sowie für seinen unermüdlichen Einsatz seinen Mitarbeitern stets die besten Möglichkeiten in Sachen Forschung zu bieten und Kooperationen aufzubauen und zu fördern. Ein besonderes Dankeschön geht auch an Prof. Matysik für die freundliche Übernahme des Erstgutachtens. Bei Prof. Heilmann bedanke ich mich für die Bereitschaft an meiner Prüfung teilzunehmen sowie Prof. Scheer für die Übernahme des Prüfungsvorsitzes. Den allergrößten Dank möchte ich meiner Betreuerin und Mentorin Dr. Katja Dettmer aussprechen. Nicht nur für ihre hervorragende fachliche Betreuung währen meiner Doktorarbeit sondern auch für die vielen freundlichen und aufbauenden Worte, die Weitergabe ihres Wissens und vor allem dafür, dass Sie mir das Gefühl gab als Mensch und Wissenschaftler wichtig und wertvoll zu sein. -
NINDS Custom Collection II
ACACETIN ACEBUTOLOL HYDROCHLORIDE ACECLIDINE HYDROCHLORIDE ACEMETACIN ACETAMINOPHEN ACETAMINOSALOL ACETANILIDE ACETARSOL ACETAZOLAMIDE ACETOHYDROXAMIC ACID ACETRIAZOIC ACID ACETYL TYROSINE ETHYL ESTER ACETYLCARNITINE ACETYLCHOLINE ACETYLCYSTEINE ACETYLGLUCOSAMINE ACETYLGLUTAMIC ACID ACETYL-L-LEUCINE ACETYLPHENYLALANINE ACETYLSEROTONIN ACETYLTRYPTOPHAN ACEXAMIC ACID ACIVICIN ACLACINOMYCIN A1 ACONITINE ACRIFLAVINIUM HYDROCHLORIDE ACRISORCIN ACTINONIN ACYCLOVIR ADENOSINE PHOSPHATE ADENOSINE ADRENALINE BITARTRATE AESCULIN AJMALINE AKLAVINE HYDROCHLORIDE ALANYL-dl-LEUCINE ALANYL-dl-PHENYLALANINE ALAPROCLATE ALBENDAZOLE ALBUTEROL ALEXIDINE HYDROCHLORIDE ALLANTOIN ALLOPURINOL ALMOTRIPTAN ALOIN ALPRENOLOL ALTRETAMINE ALVERINE CITRATE AMANTADINE HYDROCHLORIDE AMBROXOL HYDROCHLORIDE AMCINONIDE AMIKACIN SULFATE AMILORIDE HYDROCHLORIDE 3-AMINOBENZAMIDE gamma-AMINOBUTYRIC ACID AMINOCAPROIC ACID N- (2-AMINOETHYL)-4-CHLOROBENZAMIDE (RO-16-6491) AMINOGLUTETHIMIDE AMINOHIPPURIC ACID AMINOHYDROXYBUTYRIC ACID AMINOLEVULINIC ACID HYDROCHLORIDE AMINOPHENAZONE 3-AMINOPROPANESULPHONIC ACID AMINOPYRIDINE 9-AMINO-1,2,3,4-TETRAHYDROACRIDINE HYDROCHLORIDE AMINOTHIAZOLE AMIODARONE HYDROCHLORIDE AMIPRILOSE AMITRIPTYLINE HYDROCHLORIDE AMLODIPINE BESYLATE AMODIAQUINE DIHYDROCHLORIDE AMOXEPINE AMOXICILLIN AMPICILLIN SODIUM AMPROLIUM AMRINONE AMYGDALIN ANABASAMINE HYDROCHLORIDE ANABASINE HYDROCHLORIDE ANCITABINE HYDROCHLORIDE ANDROSTERONE SODIUM SULFATE ANIRACETAM ANISINDIONE ANISODAMINE ANISOMYCIN ANTAZOLINE PHOSPHATE ANTHRALIN ANTIMYCIN A (A1 shown) ANTIPYRINE APHYLLIC -
A New Crystal Form of Bovine Pancreatic Rnase a in Complex with 2
protein structure communications Acta Crystallographica Section F Structural Biology A new crystal form of bovine pancreatic RNase A in 000 and Crystallization complex with 2 -deoxyguanosine- Communications 5000-monophosphate ISSN 1744-3091 Steven B. Larson,a John S. Day,a The structure of bovine pancreatic RNase A has been determined in complex Robert Cudneyb and Alexander with 20-deoxyguanosine-50-monophosphate (dGMP) at 1.33 A˚ resolution at McPhersona* room temperature in a previously unreported unit cell belonging to space group P31. There are two molecules of nucleotide per enzyme molecule, one of which aDepartment of Molecular Biology and lies in the active-site cleft in the productive binding mode, whilst the guanine Biochemistry, The University of California, base of the other dGMP occupies the pyrimidine-specific binding site in a Irvine, CA 92697-3900, USA, and bHampton nonproductive mode such that it forms hydrogen bonds to the phosphate group Research, Aliso Viejo, CA 92656-3317, USA of the first dGMP. This is the first RNase A structure containing a guanine base in the B2 binding site. Each dGMP molecule is involved in intermolecular interactions with adjacent RNase A molecules in the lattice and the two Correspondence e-mail: [email protected] nucleotides appear to direct the formation of the crystal lattice. Because GMP may be produced during degradation of RNA, this association could represent Received 19 June 2007 an inhibitor complex and thereby affect the observed enzyme kinetics. Accepted 9 August 2007 PDB Reference: RNase A–dGMP complex, 2qca, r2qcasf. 1. Introduction Bovine pancreatic ribonuclease (EC 3.1.27.5), commonly known as RNase A, has been extensively studied by physical-chemical approaches and by X-ray crystallography for nearly 75 years. -
