DOCSLIB.ORG

K. Nicholson, Janet M. Thornton, Linda Partridge and Dominic J

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
K. Nicholson, Janet M. Thornton, Linda Partridge and Dominic J Colin Selman, Nicola D. Kerrison, Anisha Cooray, Matthew D. W. Piper, Steven J. Lingard, Richard H. Barton, Eugene F. Schuster, Eric Blanc, David Gems, Jeremy K. Nicholson, Janet M. Thornton, Linda Partridge and Dominic J. Withers Physiol Genomics 27:187-200, 2006. First published Aug 1, 2006; doi:10.1152/physiolgenomics.00084.2006 You might find this additional information useful... Supplemental material for this article can be found at: http://physiolgenomics.physiology.org/cgi/content/full/00084.2006/DC1 This article cites 64 articles, 31 of which you can access free at: http://physiolgenomics.physiology.org/cgi/content/full/27/3/187#BIBL This article has been cited by 3 other HighWire hosted articles: Gene expression profiling of the short-term adaptive response to acute caloric restriction in liver and adipose tissues of pigs differing in feed efficiency S. Lkhagvadorj, L. Qu, W. Cai, O. P. Couture, C. R. Barb, G. J. Hausman, D. Nettleton, L. L. Downloaded from Anderson, J. C. M. Dekkers and C. K. Tuggle Am J Physiol Regulatory Integrative Comp Physiol, February 1, 2010; 298 (2): R494-R507. [Abstract] [Full Text] [PDF] Comment on "Brain IRS2 Signaling Coordinates Life Span and Nutrient Homeostasis" C. Selman, S. Lingard, D. Gems, L. Partridge and D. J. Withers Science, May 23, 2008; 320 (5879): 1012b-1012b. [Abstract] [Full Text] [PDF] physiolgenomics.physiology.org Evidence for lifespan extension and delayed age-related biomarkers in insulin receptor substrate 1 null mice C. Selman, S. Lingard, A. I. Choudhury, R. L. Batterham, M. Claret, M. Clements, F. Ramadani, K. Okkenhaug, E. Schuster, E. Blanc, M. D. Piper, H. Al-Qassab, J. R. Speakman, D. Carmignac, I. C. A. Robinson, J. M. Thornton, D. Gems, L. Partridge and D. J. Withers FASEB J, March 1, 2008; 22 (3): 807-818. [Abstract] [Full Text] [PDF] Updated information and services including high-resolution figures, can be found at: http://physiolgenomics.physiology.org/cgi/content/full/27/3/187 on February 15, 2010 Additional material and information about Physiological Genomics can be found at: http://www.the-aps.org/publications/pg This information is current as of February 15, 2010 . Physiological Genomics publishes results of a wide variety of studies from human and from informative model systems with techniques linking genes and pathways to physiology, from prokaryotes to eukaryotes. It is published quarterly in January, April, July, and October by the American Physiological Society, 9650 Rockville Pike, Bethesda MD 20814-3991. Copyright © 2005 by the American Physiological Society. ISSN: 1094-8341, ESSN: 1531-2267. Visit our website at http://www.the-aps.org/. Physiol Genomics 27: 187–200, 2006. First published August 1, 2006; doi:10.1152/physiolgenomics.00084.2006. CALL FOR PAPERS Comparative Genomics Coordinated multitissue transcriptional and plasma metabonomic profiles following acute caloric restriction in mice Colin Selman,1* Nicola D. Kerrison,2* Anisha Cooray,3 Matthew D. W. Piper,4 Steven J. Lingard,1 Richard H. Barton,3 Eugene F. Schuster,2 Eric Blanc,2 David Gems,4 Jeremy K. Nicholson,3 Janet M. Thornton,2 Linda Partridge,4 and Dominic J. Withers1 1Centre for Diabetes and Endocrinology, Department of Medicine, University College London, Rayne Institute, London; 2European Molecular Biology Laboratory (EMBL)-European Bioinformatics Institute (EBI), Wellcome Trust Genome Campus, Hinxton, Cambridge; 3Biological Chemistry Section, Department of Biomolecular Medicine, Division of Surgery, Oncology, Reproductive Biology and Anaesthetics, Faculty of Medicine, Imperial College London, South