Glutamine and Leucine Provide Enhanced Protective Immunity Against Mucosal Infection with Herpes Simplex Virus Type 1

Total Page:16

File Type:pdf, Size:1020Kb

Glutamine and Leucine Provide Enhanced Protective Immunity Against Mucosal Infection with Herpes Simplex Virus Type 1 http://dx.doi.org/10.4110/in.2012.12.5.196 ORIGINAL ARTICLE pISSN 1598-2629 eISSN 2092-6685 Glutamine and Leucine Provide Enhanced Protective Immunity Against Mucosal Infection with Herpes Simplex Virus Type 1 Erdenebileg Uyangaa1, Hern-Ku Lee2 and Seong Kug Eo1* 1College of Veterinary Medicine and Bio-Safety Research Institute, Chonbuk National University, 2Department of Immunology, Chonbuk National University Medical School, Jeonju 561-756, Korea Besides their role as building blocks of protein, there are [Immune Network 2012;12(5):196-206] growing evidences that some amino acids have roles in regu- lating key metabolic pathways that are necessary for main- tenance, growth, reproduction, and immunity. Here, we eval- INTRODUCTION uated the modulatory functions of several amino acids in pro- tective immunity against mucosal infection of herpes simplex There is growing evidence that as well as being the building virus type 1 (HSV-1). We found that glutamine (Gln) and leu- blocks of proteins and polypeptides, some amino acids have cine (Leu) showed enhanced protective immunity to HSV-1 roles in regulating key metabolic pathways that are necessary mucosal infection when two administration of Gln and single for maintenance, growth, reproduction, and immunity (1). administration of Leu per day, but not when administered in combinations. Ameliorated clinical signs of HSV-1 challenged They are called functional amino acids, which include argi- mice by the intraperitoneal administration of Gln and Leu nine (Arg), cystein (Cys), glutamine (Gln), leucine (Leu), pro- were closely associated with viral burden and IFN-γ pro- line (Pro), and tryptophan (Try). Dietary supplementation duction in the vaginal tract at 2 and 4 days post-infection. In with one or a mixture of these amino acids may be beneficial addition, the enhanced production of vaginal IFN-γ appeared for ameliorating health problems at various stages of the life to be caused by NK and HSV-1 antigen-specific Th1-type cycle, and for optimizing the efficiency of metabolic functions CD4+ T cells recruited into vaginal tract of mice treated with to enhance muscle growth, milk production, and athletic per- Gln and Leu, which indicates that IFN-γ, produced by NK formance (1-5). Indeed, microarray analysis indicates that di- and Th1-type CD4+ T cells, may be critical to control the etary supplementation with Gln or Arg increases the ex- outcome of diseases caused by HSV-1 mucosal infection. pression of anti-oxidative genes, and reduces the expression Collectively, our results indicate that intraperitoneal admin- of pro-inflammatory genes in the small intestine and adipose istration of Gln and Leu following HSV-1 mucosal infection tissues (6-8). In addition, some amino acids, such as Gln, Arg, could provide beneficial effects for the modulation of pro- tective immunity, but dosage and frequency of administration and Leu are known to stimulate the phosphorylation of should be carefully considered, because higher frequency mTOR1 in a cell-specific manner, thereby regulating intra- and overdose of Gln and Leu, or their combined treatment, cellular protein turnover (9-12). showed detrimental effects to protective immunity. Protein deficiency has long been known to impair immune Received on August 29, 2012. Revised on September 13, 2012. Accepted on September 14, 2012. CC This is an open access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribu- tion, and reproduction in any medium, provided the original work is properly cited. *Corresponding Author. Tel: 82-63-270-3882; Fax: 82-63-270-3780; E-mail: [email protected] Keywords: Glutamine, Leucine, Mucosal infection, Herpes simplex virus, Protective immunity Abbreviations: Asp, asparagine; Cys, cystein; Gln, glutamine; HSV-1, herpes simplex virus type 1; Arg, arginine; IDO, in- dole amine 2,3-dioxygenase; Leu, leucine; Lys, lysine; Phe, phenylalanine; Pro, proline; Try, tryptophan 196 IMMUNE NETWORK www.immunenetwork.org Volume 12 Number 5 October 2012 Modulation of HSV-1 Protective Immunity by Gln and Leu Erdenebileg Uyangaa, et al. function and increase the susceptibility of animals