Neurotransmitter Pathways

Total Page：16

File Type：pdf, Size：1020Kb

NT Neurotransmitter Pathways P5P Tryptophan Tryptamine MAO P5P Iron BH4 Vitamin D tryptophan hydroxylase Phenylalanine hydroxylase P5P Phenylalanine Tyrosine Tyramine P5P, Fe, BH4 aromatic MAO 5-Hydroxytryptophan P5P P5P amino acid (5-HTP) Iron decarboxylase aromatic amino acid BH4 P5P decarboxylase Phenethylamine Vitamin D tyrosine hydroxylase (PEA) MAO Serotonin B2 L-Dopa N-acetyl DOPAC B3 MAO transferase P5P aromatic amino acid Iron decarboxylase Acetylserotonin MAO 5-HIAA Dopamine 3-MT hydroxyindole-0- COMT SAMe Vitamin C dopamine methyltransferase Copper B-hydroxylase B3 Melatonin Norepinephrine COMT SAMe phenylethanolamine Cortisol N-methyltransferase Normetanephrine KEY Epinephrine COMT MAO = monoamine oxidase Cofactors for MAO: B2, B3, P5P, Fe, Mg COMT = catechol-o-methyl-transferase Metanephrine Cofactors for COMT: SAMe, Mg P5P = (pyridoxal-5-phosphate) activated form of vitamin B6 BH4 = (tetrahydrobiopterin) Endogenous levels can be supported with SAMe, vitamin B3, C, Mo, Zn MTHF = (methyltetrahydrofolate) active form of folate. SAMe = endogenous levels can be supported with Mg, MTHF, and methylcobalamin supplementation. Cofactors = Enzymes = NT Neurotransmitter Pathways Cysteine Taurine “glycine cleavage system” P5P, Fe, Mo, SAMe serine hydroxymethyl glycine transferase decarboxylase CO2 Serine Glycine SAMe P5P NH3 P5P Mg metabolites Histamine Histidine methyltransferase Decarboxylase SAMe Histidine Histamine Diamine oxidase P5P P5P, Copper, Iron, B12, vitamin C metabolites Glutamine KEY glutamine glutaminase MAO = monoamine oxidase synthetase Cofactors for MAO: B2, B3, P5P, Fe, Mg glutamate COMT = catechol-o-methyl-transferase dehydrogenase (B3) Cofactors for COMT: SAMe, Mg P5P = (pyridoxal-5-phosphate) activated form alpha-ketoglutarate Glutamate Glutamic Acid of vitamin B6 BH4 = (tetrahydrobiopterin) aminotransferase (P5P) Endogenous levels can be supported with SAMe, P5P glutamate vitamin B3, C, Mo, Zn Taurine decarboxylase (GAD) MTHF = (methyltetrahydrofolate) active form of folate. SAMe = endogenous levels can be supported with Mg, MTHF, and methylcobalamin supplementation. Note: aminotransferase aka transaminase GABA Cofactors = Enzymes =.

Copy Link

Recommended publications

Neurotransmitter Resource Guide
NEUROTRANSMITTER RESOURCE GUIDE Science + Insight doctorsdata.com Doctor’s Data, Inc. Neurotransmitter RESOURCE GUIDE Table of Contents Sample Report Sample Report ........................................................................................................................................................................... 1 Analyte Considerations Phenylethylamine (B-phenylethylamine or PEA) ................................................................................................. 1 Tyrosine .......................................................................................................................................................................................... 3 Tyramine ........................................................................................................................................................................................4 Dopamine .....................................................................................................................................................................................6 3, 4-Dihydroxyphenylacetic Acid (DOPAC) ............................................................................................................... 7 3-Methoxytyramine (3-MT) ............................................................................................................................................... 9 Norepinephrine ........................................................................................................................................................................
