Neurotransmitters: Critical Amino Acids Affecting
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Effects of Basic Amino Acids and Their Derivatives on SARS-Cov-2 and Influenza-A Virus Infection
viruses Article Effects of Basic Amino Acids and Their Derivatives on SARS-CoV-2 and Influenza-A Virus Infection Ivonne Melano 1 , Li-Lan Kuo 2, Yan-Chung Lo 3, Po-Wei Sung 4, Ni Tien 5,6 and Wen-Chi Su 1,2,7,* 1 Graduate Institute of Biomedical Sciences, College of Medicine, China Medical University, Taichung 40402, Taiwan; [email protected] 2 Research Center for Emerging Viruses, China Medical University Hospital, Taichung 40402, Taiwan; [email protected] 3 Sinphar Pharmaceutical Co., Ltd., Sinphar Group, Yilan 269, Taiwan; [email protected] 4 School of Medicine, China Medical University, Taichung 40402, Taiwan; [email protected] 5 Department of Laboratory Medicine, China Medical University Hospital, Taichung 40402, Taiwan; [email protected] 6 Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung 40402, Taiwan 7 International Master’s Program of Biomedical Sciences, China Medical University, Taichung 40402, Taiwan * Correspondence: [email protected] Abstract: Amino acids have been implicated with virus infection and replication. Here, we demon- strate the effects of two basic amino acids, arginine and lysine, and their ester derivatives on infection of two enveloped viruses, SARS-CoV-2, and influenza A virus. We found that lysine and its ester derivative can efficiently block infection of both viruses in vitro. Furthermore, the arginine ester derivative caused a significant boost in virus infection. Studies on their mechanism of action revealed that the compounds potentially disturb virus uncoating rather than virus attachment and endosomal Citation: Melano, I.; Kuo, L.-L.; Lo, acidification. Our findings suggest that lysine supplementation and the reduction of arginine-rich Y.-C.; Sung, P.-W.; Tien, N.; Su, W.-C. -
Amino Acids Amino Acids
Amino Acids Amino Acids What Are Amino Acids? Essential Amino Acids Non Essential Amino Acids Amino acids are the building blocks of proteins; proteins are made of amino acids. Isoleucine Arginine (conditional) When you ingest a protein your body breaks it down into the individual aminos, Leucine Glutamine (conditional) reorders them, re-folds them, and turns them into whatever is needed by the body at Lysine Tyrosine (conditional) that time. From only 20 amino acids, the body is able to make thousands of unique proteins with different functions. Methionine Cysteine (conditional) Phenylalanine Glycine (conditional) Threonine Proline (conditional) Did You Know? Tryptophan Serine (conditional) Valine Ornithine (conditional) There are 20 different types of amino acids that can be combined to make a protein. Each protein consists of 50 to 2,000 amino acids that are connected together in a specific Histidine* Alanine sequence. The sequence of the amino acids determines each protein’s unique structure Asparagine and its specific function in the body. Asparate Popular Amino Acid Supplements How Do They Benefit Our Health? Acetyl L- Carnitine: As part of its role in supporting L-Lysine: L-Lysine, an essential amino acid, is mental function, Acetyl L-Carnitine may help needed to support proper growth and bone Proteins (amino acids) are needed by your body to maintain muscles, bones, blood, as support memory, attention span and mental development. It can also support immune function. well as create enzymes, neurotransmitters and antibodies, as well as transport and performance. store molecules. N-Acetyl Cysteine: N-Acetyl Cysteine (NAC) is a L-Arginine: L-Arginine is a nonessential amino acid form of the amino acid cysteine. -
The Role of Reduced Methionine in Mediating the Metabolic Responses to Protein Restriction Using Different Sources of Protein