Kensington, London; and 4UCL Centre for Ageing Research, Department of Biology, University College London, London, United Kingdom Downloaded from Submitted 10 May 2006; accepted in final form 28 July 2006 Selman, Colin, Nicola D. Kerrison, Anisha Cooray, Matthew D. W. of vertebrate and invertebrate species (24, 41, 46, 61). How- Piper, Steven J. Lingard, Richard H. Barton, Eugene F. Schuster, Eric ever, the mechanisms through which CR extends life span are Blanc, David Gems, Jeremy K. Nicholson, Janet M. Thornton, Linda not understood. CR is accompanied by changes in gene and Partridge, and Dominic J. Withers. Coordinated multitissue transcriptional protein expression and resultant alterations in both cellular and physiolgenomics.physiology.org and plasma metabonomic profiles following acute caloric restriction in mice. Physiol Genomics 27: 187–200, 2006. First published August 1, 2006; whole organism metabolism that are thought to underlie its doi:10.1152/physiolgenomics.00084.2006.—Caloric restriction (CR) in- effects on aging. creases healthy life span in a range of organisms. The underlying mecha- RNA transcript profiles have been useful for defining nisms are not understood but appear to include changes in gene expression, changes in gene expression following CR, leading to the protein function, and metabolism. Recent studies demonstrate that acute CR formulation of experimentally testable hypotheses. Long-term alters mortality rates within days in flies. Multitissue transcriptional changes CR in rodents attenuates many age-associated transcriptional and concomitant metabolic responses to acute CR have not been described. changes, including expression of genes involved with cellular We generated whole genome RNA transcript profiles in liver, skeletal stress, in skeletal muscle (36), hypothalamus (20), and liver muscle, colon, and hypothalamus and simultaneously measured plasma (11, 16). However, to date, most microarray mRNA expression metabolites using proton nuclear magnetic resonance in mice subjected to acute CR. Liver and muscle showed increased gene expressions associated studies in mice have been confined to single tissues and have with fatty acid metabolism and a reduction in those involved in hepatic lipid profiled only part of the genome. In addition, single-tissue on February 15, 2010 biosynthesis. Glucogenic amino acids increased in plasma, and gene expres- studies have varied widely in experimental design, bioinfor- sion for hepatic gluconeogenesis was enhanced. Increased expression of matic analysis, and mouse strains used (29), thus making direct genes for hormone-mediated signaling and decreased expression of genes comparisons between tissues difficult. Furthermore, altered involved in protein binding and development occurred in hypothalamus. Cell transcript profiles have not been related to concomitant plasma proliferation genes were decreased and cellular transport genes increased in metabolic changes. colon. Acute CR captured many, but not all, hepatic transcriptional changes Changes in gene expression following initiation of CR (or of long-term CR. Our findings demonstrate a clear transcriptional response across multiple tissues during acute CR, with congruent plasma metabolite dietary restriction; DR) appear rapid in both Drosophila and changes. Liver and muscle switched gene expression away from energeti- mice. Significant shifts in transcript profile in Drosophila cally expensive biosynthetic processes toward energy conservation and uti- occurred within 3 days following DR (47). In studies of hepatic lization processes, including fatty acid metabolism and gluconeogenesis. gene expression in mice, a rapid and cumulative shift mirroring Both muscle and colon switched gene expression away from cellular prolif- a