to disease. and cause mucocutaneous lesion, as manifested in orofacial Some amino acids, including Gln, Arg, methionine (Met), have and genital herpes (32,33). Importantly, HSV-1 is also neuro- been recognized as playing a role in the enhancement of im- tropic viruses, and establish latent infection in neurons, which mune function (13-15). The underlying mechanism may in- can be reservoirs of virus during subsequent events of volve mTOR activation, NO and glutathione synthesis, H2S sig- reactivation. The morbidity and socioeconomic burden asso- naling, and cellular redox state. In particular, catabolism of ciated with genital herpes as well as the alarming relationship Try via indoleamine 2,3-dioxygenase (IDO) appears to be crit- between genital herpes and the increased risk of acquiring ical for functions of both macrophages and lymphocytes (16). a HIV infection emphasize the need for development of an Thus, anthranilic acid (a metabolite of tryptophan via the IDO effective vaccine and/or therapeutics (32,33). Based on the pathway) inhibits production of proinflammatory cytokines accumulated results of biological functions of amino acid, we and prevents autoimmune inflammation (17). Gln is a non-es- evaluated the antiviral effect of several amino acids against sential amino acid which is also considered as an essential mucosal infection of HSV-1 in the present study. We found nutrient during multiple injury, trauma, and tumor (18-22). that Gln and Leu have specific roles in regulating protective Cell culture studies demonstrate that failure to supplement immunity against mucosal infection of HSV-1. culture media with Gln impairs the ability of lymphocytes to respond to mitogenic stimulation (23). In terminally differ- MATERIALS AND METHODS entiated macrophages, Gln may be required for the synthesis of mRNA for producing secretory proteins in immune chal- Mice, cells and viruses lenge during pinocytosis or phagocytosis (24). In addition, Female 5-to 6 week old BALB/c (H-2d) mice were purchased Gln has been shown to be beneficial in the prevention of in- from Samtako (O-San, Korea), and were maintained under fectious morbidity and mortality in seriously ill patients, due standard conditions at the animal facility of Chonbuk National to its ability to maintain the integrity of the intestinal mucosal University, according to the Institutional Guidelines. All ex- epithelium (25). It has also been suggested that Gln influences periments were conducted according to the guidelines of the the growth of immune cells, T helper function and responsive- committee on the Care of Laboratory Animal Resources. ness, and synthesis of immunoglobulin A (IgA) (21,22,26). In HSV-1 McKrae strain was propagated in Vero cells (CCL81, support, inadequate concentrations of Gln have been shown ATCC, Manassas, VA) using DMEM supplemented with 2.5% to compromise lymphocyte proliferation (27), IL-2 and IFN-γ FBS, penicillin (100 U/ml) and streptomycin (100 U/ml). The production (27,28), the expression of surface activation mark- Vero cells were infected with HSV-1 at a multiplicity of in- ers (CD25, CD45RO, and CD71) (28), and lymphokine-acti- fection (MOI) of 0.01, and were incubated in a CO2 incubator vated killer cell activity (29), and to decrease the proportion for 1 h at 37oC with shaking at 15 min intervals. After absorp- of CD4+ lymphocytes and the CD4+/CD8+ ratio (30). Leu, tion, the inoculum was removed, and 5 ml of maintenance one of branched chain amino acids, which also include iso- medium containing 2% was added. Approximately 2∼3 days leucine and valine, is an essential amino acid, and its concen- post-infection, cultures of the host cells showing an 80∼90% tration increases in skeletal muscle but decreases in plasma. cytopathic effect were harvested, and were titrated by con- It was assumed that Leu is a possible regulator of protein ventional plaque assay using Vero cells. The virus stocks turnover in muscle and the perfused liver. Also, Leu stim- were stored in aliquots at −80oC until use. ulates muscle protein synthesis under both in vitro and in vivo experimental conditions (31). The underlying mecha- Vaginal challenge nisms may involve activation of mTOR signaling to enhance The mice were pre-treated with progesterone to synchronize translation initiation and to inhibit autophagy in liver and their estrous cycles, as previously described (34). Briefly, muscle (25). Interestingly, other branched amino acids, iso- mice were subcutaneously injected with Depo-provera (DP) leucine and valine, have no effect on mTOR phosphorylation at 2 mg per mouse. Five days following the injection of DP, or muscle protein turnover (9,10), indicating a structural spe- the mice were challenged intravaginally with 106 pfu of HSV-1 cificity of Leu in cell signaling and function. McKrae strain per mouse, followed by intraperitoneal treat- Herpes simplex virus type 1 (HSV-1) is human pathogenic ment of the indicated amino acid solution daily. The mice viruses, which can replicate in cells of the epithelial lineage, were examined daily for vaginal inflammation, neurological IMMUNE NETWORK www.immunenetwork.org Volume 12 Number 5 October 2012 197 Modulation of HSV-1 Protective Immunity by Gln and Leu Erdenebileg Uyangaa, et al. illness, and
Recommended publications
  • Effects of Single Amino Acid Deficiency on Mrna Translation Are Markedly
    www.nature.com/scientificreports OPEN Efects of single amino acid defciency on mRNA translation are markedly diferent for methionine Received: 12 December 2016 Accepted: 4 May 2018 versus leucine Published: xx xx xxxx Kevin M. Mazor, Leiming Dong, Yuanhui Mao, Robert V. Swanda, Shu-Bing Qian & Martha H. Stipanuk Although amino acids are known regulators of translation, the unique contributions of specifc amino acids are not well understood. We compared efects of culturing HEK293T cells in medium lacking either leucine, methionine, histidine, or arginine on eIF2 and 4EBP1 phosphorylation and measures of mRNA translation. Methionine starvation caused the most drastic decrease in translation as assessed by polysome formation, ribosome profling, and a measure of protein synthesis (puromycin-labeled polypeptides) but had no signifcant efect on eIF2 phosphorylation, 4EBP1 hyperphosphorylation or 4EBP1 binding to eIF4E. Leucine starvation suppressed polysome formation and was the only tested condition that caused a signifcant decrease in 4EBP1 phosphorylation or increase in 4EBP1 binding to eIF4E, but efects of leucine starvation were not replicated by overexpressing nonphosphorylatable 4EBP1. This suggests the binding of 4EBP1 to eIF4E may not by itself explain the suppression of mRNA translation under conditions of leucine starvation. Ribosome profling suggested that leucine deprivation may primarily inhibit ribosome loading, whereas methionine deprivation may primarily impair start site recognition. These data underscore our lack of a full
    [Show full text]
  • Electrochemical Studies of Dl-Leucine, L-Proline and L
    ELECTROCHEMICAL STUDIES OF DL -LEUCINE, 60 L-PROLINE AND L-TRYPTOPHAN AND THEIR INTERACTION WITH COPPER AND IRON 30 c b A) M. A. Jabbar, R. J. Mannan, S. Salauddin and B. µ a Rashid 0 Department of Chemistry, University of Dhaka, ( Current Dhaka-1000, Bangladesh -30 Introduction -60 In vitro study of the charge transfer reactions coupled -800 -400 0 400 800 with chemical reactions can give important indication of Potential vs. Ag/AgCl (mV) about actual biological processes occurring in human Fig.1. Comparison of the cyclic voltammogram of system. Understanding of such charge-transfer 5.0mM (a) DL -Leucine, (b) Cu-DL -Leucine ion and mechanism will help to determine the effectiveness of (c) [Fe-DL -Leucine] in 0.1M KCl solution at a Pt- nutrition, metabolism and treatment of various biological button electrode. Scan rates 50 mV/s. disorders. In the previous research, the redox behaviour of 40 various amino acids and biochemically important compounds and their charge transfer reaction and their b interaction of metal ions were studied [1,2]. In the present 20 ) a c research, the redox behavior and the charge transfer µΑ kinetics of DL -Leucine, L-Proline and L-Tryptophan in 0 the presence and absence of copper and iron will be investigated. Current ( -20 Experimental A computerized electrochemistry system developed by -40 -800 -400 0 400 800 Advanced Analytics, Virginia, USA, (Model-2040) Potential vs. Ag/AgCl (mV) consisting of three electrodes micro-cell with a saturated Ag/AgCl reference, a Pt-wire auxiliary and a pretreated Fig.2 . Comparison of the cyclic voltammogram of Pt-button working electrode is employed to investigate 5.0mM (a) L-Proline, (b) Cu-L-Proline and (c) Fe-L- Proline in 0.1M KCl solution at a Pt-button different amino acids and metal-amino acid systems.