[Show full text]
Effects of the Inhibitor of Glutamate Decarboxylase on the Development
RSC Advances View Article Online PAPER View Journal | View Issue Effects of the inhibitor of glutamate decarboxylase on the development and GABA accumulation in Cite this: RSC Adv.,2018,8,20456 germinating fava beans under hypoxia-NaCl stress Yongqi Yin, Chao Cheng and Weiming Fang* Glutamate decarboxylase (GAD) is the key enzyme in GABA shunt, which catalyzes the a-decarboxylation of glutamate to produce GABA. A specific inhibitor for GAD is convenient to study the dynamic balances of GABA metabolism in plants. The inhibitor of GAD in germinated fava beans was screened, and its inhibitory effect on the growth and GABA accumulation in fava beans during germination under hypoxia- NaCl stress was investigated. The inhibitory effect of aminoxyacetate for fava bean GAD was better than those of other chemicals, and it increased with the increase in concentration in vivo. After aminoxyacetate (5 mM) application for 4 days during germination, the GAD activity in germinating fava beans was significantly inhibited by more than 90% in both organs. Meanwhile, the growth of fava bean Creative Commons Attribution-NonCommercial 3.0 Unported Licence. sprouts was also slightly suppressed. Moreover, the GABA contents decreased by 43.9% and 81.5% in a 4 Received 8th May 2018 day-old cotyledon and embryo, respectively, under aminoxyacetate treatment compared with that in the Accepted 23rd May 2018 control. In summary, these results showed that aminoxyacetate can serve as a specific inhibitor of GAD DOI: 10.1039/c8ra03940b in plants. At least 43.9% and 81.5% of GABA in germinating fava beans under hypoxia-NaCl stress were rsc.li/rsc-advances synthesized via GABA shunt.
[Show full text]
Metabolism of 3-Nitrotyrosine Induces Apoptotic Death in Dopaminergic Cells
6124 • The Journal of Neuroscience, June 7, 2006 • 26(23):6124–6130 Neurobiology of Disease Metabolism of 3-Nitrotyrosine Induces Apoptotic Death in Dopaminergic Cells Be´atrice Blanchard-Fillion,1 Delphine Prou,2 Manuela Polydoro,1 David Spielberg,1 Elpida Tsika,1 Zeneng Wang,5 Stanley L. Hazen,5 Michael Koval,6 Serge Przedborski,2,3,4 and Harry Ischiropoulos1,7 1Stokes Research Institute, Children’s Hospital of Philadelphia, Philadelphia, Pennsylvania 19104, Departments of 2Neurology and 3Pathology and Cell Biology and 4Center of Neurobiology and Behavior, Columbia University, New York, New York 10032, 5Department of Cardiovascular Medicine and Center for Cardiovascular Diagnostics and Prevention, Cleveland Clinic Foundation, Cleveland, Ohio 44195, and Departments of 6Physiology and 7Pharmacology, University of Pennsylvania, Philadelphia, Pennsylvania 19104 Intrastriatal injection of 3-nitrotyrosine, which is a biomarker for nitrating oxidants, provokes dopaminergic neuronal death in rats by unknown mechanisms. Herein, we show that extracellular 3-nitrotyrosine is transported via the L-aromatic amino acid transporter in nondopaminergic NT2 cells, whereas in dopaminergic PC12 cells, it is transported by both the l-aromatic amino acid and the dopamine transporters. In both cell lines, 3-nitrotyrosine is a substrate for tyrosine tubulin ligase, resulting in its incorporation into the C terminus of ␣-tubulin. In NT2 cells, incorporation of 3-nitrotyrosine into ␣-tubulin induces a progressive, reversible reorganization of the micro- tubule architecture. In PC12 cells, 3-nitrotyrosine decreases intracellular dopamine levels and is metabolized by the concerted action of the aromatic amino acid decarboxylase and monoamine oxidase. Intracellular levels of 133 ␮mol of 3-nitrotyrosine per mole of tyrosine did not alter NT2 viability but induced PC12 apoptosis.