long-term (12 mo) CR transcriptional profile was observed eration. Mice undergoing acute CR rapidly adopt many transcriptional and after 2, 4, or 8 wk of CR. A return to ad libitum (AD) levels metabolic changes of long-term CR, suggesting that the beneficial effects of reversed 90% of this long-term CR profile after 8 wk (16). This CR may require only a short-term reduction in caloric intake. suggests that these changes in gene expression during acute CR aging; microarray; gene expression may induce rapid beneficial effects on life span. In Drosophila, a dietary shift to DR altered mortality rate within days (40). However, accurate measurements of mortality rates during CALORIC RESTRICTION (CR) extends mean and maximum life acute CR have not been measured in mice, although CR span and retards various age-associated pathologies in a range initiated at 12 mo of age extended mean and maximum life span, decreased age-associated mortality, and reduced cancer * C. Selman and N. D. Kerrison contributed equally to this work. incidence (16, 49). Article published online before print. See web site for date of publication In this study, we examined acute whole genome transcrip- (http://physiolgenomics.physiology.org). tional changes following short-term CR in liver, skeletal mus- Address for reprint requests and other correspondence: C. Selman, Centre for Diabetes and Endocrinology, Dept. of Medicine, Univ. College London, cle, hypothalamus, and colon of 16-wk-old male C57BL/6 Rayne Institute, 5 University St., London WC1E 6JJ, UK (e-mail: c.selman@ mice subjected to a stepwise 16-day protocol of CR terminat- ucl.ac.uk). ing in a 48-h period of 30% CR (see supplemental data; 1094-8341/06 $8.00 Copyright © 2006 the American Physiological Society 187 188 MULTITISSUE TRANSCRIPTIONAL AND METABOLITE RESPONSE TO ACUTE CALORIC RESTRICTION Supplemental Materials are available in the online version of portion of the upper colon were removed, flash-frozen in liquid this article). In parallel, we employed a nuclear magnetic nitrogen, and stored at Ϫ80°C until RNA extraction. To minimize the resonance (NMR) metabonomic strategy capable of identifying potential for hierarchies
Load more

Recommended publications
  • Entrez Symbols Name Termid Termdesc 117553 Uba3,Ube1c
    Entrez Symbols Name TermID TermDesc 117553 Uba3,Ube1c ubiquitin-like modifier activating enzyme 3 GO:0016881 acid-amino acid ligase activity 299002 G2e3,RGD1310263 G2/M-phase specific E3 ubiquitin ligase GO:0016881 acid-amino acid ligase activity 303614 RGD1310067,Smurf2 SMAD specific E3 ubiquitin protein ligase 2 GO:0016881 acid-amino acid ligase activity 308669 Herc2 hect domain and RLD 2 GO:0016881 acid-amino acid ligase activity 309331 Uhrf2 ubiquitin-like with PHD and ring finger domains 2 GO:0016881 acid-amino acid ligase activity 316395 Hecw2 HECT, C2 and WW domain containing E3 ubiquitin protein ligase 2 GO:0016881 acid-amino acid ligase activity 361866 Hace1 HECT domain and ankyrin repeat containing, E3 ubiquitin protein ligase 1 GO:0016881 acid-amino acid ligase activity 117029 Ccr5,Ckr5,Cmkbr5 chemokine (C-C motif) receptor 5 GO:0003779 actin binding 117538 Waspip,Wip,Wipf1 WAS/WASL interacting protein family, member 1 GO:0003779 actin binding 117557 TM30nm,Tpm3,Tpm5 tropomyosin 3, gamma GO:0003779 actin binding 24779 MGC93554,Slc4a1 solute carrier family 4 (anion exchanger), member 1 GO:0003779 actin binding 24851 Alpha-tm,Tma2,Tmsa,Tpm1 tropomyosin 1, alpha GO:0003779 actin binding 25132 Myo5b,Myr6 myosin Vb GO:0003779 actin binding 25152 Map1a,Mtap1a microtubule-associated protein 1A GO:0003779 actin binding 25230 Add3 adducin 3 (gamma) GO:0003779 actin binding 25386 AQP-2,Aqp2,MGC156502,aquaporin-2aquaporin 2 (collecting duct) GO:0003779 actin binding 25484 MYR5,Myo1e,Myr3 myosin IE GO:0003779 actin binding 25576 14-3-3e1,MGC93547,Ywhah
