DOCSLIB.ORG

Amino Acid Absorption and Homeostasis in Mice Lacking the Intestinal Peptide Transporter PEPT1

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Amino Acid Absorption and Homeostasis in Mice Lacking the Intestinal Peptide Transporter PEPT1 Technische Universität München Lehrstuhl für Ernährungsphysiologie Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 Anna-Maria Näßl 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. D. Haller Prüfer der Dissertation: 1. Univ.-Prof. Dr. H. Daniel 2. Univ.-Prof. Dr. M. Klingenspor Die Dissertation wurde am 24.08.2011 bei der Technischen Universität München eingereicht und durch die Fakultät Wissenschaftszentrum Weihenstephan für Ernährung, Landnutzung und Umwelt am 06.02.2012 angenommen. Meinen Eltern Table of Content 5 Table of Content Summary ............................................................................................................................. 13 Zusammenfassung ............................................................................................................... 15 1. Introduction....................................................................................................................... 17 1.1. Peptide transport and peptide transporters – a brief history ................................................ 17 1.2. The peptide transporter PEPT1 ................................................................................................ 18 1.2.1. Mode of transport ................................................................................................................. 18 1.2.2. PEPT1 gene and protein structure ...................................................................................... 19 1.2.3. Substrates of PEPT1 ........................................................................................................... 21 1.2.4. Localization of PEPT1 .......................................................................................................... 23 1.2.4.1. PEPT1 expression in the digestive tract ................................................................... 23 1.2.4.2. Expression of PEPT1 in extra-intestinal tissue ......................................................... 24 1.2.5. Regulation of PEPT1 ........................................................................................................... 25 1.2.5.1. PEPT1 and dietary factors ........................................................................................ 25 1.2.5.2. Hormonal control of PEPT1 ...................................................................................... 26 1.2.5.3. PEPT1 in pathophysiological conditions ................................................................... 28 1.2.6. The role of PEPT2 in the organism ...................................................................................... 28 1.3. Putative role of PEPT1 in the organism ................................................................................... 29 1.4. Aim of the project ....................................................................................................................... 33 2. Results ............................................................................................................................. 35 2.1. Basal phenotypic characterization of Pept1 -/- mice ................................................................ 35 2.1.1. Body weight ......................................................................................................................... 35 2.1.2. Haploinsufficiency in heterozygous animals ........................................................................ 36 2.1.3. Characterization of tissue samples by profiling techniques ................................................. 37 2.1.4. Amino acid transport and peptide transporter expression in kidney tissue ......................... 40 2.1.5. Basal metabolic parameters reveal elevated gross energy content of feces in male and female Pept1-/- animals ........................................................................................ 42 2.1.6. Basal plasma grehlin, leptin and insulin levels .................................................................... 43 6 Table of Content 2.2. Analysis of selected parameters in body fluids and tissues in basal state ........................ 44 2.2.1. Clinical chemical parameters ............................................................................................... 44 2.2.2. Basal amino acid levels in plasma, urine and tissue in male mice ...................................... 45 2.2.3. Enzyme and urea levels in liver ........................................................................................... 49 2.3. Effects of dietary protein intake on phenotypic changes in PEPT1-deficient mice ............ 49 2.3.1. Subtle effects after administration of a low-protein diet ....................................................... 49 2.3.2. Effects of feeding a high-protein diet on Pept1 -/- mice ......................................................... 51 2.3.2.1. Metabolic parameters ............................................................................................... 51 2.3.2.2. Energy content of feces in Pept1 -/- mice is elevated when fed a HP diet ................. 53 2.3.2.3. Energy assimilation differences ................................................................................ 54 2.3.2.4. Clinical chemistry plasma and urine parameters in animals fed a HP diet ............... 54 2.3.2.5. High-protein diet alters plasma amino acid levels .................................................... 56 2.3.2.6. Liver tissue amino acid levels and enzyme activities in Pept1 -/- animals .................. 