nutrients Article The Role of Reduced Methionine in Mediating the Metabolic Responses to Protein Restriction Using Different Sources of Protein Han Fang 1 , Kirsten P. Stone 1 , Sujoy Ghosh 2,3 , Laura A. Forney 4 and Thomas W. Gettys 1,* 1 Laboratory of Nutrient Sensing & Adipocyte Signaling, 6400 Perkins Road, Pennington Biomedical Research Center, Baton Rouge, LA 70808, USA; [email protected] (H.F.); [email protected] (K.P.S.) 2 Laboratory of Computational Biology, Pennington Biomedical Research Center, Baton Rouge, LA 70808, USA; [email protected] 3 Program in Cardiovascular and Metabolic Disorders and Center for Computational Biology, Duke-NUS Medical School, Singapore 169857, Singapore 4 Department of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, 7000 Fannin St, Houston, TX 77030, USA; [email protected] * Correspondence: [email protected] Abstract: Dietary protein restriction and dietary methionine restriction (MR) produce a comparable series of behavioral, physiological, biochemical, and transcriptional responses. Both dietary regimens produce a similar reduction in intake of sulfur amino acids (e.g., methionine and cystine), and both diets increase expression and release of hepatic FGF21. Given that FGF21 is an essential mediator of the metabolic phenotype produced by both diets, an important unresolved question is whether dietary protein restriction represents de facto methionine restriction. Using diets formulated from either casein or soy protein with matched reductions in sulfur amino acids, we compared the ability Citation: Fang, H.; Stone, K.P.; of the respective diets to recapitulate the metabolic phenotype produced by methionine restriction Ghosh, S.; Forney, L.A.; Gettys, T.W. -
Amino Acid Transport Pathways in the Small Intestine of the Neonatal Rat
Pediat. Res. 6: 713-719 (1972) Amino acid neonate intestine transport, amino acid Amino Acid Transport Pathways in the Small Intestine of the Neonatal Rat J. F. FITZGERALD1431, S. REISER, AND P. A. CHRISTIANSEN Departments of Pediatrics, Medicine, and Biochemistry, and Gastrointestinal Research Laboratory, Indiana University School of Medicine and Veterans Administration Hospital, Indianapolis, Indiana, USA Extract The activity of amino acid transport pathways in the small intestine of the 2-day-old rat was investigated. Transport was determined by measuring the uptake of 1 mM con- centrations of various amino acids by intestinal segments after a 5- or 10-min incuba- tion and it was expressed as intracellular accumulation. The neutral amino acid transport pathway was well developed with intracellular accumulation values for leucine, isoleucine, valine, methionine, tryptophan, phenyl- alanine, tyrosine, and alanine ranging from 3.9-5.6 mM/5 min. The intracellular accumulation of the hydroxy-containing neutral amino acids threonine (essential) and serine (nonessential) were 2.7 mM/5 min, a value significantly lower than those of the other neutral amino acids. The accumulation of histidine was also well below the level for the other neutral amino acids (1.9 mM/5 min). The basic amino acid transport pathway was also operational with accumulation values for lysine, arginine and ornithine ranging from 1.7-2.0 mM/5 min. Accumulation of the essential amino acid lysine was not statistically different from that of nonessential ornithine. Ac- cumulation of aspartic and glutamic acid was only 0.24-0.28 mM/5 min indicating a very low activity of the acidic amino acid transport pathway. -
Meat Proteins in Human Nutrition
MEAT P80T€IN'S IN HUMAN NUTRITION J. KASTELIC Before I can begin to discuss the many questions which are implied in the title of this discussion I must beg your forbearance. I must clearly specify that I am appearing before you as a student of protein nutrition and not as an authority. This is not meant to be an apology. It is a statement which is not only pmdeut but entire1.y appropriate. And I must clear a bit of underb-msli amy before I give the su'oject before us specific consideration, ;^or I can be certain none of you came here only to listen to me reiterate the resalts of nitrogen balance studies published in the literature or to look at relmoductions of tables of data and of graphs which describe the results of the many biological value determinations of proteins that have been obt,ained frola laboratory animal experimentation with which so many of you are now familiar. It would be equally superfluous to call attention to the tremendous volume of literature that is now being published about the underlying eco- nomic, social, technological and medical problems which are confronting man in so many parts of the world today where food production is only sufficient to mainkin life. !here we were once so provincially concerned with vitamin defi- ciency diseases, we now appear to be rather singularly concerned about pro- tein malnutrition and how m might best cope with protein malnutrition in the human obliged to subsist on diets composed of protein-deficient foods. If there is still some controversy about the relative merits of proteins from plant and animal sources in 'numan nutrition it must stem from vexing economic considerations, meat animal production capabilities and problems associated with processing and storage; not fmm a lack of an appreciation of the nutritional role and functions of the amino acids which are essential to life. -
