Companion Animals: Nutrition & Health
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
The Role of Amino Acids in Liver Protein Metabolism Under a High Protein Diet
The role of amino acids in liver protein metabolism under a high protein diet : identification of amino acids signal and associated transduction pathways Nattida Chotechuang To cite this version: Nattida Chotechuang. The role of amino acids in liver protein metabolism under a high protein diet : identification of amino acids signal and associated transduction pathways. Food and Nutrition. AgroParisTech, 2010. English. NNT : 2010AGPT0026. pastel-00610998 HAL Id: pastel-00610998 https://pastel.archives-ouvertes.fr/pastel-00610998 Submitted on 25 Jul 2011 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. N° /__/__/__/__/__/__/__/__/__/__/ T H E S I S submitted to obtain the degree of Doctor of Philosophy at L’Institut des Sciences et Industries du Vivant et de l’Environnement (AgroParisTech) Speciality: Nutrition Science Presented and defended in public by Nattida CHOTECHUANG on 22nd March 2010 THE ROLE OF AMINO ACIDS IN LIVER PROTEIN METABOLISM UNDER A HIGH PROTEIN DIET: IDENTIFICATION OF AMINO ACIDS SIGNAL AND ASSOCIATED TRANSDUCTION PATHWAYS Thesis director: Daniel TOMÉ Thesis co-director: Dalila AZZOUT-MARNICHE AgroParisTech, UMR914 Nutrition Physiology and Ingestive Behaviour, F-75005 Paris to the jury: Mr. -
REVIEW ARTICLE High Molecular Mass Intracellular Proteases
Biochem J. (1989) 263, 625-633 (Printed in Great Britain) 625 REVIEW ARTICLE High molecular mass intracellular proteases A. Jennifer RIVETT Department of Biochemistry, University of Leicester, Leicester LE'l 7RH, U.K. INTRODUCTION demonstrated that intracellular proteolysis is not re- Many of the well-characterized proteolytic enzymes, stricted to the lysosomes. Since a large proportion of and particularly those for which X-ray structures are intracellular protein breakdown, especially the degra- now available, are small monomeric enzymes often dation of proteins with short half-lives, is now known to having molecular masses in the range of 20-30 kDa. occur by nonlysosomal mechanisms (Mayer & Doherty, Many of them are extracellular enzymes which are easy 1986; Bond & Beynon, 1987; Rechsteiner, 1987; Bohley, to assay and to purify. With a growing awareness of the 1987; Rivett, 1989b; Katunuma & Kominami, 1989; importance of intracellular protein turnover and Knecht & Grisolia, 1989), there is now a greater interest mechanisms of intracellular protein breakdown, interest in nonlysosomal degradation systems and in nonlyso- in the proteases responsible has also increased. Although somal proteinases, many of which have large complex some intracellular proteases, especially those found structures. within the lysosomes in animal cells, are, like extracellular In contrast to the well-known lysosomal proteases, proteases, small and highly active monomeric enzymes, soluble extralysosomal proteases often have multimeric a number of cellular proteases -
Development and Validation of a Protein-Based Risk Score for Cardiovascular Outcomes Among Patients with Stable Coronary Heart Disease
Supplementary Online Content Ganz P, Heidecker B, Hveem K, et al. Development and validation of a protein-based risk score for cardiovascular outcomes among patients with stable coronary heart disease. JAMA. doi: 10.1001/jama.2016.5951 eTable 1. List of 1130 Proteins Measured by Somalogic’s Modified Aptamer-Based Proteomic Assay eTable 2. Coefficients for Weibull Recalibration Model Applied to 9-Protein Model eFigure 1. Median Protein Levels in Derivation and Validation Cohort eTable 3. Coefficients for the Recalibration Model Applied to Refit Framingham eFigure 2. Calibration Plots for the Refit Framingham Model eTable 4. List of 200 Proteins Associated With the Risk of MI, Stroke, Heart Failure, and Death eFigure 3. Hazard Ratios of Lasso Selected Proteins for Primary End Point of MI, Stroke, Heart Failure, and Death eFigure 4. 9-Protein Prognostic Model Hazard Ratios Adjusted for Framingham Variables eFigure 5. 9-Protein Risk Scores by Event Type This supplementary material has been provided by the authors to give readers additional information about their work. Downloaded From: https://jamanetwork.com/ on 10/02/2021 Supplemental Material Table of Contents 1 Study Design and Data Processing ......................................................................................................... 3 2 Table of 1130 Proteins Measured .......................................................................................................... 4 3 Variable Selection and Statistical Modeling ........................................................................................ -