    [Show full text]
  • The Proteasomal Deubiquitinating Enzyme PSMD14 Regulates Macroautophagy by Controlling Golgi-To-ER Retrograde Transport
    Supplementary Materials The proteasomal deubiquitinating enzyme PSMD14 regulates macroautophagy by controlling Golgi-to-ER retrograde transport Bustamante HA., et al. Figure S1. siRNA sequences directed against human PSMD14 used for Validation Stage. Figure S2. Primer pairs sequences used for RT-qPCR. Figure S3. The PSMD14 DUB inhibitor CZM increases the Golgi apparatus area. Immunofluorescence microscopy analysis of the Golgi area in parental H4 cells treated for 4 h either with the vehicle (DMSO; Control) or CZM. The Golgi marker GM130 was used to determine the region of interest in each condition. Statistical significance was determined by Student's t-test. Bars represent the mean ± SEM (n =43 cells). ***P <0.001. Figure S4. CZM causes the accumulation of KDELR1-GFP at the Golgi apparatus. HeLa cells expressing KDELR1-GFP were either left untreated or treated with CZM for 30, 60 or 90 min. Cells were fixed and representative confocal images were acquired. Figure S5. Effect of CZM on proteasome activity. Parental H4 cells were treated either with the vehicle (DMSO; Control), CZM or MG132, for 90 min. Protein extracts were used to measure in vitro the Chymotrypsin-like peptidase activity of the proteasome. The enzymatic activity was quantified according to the cleavage of the fluorogenic substrate Suc-LLVY-AMC to AMC, and normalized to that of control cells. The statistical significance was determined by One-Way ANOVA, followed by Tukey’s test. Bars represent the mean ± SD of biological replicates (n=3). **P <0.01; n.s., not significant. Figure S6. Effect of CZM and MG132 on basal macroautophagy. (A) Immunofluorescence microscopy analysis of the subcellular localization of LC3 in parental H4 cells treated with either with the vehicle (DMSO; Control), CZM for 4 h or MG132 for 6 h.
    [Show full text]
  • OXALOACETATO Patent Application Title Inventors
    Method for Extending Lifespan Delaying the Onset of Age-Related Disease: OXALOACETATO Patent application title Inventors: Alan B. Cash (San Diego, CA, US) IPC8 Class: AA61K912FI USPC Class: 424 45 Class name: Drug, bio-affecting and body treating compositions effervescent or pressurized fluid containing organic pressurized fluid Publication date: 2008-11-13 Patent application number: 20080279786 Abstract: A method and composition for extending the lifespan of an individual and delaying the onset of age-related disease is provided. The method includes the administration of an effective dose of oxaloacetate, wherein the oxaloacetate acts to mimic the cellular conditions obtained under caloric restriction to provide similar benefits. The invention further includes methods and compositions for reducing the incidence or treatment of cancer. Compositions and methods for reducing body fat by administering an effective amount of oxaloacetate are likewise provided. Compositions for DNA repair in UV damaged cells is provided are also provided. Similarly, a method for treating a hang-over comprising administering an effective amount of oxaloacetate is disclosed. Claims: 1. Use of an effective lifespan-extending amount of a composition selected from the group consisting of oxaloacetate, oxaloacetic acid, an oxaloacetate salt, alpha-ketoglutarate and aspartate for the manufacture of a medicament for extending the lifespan of an organism. 2. The use of claim 1, wherein said composition is formulated for oral administration. 3. The use of claim 1, wherein said composition is formulated with a buffer. 4. The use of claim 1, wherein said organism is a mammal. 5. The use of claim 4, wherein said mammal is a human.