60 2.3.2.7. Decreased leptin levels in Pept1 -/- animals ............................................................... 63 2.3.3. Gender aspects in the effects of a high-protein diet ............................................................ 64 2.3.3.1. Modified clinical chemistry plasma parameters in female Pept1 -/- mice ................... 65 2.3.3.2. Alterations in plasma and liver amino acids of female Pept1 -/- mice on a high-protein diet ......................................................................................................... 65 2.3.3.3. Enzyme activities and urea concentration in liver tissue .......................................... 68 2.3.4. Effects of a carbohydrate administration ............................................................................. 69 2.3.4.1. Administration of a high-protein diet and water enriched with glucose ..................... 69 2.3.4.2. Blood glucose and insulin secretion after an oral glucose tolerance test ................. 71 2.4. Effects of an acute protein administration by gavage ........................................................... 72 2.4.1. Changes in plasma amino acids after administration of a low dose of 15 N-labeled protein .................................................................................................................................. 72 2.4.2. Effects of a high intragastric protein load on plasma and liver amino acid levels in Pept1 +/+ and Pept1 -/- animals ........................................................................................... 76 3. Discussion ........................................................................................................................ 81 3.1. Basal phenotypic characterization ........................................................................................... 81 3.2. PEPT1 in response to different protein contents ................................................................... 85 3.3. Conclusion ................................................................................................................................. 93 Table of Content 7 4. Materials and Methods ..................................................................................................... 97 4.1. Chemicals and consumables ................................................................................................... 97 4.2. Laboratory animals .................................................................................................................... 97 4.2.1. Mouse husbandry ................................................................................................................ 97 4.2.2. Genotyping........................................................................................................................... 97 4.2.3. Data sampling for body weight ............................................................................................ 98 4.2.4. Bomb calorimetry of feces samples ..................................................................................... 98 4.3. Dietary intervention studies...................................................................................................... 98 4.3.1. Dietary intervention study with low, medium and high protein content for 5 days in male mice ......................................................................................................................... 98 4.3.2. Dietary intervention study in female mice for 5 days ........................................................... 99 4.3.3. Dietary intervention study for 18 days ................................................................................. 99 4.3.4. 24-hour dietary intervention study ......................................................................................
Load more

Recommended publications
  • Amino Acid & Protein
    Amino Acid & Protein DR. MD. MAHBUBUR RAHMAN MBBS, M. Phil . MSc.(Biotechnology) DEPT. OF BIOCHEMISTRY RAJSHAHI MEDICAL COLLEGE At the end of the session Student will be able to • Definition of amino acid, formation of peptide bond & its property • Biomedical importance of AA • Protein cycle At the end of the session Student will be able to • Classification of AA, • Isoelectric pH and 2D electrophoresis • Protein – definition, classification & structure, • purification of protein Biomedical Importance • Monomeric unit of Protein/ Polypeptide • Amino acid and their derivatives participate in diverse cellular function • Further discussed in functional classification Biomedical Importance Peptide performs prominent role in neuroendocrine system eg. Hormone , Neurotransmitter, Transporter Human lack of capability to synthesize 10 of the 20 common A-Acid (most of them α amino acid) Diversity of Protein function Enzyme and hormone regulate metabolism muscle movement by protein (contractile protein) Collagen fiber forms bone Ig fights against infectious Bacteria & viruses Bacitracin and gramicidin act a antibiotic Bleomycin act anticancer agent Amino Acid Are organic acid having both carboxyl group and amino group attach to same carbon atom. Peptide Bond In protein, amino acids are joined covalently By peptide Bond which are amide linkage Between the α-carboxyl group of one amino acid and the α- amino group of another Characteristic of peptide bond Net charge of amino acid at neutral pH • At physiologic pH all amino acid have a negatively charged group (- COO-) and positively charged group ( - NH3).----- is called amphoteric( ampholyte) Isoelectric pH The pH at which amino bears no net charge. The pH at which amino acid are electrically neutral that is the sum of positive charge equals the sum of negative charge Optical properties of amino acid α carbon of each amino acid are attached to four different group there fore amino acid have optical isomerism.