Human Induced Pluripotent Stem Cell–Derived Podocytes Mature Into Vascularized Glomeruli Upon Experimental Transplantation
BASIC RESEARCH www.jasn.org Human Induced Pluripotent Stem Cell–Derived Podocytes Mature into Vascularized Glomeruli upon Experimental Transplantation † Sazia Sharmin,* Atsuhiro Taguchi,* Yusuke Kaku,* Yasuhiro Yoshimura,* Tomoko Ohmori,* ‡ † ‡ Tetsushi Sakuma, Masashi Mukoyama, Takashi Yamamoto, Hidetake Kurihara,§ and | Ryuichi Nishinakamura* *Department of Kidney Development, Institute of Molecular Embryology and Genetics, and †Department of Nephrology, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan; ‡Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Hiroshima, Japan; §Division of Anatomy, Juntendo University School of Medicine, Tokyo, Japan; and |Japan Science and Technology Agency, CREST, Kumamoto, Japan ABSTRACT Glomerular podocytes express proteins, such as nephrin, that constitute the slit diaphragm, thereby contributing to the filtration process in the kidney. Glomerular development has been analyzed mainly in mice, whereas analysis of human kidney development has been minimal because of limited access to embryonic kidneys. We previously reported the induction of three-dimensional primordial glomeruli from human induced pluripotent stem (iPS) cells. Here, using transcription activator–like effector nuclease-mediated homologous recombination, we generated human iPS cell lines that express green fluorescent protein (GFP) in the NPHS1 locus, which encodes nephrin, and we show that GFP expression facilitated accurate visualization of nephrin-positive podocyte formation in -
©Ferrata Storti Foundation
Original Articles T-cell/histiocyte-rich large B-cell lymphoma shows transcriptional features suggestive of a tolerogenic host immune response Peter Van Loo,1,2,3 Thomas Tousseyn,4 Vera Vanhentenrijk,4 Daan Dierickx,5 Agnieszka Malecka,6 Isabelle Vanden Bempt,4 Gregor Verhoef,5 Jan Delabie,6 Peter Marynen,1,2 Patrick Matthys,7 and Chris De Wolf-Peeters4 1Department of Molecular and Developmental Genetics, VIB, Leuven, Belgium; 2Department of Human Genetics, K.U.Leuven, Leuven, Belgium; 3Bioinformatics Group, Department of Electrical Engineering, K.U.Leuven, Leuven, Belgium; 4Department of Pathology, University Hospitals K.U.Leuven, Leuven, Belgium; 5Department of Hematology, University Hospitals K.U.Leuven, Leuven, Belgium; 6Department of Pathology, The Norwegian Radium Hospital, University of Oslo, Oslo, Norway, and 7Department of Microbiology and Immunology, Rega Institute for Medical Research, K.U.Leuven, Leuven, Belgium Citation: Van Loo P, Tousseyn T, Vanhentenrijk V, Dierickx D, Malecka A, Vanden Bempt I, Verhoef G, Delabie J, Marynen P, Matthys P, and De Wolf-Peeters C. T-cell/histiocyte-rich large B-cell lymphoma shows transcriptional features suggestive of a tolero- genic host immune response. Haematologica. 2010;95:440-448. doi:10.3324/haematol.2009.009647 The Online Supplementary Tables S1-5 are in separate PDF files Supplementary Design and Methods One microgram of total RNA was reverse transcribed using random primers and SuperScript II (Invitrogen, Merelbeke, Validation of microarray results by real-time quantitative Belgium), as recommended by the manufacturer. Relative reverse transcriptase polymerase chain reaction quantification was subsequently performed using the compar- Ten genes measured by microarray gene expression profil- ative CT method (see User Bulletin #2: Relative Quantitation ing were validated by real-time quantitative reverse transcrip- of Gene Expression, Applied Biosystems). -