    [Show full text]
  • Comparative Analysis of the Ubiquitin-Proteasome System in Homo Sapiens and Saccharomyces Cerevisiae
    Comparative Analysis of the Ubiquitin-proteasome system in Homo sapiens and Saccharomyces cerevisiae Inaugural-Dissertation zur Erlangung des Doktorgrades der Mathematisch-Naturwissenschaftlichen Fakultät der Universität zu Köln vorgelegt von Hartmut Scheel aus Rheinbach Köln, 2005 Berichterstatter: Prof. Dr. R. Jürgen Dohmen Prof. Dr. Thomas Langer Dr. Kay Hofmann Tag der mündlichen Prüfung: 18.07.2005 Zusammenfassung I Zusammenfassung Das Ubiquitin-Proteasom System (UPS) stellt den wichtigsten Abbauweg für intrazelluläre Proteine in eukaryotischen Zellen dar. Das abzubauende Protein wird zunächst über eine Enzym-Kaskade mit einer kovalent gebundenen Ubiquitinkette markiert. Anschließend wird das konjugierte Substrat vom Proteasom erkannt und proteolytisch gespalten. Ubiquitin besitzt eine Reihe von Homologen, die ebenfalls posttranslational an Proteine gekoppelt werden können, wie z.B. SUMO und NEDD8. Die hierbei verwendeten Aktivierungs- und Konjugations-Kaskaden sind vollständig analog zu der des Ubiquitin- Systems. Es ist charakteristisch für das UPS, daß sich die Vielzahl der daran beteiligten Proteine aus nur wenigen Proteinfamilien rekrutiert, die durch gemeinsame, funktionale Homologiedomänen gekennzeichnet sind. Einige dieser funktionalen Domänen sind auch in den Modifikations-Systemen der Ubiquitin-Homologen zu finden, jedoch verfügen diese Systeme zusätzlich über spezifische Domänentypen. Homologiedomänen lassen sich als mathematische Modelle in Form von Domänen- deskriptoren (Profile) beschreiben. Diese Deskriptoren können wiederum dazu verwendet werden, mit Hilfe geeigneter Verfahren eine gegebene Proteinsequenz auf das Vorliegen von entsprechenden Homologiedomänen zu untersuchen. Da die im UPS involvierten Homologie- domänen fast ausschließlich auf dieses System und seine Analoga beschränkt sind, können domänen-spezifische Profile zur Katalogisierung der UPS-relevanten Proteine einer Spezies verwendet werden. Auf dieser Basis können dann die entsprechenden UPS-Repertoires verschiedener Spezies miteinander verglichen werden.
    [Show full text]
  • 1Tt5 Lichtarge Lab 2006
    Pages 1–21 1tt5 Evolutionary trace report by report maker January 22, 2010 4 Notes on using trace results 19 4.1 Coverage 19 4.2 Known substitutions 19 4.3 Surface 19 4.4 Number of contacts 19 4.5 Annotation 19 4.6 Mutation suggestions 19 5 Appendix 19 5.1 File formats 19 5.2 Color schemes used 19 5.3 Credits 20 5.3.1 Alistat 20 5.3.2 CE 20 5.3.3 DSSP 20 5.3.4 HSSP 20 5.3.5 LaTex 20 5.3.6 Muscle 20 5.3.7 Pymol 20 5.4 Note about ET Viewer 20 5.5 Citing this work 20 CONTENTS 5.6 About report maker 20 5.7 Attachments 20 1 Introduction 1 2 Chain 1tt5A 1 1 INTRODUCTION 2.1 Q13564 overview 1 From the original Protein Data Bank entry (PDB id 1tt5): 2.2 Multiple sequence alignment for 1tt5A 1 Title: Structure of appbp1-uba3-ubc12n26: a unique e1-e2 interac- 2.3 Residue ranking in 1tt5A 2 tion required for optimal conjugation of the ubiquitin-like protein 2.4 Top ranking residues in 1tt5A and their position on nedd8 the structure 2 Compound: Mol id: 1; molecule: amyloid protein-binding pro- 2.4.1 Clustering of residues at 25% coverage. 2 tein 1; chain: a, c; synonym: appbp1; engineered: yes; mol id: 2; 2.4.2 Overlap with known functional surfaces at molecule: ubiquitin-activating enzyme e1c isoform 1; chain: b, d; 25% coverage. 3 fragment: residues 33-463; synonym: uba3, nedd8-activating enzyme 2.4.3 Possible novel functional surfaces at 25% huba3; engineered: yes; mol id: 3; molecule: ubiquitin-conjugating coverage.