    [Show full text]
  • Amino Acid Chemistry
    Handout 4 Amino Acid and Protein Chemistry ANSC 619 PHYSIOLOGICAL CHEMISTRY OF LIVESTOCK SPECIES Amino Acid Chemistry I. Chemistry of amino acids A. General amino acid structure + HN3- 1. All amino acids are carboxylic acids, i.e., they have a –COOH group at the #1 carbon. 2. All amino acids contain an amino group at the #2 carbon (may amino acids have a second amino group). 3. All amino acids are zwitterions – they contain both positive and negative charges at physiological pH. II. Essential and nonessential amino acids A. Nonessential amino acids: can make the carbon skeleton 1. From glycolysis. 2. From the TCA cycle. B. Nonessential if it can be made from an essential amino acid. 1. Amino acid "sparing". 2. May still be essential under some conditions. C. Essential amino acids 1. Branched chain amino acids (isoleucine, leucine and valine) 2. Lysine 3. Methionine 4. Phenyalanine 5. Threonine 6. Tryptophan 1 Handout 4 Amino Acid and Protein Chemistry D. Essential during rapid growth or for optimal health 1. Arginine 2. Histidine E. Nonessential amino acids 1. Alanine (from pyruvate) 2. Aspartate, asparagine (from oxaloacetate) 3. Cysteine (from serine and methionine) 4. Glutamate, glutamine (from α-ketoglutarate) 5. Glycine (from serine) 6. Proline (from glutamate) 7. Serine (from 3-phosphoglycerate) 8. Tyrosine (from phenylalanine) E. Nonessential and not required for protein synthesis 1. Hydroxyproline (made postranslationally from proline) 2. Hydroxylysine (made postranslationally from lysine) III. Acidic, basic, polar, and hydrophobic amino acids A. Acidic amino acids: amino acids that can donate a hydrogen ion (proton) and thereby decrease pH in an aqueous solution 1.
    [Show full text]
  • Nucleotide Base Coding and Am1ino Acid Replacemients in Proteins* by Emil L
    VOL. 48, 1962 BIOCHEMISTRY: E. L. SAIITH 677 18 Britten, R. J., and R. B. Roberts, Science, 131, 32 (1960). '9 Crestfield, A. M., K. C. Smith, and F. WV. Allen, J. Biol. Chem., 216, 185 (1955). 20 Gamow, G., Nature, 173, 318 (1954). 21 Brenner, S., these PROCEEDINGS, 43, 687 (1957). 22 Nirenberg, M. WV., J. H. Matthaei, and 0. WV. Jones, unpublished data. 23 Crick, F. H. C., L. Barnett, S. Brenner, and R. J. Watts-Tobin, Nature, 192, 1227 (1961). 24 Levene, P. A., and R. S. Tipson, J. Biol. Ch-nn., 111, 313 (1935). 25 Gierer, A., and K. W. Mundry, Nature, 182, 1437 (1958). 2' Tsugita, A., and H. Fraenkel-Conrat, J. Mllot. Biol., in press. 27 Tsugita, A., and H. Fraenkel-Conrat, personal communication. 28 Wittmann, H. G., Naturwissenschaften, 48, 729 (1961). 29 Freese, E., in Structure and Function of Genetic Elements, Brookhaven Symposia in Biology, no. 12 (1959), p. 63. NUCLEOTIDE BASE CODING AND AM1INO ACID REPLACEMIENTS IN PROTEINS* BY EMIL L. SMITHt LABORATORY FOR STUDY OF HEREDITARY AND METABOLIC DISORDERS AND THE DEPARTMENTS OF BIOLOGICAL CHEMISTRY AND MEDICINE, UNIVERSITY OF UTAH COLLEGE OF MEDICINE Communicated by Severo Ochoa, February 14, 1962 The problem of which bases of messenger or template RNA' specify the coding of amino acids in proteins has been largely elucidated by the use of synthetic polyri- bonucleotides.2-7 For these triplet nucleotide compositions (Table 1), it is of in- terest to examine some of the presently known cases of amino acid substitutions in polypeptides or proteins of known structure.