Protein and Amino Acid Requirements for Poultry by Todd J
PURDUE EXTENSION Animal Sciences AS-584-W Protein and Amino Acid Requirements for Poultry by Todd J. Applegate - Purdue University Roselina Angel – University of Maryland, College Park Introduction Essential amino acids must be supplied by the diet, This fact sheet has been developed to support the and a sufficient amount of non-essential amino acids implementation of the Natural Resources Conservation must also be supplied to prevent the conversion of Service Feed Management 592 Practice Standard. essential amino acids into non-essential amino acid. The Feed Management 592 Practice Standard was Additionally, if the amino acids supplied are not in adopted by NRCS in 2003 as another tool to assist the proper, or ideal, ratio in relation to the needs of with addressing resource concerns on livestock and the animal, then amino acids in excess of the least poultry operations. Feed management can assist with limiting amino acid will be deaminated and likely used reducing the import of nutrients to the farm and reduce as a source of energy rather than toward body protein the excretion of nutrients in manure. synthesis. This breakdown of amino acids will also Dietary crude protein (CP) requirements are result in higher nitrogenous excretions. somewhat of a misnomer as the requirement is The best way to reduce N in poultry excreta is to based on the amino acids content of the protein. lower the amount of CP that is fed by supplementing Once digested and absorbed, amino acids are used diets with amino acids. Reductions in the non-essential as the building blocks of structural proteins (muscle, amino acid pool, coupled with supplying a more skin, ligaments), metabolic proteins, enzymes, and “ideal” amino acid profile in the diet can substantially precursors of several body components. -
Role and Characteristics of Selected Amino Acid and Peptide Transporters in Epithelial Cells
TECHNISCHE UNIVERSITÄT MÜNCHEN Lehrstuhl für Ernährungsphysiologie Role and characteristics of selected amino acid and peptide transporters in epithelial cells Alexander Georg Nickel Vollständiger Abdruck der von der Fakultät Wissenschaftszentrum Weihenstephan für Ernährung, Landnutzung und Umwelt der Technischen Universität München zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften genehmigten Dissertation. Vorsitzender: Univ.-Prof. Dr. M. Schemann Prüfer der Dissertation: 1. Univ.-Prof. Dr. H. Daniel 2. Univ.-Prof. Dr. Th. F. Hofmann Die Dissertation wurde am 12.05.2009 bei der Technischen Universität München eingereicht und durch die Fakultät Wissenschaftszentrum Weihenstephan für Ernährung, Landnutzung und Umwelt am 01.09.2009 angenommen. A 2 Zum Erfolg braucht der Forscher die vier großen "G": Geist, Geduld, Geld und Glück. Paul Ehrlich 3 Table of contents 1 Characteristics of L-proline transport in OK cells................................................................ 10 1.1 Introduction ............................................................................................................. 10 1.1.1 Physiological importance of amino acids..................................................... 10 1.1.2 Basic principles of amino acid transport...................................................... 10 1.1.3 Amino acid transport in kidney .................................................................... 11 1.1.3.1 Apical amino acid transporters of the kidney proximal tubule ..................... 12 1.1.3.2 -
Metabolism of Methionine in the Newborn Infant: Response to the Parenteral and Enteral Administration of Nutrients