    [Show full text]
  • NAE1 Antibody Cat
    NAE1 Antibody Cat. No.: 56-829 NAE1 Antibody NAE1 Antibody immunohistochemistry analysis in formalin fixed and paraffin embedded human brain tissue followed by peroxidase conjugation of the secondary antibody and DAB staining. Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human HOMOLOGY: Predicted species reactivity based on immunogen sequence: Monkey, Rat This NAE1 antibody is generated from rabbits immunized with a KLH conjugated synthetic IMMUNOGEN: peptide between 172-200 amino acids from the Central region of human NAE1. TESTED APPLICATIONS: IHC-P, WB For WB starting dilution is: 1:1000 APPLICATIONS: For IHC-P starting dilution is: 1:10~50 September 26, 2021 1 https://www.prosci-inc.com/nae1-antibody-56-829.html PREDICTED MOLECULAR 60 kDa WEIGHT: Properties This antibody is purified through a protein A column, followed by peptide affinity PURIFICATION: purification. CLONALITY: Polyclonal ISOTYPE: Rabbit Ig CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: Supplied in PBS with 0.09% (W/V) sodium azide. CONCENTRATION: batch dependent Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies STORAGE CONDITIONS: care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. Additional Info OFFICIAL SYMBOL: NAE1 NEDD8-activating enzyme E1 regulatory subunit, Amyloid beta precursor protein-binding ALTERNATE NAMES: protein 1, 59 kDa, APP-BP1, Amyloid protein-binding protein 1, Proto-oncogene protein 1, NAE1, APPBP1 ACCESSION NO.: Q13564 PROTEIN GI NO.: 50400302 GENE ID: 8883 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References The protein encoded by this gene binds to the beta-amyloid precursor protein.
    [Show full text]
  • UBA3 Antibody / UBE1C (F54550)
    UBA3 Antibody / UBE1C (F54550) Catalog No. Formulation Size F54550-0.4ML In 1X PBS, pH 7.4, with 0.09% sodium azide 0.4 ml F54550-0.08ML In 1X PBS, pH 7.4, with 0.09% sodium azide 0.08 ml Bulk quote request Availability 1-3 business days Species Reactivity Human, Mouse Format Purified Clonality Polyclonal (rabbit origin) Isotype Rabbit Ig Purity Antigen affinity purified UniProt Q8TBC4 Localization Nuclear, cytoplasmic Applications Western blot : 1:500-1:2000 Immunohistochemistry (FFPE) : 1:25 Limitations This UBA3 antibody is available for research use only. Western blot testing of human HL60 cell lysate with UBA3 antibody. Expected molecular weight ~52 kDa. Western blot testing of mouse brain lysate with UBA3 antibody. Expected molecular weight ~52 kDa. Western blot testing of 1) non-transfected and 2) transfected 293 cell lysate with UBA3 antibody. Predicted molecular weight ~52 kDa. IHC testing of FFPE human cancer tissue with UBA3 antibody. HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to staining. Description The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E1 ubiquitin-activating enzyme family. The encoded enzyme associates with AppBp1, an amyloid beta precursor protein binding protein, to form a heterodimer, and then the enzyme complex activates NEDD8, a ubiquitin-like protein, which regulates cell division, signaling and embryogenesis.
    [Show full text]
  • Program in Human Neutrophils Fails To
    Downloaded from http://www.jimmunol.org/ by guest on September 25, 2021 is online at: average * The Journal of Immunology Anaplasma phagocytophilum , 20 of which you can access for free at: 2005; 174:6364-6372; ; from submission to initial decision 4 weeks from acceptance to publication J Immunol doi: 10.4049/jimmunol.174.10.6364 http://www.jimmunol.org/content/174/10/6364 Insights into Pathogen Immune Evasion Mechanisms: Fails to Induce an Apoptosis Differentiation Program in Human Neutrophils Dori L. Borjesson, Scott D. Kobayashi, Adeline R. Whitney, Jovanka M. Voyich, Cynthia M. Argue and Frank R. DeLeo cites 28 articles Submit online. Every submission reviewed by practicing scientists ? is published twice each month by Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts http://jimmunol.org/subscription Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html http://www.jimmunol.org/content/suppl/2005/05/03/174.10.6364.DC1 This article http://www.jimmunol.org/content/174/10/6364.full#ref-list-1 Information about subscribing to The JI No Triage! Fast Publication! Rapid Reviews! 30 days* • Why • • Material References Permissions Email Alerts Subscription Supplementary The Journal of Immunology The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2005 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. This information is current as of September 25, 2021. The Journal of Immunology Insights into Pathogen Immune Evasion Mechanisms: Anaplasma phagocytophilum Fails to Induce an Apoptosis Differentiation Program in Human Neutrophils1 Dori L.
