( 12 ) United States Patent
Total Page:16
File Type:pdf, Size:1020Kb

Load more
Recommended publications
-
Transcriptomic and Proteomic Profiling Provides Insight Into
BASIC RESEARCH www.jasn.org Transcriptomic and Proteomic Profiling Provides Insight into Mesangial Cell Function in IgA Nephropathy † † ‡ Peidi Liu,* Emelie Lassén,* Viji Nair, Celine C. Berthier, Miyuki Suguro, Carina Sihlbom,§ † | † Matthias Kretzler, Christer Betsholtz, ¶ Börje Haraldsson,* Wenjun Ju, Kerstin Ebefors,* and Jenny Nyström* *Department of Physiology, Institute of Neuroscience and Physiology, §Proteomics Core Facility at University of Gothenburg, University of Gothenburg, Gothenburg, Sweden; †Division of Nephrology, Department of Internal Medicine and Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan; ‡Division of Molecular Medicine, Aichi Cancer Center Research Institute, Nagoya, Japan; |Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, Sweden; and ¶Integrated Cardio Metabolic Centre, Karolinska Institutet Novum, Huddinge, Sweden ABSTRACT IgA nephropathy (IgAN), the most common GN worldwide, is characterized by circulating galactose-deficient IgA (gd-IgA) that forms immune complexes. The immune complexes are deposited in the glomerular mesangium, leading to inflammation and loss of renal function, but the complete pathophysiology of the disease is not understood. Using an integrated global transcriptomic and proteomic profiling approach, we investigated the role of the mesangium in the onset and progression of IgAN. Global gene expression was investigated by microarray analysis of the glomerular compartment of renal biopsy specimens from patients with IgAN (n=19) and controls (n=22). Using curated glomerular cell type–specific genes from the published literature, we found differential expression of a much higher percentage of mesangial cell–positive standard genes than podocyte-positive standard genes in IgAN. Principal coordinate analysis of expression data revealed clear separation of patient and control samples on the basis of mesangial but not podocyte cell–positive standard genes. -
Supplemental Information For
Supplemental Information for: Gene Expression Profiling of Pediatric Acute Myelogenous Leukemia Mary E. Ross, Rami Mahfouz, Mihaela Onciu, Hsi-Che Liu, Xiaodong Zhou, Guangchun Song, Sheila A. Shurtleff, Stanley Pounds, Cheng Cheng, Jing Ma, Raul C. Ribeiro, Jeffrey E. Rubnitz, Kevin Girtman, W. Kent Williams, Susana C. Raimondi, Der-Cherng Liang, Lee-Yung Shih, Ching-Hon Pui & James R. Downing Table of Contents Section I. Patient Datasets Table S1. Diagnostic AML characteristics Table S2. Cytogenetics Summary Table S3. Adult diagnostic AML characteristics Table S4. Additional T-ALL characteristics Section II. Methods Table S5. Summary of filtered probe sets Table S6. MLL-PTD primers Additional Statistical Methods Section III. Genetic Subtype Discriminating Genes Figure S1. Unsupervised Heirarchical clustering Figure S2. Heirarchical clustering with class discriminating genes Table S7. Top 100 probe sets selected by SAM for t(8;21)[AML1-ETO] Table S8. Top 100 probe sets selected by SAM for t(15;17) [PML-RARα] Table S9. Top 63 probe sets selected by SAM for inv(16) [CBFβ-MYH11] Table S10. Top 100 probe sets selected by SAM for MLL chimeric fusion genes Table S11. Top 100 probe sets selected by SAM for FAB-M7 Table S12. Top 100 probe sets selected by SAM for CBF leukemias (whole dataset) Section IV. MLL in combined ALL and AML dataset Table S13. Top 100 probe sets selected by SAM for MLL chimeric fusions irrespective of blast lineage (whole dataset) Table S14. Class discriminating genes for cases with an MLL chimeric fusion gene that show uniform high expression, irrespective of blast lineage Section V. -
Prokaryotic Origins of the Non-Animal Peroxidase Superfamily and Organelle-Mediated Transmission to Eukaryotes
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Genomics 89 (2007) 567–579 www.elsevier.com/locate/ygeno Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes Filippo Passardi a, Nenad Bakalovic a, Felipe Karam Teixeira b, Marcia Margis-Pinheiro b,c, ⁎ Claude Penel a, Christophe Dunand a, a Laboratory of Plant Physiology, University of Geneva, Quai Ernest-Ansermet 30, CH-1211 Geneva 4, Switzerland b Department of Genetics, Institute of Biology, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil c Department of Genetics, Federal University of Rio Grande do Sul, Rio Grande do Sul, Brazil Received 16 June 2006; accepted 18 January 2007 Available online 13 March 2007 Abstract Members of the superfamily of plant, fungal, and bacterial peroxidases are known to be present in a wide variety of living organisms. Extensive searching within sequencing projects identified organisms containing sequences of this superfamily. Class I peroxidases, cytochrome c peroxidase (CcP), ascorbate peroxidase (APx), and catalase peroxidase (CP), are known to be present in bacteria, fungi, and plants, but have now been found in various protists. CcP sequences were detected in most mitochondria-possessing organisms except for green plants, which possess only ascorbate peroxidases. APx sequences had previously been observed only in green plants but were also found in chloroplastic protists, which acquired chloroplasts by secondary endosymbiosis. CP sequences that are known to be present in prokaryotes and in Ascomycetes were also detected in some Basidiomycetes and occasionally in some protists. -