0031-3998/08/6404-0381 Vol. 64, No. 4, 2008 PEDIATRIC RESEARCH Printed in U.S.A. Copyright © 2008 International Pediatric Research Foundation, Inc. Metabolism of Methionine in the Newborn Infant: Response to the Parenteral and Enteral Administration of Nutrients BIJU THOMAS, LOURDES L. GRUCA, CAROLE BENNETT, PRABHU S. PARIMI, RICHARD W. HANSON, AND SATISH C. KALHAN Department of Pediatrics [B.T., P.S.P.], MetroHealth Medical Center, Cleveland, Ohio 44109, Department of Medicine [L.L.G., C.B., R.W.H., S.C.K.], Cleveland Clinic Lerner College of Medicine, Cleveland, Ohio 44195, Department of Biochemistry [R.W.H.], Case Western Reserve University, Cleveland, Ohio 44106 ABSTRACT: The rates of transmethylation and transsulfuration of birth and of nutrient interventions on the transsulfuration of methionine were quantified using [1-13C]methionine and methionine is unknown. 2 [C H3]methionine tracers in newborn infants born at term gestation The synthesis of cysteine from homocysteine and serine is and in prematurely born low birth weight infants. Whole body rate of regulated by an individual’s nutrient state and by the relative 2 protein breakdown was also measured using [ H5]phenylalanine. The concentration of insulin, glucagon and adrenal corticosteroids response to enteral formula feeding and parenteral nutrition was (10–12). Insulin has a repressive effect on hepatic CGL and on examined in full term and prematurely born babies, respectively. The cystathionine  synthase (CBS), whereas glucagon and glu- relative rates of appearance of methionine and phenylalanine were cocorticoids increase the hepatic activity of these enzymes. comparable to the amino acid composition of mixed body proteins. -
L-Tryptophan, the FDA, and the Regulation of Amino Acids Carter Anne Mcgowan
Cornell Journal of Law and Public Policy Volume 3 Article 10 Issue 2 Spring 1994 Learning the Hard Way: L-Tryptophan, the FDA, and the Regulation of Amino Acids Carter Anne McGowan Follow this and additional works at: http://scholarship.law.cornell.edu/cjlpp Part of the Law Commons Recommended Citation McGowan, Carter Anne (1994) "Learning the Hard Way: L-Tryptophan, the FDA, and the Regulation of Amino Acids," Cornell Journal of Law and Public Policy: Vol. 3: Iss. 2, Article 10. Available at: http://scholarship.law.cornell.edu/cjlpp/vol3/iss2/10 This Article is brought to you for free and open access by the Journals at Scholarship@Cornell Law: A Digital Repository. It has been accepted for inclusion in Cornell Journal of Law and Public Policy by an authorized administrator of Scholarship@Cornell Law: A Digital Repository. For more information, please contact [email protected]. LEARNING THE HARD WAY: L-TRYPTOPHAN, THE FDA, AND THE REGULATION OF AMINO ACIDS I sit before you helpless, broke, alone and in unyielding, relentless pain .... For those who have died and for those of us who live with cloudy futures, the lack of action is too little, too late. We have needed help with our orphan dis- ease. We need help now .... The U.S. Government is totally ineffective, and each agonizing day we grow more fragile. For those who appear to be in remission, we rejoice. But we cannot say with certainty that anyone is cured as long as the exact cause and cure is not found. For many of us, it is too late. -
The Diverse Functions of Non-Essential Amino Acids in Cancer
cancers Review The Diverse Functions of Non-Essential Amino Acids in Cancer Bo-Hyun Choi and Jonathan L. Coloff * Department of Physiology and Biophysics, University of Illinois Cancer Center, University of Illinois at Chicago, Chicago, IL 60612, USA; [email protected] * Correspondence: coloff@uic.edu Received: 16 April 2019; Accepted: 10 May 2019; Published: 15 May 2019 Abstract: Far beyond simply being 11 of the 20 amino acids needed for protein synthesis, non-essential amino acids play numerous important roles in tumor metabolism. These diverse functions include providing precursors for the biosynthesis of macromolecules, controlling redox status and antioxidant systems, and serving as substrates for post-translational and epigenetic modifications. This functional diversity has sparked great interest in targeting non-essential amino acid metabolism for cancer therapy and has motivated the development of several therapies that are either already used in the clinic or are currently in clinical trials. In this review, we will discuss the important roles that each of the 11 non-essential amino acids play in cancer, how their metabolic pathways are linked, and how researchers are working to overcome the unique challenges of targeting non-essential amino acid metabolism for cancer therapy. Keywords: aspartate; asparagine; arginine; cysteine; glutamate; glutamine; glycine; proline; serine; cancer 1. Introduction It is now well established that tumors display different metabolic phenotypes than normal tissues [1]. The first observed and most studied metabolic phenotype of tumors is that of increased glucose uptake and glycolysis [2,3], a metabolic phenotype that is exploited in the clinic to image human tumors and metastases via 18flurodeoxyglucose positron emission tomography (18FDG-PET) [4]. -