    [Show full text]
  • Evidence for a Catabolic Role of Glucagon During an Amino Acid Load
    Evidence for a catabolic role of glucagon during an amino acid load. M R Charlton, … , D B Adey, K S Nair J Clin Invest. 1996;98(1):90-99. https://doi.org/10.1172/JCI118782. Research Article Despite the strong association between protein catabolic conditions and hyperglucagonemia, and enhanced glucagon secretion by amino acids (AA), glucagon's effects on protein metabolism remain less clear than on glucose metabolism. To clearly define glucagon's catabolic effect on protein metabolism during AA load, we studied the effects of glucagon on circulating AA and protein dynamics in six healthy subjects. Five protocols were performed in each subject using somatostatin to inhibit the secretion of insulin, glucagon, and growth hormone (GH) and selectively replacing these hormones in different protocols. Total AA concentration was the highest when glucagon, insulin, and GH were low. Selective increase of glucagon levels prevented this increment in AA. Addition of high levels of insulin and GH to high glucagon had no effect on total AA levels, although branched chain AA levels declined. Glucagon mostly decreased glucogenic AA and enhanced glucose production. Endogenous leucine flux, reflecting proteolysis, decreased while leucine oxidation increased in protocols where AA were infused and these changes were unaffected by the hormones. Nonoxidative leucine flux reflecting protein synthesis was stimulated by AA, but high glucagon attenuated this effect. Addition of GH and insulin partially reversed the inhibitory effect of glucagon on protein synthesis. We conclude that glucagon is the pivotal hormone in amino acid disposal during an AA load and, by reducing the availability of AA, […] Find the latest version: https://jci.me/118782/pdf Evidence for a Catabolic Role of Glucagon during an Amino Acid Load Michael R.
    [Show full text]
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
    [Show full text]
  • Blood Metabolite Signature of Metabolic Syndrome Implicates
    International Journal of Molecular Sciences Article Blood Metabolite Signature of Metabolic Syndrome Implicates Alterations in Amino Acid Metabolism: Findings from the Baltimore Longitudinal Study of Aging (BLSA) and the Tsuruoka Metabolomics Cohort Study (TMCS) Jackson A. Roberts 1 , Vijay R. Varma 1, Chiung-Wei Huang 2, Yang An 2, Anup Oommen 3 , Toshiko Tanaka 4 , Luigi Ferrucci 4, Palchamy Elango 4, Toru Takebayashi 5, Sei Harada 5 , Miho Iida 5 and Madhav Thambisetty 1,* 1 Clinical and Translational Neuroscience Section, Laboratory of Behavioral Neuroscience, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA; [email protected] (J.A.R.); [email protected] (V.R.V.) 2 Brain Aging and Behavior Section, Laboratory of Behavioral Neuroscience, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA; [email protected] (C.-W.H.); [email protected] (Y.A.) 3 Glycoscience Group, National Centre for Biomedical Engineering Science, National University of Ireland Galway, Galway H91-TK33, Ireland; [email protected] 4 Translational Gerontology Branch, National Institute on Aging, NIH, Baltimore, MD 21224, USA; [email protected] (T.T.); [email protected] (L.F.); [email protected] (P.E.) 5 Department of Preventive Medicine and Public Health, Keio University, Tokyo 160-8282, Japan; [email protected] (T.T.); [email protected] (S.H.); [email protected] (M.I.) * Correspondence: [email protected]; Tel.: +1-(410)-558-8572; Fax: +1-(410)-558-8302 Received: 19 December 2019; Accepted: 10 February 2020; Published: 13 February 2020 Abstract: Rapid lifestyle and dietary changes have contributed to a rise in the global prevalence of metabolic syndrome (MetS), which presents a potential healthcare crisis, owing to its association with an increased burden of multiple cardiovascular and neurological diseases.
    [Show full text]
  • Biochemistry - Problem Drill 20: Amino Acid Metabolism
    Biochemistry - Problem Drill 20: Amino Acid Metabolism Question No. 1 of 10 Instructions: (1) Read the problem and answer choices carefully (2) Work the problems on paper as needed (3) Pick the answer (4) Go back to review the core concept tutorial as needed. 1. ________ is the reaction between an amino acid and an alpha keto acid. (A) Ketogenic (B) Aminogenic (C) Transamination Question (D) Carboxylation (E) Glucogenic A. Incorrect! No, consider the amino acid and keto acid structure when answering this question. B. Incorrect! No, consider the amino acid and keto acid structure when answering this question. C. Correct! Yes, Transamination is the reaction between an amino acid and an alpha keto acid. Feedback D. Incorrect! No, consider the amino acid and keto acid structure when answering this question. E. Incorrect! No, consider the amino acid and keto acid structure when answering this question. Transamination is the reaction between an amino acid and an alpha keto acid. The correct answer is (C). Solution RapidLearningCenter.com © Rapid Learning Inc. All Rights Reserved Question No. 2 of 10 Instructions: (1) Read the problem statement and answer choices carefully (2) Work the problems on paper as needed (3) Pick the answer (4) Go back to review the core concept tutorial as needed. 2. Lysine and leucine are examples of what? (A) Ketogenic amino acids. (B) Nonessential amino acids. (C) Non-ketogenic amino acids. (D) Glucogenic amino acids. Question (E) None of the above A. Correct! Yes, lysine and leucine are examples of ketogenic amino acids. B. Incorrect No, this is not a correct response.
    [Show full text]
  • Frontiersin.Org 1 April 2015 | Volume 9 | Article 123 Saunders Et Al
    ORIGINAL RESEARCH published: 28 April 2015 doi: 10.3389/fnins.2015.00123 Influx mechanisms in the embryonic and adult rat choroid plexus: a transcriptome study Norman R. Saunders 1*, Katarzyna M. Dziegielewska 1, Kjeld Møllgård 2, Mark D. Habgood 1, Matthew J. Wakefield 3, Helen Lindsay 4, Nathalie Stratzielle 5, Jean-Francois Ghersi-Egea 5 and Shane A. Liddelow 1, 6 1 Department of Pharmacology and Therapeutics, University of Melbourne, Parkville, VIC, Australia, 2 Department of Cellular and Molecular Medicine, University of Copenhagen, Copenhagen, Denmark, 3 Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, Australia, 4 Institute of Molecular Life Sciences, University of Zurich, Zurich, Switzerland, 5 Lyon Neuroscience Research Center, INSERM U1028, Centre National de la Recherche Scientifique UMR5292, Université Lyon 1, Lyon, France, 6 Department of Neurobiology, Stanford University, Stanford, CA, USA The transcriptome of embryonic and adult rat lateral ventricular choroid plexus, using a combination of RNA-Sequencing and microarray data, was analyzed by functional groups of influx transporters, particularly solute carrier (SLC) transporters. RNA-Seq Edited by: Joana A. Palha, was performed at embryonic day (E) 15 and adult with additional data obtained at University of Minho, Portugal intermediate ages from microarray analysis. The largest represented functional group Reviewed by: in the embryo was amino acid transporters (twelve) with expression levels 2–98 times Fernanda Marques, University of Minho, Portugal greater than in the adult. In contrast, in the adult only six amino acid transporters Hanspeter Herzel, were up-regulated compared to the embryo and at more modest enrichment levels Humboldt University, Germany (<5-fold enrichment above E15).
    [Show full text]
  • Part 3 Metabolism of Proteins and Nucleic Acids Частина 3 Обмін Білків І Нуклеїнових Кислот
    МІНІСТЕРСТВО ОХОРОНИ ЗДОРОВ'Я УКРАЇНИ Харківський національний медичний університет PART 3 METABOLISM OF PROTEINS AND NUCLEIC ACIDS Self-Study Guide for Students of General Medicine Faculty in Biochemistry ЧАСТИНА 3 ОБМІН БІЛКІВ І НУКЛЕЇНОВИХ КИСЛОТ Методичні вказівки для підготовки до практичних занять з біологічної хімії (для студентів медичних факультетів) Затверджено вченою радою ХНМУ Протокол № 1 від 26.01.2017 р. Approved by the Scientific Council of KhNMU. Protocol 1 (January 26, 2017) Харків ХНМУ 2017 Metabolism of proteins and nucleic acids : self-study guide for students of general medicine faculty in biochemistry. Part 3: / Comp. : O. Nakonechna, S. Stetsenko, L. Popova, A. Tkachenko. – Kharkiv : KhNMU, 2017. – 56 p. Compilers Nakonechna O. Stetsenko S. Popova L. Tkachenko A. Обмін білків та нуклеїнових кислот : метод. вказ. для підготовки до практ. занять з біологічної хімії (для студ. мед. ф-тів). Ч 3. / упоряд. О.А. Наконечна, С.О. Стеценко, Л.Д. Попова, А.С. Ткаченко. – Харків : ХНМУ, 2017. – 56 с. Упорядники О.А. Наконечна С.О. Стеценко Л.Д. Попова А.С. Ткаченко - 2 - SOURCES For preparing to practical classes in "Biological Chemistry" Basic Sources 1. Біологічна і біоорганічна хімія: у 2 кн.: підруч. Біологічна хімія / Ю.І. Губ- ський, І.В. Ніженковська, М.М. Корда, В.І. Жуков та ін. ; за ред. Ю.І. Губського, І.В. Ніженковської. – Кн. 2. – Київ : ВСВ «Медицина», 2016. – 544 с. 2. Губський Ю.І. Біологічна хімія : підруч. / Ю.І. Губський – Київ– Вінниця: Нова книга, 2007. – 656 с. 3. Губський Ю.І. Біологічна хімія / Губський Ю.І. – Київ–Тернопіль : Укр- медкнига, 2000. – 508 с. 4. Гонський Я.І.
    [Show full text]
  • Associations of SLC6A20 Genetic Polymorphisms with Hirschsprung's
    Bioscience Reports (2019) 39 BSR20182290 https://doi.org/10.1042/BSR20182290 Research Article Associations of SLC6A20 genetic polymorphisms with Hirschsprung’s disease in a Southern Chinese population * * Xiaoli Xie , Qiuming He , Lihua Huang, Le Li, Yuxiao Yao, Huimin Xia, Jinglu Zhao, Wei Zhong and Downloaded from http://portlandpress.com/bioscirep/article-pdf/39/8/BSR20182290/863686/bsr-2018-2290.pdf by guest on 29 September 2021 Yan Zhang Department of Pediatric Surgery, Guangzhou Institute of Pediatrics, Guangzhou Women and Children’s Medical Center, Guangzhou Medical University, Guangzhou 510623, Guangdong, China Correspondence: Wei Zhong ([email protected]) or Yan Zhang ([email protected]) Hirschsprung’s disease (HSCR) is a neurodevelopmental disorder characterized by the ab- sence of nerves in intestine with strong genetic components. SLC6A20 was found to be associated with HSCR in Korean population waiting for replication in an independent co- hort. In the present study, ten single nucleotide polymorphisms (SNPs) in the SLC6A20 were selected from Southern Chinese with 1470 HSCR cases and 1473 ethnically matched healthy controls. Our results indicated that SNP rs7640009 was associated with HSCR and SLC6A20 has a gene–dose effect in the extent of the aganglionic segment during enteric nervous system (ENS) development. It is the first time to reveal the relationship between SNP rs2191026 and HSCR-associated enterocolitis (HAEC) susceptibility. Introduction Hirschsprung’s disease (HSCR) is a congenital disease characterized by the absence of intrinsic ganglion cells in the submucosal and myenteric plexuses of the intestinal tract involving a variable portion. It is common that HSCR leads to the mechanical intestinal obstruction in infants and children.
    [Show full text]
  • Epigenetic Mechanisms Are Involved in the Oncogenic Properties of ZNF518B in Colorectal Cancer
    Epigenetic mechanisms are involved in the oncogenic properties of ZNF518B in colorectal cancer Francisco Gimeno-Valiente, Ángela L. Riffo-Campos, Luis Torres, Noelia Tarazona, Valentina Gambardella, Andrés Cervantes, Gerardo López-Rodas, Luis Franco and Josefa Castillo SUPPLEMENTARY METHODS 1. Selection of genomic sequences for ChIP analysis To select the sequences for ChIP analysis in the five putative target genes, namely, PADI3, ZDHHC2, RGS4, EFNA5 and KAT2B, the genomic region corresponding to the gene was downloaded from Ensembl. Then, zoom was applied to see in detail the promoter, enhancers and regulatory sequences. The details for HCT116 cells were then recovered and the target sequences for factor binding examined. Obviously, there are not data for ZNF518B, but special attention was paid to the target sequences of other zinc-finger containing factors. Finally, the regions that may putatively bind ZNF518B were selected and primers defining amplicons spanning such sequences were searched out. Supplementary Figure S3 gives the location of the amplicons used in each gene. 2. Obtaining the raw data and generating the BAM files for in silico analysis of the effects of EHMT2 and EZH2 silencing The data of siEZH2 (SRR6384524), siG9a (SRR6384526) and siNon-target (SRR6384521) in HCT116 cell line, were downloaded from SRA (Bioproject PRJNA422822, https://www.ncbi. nlm.nih.gov/bioproject/), using SRA-tolkit (https://ncbi.github.io/sra-tools/). All data correspond to RNAseq single end. doBasics = TRUE doAll = FALSE $ fastq-dump -I --split-files SRR6384524 Data quality was checked using the software fastqc (https://www.bioinformatics.babraham. ac.uk /projects/fastqc/). The first low quality removing nucleotides were removed using FASTX- Toolkit (http://hannonlab.cshl.edu/fastxtoolkit/).
    [Show full text]
  • Metabolism of Branched-Chain Amino Acids Branched-Chain Amino Acids
    Metabolism of Branched-chain Amino acids Branched-chain Amino acids Leu, Ile, Val are the branched chain and essential amino acid Branched-chain Amino acids • Valine (Val) is glucogenic amino acid • Leucine (Leu) is ketogenic aminoacid • Isoleucine (Ile) is both glucogenic and ketogenic amino acid • These amino acids serve as an alternate source of fuel for the brain especially under conditions of starvation. Metabolism of branched-chain AAs The first three metabolic reactions are common to the branched chain amino acids 1. Transamination 2. Oxidative decarboxylation 3. Dehydrogenation Branched chain amino acid degradation 3. Dehydrogenation Acyl-CoA dehydrogeanse by FAD coenzyme The degradation of the branched- chain amino acids (A) isoleucine, (B) valine, and (C) leucine. For IsoLeucine After the three steps, for Ile, 4. Enoyl-CoA hydratase 5. -hydroxyacyl-CoA dehydrogenase 6. Acetyl-CoA acetyltransferase Last 3 steps similar to fatty acid oxidation For Valine: 4. Enoyl-CoA hydratase 5. -hydroxy-isobutyryl- CoA hydrolase 6. hydroxyisobutyrate dehydrogenase 7. Methylmalonate semialdehyde dehydrogenase Last 3 steps similar to fatty acid oxidation For Leucine: 4. -methylcrotonyl-CoA carboxylase 5. -methylglutaconyl-CoA hydratase 6. HMG-CoA lyase Branched Chain Amino Acids • Isoleucine • Leucine • Valine • Important sources of Krebs intermediates under certain conditions Amino Acid as Energy Source in Skeletal Muscle • Oxidation of Branched Chain Amino Acid yield between 32- 43 ATP Comparable to complete oxidation of glucose • Amino Acid
    [Show full text]
  • M O N T I F F, I
    MONTIFF INC Don Tyson’s Advanced Nutraceuticals GLUCA-BALANCE An amino acid formula high in glycogenic amino acids, which the body converts into glucose to help balance blood sugar levels that are low with hypoglycemia. Also recommended for other biochemical imbalances requiring glycogenic amino acids. Each capsule contains14 amino acids with a total of 700mg.of the following: L-Alanine, L-Lysine HCL, L-Leucine, Glycine, L-Valine, L-Isoleucine, L-Threonine, L-Glutamine, L-Arginine HCL, L-Histidine, L- Phenylalanine, L-Tyrosine, L-Methionine, L-Proline, plus precursor Ornithine-α-Ketoglutarate, and Di- peptides L-Alanyl-L-Glutamine, and L-Glycyl-L-Glutamine. RECOMMENDED FOR: • Individuals with hypoglycemia. • Stabilizing low blood glucose levels and helping to eliminate mid morning and mid afternoon fatigue. • Aids in mental alertness and memory function. • May be helpful in alcoholic management in conjunction with additional L-Glutamine. • Helping to eliminate the craving for sweets. • For those whose plasma or urine profiles indicate an imbalance of these amino acids. WHAT ARE GLYCOGENIC AMINO ACIDS? These are the amino acids that can be converted by the body into glucose to produce energy. The brain requires 125-150g or 75% of the available glucose in the body, for its energy source, to maintain normal brain metabolism. While many amino acids can be converted into glucose, Alanine and Glutamine are the primary glycogenic amino acids. Because amino acids are converted into glucose at different rates, a mixture of glycogenic amino acids permits the blood glucose levels to maintain over a longer period of time. Gluconeogenesis is the process of converting amino acids, lactate and glycerol into glucose for the brain.
    [Show full text]
  • 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
    [Show full text]