Linking Phencyclidine Intoxication to the Tryptophan-Kynurenine Pathway Therapeutic Implications for Schizophrenia
Neurochemistry International 125 (2019) 1–6 Contents lists available at ScienceDirect Neurochemistry International journal homepage: www.elsevier.com/locate/neuint Linking phencyclidine intoxication to the tryptophan-kynurenine pathway: Therapeutic implications for schizophrenia T ∗ Hidetsugu Fujigakia, ,1, Akihiro Mourib,c,1, Yasuko Yamamotoa, Toshitaka Nabeshimac,d, Kuniaki Saitoa,c,d,e a Department of Disease Control and Prevention, Fujita Health University Graduate School of Health Sciences, 1-98 Dengakugakubo, Kutsukake-cho, Toyoake, Aichi 470- 1192, Japan b Department of Regulatory Science, Fujita Health University Graduate School of Health Sciences, 1-98 Dengakugakubo, Kutsukake-cho, Toyoake, Aichi 470-1192, Japan c Japanese Drug Organization of Appropriate Use and Research, 3-1509 Omoteyama, Tenpaku-ku, Nagoya, Aichi 468-0069, Japan d Advanced Diagnostic System Research Laboratory, Fujita Health University Graduate School of Health Sciences, 1-98 Dengakugakubo, Kutsukake-cho, Toyoake, Aichi 470-1192, Japan e Human Health Sciences, Graduate School of Medicine and Faculty of Medicine, Kyoto University, 54 Shogoinkawahara-cho, Sakyo-ku, Kyoto 606-8507, Japan ARTICLE INFO ABSTRACT Keywords: Phencyclidine (PCP) is a dissociative anesthetic that induces psychotic symptoms and neurocognitive deficits in Phencyclidine rodents similar to those observed in schizophrenia patients. PCP administration in healthy human subjects in- Kynurenic acid duces schizophrenia-like symptoms such as positive and negative symptoms, and a range of cognitive deficits. It Quinolinic acid has been reported that PCP, ketamine, and related drugs such as N-methyl-D-aspartate-type (NMDA) glutamate Kynurenine pathway receptor antagonists, induce behavioral effects by blocking neurotransmission at NMDA receptors. Further, Schizophrenia NMDA receptor antagonists reproduce specific aspects of the symptoms of schizophrenia. -
GRAS Notice (GRN) No. 719, Orange Pomace
GRAS Notice (GRN) No. 719 https://www.fda.gov/Food/IngredientsPackagingLabeling/GRAS/NoticeInventory/default.htm SAFETY EVALUATION DOSSIER SUPPORTING A GENERALLY RECOGNIZED AS SAFE (GRAS) CONCLUSION FOR ORANGE POMACE SUBMITTED BY: PepsiCo, Inc. 700 Anderson Hill Road Purchase, NY 10577 SUBMITTED TO: U.S. Food and Drug Administration Center for Food Safety and Applied Nutrition Office of Food Additive Safety HFS-200 5100 Paint Branch Parkway College Park, MD 20740-3835 CONTACT FOR TECHNICAL OR OTHER INFORMATION: Andrey Nikiforov, Ph.D. Toxicology Regulatory Services, Inc. 154 Hansen Road, Suite 201 Charlottesville, VA 22911 July 3, 2017 Table of Contents Part 1. SIGNED STATEMENTS AND CERTIFICATION ...........................................................1 A. Name and Address of Notifier .............................................................................................1 B. Name of GRAS Substance ...................................................................................................1 C. Intended Use and Consumer Exposure ................................................................................1 D. Basis for GRAS Conclusion ................................................................................................2 E. Availability of Information ..................................................................................................3 Part 2. IDENTITY, METHOD OF MANUFACTURE, SPECIFICATIONS, AND PHYSICAL OR TECHNICAL EFFECT.................................................................................................4 -