New Automatically Built Profiles for a Better Understanding of the Peroxidase Superfamily Evolution
University of Geneva Practical training report submitted for the Master Degree in Proteomics and Bioinformatics New automatically built profiles for a better understanding of the peroxidase superfamily evolution presented by Dominique Koua Supervisors: Dr Christophe DUNAND Dr Nicolas HULO Laboratory of Plant Physiology, Dr Christian J.A. SIGRIST University of Geneva Swiss Institute of Bioinformatics PROSITE group. Geneva, April, 18th 2008 Abstract Motivation: Peroxidases (EC 1.11.1.x), which are encoded by small or large multigenic families, are involved in several important physiological and developmental processes. These proteins are extremely widespread and present in almost all living organisms. An important number of haem and non-haem peroxidase sequences are annotated and classified in the peroxidase database PeroxiBase (http://peroxibase.isb-sib.ch). PeroxiBase contains about 5800 peroxidase sequences classified as haem peroxidases and non-haem peroxidases and distributed between thirteen superfamilies and fifty subfamilies, (Passardi et al., 2007). However, only a few classification tools are available for the characterisation of peroxidase sequences: InterPro motifs, PRINTS and specifically designed PROSITE profiles. However, these PROSITE profiles are very global and do not allow the differenciation between very close subfamily sequences nor do they allow the prediction of specific cellular localisations. Due to the rapid growth in the number of available sequences, there is a need for continual updates and corrections of peroxidase protein sequences as well as for new tools that facilitate acquisition and classification of existing and new sequences. Currently, the PROSITE generalised profile building manner and their usage do not allow the differentiation of sequences from subfamilies showing a high degree of similarity. -
Characterization of Lignin-Modifying Enzymes of the Selective White-Rot
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Helsingin yliopiston digitaalinen arkisto Characterization of the lignin-modifying enzymes of the selective white-rot fungus Physisporinus rivulosus Terhi K. Hakala Department of Applied Chemistry and Microbiology Division of Microbiology Faculty of Agriculture and Forestry and Viikki Graduate School in Biosciences University of Helsinki Academic dissertation To be presented, with the permission of the Faculty of Agriculture and Forestry of the University of Helsinki, for public criticism in Auditorium 1, Viikki Infocenter, Viikinkaari 11, on October 19th 2007 at 12 o’clock noon. Helsinki 2007 Supervisor: Professor Annele Hatakka Department of Applied Chemistry and Microbiology University of Helsinki Finland Reviewers: Docent Kristiina Kruus VTT Espoo, Finland Professor Martin Hofrichter Environmental Biotechnology International Graduate School Zittau, Germany Opponent: Professor Kurt Messner Institute of Chemical Engineering Vienna University of Technology Wien, Austria ISSN 1795-7079 ISBN 978-952-10-4172-3 (paperback) ISBN 978-952-10-4173-0 (PDF) Helsinki University Printing House Helsinki 2007 Cover photo: Spruce wood chips (KCL, Lea Kurlin) 2 Contents Contents..................................................................................................................................................3 List of original publications....................................................................................................................4 -
Ioides Species Kazuhiro Takagi, Kunihiko Fujii, Ken-Ichi Yamazaki, Naoki Harada and Akio Iwasaki Download PDF (313.9 KB) View HTML
Aquaculture Journals – Table of Contents With the financial support of Flemish Interuniversity Councel Aquaculture Journals – Table of Contents September 2012 Information of interest !! Animal Feed Science and Technology * Antimicrobial Agents and Chemotherapy Applied and Environmental Microbiology Applied Microbiology and Biotechnology Aqua Aquaculture * Aquaculture Economics & Management Aquacultural Engineering * Aquaculture International * Aquaculture Nutrition * Aquaculture Research * Current Opinion in Microbiology * Diseases of Aquatic Organisms * Fish & Shellfish Immunology * Fisheries Science * Hydrobiologia * Indian Journal of Fisheries International Journal of Aquatic Science Journal of Applied Ichthyology * Journal of Applied Microbiology * Journal of Applied Phycology Journal of Aquaculture Research and Development Journal of Experimental Marine Biology and Ecology * Journal of Fish Biology Journal of Fish Diseases * Journal of Invertebrate Pathology* Journal of Microbial Ecology* