The Antioxidant Effect of Beta-Alanine Or Carnosine Supplementation on Exercise
Total Page:16
File Type:pdf, Size:1020Kb

Load more
Recommended publications
-
Insights Into the Molecular Basis for Substrate Binding and Specificity of the Wild-Type L-Arginine/Agmatine Antiporter Adic
Insights into the molecular basis for substrate binding and specificity of the wild-type L-arginine/agmatine antiporter AdiC Hüseyin Ilgüa,b,1, Jean-Marc Jeckelmanna,b,1, Vytautas Gapsysc, Zöhre Ucuruma,b, Bert L. de Grootc, and Dimitrios Fotiadisa,b,2 aInstitute of Biochemistry and Molecular Medicine, University of Bern, CH-3012 Bern, Switzerland; bSwiss National Centre of Competence in Research TransCure, University of Bern, CH-3012 Bern, Switzerland; and cComputational Biomolecular Dynamics Group, Max-Planck-Institute for Biophysical Chemistry, D-37077 Goettingen, Germany Edited by Christopher Miller, Howard Hughes Medical Institute, Brandeis University, Waltham, MA, and approved July 26, 2016 (received for review April 4, 2016) Pathogenic enterobacteria need to survive the extreme acidity of Arg-bound states (10). The two outward-open, substrate-free the stomach to successfully colonize the human gut. Enteric bacteria structures are at the reasonable and moderate resolutions of 3.2 Å circumvent the gastric acid barrier by activating extreme acid- (8) and 3.6 Å (9), respectively, and the only ones available of wild- resistance responses, such as the arginine-dependent acid resistance type AdiC (AdiC-wt). The two other structures are with bound system. In this response, L-arginine is decarboxylated to agmatine, Arg and at 3-Å resolution, and could only be obtained as a result thereby consuming one proton from the cytoplasm. In Escherichia of the introduction of specific point mutations: AdiC-N22A (10) coli,theL-arginine/agmatine antiporter AdiC facilitates the export and AdiC-N101A (11). The N101A mutation results in a defective of agmatine in exchange of L-arginine, thus providing substrates for AdiC protein unable to bind Arg and with a dramatically de- further removal of protons from the cytoplasm and balancing the creased turnover rate compared with wild-type (11). -
Separation of Isomers <Emphasis Type="Italic">L </Emphasis>-Alanine and Sarcosine in Urine by Electrospra
SHORT COMMUNICATION Separation of Isomers L-Alanine and Sarcosine in Urine by Electrospray Ionization and Tandem Differential Mobility Analysis-Mass Spectrometry Pablo Martínez-Lozanoa and Juan Rusb a Institute for Biomedical Technologies-National Research Council, Milan, Italy b SEADM, Valladolid, Spain Sarcosine, an isomer of L-alanine, has been proposed as a prostate cancer progression biomarker [1]. Both compounds are detected in urine, where the measured sarcosine/alanine ratio has been found to be higher in prostate biopsy-positive group versus controls. We present here preliminary evidence showing that urine samples spiked with sarcosine/alanine can be partially resolved in 3 min via tandem differential mobility analysis-mass spectrometry (DMA-MS). Based on the calibration curves obtained for two mobility peaks, we finally estimate their concentration ratio in urine. (J Am Soc Mass Spectrom 2010, 21, 1129–1132) © 2010 American Society for Mass Spectrometry rostate cancer is a leading cause of death among the tive-ion mode at the DMA entrance slit. Our nanospray male population. Sarcosine, an isomer of alanine, parameters were: capillary 360 m o.d., 50 m i.d., length Pwas recently proposed as a prostate cancer progres- 22 cm, driving pressure 75 mbar, and 3.8 kV. The ions sion biomarker [1]. In particular, the sarcosine/alanine entered the separation region propelled by an electric field ratio was found to be significantly higher in urine derived and against a counterflow gas (0.2 L/min). Sheath gas from biopsy-positive prostate cancer patients compared flow was kept constant, and the classification voltage was with biopsy-negative controls. -
Beta Alanine
PERFORMANCE ENHANCERS FACTS AND BOTTOM LINE BETA ALANINE What is it? B-alanine is a naturally occurring amino acid (a non-essential amino acid) not used by the body to make muscle tissue. Rather, research has shown that B-alanine works by increasing the muscle content of an important compound – carnosine. In fact, the production of carnosine is limited by the availability of B-alanine. Carnosine is highly concentrated in muscle tissue where its role is primarily to soak up hydrogen ions. Does it work? B-alanine is one of the few dietary supplements that actually have good scientific evidence that it can possibly enhance performance. How does it work? When you exercise intensely the body produces hydrogen ions. The longer you exercise the more hydrogen ions you produce and this reduces the pH level in your muscles. Muscles work best in a very specific pH range and when the pH drops below that level then muscular performance also starts to decrease. Anything that helps to prevent or delay that drop in pH will help delay muscle fatigue. This is where B-alanine has proven to be very helpful. Beta-alanine increases the levels of carnosine in your slow and fast twitch muscle fibers and carnosine is a buffer that basically soaks up hydrogen ions and so reduces the drop in pH. By keeping your hydrogen ion levels lower, B-alanine allows you to train harder and longer. The bottom line is that B-alanine works by increasing the hydrogen ion buffering abilities of your muscles. What benefits does it offer? B-alanine has been shown to increase muscle strength, increase muscle mass, increase anaerobic endurance, increase aerobic endurance and increase exercise capacity. -
Mechanistic Insights on the Reduction of Glutathione Disulfide by Protein Disulfide Isomerase
Mechanistic insights on the reduction of glutathione disulfide by protein disulfide isomerase Rui P. P. Nevesa, Pedro Alexandrino Fernandesa, and Maria João Ramosa,1 aUnidade de Ciências Biomoleculares Aplicadas, Rede de Química e Tecnologia, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, 4169-007 Porto, Portugal Edited by Donald G. Truhlar, University of Minnesota, Minneapolis, MN, and approved May 9, 2017 (received for review November 22, 2016) We explore the enzymatic mechanism of the reduction of glutathione of enzymes, which are responsible for the reduction and isomer- disulfide (GSSG) by the reduced a domain of human protein disulfide ization of disulfide bonds, through thiol-disulfide exchange. isomerase (hPDI) with atomistic resolution. We use classical molecular dynamics and hybrid quantum mechanics/molecular mechanics cal- Structure and Function of PDI culations at the mPW1N/6–311+G(2d,2p):FF99SB//mPW1N/6–31G(d): Human protein disulfide isomerase (hPDI) is a U-shaped enzyme FF99SB level. The reaction proceeds in two stages: (i) a thiol-disulfide with 508 residues. Its tertiary structure is composed of four exchange through nucleophilic attack of the Cys53-thiolate to the thioredoxin-like domains (a, b, b′,anda′) and a fifth tail-shaped c GSSG-disulfide followed by the deprotonation of Cys56-thiol by domain (Fig. 1) (14, 15). The maximum activity of hPDI is observed Glu47-carboxylate and (ii) a second thiol-disulfide exchange between when all domains of PDI contribute synergistically to its function (16). the Cys56-thiolate and the mixed disulfide intermediate formed in Similar to thioredoxin, the a and a′ domains have a catalytic the first step. -
Degradation of Glutathione in Plant Cells
Degradation of Glutathione in Plant Cells: Evidence against the Participation of a y-Glutamyltranspeptidase Reinhard Steinkamp and Heinz Rennenberg Botanisches Institut der Universität zu Köln, Gyrhofstr. 15, D-5000 Köln 41, Bundesrepublik Deutschland Z. Naturforsch. 40c, 29 — 33 (1985); received August 31/October 4, 1984 Tobacco, Glutathione Catabolism, y-Glutamylcysteine, y-Glutamyltranspeptidase, y-Glutamyl- cyclotransferase When y-glutamyltranspeptidase activity in tobacco cells was measured using the artificial substrate y-glutamyl-/?-nitroanilide, liberation of p-nitroaniline was not reduced, but stimulated by addition of glutathione. Therefore, glutathione was not acting as a donator, but as an acceptor of y-glutamyl moieties in the assay mixture, suggesting that y-glutamyltranspeptidase is not participating in degradation of glutathione. Feeding experiments with [^S-cysJglutathione sup ported this conclusion. When tobacco cells were supplied with this peptide as sole sulfur source, glutathione and y-glutamylcysteine were the only labelled compounds found inside the cells. The low rate of uptake of glutathione apparently prevented the accumulation of measurable amounts of radioactivity in the cysteine pool. A y-glutamylcyclotransferase, responsible for the conversion of y-glutamylcysteine to 5-oxo-proline and cysteine was found in ammonium sulfate precipitates of tobacco cell homogenates. The enzyme showed high activities with y-glutamylmethionine and y-glutamylcysteine, but not with other y-glutamyldipeptides or glutathione. From these and previously published experiments [(Rennenberg et al., Z. Naturforsch. 3 5 c, 70 8 -7 1 1 (1980)], it is concluded that glutathione is degraded in tobacco cells via the following pathway: y-glu-cys- gly —> y-glu-cys ->• 5-oxo-proline -* glu. Introduction the cysteine conjugate by the action of a y-gluta myltranspeptidase (Fig. -
Poly(L-Alanine) As a Universal Reference Material for Understanding Protein Energies and Structures TERESA HEAD-GORDON, FRANK H
Proc. Nati. Acad. Sci. USA Vol. 89, pp. 11513-11517, December 1992 Biophysics Poly(L-alanine) as a universal reference material for understanding protein energies and structures TERESA HEAD-GORDON, FRANK H. STILLINGER, MARGARET H. WRIGHT, AND DAVID M. GAY AT&T Bell Laboratories, Murray Hill, NJ 07974 Contributed by Frank H. Stillinger, June 17, 1992 ABSTRACT We present a proposition, the "poly(L- alanine) hypothesis," which asserts that the native backbone geometry for any polypeptide or protein of M residues has a closely mimicking, mechanically stable, image in poly(L- POLY-L-ALANINE alanine) of the same number of residues. Using a molecular co mechanics force field to represent the relevant potential energy a: hypersurfaces, we have carried out calculations over a wide z range of M values to show that poly(L-alanine) possesses the w structural versatility necessary to satisfy the proposition. These w include poly(L-alanine) representatives of minima correspond- U- ing to secondary and supersecondary structures, as well as PROTEIN poly(L-alanine) images for tertiary structures of the naturally occurring proteins bovine pancreatic trypsin inhibitor, crambin, ribonuclease A, and superoxide dismutase. The suc- cessful validation of the hypothesis presented in this paper BACKBONE COORDINATES indicates that poly(L-alanine) will serve as a good reference FIG. 1. Topographic basis ofthe poly(L-alanine) hypothesis. Free material in thermodynamic perturbation theory and calcula- energy hypersurfaces are compared for a given protein and for tions aimed at evaluating relative free energies for competing poly(L-alanine) with the same number of residues. candidate tertiary structures in real polypeptides and proteins. -
Alcohol Use Disorder
Section: A B C D E Resources References Alcohol Use Disorder (AUD) Tool This tool is designed to support primary care providers (family physicians and primary care nurse practitioners) in screening, diagnosing and implementing pharmacotherapy treatments for adult patients (>18 years) with Alcohol Use Disorder (AUD). Primary care providers should routinely offer medication for moderate and severe AUD. Pharmacotherapy alone to treat AUD is better than no therapy at all.1 Pharmacotherapy is most effective when combined with non-pharmacotherapy, including behavioural therapy, community reinforcement, motivational enhancement, counselling and/or support groups. 2,3 TABLE OF CONTENTS pg. 1 Section A: Screening for AUD pg. 7 Section D: Non-Pharmacotherapy Options pg. 4 Section B: Diagnosing AUD pg. 8 Section E: Alcohol Withdrawal pg. 5 Section C: Pharmacotherapy Options pg. 9 Resources SECTION A: Screening for AUD All patients should be screened routinely (e.g. annually or when indicators are observed) with a recommended tool like the AUDIT. 2,3 It is important to screen all patients and not just patients eliciting an index of suspicion for AUD, since most persons with AUD are not recognized. 4 Consider screening for AUD when any of the following indicators are observed: • After a recent motor vehicle accident • High blood pressure • Liver disease • Frequent work avoidance (off work slips) • Cardiac arrhythmia • Chronic pain • Rosacea • Insomnia • Social problems • Rhinophyma • Exacerbation of sleep apnea • Legal problems Special Patient Populations A few studies have reviewed AUD in specific patient populations, including youth, older adults and pregnant or breastfeeding patients. The AUDIT screening tool considered these populations in determining the sensitivity of the tool. -
Sulfhydryl Reduction of Methylene Blue with Reference to Alterations in Malignant Neoplastic Disease
Sulfhydryl Reduction of Methylene Blue With Reference to Alterations in Malignant Neoplastic Disease Maurice M. Black, M. D. (From the Department of Biochemistry, New York Medical College, New York 29, N. t;., and the Brooklyn Cancer Institute, Brooklyn 9, N. Y.) (Received for publication May 8, 1947) A significant decrease in methylene blue re- reactivity is less than half that of the cysteine. It is ducing power of plasma from patients with malig- noteworthy also that the resultant leuco mixture nant neoplastic disease was previously reported did not revert back to colored methylene blue on (1). At that time it was suggested that change in a cooling, as was the case with methylene blue re- reducing group of the albumin molecule was a duction by plasma. likely source of this alteration. Similar conclusions Similar relationships were investigated between were reported also by Savignac and associates (7) cysteine and different concentrations of methylene as the result of analogous studies. blue. As seen in Fig. 2, similar curves are obtained, In an attempt to evaluate the effect of the sulf- but the position of the curve on the graph varies hydryl group on the reduction of methylene blue, a with the concentration of the methylene blue used. study was undertaken with various compounds of It should be noted that there is no appreciable known -SH and S-S structures. In addition, an difference in the reducing time of methylene blue attempt was made to establish a standard method on varying the concentrations between 0.10 per of calibration of various lots of methylene blue, so cent and 0.2 per cent, although 0.08 per cent shows that more uniform results would be possible in the a decided difference. -
A Review of Dietary (Phyto)Nutrients for Glutathione Support
nutrients Review A Review of Dietary (Phyto)Nutrients for Glutathione Support Deanna M. Minich 1,* and Benjamin I. Brown 2 1 Human Nutrition and Functional Medicine Graduate Program, University of Western States, 2900 NE 132nd Ave, Portland, OR 97230, USA 2 BCNH College of Nutrition and Health, 116–118 Finchley Road, London NW3 5HT, UK * Correspondence: [email protected] Received: 8 July 2019; Accepted: 23 August 2019; Published: 3 September 2019 Abstract: Glutathione is a tripeptide that plays a pivotal role in critical physiological processes resulting in effects relevant to diverse disease pathophysiology such as maintenance of redox balance, reduction of oxidative stress, enhancement of metabolic detoxification, and regulation of immune system function. The diverse roles of glutathione in physiology are relevant to a considerable body of evidence suggesting that glutathione status may be an important biomarker and treatment target in various chronic, age-related diseases. Yet, proper personalized balance in the individual is key as well as a better understanding of antioxidants and redox balance. Optimizing glutathione levels has been proposed as a strategy for health promotion and disease prevention, although clear, causal relationships between glutathione status and disease risk or treatment remain to be clarified. Nonetheless, human clinical research suggests that nutritional interventions, including amino acids, vitamins, minerals, phytochemicals, and foods can have important effects on circulating glutathione which may translate to clinical benefit. Importantly, genetic variation is a modifier of glutathione status and influences response to nutritional factors that impact glutathione levels. This narrative review explores clinical evidence for nutritional strategies that could be used to improve glutathione status. -
Muscle Wasting and Aging: Experimental Models, Fatty Infiltrations, and Prevention Thomas Brioche, Allan Pagano, Guillaume Py, Angèle Chopard
Muscle wasting and aging: Experimental models, fatty infiltrations, and prevention Thomas Brioche, Allan Pagano, Guillaume Py, Angèle Chopard To cite this version: Thomas Brioche, Allan Pagano, Guillaume Py, Angèle Chopard. Muscle wasting and aging: Experi- mental models, fatty infiltrations, and prevention. Molecular Aspects of Medicine, Elsevier, 2016,32 p. 10.1016/j.mam.2016.04.006. hal-01837630 HAL Id: hal-01837630 https://hal.archives-ouvertes.fr/hal-01837630 Submitted on 28 May 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution - ShareAlike| 4.0 International License Accepted Manuscript Title: Muscle wasting and aging: experimental models, fatty infiltrations, and prevention Author: Thomas Brioche, Allan F. Pagano, Guillaume Py, Angèle Chopard PII: S0098-2997(15)30021-2 DOI: http://dx.doi.org/doi: 10.1016/j.mam.2016.04.006 Reference: JMAM 642 To appear in: Molecular Aspects of Medicine Received date: 19-12-2015 Revised date: 13-4-2016 Accepted date: 13-4-2016 Please cite this article as: Thomas Brioche, Allan F. Pagano, Guillaume Py, Angèle Chopard, Muscle wasting and aging: experimental models, fatty infiltrations, and prevention, Molecular Aspects of Medicine (2016), http://dx.doi.org/doi: 10.1016/j.mam.2016.04.006. -
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. -
Figure S1. Heat Map of R (Pearson's Correlation Coefficient)
Figure S1. Heat map of r (Pearson’s correlation coefficient) value among different samples including replicates. The color represented the r value. Figure S2. Distributions of accumulation profiles of lipids, nucleotides, and vitamins detected by widely-targeted UPLC-MC during four fruit developmental stages. The colors indicate the proportional content of each identified metabolites as determined by the average peak response area with R scale normalization. PS1, 2, 3, and 4 represents fruit samples collected at 27, 84, 125, 165 Days After Anthesis (DAA), respectively. Three independent replicates were performed for each stages. Figure S3. Differential metabolites of PS2 vs PS1 group in flavonoid biosynthesis pathway. Figure S4. Differential metabolites of PS2 vs PS1 group in phenylpropanoid biosynthesis pathway. Figure S5. Differential metabolites of PS3 vs PS2 group in flavonoid biosynthesis pathway. Figure S6. Differential metabolites of PS3 vs PS2 group in phenylpropanoid biosynthesis pathway. Figure S7. Differential metabolites of PS4 vs PS3 group in biosynthesis of phenylpropanoids pathway. Figure S8. Differential metabolites of PS2 vs PS1 group in flavonoid biosynthesis pathway and phenylpropanoid biosynthesis pathway combined with RNA-seq results. Table S1. A total of 462 detected metabolites in this study and their peak response areas along the developmental stages of apple fruit. mix0 mix0 mix0 Index Compounds Class PS1a PS1b PS1c PS2a PS2b PS2c PS3a PS3b PS3c PS4a PS4b PS4c ID 1 2 3 Alcohols and 5.25E 7.57E 5.27E 4.24E 5.20E