Supporting Information
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Supplementary Material for “Characterization of the Opossum Immune Genome Provides Insights Into the Evolution of the Mammalian Immune System”
Supplementary material for “Characterization of the opossum immune genome provides insights into the evolution of the mammalian immune system” Katherine Belov1*, Claire E. Sanderson1, Janine E. Deakin2, Emily S.W. Wong1, Daniel Assange3, Kaighin A. McColl3, Alex Gout3,4, Bernard de Bono5, Terence P. Speed3, John Trowsdale5, Anthony T. Papenfuss3 1. Faculty of Veterinary Science, University of Sydney, Sydney, Australia 2. ARC Centre for Kangaroo Genomics, Research School of Biological Sciences, The Australian National University, Canberra, Australia 3. Bioinformatics Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Australia 4. Department of Medical Biology, The University of Melbourne, Parkville, Australia 5. Immunology Division, University of Cambridge, Cambridge, UK *Corresponding author: K. Belov, Faculty of Veterinary Science, University of Sydney, NSW 2006, Australia ph 61 2 9351 3454, fx 61 2 9351 3957, email [email protected] MHC paralogous regions Only 36 of the 114 genes in the opossum MHC have paralogs in one of the three paralogous regions (Supplementary Table 1). Genes represented in at least three of the four paralogous regions (13 genes) were used to compare gene order, revealing rearrangements between the four regions in opossum. Table 1: MHC genes with paralogs on opossum chromosomes 1, 2 and 3, corresponding to MHC paralogous regions on human chromosomes 9, 1 and 19 respectively. MHC Chromosome 1 Chromosome 2 Chromosome 3 (Human Chr 9) (Human Chr 1) (Human Chr 19) AGPAT1 AGPAT2 AIF1 C9orf58 ATP6V1G2 ATP6V1G1 ATP6V1G3 B3GALT4 B3GALT2 BAT1 DDX39 BAT2 KIAA0515 BAT2D1 BRD2 BRD3 BRDT BRD4 C4 C5 C3 SLC44A4 SLC44A5 SLC44A2 CLIC1 CLIC3 CLIC4 COL11A2 COL5A1 COL11A1 COL5A3 CREBL1 ATF6 DDAH2 DDAH1 DDR1 DDR2 EGFL8 EGFL7 EHMT2 EHMT1 GPX5 GPX4 MHC Class I CD1 HSPA1A HSPA5 MDC1 PRG4 NOTCH4 NOTCH1 NOTCH2 NOTCH3 PBX2 PBX3 PBX1 PBX4 PHF1 MTF2 PRSS16 DPP7 PSMB9 PSMB7 RGL2 RALGDS RGL1 RGL3 RING1 RNF2 RXRB RXRA RXRG SYNGAP1 RASAL2 TAP ABCA2 TNF/LTA/LTB TNFSF8/TNFSF15 TNFSF4 CD70/TNFSF9/ TNFSF14/ TNXB TNC TNR Table 2. -
Decreased Plasma Concentrations of Apolipoprotein M in Sepsis And
Kumaraswamy et al. Critical Care 2012, 16:R60 http://ccforum.com/content/16/2/R60 RESEARCH Open Access Decreased plasma concentrations of apolipoprotein M in sepsis and systemic inflammatory response syndromes Sunil B Kumaraswamy1, Adam Linder2, Per Åkesson2 and Björn Dahlbäck1* Abstract Introduction: Apolipoprotein M (apoM) is present in 5% of high-density lipoprotein (HDL) particles in plasma. It is a carrier of sphingosine-1-phosphate (S1P), which is important for vascular barrier protection. The aim was to determine the plasma concentrations of apoM during sepsis and systemic inflammatory response syndrome (SIRS) and correlate them to levels of apolipoprotein A-I (apoA1), apolipoprotein B (apoB), HDL-, and low-density lipoprotein (LDL)-cholesterol. Methods: Plasma samples from patients with (1), severe sepsis with shock (n = 26); (2), severe sepsis without shock (n = 44); (3), sepsis (n = 100); (4), infections without SIRS (n = 43); and (5) SIRS without infection (n = 20) were analyzed. The concentrations of apoM, apoA1, and apoB were measured with enzyme-linked immunosorbent assays (ELISAs). Total, HDL-, and LDL-cholesterol concentrations were measured with a commercial HDL/LDL cholesterol test. Results: ApoM concentrations correlated negatively to acute-phase markers. Thus, apoM behaved as a negative acute-phase protein. Decreased values were observed in all patient groups (P < 0.0001), with the most drastic decreases observed in the severely sick patients. ApoM levels correlated strongly to those of apoA1, apoB, HDL, and LDL cholesterol. The HDL and LDL cholesterol levels were low in all patient groups, as compared with controls (P < 0.0001), in particular, HDL cholesterol. ApoA1 and apoB concentrations were low only in the more severely affected patients. -