Effect of Acute and Chronic Alcohol Treatment and Their Superimposition on Lysosomal, Cytoplasmic, and Proteosomal Protease Activities in Rat Skeletal Muscle in Vivo
Effect of Acute and Chronic Alcohol Treatment and Their Superimposition on Lysosomal, Cytoplasmic, and Proteosomal Protease Activities in Rat Skeletal Muscle In Vivo M. Koll, S. Ahmed, D. Mantle, T.M. Donohue, T.N. Palmer, U.A. Simanowski, H.K. Seitz, T.J. Peters, and V.R. Preedy Alcohol can be considered as a nutritional toxin when ingested in excess amounts and leads to skeletal muscle myopathy. We hypothesized that altered protease activities contribute to this phenomenon, and that differential effects on protease activities may occur when: (1) rats at different stages in their development are administered alcohol in vivo; (2) acute ethanol treatment is superimposed on chronic alcohol-feeding in vivo; and (3) muscles are exposed to alcohol and acetaldehyde in vivo and in vitro. In acute studies, rats weighing approximately 0.1 kg (designated immature) or approximately 0.25 kg (designated mature) body weight (BW) were dosed acutely with alcohol (75 mmol/kg BW; intraperitoneal [IP], 2.5 hours prior to killing) or identically treated with 0.15 mol/L NaCl as controls. In chronic studies, rats (approximately 0.1 kg BW) were fed between 1 to 6 weeks, with 35% of dietary energy as ethanol, controls were identically treated with isocaloric glucose. Other studies included administration of cyanamide (aldehyde dehydrogenase inhibitor) in vivo or addition of alcohol and acetal- dehyde to muscle preparations in vitro. At the end of the treatments, cytoplasmic (alanyl-, arginyl-, leucyl-, prolyl-, tripeptidyl- aminopeptidase and dipeptidyl aminopeptidase IV), lysosomal (cathepsins B, D, H, and L, dipeptidyl aminopeptidase I and II), proteasomal (chymotrypsin-, trypsin-like, and peptidylglutamyl peptide hydrolase activities) and Ca2؉-activated (micro- and milli-calpain and calpastatin) activities were assayed. -
Endogenous Inhibitor for Calcium-Dependent Cysteine
Proc. Nati. Acad. Sci. USA Vol. 84, pp. 3590-3594, June 1987 Biochemistry Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites YASUFUMI EMORI*, HIROSHI KAWASAKI*, SHINOBU IMAJOH*, KAZUTOMO IMAHORIt, AND KoICHI SUZUKI* *Department of Molecular Biology, The Tokyo Metropolitan Institute of Medical Science, Honkomagome, Bunkyo-ku, Tokyo 113, Japan; and tMitsubishi-Kasei Institute of Life Sciences, 11 Minamiooya, Machida-shi, Tokyo 194, Japan Communicated by H. A. Scheraga, February 2, 1987 ABSTRACT A cDNA encoding an endogenous inhibitor, MATERIALS AND METHODS termed calpastatin, for calcium-dependent cysteine protease (calpain, EC 3.4.22.17) was cloned by screening rabbit cDNA Purification of Calpastatin from Rabbit Liver and the libraries with a synthetic oligodeoxynudeotide probe based on Designing of an Oligodeoxynucleotide Probe. Calpastatin was the amino acid sequence of the purified protein. The purified from rabbit liver essentially as described (13). The partial purified inhibitor gave a single band on NaDodSO4/poly- deduced amino acid sequence contains 718 amino acid residues acrylamide gel electrophoresis, and its various properties (Mr, 76,964), and the mature protein corresponds to the were similar to those of the human liver inhibitor (13). deduced sequence from the 80th residue of the primary Purified calpastatin was digested with trypsin or endopep- translation product (resultant Mr, 68,113). This deduced mo- tidase Arg-C (Boehringer Mannheim), and then the peptides lecular weight is significantly lower than that determined by generated were separated by HPLC on a Hitachi Gel 3063 NaDodSO4/polyacrylamide gel electrophoresis, suggesting the column. -
Human and Monkey Lenses Cultured with Calcium Ionophore Form B