    [Show full text]
  • 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.
    [Show full text]
  • Leucine Meal Increases Glutamine and Total Nitrogen Release from Forearm Muscle
    Leucine meal increases glutamine and total nitrogen release from forearm muscle. T T Aoki, … , G F Fitzpatrick, D C Knight J Clin Invest. 1981;68(6):1522-1528. https://doi.org/10.1172/JCI110406. Research Article To assess the consequences of elevated branched chain amino acid levels on alanine, glutamine, and ammonia metabolism in muscle, L-leucine meals (14.7 g) were consumed by six normal postabsorptive individuals. Bilateral forearm studies were performed, and the dominant arm was subjected to 15 min of light exercise, using a calibrated dynamometer, beginning 45 min after the ingestion of the meal. Large uptakes of leucine were seen across both forearm muscle beds within 30 min of the meal. After exercise, blood flow in the dominant arm increased from 3.1 +/- 0.4 to 5.2 +/- 0.9 ml/100 ml forearm per minute (mean +/- SEM, P less than 0.005). Glutamine flux out of the dominant forearm increased threefold after the ingestion of the leucine meal and increased eightfold over base line after exercise. Less marked changes (significant only at 90 min) in the nonexercised, nondominant arm were also seen. Alanine flux out of the dominant forearm muscle bed increased modestly at 75 and 90 min. No significant change in ammonia flux across either forearm muscle bed was noted. Unexpectedly, large and significant net nitrogen loss from both forearm muscle beds was documented. Thus, following the ingestion of a leucine meal and light exercise, the primary means by which excess nitrogen is routed out of muscle is via glutamine formation and release with alanine […] Find the latest version: https://jci.me/110406/pdf Leucine Meal Increases Glutamine and Total Nitrogen Release from Forearm Muscle THOMAS T.
    [Show full text]
  • Amino Acid Degradation
    BI/CH 422/622 OUTLINE: OUTLINE: Protein Degradation (Catabolism) Digestion Amino-Acid Degradation Inside of cells Protein turnover Dealing with the carbon Ubiquitin Fates of the 29 Activation-E1 Seven Families Conjugation-E2 nitrogen atoms in 20 1. ADENQ Ligation-E3 AA: Proteosome 2. RPH 9 ammonia oxidase Amino-Acid Degradation 18 transamination Ammonia 2 urea one-carbon metabolism free transamination-mechanism to know THF Urea Cycle – dealing with the nitrogen SAM 5 Steps Carbamoyl-phosphate synthetase 3. GSC Ornithine transcarbamylase PLP uses Arginino-succinate synthetase Arginino-succinase 4. MT – one carbon metabolism Arginase 5. FY – oxidase vs oxygenase Energetics Urea Bi-cycle 6. KW – Urea Cycle – dealing with the nitrogen 7. BCAA – VIL Feeding the Urea Cycle Glucose-Alanine Cycle Convergence with Fatty acid-odd chain Free Ammonia Overview Glutamine Glutamate dehydrogenase Overall energetics Amino Acid A. Concepts 1. ConvergentDegradation 2. ketogenic/glucogenic 3. Reactions seen before The SEVEN (7) Families B. Transaminase (A,D,E) / Deaminase (Q,N) Family C. Related to biosynthesis (R,P,H; C,G,S; M,T) 1.Glu Family a. Introduce oxidases/oxygenases b. Introduce one-carbon metabolism (1C) 2.Pyruvate Family a. PLP reactions 3. a-Ketobutyric Family (M,T) a. 1-C metabolism D. Dedicated 1. Aromatic Family (F,Y) a. oxidases/oxygenases 2. a-Ketoadipic Family (K,W) 3. Branched-chain Family (V,I,L) E. Convergence with Fatty Acids: propionyl-CoA 29 N 1 Amino Acid Degradation • Intermediates of the central metabolic pathway • Some amino acids result in more than one intermediate. • Ketogenic amino acids can be converted to ketone bodies.
    [Show full text]
  • Histidine: a Systematic Review on Metabolism and Physiological Effects in Human and Different Animal Species
    nutrients Review Histidine: A Systematic Review on Metabolism and Physiological Effects in Human and Different Animal Species Joanna Moro 1, Daniel Tomé 1, Philippe Schmidely 2, Tristan-Chalvon Demersay 3 and Dalila Azzout-Marniche 1,* 1 AgroParisTech, Université Paris-Saclay, INRAE, UMR PNCA, 75005 Paris, France; [email protected] (J.M.); [email protected] (D.T.) 2 AgroParisTech, Université Paris-Saclay, INRAE, UMR0791 Mosar, 75005 Paris, France; [email protected] 3 Ajinomoto Animal Nutrition Europe, 75017 Paris, France; [email protected] * Correspondence: [email protected]; Tel.: +33-1-44087244 Received: 1 April 2020; Accepted: 8 May 2020; Published: 14 May 2020 Abstract: Histidine is an essential amino acid (EAA) in mammals, fish, and poultry. We aim to give an overview of the metabolism and physiological effects of histidine in humans and different animal species through a systematic review following the guidelines of PRISMA (Preferred Reporting Items for Systematic Reviews and Meta-Analyses). In humans, dietary histidine may be associated with factors that improve metabolic syndrome and has an effect on ion absorption. In rats, histidine supplementation increases food intake. It also provides neuroprotection at an early stage and could protect against epileptic seizures. In chickens, histidine is particularly important as a limiting factor for carnosine synthesis, which has strong anti-oxidant effects. In fish, dietary histidine may be one of the most important factors in preventing cataracts. In ruminants, histidine is a limiting factor for milk protein synthesis and could be the first limiting AA for growth. In excess, histidine supplementation can be responsible for eating and memory disorders in humans and can induce growth retardation and metabolic dysfunction in most species.
    [Show full text]
  • Plasma Concentrations and Intakes of Amino Acids in Male Meat-Eaters, fish-Eaters, Vegetarians and Vegans: a Cross-Sectional Analysis in the EPIC-Oxford Cohort
    European Journal of Clinical Nutrition (2016) 70, 306–312 OPEN © 2016 Macmillan Publishers Limited All rights reserved 0954-3007/16 www.nature.com/ejcn ORIGINAL ARTICLE Plasma concentrations and intakes of amino acids in male meat-eaters, fish-eaters, vegetarians and vegans: a cross-sectional analysis in the EPIC-Oxford cohort JA Schmidt1, S Rinaldi2, A Scalbert2, P Ferrari2, D Achaintre2, MJ Gunter3, PN Appleby1, TJ Key1 and RC Travis1 BACKGROUND/OBJECTIVES: We aimed to investigate the differences in plasma concentrations and in intakes of amino acids between male meat-eaters, fish-eaters, vegetarians and vegans in the Oxford arm of the European Prospective Investigation into Cancer and Nutrition. SUBJECTS/METHODS: This cross-sectional analysis included 392 men, aged 30–49 years. Plasma amino acid concentrations were measured with a targeted metabolomic approach using mass spectrometry, and dietary intake was assessed using a food frequency questionnaire. Differences between diet groups in mean plasma concentrations and intakes of amino acids were examined using analysis of variance, controlling for potential confounding factors and multiple testing. RESULTS: In plasma, concentrations of 6 out of 21 amino acids varied significantly by diet group, with differences of − 13% to +16% between meat-eaters and vegans. Concentrations of methionine, tryptophan and tyrosine were highest in fish-eaters and vegetarians, followed by meat-eaters, and lowest in vegans. A broadly similar pattern was seen for lysine, whereas alanine concentration was highest in fish-eaters and lowest in meat-eaters. For glycine, vegans had the highest concentration and meat-eaters the lowest. Intakes of all 18 dietary amino acids differed by diet group; for the majority of these, intake was highest in meat-eaters followed by fish-eaters, then vegetarians and lowest in vegans (up to 47% lower than in meat-eaters).
    [Show full text]
  • Structure and Functions of Amino Acids and Proteins
    Structure of Amino Acids DR. KIRAN MEENA 05/9/2019 8:00-9:00 AM Specific Learning Objectives 1. General Structure of amino acids 2. Amino acids classification based on: •Standard and Non-standard amino acids (aa) •Essential and non-essential aa •Ketogenic and Glucogenic aa •Side chain functional group 3. Function of essential amino acids Introduction •Amino acids as a building blocks of peptides and proteins •Proteins are made up of hundreds of smaller units called amino acids that are attached to one another by peptide bonds, forming a long chain. •Protein as a string of beads where each bead is an amino acid. www.khanacademy.org Genetic Code Specifies 20 L-α-Amino Acids •Proteins are synthesized from the set of 20 L-α-amino acids encoded by nucleotide triplets called codons. •Common amino acids are those for which at least one specific codon exists in the DNA genetic code. •Sequences of peptides and proteins represent by using one- and three letter abbreviations for each amino acid. Genetic information is transcribed from a DNA sequence into mRNA and then translated to amino acid sequence of a protein Fig. 2.1. Textbook of Biochemistry with Clinical Correlations, 4th edition by Thomas M Devlin General Structure of Common Amino Acids •General structure of amino acids , group and a variable side chain •Side chain determines: protein folding, binding to specific ligand and interaction with its environment •Amino acids consists of a constant COOH (R is side chain) + - •At neutral pH, H2N- protonated to H3N -, and –COOH deprotonated to –COO Fig.4.2.
    [Show full text]
  • Chain Amino Acids in Pseudomonas Aeruginosa
    JOUtNAL OF BACTERIOLOGY, Mar. 1980, p. 1055-1063 Vol. 141, No. 3 0021-9193/80/03-1055/09$02.00/0 Purification and Properties of a Binding Protein for Branched- Chain Amino Acids in Pseudomonas aeruginosa TOSHIMITSU HOSHINO* AND MAKOTO KAGEYAMA Mitsubishi-Kasei Institute ofLife Sciences, Machida-shi, Tokyo 194, Japan A binding protein for branched-chain amino acids was purified to a homoge- neous state from shock fluid of Pseudomonas aeruginosa PML14. It was a monomeric protein with an apparent molecular weight of4.3 x 10' or 4.0 x 10' by sodium dodecyl sulfate-polyacrylamide gel electrophoresis or gel filtration, re- spectively. The isoelectric point was determined to be pH 4.1 by electrofocusing. Amino acid analysis of the protein showed that aspartic acid, glutamic acid, glycine, and alanine were major components and that the protein contained only one residue each of tryptophan and cysteine per molecule. The binding protein contained no sugar. The binding activity of the protein was specific for the branched-chain amino acids. The protein also bound alanine and threonine with lower affinity. The dissociation constants of this protein for leucine, isoleucine, and valine were found to be 0.4, 0.3, and 0.5 !M, respectively. Mutants defective in the production of the binding protein were identified among the mutants deficient in a transport system for branched-chain amino acids (LIV-I). The revertants from these mutants to LIV-I-positive phenotype simultaneously re- covered normal levels of the binding protein. These findings suggest strongly the association of the binding protein with the LIV-I transport system.
    [Show full text]
  • 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.
    [Show full text]