    [Show full text]
  • Tissue-Specific Disallowance of Housekeeping Genes
    Downloaded from genome.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Tissue-specific disallowance of housekeeping genes: the other face of cell differentiation Lieven Thorrez1,2,4, Ilaria Laudadio3, Katrijn Van Deun4, Roel Quintens1,4, Nico Hendrickx1,4, Mikaela Granvik1,4, Katleen Lemaire1,4, Anica Schraenen1,4, Leentje Van Lommel1,4, Stefan Lehnert1,4, Cristina Aguayo-Mazzucato5, Rui Cheng-Xue6, Patrick Gilon6, Iven Van Mechelen4, Susan Bonner-Weir5, Frédéric Lemaigre3, and Frans Schuit1,4,$ 1 Gene Expression Unit, Dept. Molecular Cell Biology, Katholieke Universiteit Leuven, 3000 Leuven, Belgium 2 ESAT-SCD, Department of Electrical Engineering, Katholieke Universiteit Leuven, 3000 Leuven, Belgium 3 Université Catholique de Louvain, de Duve Institute, 1200 Brussels, Belgium 4 Center for Computational Systems Biology, Katholieke Universiteit Leuven, 3000 Leuven, Belgium 5 Section of Islet Transplantation and Cell Biology, Joslin Diabetes Center, Harvard University, Boston, MA 02215, US 6 Unité d’Endocrinologie et Métabolisme, University of Louvain Faculty of Medicine, 1200 Brussels, Belgium $ To whom correspondence should be addressed: Frans Schuit O&N1 Herestraat 49 - bus 901 3000 Leuven, Belgium Email: [email protected] Phone: +32 16 347227 , Fax: +32 16 345995 Running title: Disallowed genes Keywords: disallowance, tissue-specific, tissue maturation, gene expression, intersection-union test Abbreviations: UTR UnTranslated Region H3K27me3 Histone H3 trimethylation at lysine 27 H3K4me3 Histone H3 trimethylation at lysine 4 H3K9ac Histone H3 acetylation at lysine 9 BMEL Bipotential Mouse Embryonic Liver Downloaded from genome.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Abstract We report on a hitherto poorly characterized class of genes which are expressed in all tissues, except in one.
    [Show full text]
  • The Hsp70 Chaperone System: Distinct Roles in Erythrocyte Formation and Maintenance
    SUPPLEMENTARY APPENDIX The Hsp70 chaperone system: distinct roles in erythrocyte formation and maintenance Yasith Mathangasinghe, 1 Bruno Fauvet, 2 Stephen M. Jane, 3,4 Pierre Goloubinoff 2 and Nadinath B. Nillegoda 1 1Australian Regenerative Medicine Institute, Monash University, Clayton, Victoria, Australia; 2Department of Plant Molecular Biology, Lau - sanne University, Lausanne, Switzerland; 3Central Clinical School, Monash University, Prahran, Victoria, Australia and 4Department of Hematology, Alfred Hospital, Monash University, Prahran, Victoria, Australia ©2021 Ferrata Storti Foundation. This is an open-access paper. doi:10.3324/haematol. 2019.233056 Received: July 29, 2019. Accepted: September 25, 2020. Pre-published: April 8, 2021. Correspondence: NADINATH B. NILLEGODA - [email protected] Supplementary material Table S1: Mass fractions of individual chaperone proteins from Jurkat cells and mature erythrocytes. Table S2: Mass fractions of chaperone groups in Jurkat cells and mature erythrocytes. Table S3: Mass fractions of individual ubiquitin proteasome system proteins from Jurkat cells and mature erythrocytes. Table S4: Mass fractions of ubiquitin proteasome system protein groups from Jurkat cells and mature erythrocytes. Figure S1: Expression profiles of selected chaperone systems in red cell progenitors, erythroblasts and mature erythrocytes1,2 versus unstressed and heat-shocked Jurkat cells,3 obtained from quantitative proteomics data. The black dotted line represents the median relative abundance of non-hemoglobin proteins in each cell type. Inset: zoom on the HSP70/110, HSP90 and HSP60 categories in unstressed versus heat- shocked Jurkat cells. CT indicates control/unstressed; HS stands for heat-shocked (41°C for 4 hours). References 1. Gautier E-F, Ducamp S, Leduc M, et al. Comprehensive proteomic analysis of human erythropoiesis.