Human and Monkey Lenses Cultured with Calcium Ionophore Form ␣B-Crystallin Lacking the C-Terminal Lysine, a Prominent Feature of Some Human Cataracts Emi Nakajima,1,2 Larry L. David,3 Michael A. Riviere,2 Mitsuyoshi Azuma,1,2 and Thomas R. Shearer2 PURPOSE. Elevation of lens calcium occurs in both human and ataracts are opacities in the lens of the eye. This disease is experimental animal cataracts, and opacification may result Cthe leading cause of preventable blindness in the world,1 from calcium-activated proteolysis. The purpose of the present yet an effective therapeutic strategy to slow the rate of cataract study was to determine whether calcium accumulation in cul- progression is unavailable. The human lens faces several chal- tured human and Macaca mulatta lenses results in proteolysis lenges in attempting to remain transparent during its long of crystallins, the major lens proteins. lifespan. It is exposed to several possible oxidants,2,3 under- 4 METHODS. Two-dimensional electrophoresis and mass spec- goes a large number of posttranslational modifications, and is trometry were used to construct detailed maps of human and unable to replace the damaged proteins contained in its oldest 5 monkey lens crystallins so that proteolysis after calcium accu- central region because of a programmed loss of organelles. mulation could be monitored and the altered crystallins iden- Opacification results from a loss of the short-range order of tified. Human and macaque lenses cultured in A23187 showed crystallins, the major proteins of the lens, due to their aggre- elevated lenticular calcium and superficial cortical opacities. gation on unfolding or separation into protein-rich and -poor 6 The carboxypeptidase E (CPE) gene is expressed in human phases. -
A Genomic Analysis of Rat Proteases and Protease Inhibitors
A genomic analysis of rat proteases and protease inhibitors Xose S. Puente and Carlos López-Otín Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Instituto Universitario de Oncología, Universidad de Oviedo, 33006-Oviedo, Spain Send correspondence to: Carlos López-Otín Departamento de Bioquímica y Biología Molecular Facultad de Medicina, Universidad de Oviedo 33006 Oviedo-SPAIN Tel. 34-985-104201; Fax: 34-985-103564 E-mail: [email protected] Proteases perform fundamental roles in multiple biological processes and are associated with a growing number of pathological conditions that involve abnormal or deficient functions of these enzymes. The availability of the rat genome sequence has opened the possibility to perform a global analysis of the complete protease repertoire or degradome of this model organism. The rat degradome consists of at least 626 proteases and homologs, which are distributed into five catalytic classes: 24 aspartic, 160 cysteine, 192 metallo, 221 serine, and 29 threonine proteases. Overall, this distribution is similar to that of the mouse degradome, but significatively more complex than that corresponding to the human degradome composed of 561 proteases and homologs. This increased complexity of the rat protease complement mainly derives from the expansion of several gene families including placental cathepsins, testases, kallikreins and hematopoietic serine proteases, involved in reproductive or immunological functions. These protease families have also evolved differently in the rat and mouse genomes and may contribute to explain some functional differences between these two closely related species. Likewise, genomic analysis of rat protease inhibitors has shown some differences with the mouse protease inhibitor complement and the marked expansion of families of cysteine and serine protease inhibitors in rat and mouse with respect to human. -
Role of Calpain and Caspase System in the Regulation of N-Myristoyltransferase in Human Colon Cancer (Review)
823-827 26/3/07 20:04 Page 823 INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE 19: 823-827, 2007 823 Role of calpain and caspase system in the regulation of N-myristoyltransferase in human colon cancer (Review) PONNIAH SELVAKUMAR and RAJENDRA K. SHARMA Department of Pathology and Laboratory Medicine, College of Medicine and Health Research Division, Saskatchewan Cancer Agency, University of Saskatchewan, Saskatoon, Saskatchewan S7N 4H4, Canada Received October 18, 2006; Accepted December 1, 2006 Abstract. A number of viral and eukaryotic proteins which oncogenesis (2-8). The processes of myristoylation is catalyzed undergo a lipophilic modification by the enzyme N-myristoyl- by the ubiquitously distributed eukaryotic enzyme N-myristoyl- transferase (NMT: NMT1 and NMT2) are required for signal transferase (NMT), which is a member of Glycylpeptide transduction and regulatory functions. We reported a higher N-tetradecanoyltransferase (GNAT, EC 2.3.1.97) (2-8). NMT expression of NMT2 in most of the cases of cancerous exists in several distinct forms varying in either apparent tissues compared to normal tissues by Western blot analysis. molecular weight and/or subcellular distribution (9-13). King Furthermore, protein-protein interaction of NMTs revealed and Sharma (9) provided the first evidence for the existence of that m-calpain interacts with NMT1 while caspase-3 interacts multiple forms of bovine brain NMT. Later, McIlhinney et al with NMT2. Our findings provide the first evidence of higher (10) also identified two forms of NMT in bovine brain cortex. expression of NMT2 in human colorectal adenocarcinomas and Subsequently, Glover and Felsted (11) showed that bovine the interaction of both forms of NMT with various signaling brain NMT exists as a heterogeneous mixture of NMT molecules. -
Defining Physiological Differences Between Gilts Divergently Selected for Residual Feed Intake Amanda Jean Harris Iowa State University
Iowa State University Capstones, Theses and Graduate Theses and Dissertations Dissertations 2012 Defining physiological differences between gilts divergently selected for residual feed intake Amanda Jean Harris Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/etd Part of the Agriculture Commons, and the Animal Sciences Commons Recommended Citation Harris, Amanda Jean, "Defining physiological differences between gilts divergently selected for residual feed intake" (2012). Graduate Theses and Dissertations. 12775. https://lib.dr.iastate.edu/etd/12775 This Thesis is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Graduate Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. Defining physiological differences between gilts divergently selected for residual feed intake by Amanda Jean Harris A thesis submitted to the graduate faculty in partial fulfillment of the requirements for the degree of MASTER OF SCIENCE Major: Animal Physiology Program of Study Committee: Nicholas K. Gabler, Major Professor John F. Patience Jack C. M. Dekkers Jason W. Ross Iowa State University Ames, Iowa 2012 Copyright © Amanda Jean Harris, 2012. All rights reserved. ii Table of Contents Table of Contents ...................................................................................................... -
Effects of Calpastatin and Μ-Calpain Markers in Beef Cattle On
Effects of calpastatin and -calpain markers in beef cattle on tenderness traits1,2 E. Casas,*3 S. N. White,* T. L. Wheeler,* S. D. Shackelford,* M. Koohmaraie,* D. G. Riley,† C. C. Chase Jr.,† D. D. Johnson,‡ and T. P. L. Smith* *USDA, ARS, U.S. Meat Animal Research Center, Clay Center, NE 68933; †USDA, ARS, Subtropical Agricultural Research Station, Brooksville, FL 34601; and ‡University of Florida, Gainesville 32611 ABSTRACT: The objective of this study was to assess and tenderness score in the GPE7 and GPE8 popula- the association of single nucleotide polymorphisms tions. Animals inheriting the TT genotype at CAST had (SNP) developed at the calpastatin (CAST) and -cal- meat that was more tender than those inheriting the pain (CAPN1) genes with meat tenderness and palat- CC genotype. The marker at the CAPN1 gene was sig- ability traits in populations with diverse genetic back- nificant (P < 0.03) for tenderness score in GPE7 and grounds. Three populations were used in the study. GPE8. Animals inheriting the CC genotype at CAPN1 One population consisted of Bos taurus that included had meat that was more tender than those inheriting crossbred animals derived from Hereford, Angus, Red the TT genotype. Markers at the CAST and CAPN1 Angus, Limousin, Charolais, Gelbvieh, and Simmental genes were associated with flavor intensity in the GPE8 (GPE7; n = 539). Another population consisted of Bos population. Animals inheriting the CC genotype at taurus with Bos indicus influence, including crossbred CAST and the TT genotype at CAPN1 produced steaks animals from Hereford, Angus, Brangus, Beefmaster, with an intense flavor when compared with the other Bonsmara, and Romosinuano (GPE8; n = 580).