[Show full text]
Mechanism–Based Inhibitors for Copper Amine Oxidases
MECHANISM–BASED INHIBITORS FOR COPPER AMINE OXIDASES: SYNTHESIS, MECHANISM, AND ENZYMOLOGY By BO ZHONG Submitted in partial fulfillment of the requirements For the degree of Doctor of Philosophy Thesis Adviser: Dr. Lawrence M. Sayre, Dr Irene Lee Department of Chemistry CASE WESTERN RESERVE UNIVERSITY January, 2010 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. Table of Contents Table of Contents ............................................................................................................... I List of Tables .................................................................................................................... V List of Figures .................................................................................................................. VI List of Schemes ................................................................................................................ XI Acknowledgements
[Show full text]
Serum Diamine Oxidase Activity As a Predictor of Gastrointestinal Toxicity and Malnutrition Due to Anticancer Drugs1
Serum diamine oxidase activity as a predictor of gastrointestinal toxicity and malnutrition due to anticancer drugs1 Jinsei Miyoshi1, Hiroshi Miyamoto1, Takahiro Goji1, Tatsuya Taniguchi1, Tetsu Tomonari1, Masahiro Sogabe2, Tetsuo Kimura1, Shinji Kitamura1, Koichi Okamoto1, Yasuteru Fujino1, Naoki Muguruma1, Toshiya Okahisa2, Tetsuji Takayama1 1Department of Gastroenterology and Oncology, Institute of Health Biosciences, University of Tokushima Graduate School, 3-18-15, Kuramoto-cho, Tokushima city, 770-8503, Japan 2Department of General Medicine and Community Health Science, Institute of HealthArticle Biosciences, University of Tokushima Graduate School, Tokushima, Japan Correspondence to: Prof. Tetsuji Takayama, Department of Gastroenterology and Oncology, Institute of Health Biosciences, University of Tokushima Graduate School, Tokushima, Japan E-mail:[email protected] Tel: +81-88-633-7124; Fax: +81-88-633-9235; Article type: Original Article Short title: DAO activity as predictor of GI toxicity Abstract This article has been accepted for publication and undergone full peer review but has not been through the copyediting, typesetting, pagination and proofreading process, which may lead to differences between this version and the Version of Record. Please cite this article as doi: 10.1111/jgh.13004 Accepted 1 This article is protected by copyright. All rights reserved. Background and Aim: Objective evaluation of intestinal mucosal damage due to anticancer drugs is generally difficult. Serum diamine oxidase (DAO) activity is reported to reflect the integrity and maturity of the small intestinal mucosa. Therefore, we investigated whether serum DAO activity is an indicator of gastrointestinal toxicity or nutritional status in patients receiving chemotherapy. Methods: We prospectively enrolled 20 patients with unresectable metastatic gastric cancer who received oral S-1 (80 mg/m2) on days 1–14, and 2 2 intravenousArticle cisplatin (60 mg/m ) and docetaxel (50 mg/m ) on day 8 every 3 weeks.
[Show full text]
MECHANISTIC STUDIES on DIAMINE OXIDASE a Thesis
MECHANISTIC STUDIES ON DIAMINE OXIDASE A thesis presented in part fulfilm ent of the requirements for the Degree of Doctor of Philosophy by Stephen Scott Gavin Department of Organic Chemistry University of Glasgow July 1995 ProQuest Number: 13832535 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 com plete 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 13832535 Published by ProQuest LLC(2019). Copyright of the Dissertation is held by the Author. All rights reserved. This work is protected against unauthorized copying under Title 17, United States C ode Microform Edition © ProQuest LLC. ProQuest LLC. 789 East Eisenhower Parkway P.O. Box 1346 Ann Arbor, Ml 48106- 1346 10ZW ) IE a Fx JtTI imun;; -;r,T j u s M r r f ( To m y wife Hazel and all m y family, One Love, One Blood. ACKNOWLEDGEMENTS I would like to offer my sincere thanks to Professor D. J. Robins for his guidance, both technically and personally, through the many challenges I have faced during my research. In particular for his help and patience in the writing of this thesis. I am most grateful to Dr. A. Cooper for his assistance with the biophysical work carried out as part of this thesis. I am also grateful for the help I received from the departmental technical staff during my studies.
[Show full text]
Histamine Metabolism