Stelios Pavlidis3, Matthew Loza3, Fred Baribaud3, Anthony
Supplementary Data Th2 and non-Th2 molecular phenotypes of asthma using sputum transcriptomics in UBIOPRED Chih-Hsi Scott Kuo1.2, Stelios Pavlidis3, Matthew Loza3, Fred Baribaud3, Anthony Rowe3, Iaonnis Pandis2, Ana Sousa4, Julie Corfield5, Ratko Djukanovic6, Rene 7 7 8 2 1† Lutter , Peter J. Sterk , Charles Auffray , Yike Guo , Ian M. Adcock & Kian Fan 1†* # Chung on behalf of the U-BIOPRED consortium project team 1Airways Disease, National Heart & Lung Institute, Imperial College London, & Biomedical Research Unit, Biomedical Research Unit, Royal Brompton & Harefield NHS Trust, London, United Kingdom; 2Department of Computing & Data Science Institute, Imperial College London, United Kingdom; 3Janssen Research and Development, High Wycombe, Buckinghamshire, United Kingdom; 4Respiratory Therapeutic Unit, GSK, Stockley Park, United Kingdom; 5AstraZeneca R&D Molndal, Sweden and Areteva R&D, Nottingham, United Kingdom; 6Faculty of Medicine, Southampton University, Southampton, United Kingdom; 7Faculty of Medicine, University of Amsterdam, Amsterdam, Netherlands; 8European Institute for Systems Biology and Medicine, CNRS-ENS-UCBL, Université de Lyon, France. †Contributed equally #Consortium project team members are listed under Supplementary 1 Materials *To whom correspondence should be addressed: [email protected] 2 List of the U-BIOPRED Consortium project team members Uruj Hoda & Christos Rossios, Airways Disease, National Heart & Lung Institute, Imperial College London, UK & Biomedical Research Unit, Biomedical Research Unit, Royal -
Viewed the Thesis/Dissertation in Its Final Electronic Format and Certify That It Is an Accurate Copy of the Document Reviewed and Approved by the Committee
U UNIVERSITY OF CINCINNATI Date: I, , hereby submit this original work as part of the requirements for the degree of: in It is entitled: Student Signature: This work and its defense approved by: Committee Chair: Approval of the electronic document: I have reviewed the Thesis/Dissertation in its final electronic format and certify that it is an accurate copy of the document reviewed and approved by the committee. Committee Chair signature: Investigation of Phosphorylated Proteins and Peptides in Human Cerebrospinal Fluid via High-Performance Liquid Chromatography Coupled to Elemental and Molecular Mass Spectrometry A thesis submitted to the Graduate School of the University of Cincinnati In partial fulfillment of the Requirements for the degree of MASTER OF SCIENCE In the Department of Chemistry of the College of Arts and Sciences By ORVILLE DEAN STUART B.S., Chemistry The University of Texas at Tyler, Tyler, Texas May 2006 Committee Chair: Joseph A. Caruso, Ph.D Abstract Cerebrospinal fluid (CSF) surrounds and serves as a protective media for the brain and central nervous system (CNS). This fluid remains isolated from other biological matrices in normal bodily conditions, therefore, an in depth analysis of CSF has the potential to reveal important details and malfunctions of many diseases that plague the nervous system. Because phosphorylation of a wide variety of proteins governs the activity of biological enzymes and systems, a method for the detection of 31P in proteins found in human cerebrospinal fluid by high-performance liquid chromatography (HPLC) coupled to inductively coupled plasma mass spectrometry (ICPMS) is described. Specifically, it is of interest to compare phosphorylated proteins/peptides from patients suffering from post subarachnoid hemorrhage (SAH) arterial vasospasms against CSF from non-diseased patients. -
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. -