    [Show full text]
  • GENE LIST ANTI-CORRELATED Systematic Common Description
    GENE LIST ANTI-CORRELATED Systematic Common Description 210348_at 4-Sep Septin 4 206155_at ABCC2 ATP-binding cassette, sub-family C (CFTR/MRP), member 2 221226_s_at ACCN4 Amiloride-sensitive cation channel 4, pituitary 207427_at ACR Acrosin 214957_at ACTL8 Actin-like 8 207422_at ADAM20 A disintegrin and metalloproteinase domain 20 216998_s_at ADAM5 synonym: tMDCII; Homo sapiens a disintegrin and metalloproteinase domain 5 (ADAM5) on chromosome 8. 216743_at ADCY6 Adenylate cyclase 6 206807_s_at ADD2 Adducin 2 (beta) 208544_at ADRA2B Adrenergic, alpha-2B-, receptor 38447_at ADRBK1 Adrenergic, beta, receptor kinase 1 219977_at AIPL1 211560_s_at ALAS2 Aminolevulinate, delta-, synthase 2 (sideroblastic/hypochromic anemia) 211004_s_at ALDH3B1 Aldehyde dehydrogenase 3 family, member B1 204705_x_at ALDOB Aldolase B, fructose-bisphosphate 220365_at ALLC Allantoicase 204664_at ALPP Alkaline phosphatase, placental (Regan isozyme) 216377_x_at ALPPL2 Alkaline phosphatase, placental-like 2 221114_at AMBN Ameloblastin, enamel matrix protein 206892_at AMHR2 Anti-Mullerian hormone receptor, type II 217293_at ANGPT1 Angiopoietin 1 210952_at AP4S1 Adaptor-related protein complex 4, sigma 1 subunit 207158_at APOBEC1 Apolipoprotein B mRNA editing enzyme, catalytic polypeptide 1 213611_at AQP5 Aquaporin 5 216219_at AQP6 Aquaporin 6, kidney specific 206784_at AQP8 Aquaporin 8 214490_at ARSF Arylsulfatase F 216204_at ARVCF Armadillo repeat gene deletes in velocardiofacial syndrome 214070_s_at ATP10B ATPase, Class V, type 10B 221240_s_at B3GNT4 UDP-GlcNAc:betaGal
    [Show full text]
  • Anti-NAE1 / APPBP1 Antibody (ARG59180)
    Product datasheet [email protected] ARG59180 Package: 100 μl anti-NAE1 / APPBP1 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes NAE1 / APPBP1 Tested Reactivity Hu Predict Reactivity Ms, Rat Tested Application IHC-P Host Rabbit Clonality Polyclonal Isotype IgG Target Name NAE1 / APPBP1 Antigen Species Human Immunogen KLH-conjugated synthetic peptide within aa. 430-459 of Human NAE1 / APPBP1. Conjugation Un-conjugated Alternate Names APP-BP1; APPBP1; A-116A10.1; Amyloid protein-binding protein 1; HPP1; Amyloid beta precursor protein-binding protein 1, 59 kDa; NEDD8-activating enzyme E1 regulatory subunit; ula-1; Proto- oncogene protein 1 Application Instructions Application table Application Dilution IHC-P 1:50 - 1:100 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Calculated Mw 60 kDa Properties Form Liquid Purification Purification with Protein G. Buffer PBS and 0.09% (W/V) Sodium azide. Preservative 0.09% (W/V) Sodium azide. Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C or below. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol NAE1 Gene Full Name NEDD8 activating enzyme E1 subunit 1 Background The protein encoded by this gene binds to the beta-amyloid precursor protein.
    [Show full text]