Edited by Holger Stark Chapter 3 Histamine Metabolism H.G. Schwelberger1, F. Ahrens2, W.A. Fogel3, F. Sánchez-Jiménez4 1Molecular Biology Laboratory, Department of Visceral, Transplantation and Thoracic Surgery, Medical University Innsbruck, Austria, e-mail: [email protected] 2Department of Veterinary Science, Institute of Animal Physiology, Ludwig-Maximilians University Munich, Germany 3Department of Hormone Biochemistry, Medical University of Lodz, Poland 4Department of Molecular Biology and Biochemistry, University of Malaga, Spain Abstract Histamine is formed by decarboxylation of the amino acid L-histidine, a process catalyzed by histidine decarboxylase (HDC) and can be inactivated either by methylation of the imidazole ring, catalyzed by histamine N-methyltransferase (HMT) or by oxidative deamination of the primary amino group, catalyzed by diamine oxidase (DAO). This chapter describes the enzymatic reactions and the properties of the enzymes involved, including their structures, their cellular localization, their genes, expression and regulation, and the determination of their enzymatic activities. It also addresses cellular histamine transport, storage and release. Further, it discusses alterations in histamine metabolism associated with human diseases and how this might affect histamine receptor signaling. 3.1. Introduction Histamine [2-(1H-Imidazol-4-yl)ethanamine] is an important mediator of many biological processes including inflammation, gastric acid secretion, neuromodulation, and regulation of immune function
[Show full text]
Modism VA-098 / VA-949 Supports Neurological Development Via Methylation Cycle & the Collateral Pathways
Modism VA-098 / VA-949 Supports Neurological Development Via Methylation Cycle & The Collateral Pathways Key Features: Serving Size: 1 scoop (4.2 g) • With key cofactors of multiple metabolic pathways 42 servings per container implicated in the clinical presentations of ASD & ADHD. Ingredients (per scoop): Vitamin B1 (from thiamine HCl).................................................10 mg • Supports the collateral metabolic pathways of the Vitamin B2 (from riboflavin-5’-phosphate).................................10 mg methylation cycle and reduce the symptoms of metabolic Vitamin B3 (Niacinamide)............................................................25 mg overload from methylation enhancement. Vitamin B6 (from calcium pyridoxal-5’-phosphate).....................25 mg 5-MTHF (from calcium 5-methylfolate)..................................250 mcg • The inclusion of S. boulardii helps to support the gut flora Vitamin B12 (methylcobalamin).............................................250 mcg in cases of opportunistic bacteria overgrowth, particularly Vitamin D3 (cholecalciferol) (12.5 mcg)....................................500 IU Clostridium spp. and Candida albicans. Magnesium (from magnesium citrate)......................................125 mg Molybdenum (from molybdenum glycinate)...........................200 mcg Copper (from copper bisglycinate).........................................200 mcg Indication: Zinc (from zinc gluconate).............................................................6 mg Support the neurological development
[Show full text]
Role of Monoamine Oxidase Activity in Alzheimer's Disease
molecules Review Role of Monoamine Oxidase Activity in Alzheimer’s Disease: An Insight into the Therapeutic Potential of Inhibitors Tapan Behl 1,*, Dapinder Kaur 1, Aayush Sehgal 1, Sukhbir Singh 1, Neelam Sharma 1, Gokhan Zengin 2, Felicia Liana Andronie-Cioara 3 , Mirela Marioara Toma 4,5, Simona Bungau 4,5,* and Adrian Gheorghe Bumbu 6 1 Department of Pharmacology, Chitkara College of Pharmacy, Chitkara University, Rajpura 140401, Punjab, India; [email protected] (D.K.); [email protected] (A.S.); [email protected] (S.S.); [email protected] (N.S.) 2 Department of Biology, Faculty of Science, Selcuk University Campus, 42130 Konya, Turkey; [email protected] 3 Department of Psycho-Neuroscience and Recovery, Faculty of Medicine and Pharmacy, University of Oradea, 410073 Oradea, Romania; [email protected] 4 Department of Pharmacy, Faculty of Medicine and Pharmacy, University of Oradea, 410028 Oradea, Romania; [email protected] 5 Doctoral School of Biomedical Sciences, University of Oradea, 410073 Oradea, Romania 6 Department of Surgical Disciplines, Faculty of Medicine and Pharmacy, University of Oradea, 410073 Oradea, Romania; [email protected] * Correspondence: [email protected] (T.B.); [email protected] (S.B.) Abstract: Despite not being utilized as considerably as other antidepressants in the therapy of Citation: Behl, T.; Kaur, D.; Sehgal, depression, the monoamine oxidase inhibitors (MAOIs) proceed to hold a place in neurodegeneration A.; Singh, S.; Sharma, N.; Zengin, G.; and to have a somewhat broad spectrum in respect of the treatment of neurological and psychiatric Andronie-Cioara, F.L.; Toma, M.M.; conditions. Preclinical and clinical studies on MAOIs have been developing in recent times, especially Bungau, S.; Bumbu, A.G.