ABCG1 (ABC8), the Human Homolog of the Drosophila White Gene, Is a Regulator of Macrophage Cholesterol and Phospholipid Transport
ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a regulator of macrophage cholesterol and phospholipid transport Jochen Klucken*, Christa Bu¨ chler*, Evelyn Orso´ *, Wolfgang E. Kaminski*, Mustafa Porsch-Ozcu¨ ¨ ru¨ mez*, Gerhard Liebisch*, Michael Kapinsky*, Wendy Diederich*, Wolfgang Drobnik*, Michael Dean†, Rando Allikmets‡, and Gerd Schmitz*§ *Institute for Clinical Chemistry and Laboratory Medicine, University of Regensburg, 93042 Regensburg, Germany; †National Cancer Institute, Laboratory of Genomic Diversity, Frederick, MD 21702-1201; and ‡Departments of Ophthalmology and Pathology, Columbia University, Eye Research Addition, New York, NY 10032 Edited by Jan L. Breslow, The Rockefeller University, New York, NY, and approved November 3, 1999 (received for review June 14, 1999) Excessive uptake of atherogenic lipoproteins such as modified low- lesterol transport. Although several effector molecules have been density lipoprotein complexes by vascular macrophages leads to proposed to participate in macrophage cholesterol efflux (6, 9), foam cell formation, a critical step in atherogenesis. Cholesterol efflux including endogenous apolipoprotein E (10) and the cholesteryl mediated by high-density lipoproteins (HDL) constitutes a protective ester transfer protein (11), the detailed molecular mechanisms mechanism against macrophage lipid overloading. The molecular underlying cholesterol export in these cells have not yet been mechanisms underlying this reverse cholesterol transport process are characterized. currently not fully understood. To identify effector proteins that are Recently, mutations of the ATP-binding cassette (ABC) trans- involved in macrophage lipid uptake and release, we searched for porter ABCA1 gene have been causatively linked to familial HDL genes that are regulated during lipid influx and efflux in human deficiency and Tangier disease (12–14). -
743914V1.Full.Pdf
bioRxiv preprint doi: https://doi.org/10.1101/743914; this version posted August 24, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 Cross-talks of glycosylphosphatidylinositol biosynthesis with glycosphingolipid biosynthesis 2 and ER-associated degradation 3 4 Yicheng Wang1,2, Yusuke Maeda1, Yishi Liu3, Yoko Takada2, Akinori Ninomiya1, Tetsuya 5 Hirata1,2,4, Morihisa Fujita3, Yoshiko Murakami1,2, Taroh Kinoshita1,2,* 6 7 1Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan 8 2WPI Immunology Frontier Research Center, Osaka University, Suita, Osaka 565-0871, 9 Japan 10 3Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, 11 School of Biotechnology, Jiangnan University, Wuxi, Jiangsu 214122, China 12 4Current address: Center for Highly Advanced Integration of Nano and Life Sciences (G- 13 CHAIN), Gifu University, 1-1 Yanagido, Gifu-City, Gifu 501-1193, Japan 14 15 *Correspondence and requests for materials should be addressed to T.K. (email: 16 [email protected]) 17 18 19 Glycosylphosphatidylinositol (GPI)-anchored proteins and glycosphingolipids interact with 20 each other in the mammalian plasma membranes, forming dynamic microdomains. How their 21 interaction starts in the cells has been unclear. Here, based on a genome-wide CRISPR-Cas9 22 genetic screen for genes required for GPI side-chain modification by galactose in the Golgi 23 apparatus, we report that b1,3-galactosyltransferase 4 (B3GALT4), also called GM1 24 ganglioside synthase, additionally functions in transferring galactose to the N- 25 acetylgalactosamine side-chain of GPI. -
CSNK2B Monoclonal Antibody Catalog Number:67866-1-Ig