Agmatine Modulates Spontaneous Activity in Neurons of the Rat Medial
Weiss et al. Translational Psychiatry (2018) 8:201 DOI 10.1038/s41398-018-0254-z Translational Psychiatry ARTICLE Open Access Agmatine modulates spontaneous activity in neurons of the rat medial habenular complex—a relevant mechanism in the pathophysiology and treatment of depression? Torsten Weiss1,RenéBernard2, Hans-Gert Bernstein3,RüdigerW.Veh1 and Gregor Laube1 Abstract The dorsal diencephalic conduction system connects limbic forebrain structures to monaminergic mesencephalic nuclei via a distinct relay station, the habenular complexes. Both habenular nuclei, the lateral as well as the medial nucleus, are considered to play a prominent role in mental disorders like major depression. Herein, we investigate the effect of the polyamine agmatine on the electrical activity of neurons within the medial habenula in rat. We present evidence that agmatine strongly decreases spontaneous action potential firing of medial habenular neurons by activating I1-type imidazoline receptors. Additionally, we compare the expression patterns of agmatinase, an enzyme capable of inactivating agmatine, in rat and human habenula. In the medial habenula of both species, agmatinase is similarly distributed and observed in neurons and, in particular, in distinct neuropil areas. The putative relevance of 1234567890():,; 1234567890():,; 1234567890():,; 1234567890():,; these findings in the context of depression is discussed. It is concluded that increased activity of the agmatinergic system in the medial habenula may strengthen midbrain dopaminergic activity. Consequently, -
Functional and Structural Variation Among Sticholysins, Pore-Forming Proteins from the Sea Anemone Stichodactyla Helianthus
International Journal of Molecular Sciences Review Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea Anemone Stichodactyla helianthus Esperanza Rivera-de-Torre 1,2,3 , Juan Palacios-Ortega 1,2 , J. Peter Slotte 1,2, José G. Gavilanes 1, Álvaro Martínez-del-Pozo 1 and Sara García-Linares 1,* 1 Departamento de Bioquímica y Biología Molecular, Universidad Complutense, 28040 Madrid, Spain; [email protected] (E.R.-d.-T.); [email protected] (J.P.-O.); jpslotte@abo.fi (J.P.S.); [email protected] (J.G.G.); [email protected] (Á.M.-d.-P.) 2 Department of Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland 3 Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kongens Lyngby, Denmark * Correspondence: [email protected] Received: 19 October 2020; Accepted: 20 November 2020; Published: 24 November 2020 Abstract: Venoms constitute complex mixtures of many different molecules arising from evolution in processes driven by continuous prey–predator interactions. One of the most common compounds in these venomous cocktails are pore-forming proteins, a family of toxins whose activity relies on the disruption of the plasmatic membranes by forming pores. The venom of sea anemones, belonging to the oldest lineage of venomous animals, contains a large amount of a characteristic group of pore-forming proteins known as actinoporins. They bind specifically to sphingomyelin-containing membranes and suffer a conformational metamorphosis that drives them to make pores. This event usually leads cells to death by osmotic shock. Sticholysins are the actinoporins produced by Stichodactyla helianthus. Three different isotoxins are known: Sticholysins I, II, and III. -