[Show full text]
Development of a Quantitative UPLC/MS/MS Assay for the Simultaneous Quantification of Acetylcholine, Histamine, and Their Metabo
Development of a Quantitative UPLC/MS/MS Assay for the Simultaneous Quantification of Acetylcholine, Histamine, and their Metabolites in Human Cerebrospinal Fluid (CSF) Using a CORTECS UPLC HILIC Column to Improve Peak Resolution, Sensitivity, and Speed of Analysis Mary E. Lame, Erin E. Chambers, and Kenneth J. Fountain Waters Corporation, Milford, MA, USA APPLICATION BENEFITS INT RODUC T ION ■■ Resolution of the CORTECS™ UPLC® Biochemical biomarkers, derived from HILIC Column provides simultaneous bodily fluids, are often employed in quantification of ACh, HA, and drug discovery and development as their metabolites a useful way of identifying disease or effectiveness of drug treatment. ■■ Total run time of 2.5 minutes meets high throughput screening demands Acetylcholine (ACh) and Histamine (HA) are highly polar neurotransmitters and ■■ Simple sample preparation (<15 minutes) Meet the scientist behind the application and hear a short summary of her work.* are present in almost all mammalian in a 96-well format tissues. They play a role in sleep ■■ High sensitivity achieved with the regulation, memory and learning, and immune responses.1-3 A decrease in Xevo® TQ-S MS facilitates use of smaller ACh levels in the brain is a known contributor to memory dysfunction, and sample volumes and higher dilution is in particularly short supply in people with Alzheimer’s Disease.1 Thus, volumes than previously reported increased release of ACh is extensively researched in treatments of these cognitive disorders. Histamine is derived from the decarboxylation of the amino acid, histidine. WATERS SOLUTIONS Histamine is either stored or rapidly inactivated by its primary degradative enzymes, histamine-N-methyltransferase, or diamine oxidase, and ACQUITY UPLC® System metabolized to two major metabolites, tele-Methylhistamine (t-mHA) and Xevo TQ-S Mass Spectrometer tele-methylimidazoleacetic acid (t-MIAA).
[Show full text]
Diamine Oxidase from Porcine Kidney
Diamine Oxidase from porcine kidney Product Number D 7876 Storage Temperature -0 °C Product Description Precautions and Disclaimer Enzyme Commission (EC) Number: 1.4.3.6 For Laboratory Use Only. Not for drug, household or CAS Number: 9001-53-0 other uses. Molecular Weight: 170 kDa1 Extinction Coefficient: E1% = 12.8 (280 nm)2 Preparation Instructions This enzyme is soluble in 100 mM sodium phosphate Diamine oxidase from porcine kidney is a homodimer buffer, pH 7.2 (10 mg/ml). consisting of 2 equal subunits with a molecular weight of 87 kDa each. Each subunit contains one molecule References of pyridoxal phosphate and one atom of copper.2 The 1. Rinaldi, A., et al., Diamine oxidase from pig enzyme is a glycoprotein containing 5% hexose, kidney: new purification method and amino acid 3.3% glucosamine, 2.6% N-acetylglucosamine, and composition. Prep. Biochem., 12, 11-28 (1982). 0.25% N-acetylneuraminic acid. The enzyme exhibits 2. Methods in Enzymology, Vol. 17B, Taylor, H., and a high affinity for concanavalin A.3 Tabor, C. W., Eds., Academic Press (New York, NY: 1971), pp. 735-740. Diamine oxidase from porcine kidney catalyzes the 3. Shah, M.A., and Ali, R., The glycoprotein nature of oxidation of monoamines, diamines, and histamine to pig kidney diamine oxidase. Role of disulphide aldehydes, ammonia, and hydrogen peroxide. The pH groups and arginine residues in the concanavalin optimum is 6.3-7.4 when cadverine and histamine are A-diamine oxidase interaction. Biochem. J., 253, utilized as substrates.2 The activity of the enzyme at 103-107 (1988).
[Show full text]
Sample Taking Problems in Measuring Actual Histamine Levels Of
Gut: first published as 10.1136/gut.26.11.1165 on 1 November 1985. Downloaded from Gut, 1985, 26, 1165-1178 Alimentary tract and pancreas Sample taking problems in measuring actual histamine levels of human gastroduodenal mucosa: specific and general relevance in clinical trials on peptic ulcer pathogenesis and selective proximal vagotomy K P THON, W LORENZ, Ch OHMANN, D WEBER, H ROHDE, AND H D ROHER From the Surgical Clinic and Department of Theoretical Surgery, Centre of Operative Medicine I, University of MarburglLahn, FRG SUMMARY Changes in histamine storage in the oxyntic mucosa of duodenal ulcer patients and their reversal by vagotomy and the histamine H2-antagonist cimetidine supported the hypothesis that histamine could be a causal factor in peptic ulcer pathogenesis. The specificity of these findings was impaired by problems in biopsy taking, however, and in the preparative steps before measuring the actual histamine contents in all parts of the gastric mucosa and in the duodenum. A prospective trial was carried out in 190 patients to identify these sources of bias and to overcome them by appropriate study designs.1 Usually a direct correlation was found between weight of biopsy and mucosal histamine content. This problem was solved by selecting a biopsy forceps producing smaller variations in sample size, by limiting the time of cold ischaemia to four to five minutes only and by taking three biopsy specimens for each single histamine value.2 The actual histamine content of mucosal biopsies remained constant for about four to five minutes only. The 'disappearance' rate was faster in control subjects than in duodenal ulcer patients.
[Show full text]