For Research Use Only CSNK2B Monoclonal antibody www.ptgcn.com Catalog Number:67866-1-Ig Catalog Number: GenBank Accession Number: CloneNo.: Basic Information 67866-1-Ig BC112017 1B5A6 Size: GeneID (NCBI): Recommended Dilutions: 1000 μg/ml 1460 WB 1:5000-1:20000 Source: Full Name: IF 1:200-1:800 Mouse casein kinase 2, beta polypeptide Isotype: Calculated MW: IgG1 215 aa, 25 kDa Purification Method: Observed MW: Protein G purification 27 kDa Immunogen Catalog Number: AG19180 Applications Tested Applications: Positive Controls: IF, WB,ELISA WB : A549 cells; LNCaP cells, HeLa cells, Jurkat cells, Species Specificity: pig brain tissue, rat brain tissue, mouse brain tissue Human, mouse, rat, pig IF : HeLa cells; CSNK2B is a ubiquitous protein kinase which regulates metabolic pathways, signal transduction, transcription, Background Information translation, and replication. The enzyme is composed of three subunits, alpha, alpha prime and beta, which form a tetrameric holoenzyme. The alpha and alpha prime subunits are catalytic, while the beta subunit serves regulatory functions. The enzyme localizes to the endoplasmic reticulum and the Golgi apparatus. It participates in Wnt signaling, and plays a complex role in regulating the basal catalytic activity of the alpha subunit. Storage: Storage Store at -20ºC. Stable for one year after shipment. Storage Buffer: PBS with 0.02% sodium azide and 50% glycerol pH 7.3. Aliquoting is unnecessary for -20ºC storage For technical support and original validation data for this product please contact: This product is exclusively available under Proteintech T: 4006900926 E: [email protected] W: ptgcn.com Group brand and is not available to purchase from any other manufacturer. -
Genome-Wide Analysis of Differential Transcriptional and Epigenetic
bioRxiv preprint doi: https://doi.org/10.1101/083246; this version posted October 26, 2016. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. 1 Genome-wide Analysis of Differential Transcriptional and 2 Epigenetic Variability Across Human Immune Cell Types 3 Simone Ecker,1,2,* Lu Chen,3,4 Vera Pancaldi,1 Frederik O. Bagger,4,5,6 José María Fernández,1 Enrique Carrillo de 4 Santa Pau,1 David Juan,1 Alice L. Mann,3 Stephen Watt,3 Francesco Paolo Casale,6 Nikos Sidiropoulos,7,8,9 Nicolas 5 Rapin,7,8,9 Angelika Merkel,10 BLUEPRINT Consortium, Henk Stunnenberg,11 Oliver Stegle,6 Mattia Frontini,4,5,12 Kate 6 Downes,4,5 Tomi Pastinen,13 Taco W. Kuijpers,14,15 Daniel Rico,1,17 Alfonso Valencia,1,17 Stephan Beck,2,17 Nicole 7 Soranzo3,4,17,* and Dirk S. Paul2,16,17,* 8 9 1Structural Biology and Biocomputing Programme, Spanish National Cancer Research Center (CNIO), Melchor Fernández Almagro 3, 28029 Madrid, Spain 10 2UCL Cancer Institute, University College London, 72 Huntley Street, London, WC1E 6BT, UK 11 3Department of Human Genetics, Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1HH, UK 12 4Department of Haematology, University of Cambridge, Cambridge Biomedical Campus, Long Road, Cambridge, CB2 0PT, UK 13 5National Health Service (NHS) Blood and Transplant, Cambridge Biomedical Campus, Long Road, Cambridge, CB2 -
A Comprehensive Mapping of the Structure and Gene Organisation in the Sheep MHC Class I Region N
Siva Subramaniam et al. BMC Genomics (2015) 16:810 DOI 10.1186/s12864-015-1992-4 RESEARCH ARTICLE Open Access A comprehensive mapping of the structure and gene organisation in the sheep MHC class I region N. Siva Subramaniam1, EF Morgan1, JD Wetherall1, MJ Stear2,3* and DM Groth1 Abstract Background: The major histocompatibility complex (MHC) is a chromosomal region that regulates immune responsiveness in vertebrates. This region is one of the most important for disease resistance because it has been associated with resistance or susceptibility to a wide variety of diseases and because the MHC often accounts for more of the variance than other loci. Selective breeding for disease resistance is becoming increasingly common in livestock industries, and it is important to determine how this will influence MHC polymorphism and resistance to diseases that are not targeted for selection. However, in sheep the order and sequence of the protein coding genes is controversial. Yet this