Central Nervous System Dysfunction and Erythrocyte Guanosine Triphosphate Depletion in Purine Nucleoside Phosphorylase Deficiency
Arch Dis Child: first published as 10.1136/adc.62.4.385 on 1 April 1987. Downloaded from Archives of Disease in Childhood, 1987, 62, 385-391 Central nervous system dysfunction and erythrocyte guanosine triphosphate depletion in purine nucleoside phosphorylase deficiency H A SIMMONDS, L D FAIRBANKS, G S MORRIS, G MORGAN, A R WATSON, P TIMMS, AND B SINGH Purine Laboratory, Guy's Hospital, London, Department of Immunology, Institute of Child Health, London, Department of Paediatrics, City Hospital, Nottingham, Department of Paediatrics and Chemical Pathology, National Guard King Khalid Hospital, Jeddah, Saudi Arabia SUMMARY Developmental retardation was a prominent clinical feature in six infants from three kindreds deficient in the enzyme purine nucleoside phosphorylase (PNP) and was present before development of T cell immunodeficiency. Guanosine triphosphate (GTP) depletion was noted in the erythrocytes of all surviving homozygotes and was of equivalent magnitude to that found in the Lesch-Nyhan syndrome (complete hypoxanthine-guanine phosphoribosyltransferase (HGPRT) deficiency). The similarity between the neurological complications in both disorders that the two major clinical consequences of complete PNP deficiency have differing indicates copyright. aetiologies: (1) neurological effects resulting from deficiency of the PNP enzyme products, which are the substrates for HGPRT, leading to functional deficiency of this enzyme. (2) immunodeficiency caused by accumulation of the PNP enzyme substrates, one of which, deoxyguanosine, is toxic to T cells. These studies show the need to consider PNP deficiency (suggested by the finding of hypouricaemia) in patients with neurological dysfunction, as well as in T cell immunodeficiency. http://adc.bmj.com/ They suggest an important role for GTP in normal central nervous system function. -
Impact of Citicoline Over Cognitive Impairments After General Anesthesia
International Journal of Science and Research (IJSR) ISSN: 2319-7064 ResearchGate Impact Factor (2018): 0.28 | SJIF (2018): 7.426 Impact of Citicoline over Cognitive Impairments after General Anesthesia Kameliya Tsvetanova Department “Anesthesiology and Resuscitation“, Medical University – Pleven, Bulgaria Abstract: Postoperative cognitive delirium - POCD is chronic damage with deterioration of the memory, the attention and the speed of the processing of the information after anesthesia and operation. It is admitted that anesthetics and other perioperative factors are able to cause cognitive impairments through induction of apoptosis, neuro-inflammation, mitochondrial dysfunction and so on. More and more medicaments are used in modern medicine, as, for instance, Citicoline, which are in a position significantly to reduce this unpleasant complication of the anesthesia. Keywords: Postoperative cognitive delirium, anesthesia, Citicoline. 1. Introduction Therefore, Citocoline is the main intracellular precursor of phospholipid phosphatidyl choline. (13), (14), (15), (16), It is known that anesthetics and other perioperative factors (17), (18), (19), (20), (21), (22), (23), (24), (25), (26) are able to cause cognitive impairments through induction of apoptosis, neuro-inflammation, mitochondrial dysfunction It exerts impact over the cholinergic system and acts as a and so on. choline donor for the enhanced synthesis of acetylcholine. Chronic damage with deterioration of the memory, the attention and the speed of the processing of the information