24Amino Acids, Peptides, and Proteins
WADEMC24_1153-1199hr.qxp 16-12-2008 14:15 Page 1153 CHAPTER COOϪ a -h eli AMINO ACIDS, x ϩ PEPTIDES, AND NH3 PROTEINS Proteins are the most abundant organic molecules 24-1 in animals, playing important roles in all aspects of cell structure and function. Proteins are biopolymers of Introduction 24A-amino acids, so named because the amino group is bonded to the a carbon atom, next to the carbonyl group. The physical and chemical properties of a protein are determined by its constituent amino acids. The individual amino acid subunits are joined by amide linkages called peptide bonds. Figure 24-1 shows the general structure of an a-amino acid and a protein. α carbon atom O H2N CH C OH α-amino group R side chain an α-amino acid O O O O O H2N CH C OH H2N CH C OH H2N CH C OH H2N CH C OH H2N CH C OH CH3 CH2OH H CH2SH CH(CH3)2 alanine serine glycine cysteine valine several individual amino acids peptide bonds O O O O O NH CH C NH CH C NH CH C NH CH C NH CH C CH3 CH2OH H CH2SH CH(CH3)2 a short section of a protein a FIGURE 24-1 Structure of a general protein and its constituent amino acids. The amino acids are joined by amide linkages called peptide bonds. 1153 WADEMC24_1153-1199hr.qxp 16-12-2008 14:15 Page 1154 1154 CHAPTER 24 Amino Acids, Peptides, and Proteins TABLE 24-1 Examples of Protein Functions Class of Protein Example Function of Example structural proteins collagen, keratin strengthen tendons, skin, hair, nails enzymes DNA polymerase replicates and repairs DNA transport proteins hemoglobin transports O2 to the cells contractile proteins actin, myosin cause contraction of muscles protective proteins antibodies complex with foreign proteins hormones insulin regulates glucose metabolism toxins snake venoms incapacitate prey Proteins have an amazing range of structural and catalytic properties as a result of their varying amino acid composition. -
Degradation of Amino Acids
• The catabolism of the amino acids found in proteins involves the removal of α-amino groups, followed by the breakdown of the resulting carbon skeletons. These pathways converge to form seven intermediate products: oxaloacetate, α-ketoglutarate, pyruvate, fumarate, succinyl CoA, acetyl Coa, and acetoacetyl CoA. These products directly enter the pathways of intermediary metabolism, resulting either in the synthesis of glucose or lipid, or in the production of energy through their oxidation to CO2 and water by the citric acid cycle. The figure provides an overview of these pathways, with a more detailed summary presented later. GLUCOGENIC AND KETOGENIC AMINO ACIDS" Amino Acids can be classified as glucogenic or ketogenic based on which of the seven intermediates are produced during their catabolism. Glucogenic amino acids Amino acids whose catabolism yield pyruvate or one of the intermediates of the citric acid cycle are termed glucogenic or glycogenic. These intermediates are substrates for gluconeogenesis and, therefore, can give rise to the net formation of glucose or glycogen in the liver and glycogen in the muscle. Ketogenic amino acids Amino acids whose catabolism yield either acetoacetate or one of its precursor are termed ketogenic. Acetoacetate is one of the “ketone bodies”, which also include 3-hydroxybutyrate and acetone. Leucine and lysine are the only exclusively ketogenic amino acids found in proteins. Their carbon skeletons are not substrates for gluconeogenesis and, therefore, cannot give rise to the net formation of glucose or glycogen in the liver, or glycogen in the muscle. CATABOLISM OF THE CARBON SKELETONS OF AMINO ACIDS The pathways by which amino acids are catabolized, are conveniently organized according to which (or more) of the seven intermediates listed above is produced from a particular amino acid.