information is needed to determine precisely how the MHC influences resistance and susceptibility to disease. Methods: CHORI bacterial artificial chromosomes (BACs) known to contain sequences from the sheep MHC class I region were sub-cloned, and the clones partially sequenced. The resulting sequences were analysed and re-assembled to identify gene content and organisation within each BAC. The low resolution MHC class I physical map was then compared to the cattle reference genome, the Chinese Merino sheep MHC map published by Gao, et al. (2010) and the recently available sheep reference genome. Results: Immune related class I genes are clustered into 3 blocks; beta, kappa and a novel block not previously identified in other organisms. -
The Porcine Major Histocompatibility Complex and Related Paralogous Regions: a Review Patrick Chardon, Christine Renard, Claire Gaillard, Marcel Vaiman
The porcine Major Histocompatibility Complex and related paralogous regions: a review Patrick Chardon, Christine Renard, Claire Gaillard, Marcel Vaiman To cite this version: Patrick Chardon, Christine Renard, Claire Gaillard, Marcel Vaiman. The porcine Major Histocom- patibility Complex and related paralogous regions: a review. Genetics Selection Evolution, BioMed Central, 2000, 32 (2), pp.109-128. 10.1051/gse:2000101. hal-00894302 HAL Id: hal-00894302 https://hal.archives-ouvertes.fr/hal-00894302 Submitted on 1 Jan 2000 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. Genet. Sel. Evol. 32 (2000) 109–128 109 c INRA, EDP Sciences Review The porcine Major Histocompatibility Complex and related paralogous regions: a review Patrick CHARDON, Christine RENARD, Claire ROGEL GAILLARD, Marcel VAIMAN Laboratoire de radiobiologie et d’etude du genome, Departement de genetique animale, Institut national de la recherche agronomique, Commissariat al’energie atomique, 78352, Jouy-en-Josas Cedex, France (Received 18 November 1999; accepted 17 January 2000) Abstract – The physical alignment of the entire region of the pig major histocompat- ibility complex (MHC) has been almost completed. In swine, the MHC is called the SLA (swine leukocyte antigen) and most of its class I region has been sequenced. -
Genome-Wide Gene and Pathway Analysis
European Journal of Human Genetics (2010) 18, 1045–1053 & 2010 Macmillan Publishers Limited All rights reserved 1018-4813/10 www.nature.com/ejhg ARTICLE Genome-wide gene and pathway analysis Li Luo1, Gang Peng1, Yun Zhu2, Hua Dong1,2, Christopher I Amos3 and Momiao Xiong*,1 Current GWAS have primarily focused on testing association of single SNPs. To only test for association of single SNPs has limited utility and is insufficient to dissect the complex genetic structure of many common diseases. To meet conceptual and technical challenges raised by GWAS, we suggest gene and pathway-based GWAS as complementary to the current single SNP-based GWAS. This publication develops three statistics for testing association of genes and pathways with disease: linear combination test, quadratic test and decorrelation test, which take correlations among SNPs within a gene or genes within a pathway into account. The null distribution of the suggested statistics is examined and the statistics are applied to GWAS of rheumatoid arthritis in the Wellcome Trust Case–Control Consortium and the North American Rheumatoid Arthritis Consortium studies. The preliminary results show that the suggested gene and pathway-based GWAS offer several remarkable features. First, not only can they identify the genes that have large genetic effects, but also they can detect new genes in which each single SNP conferred a small amount of disease risk, and their joint actions can be implicated in the development of diseases. Second, gene and pathway-based analysis can allow the formation of the core of pathway definition of complex diseases and unravel the functional bases of an association finding.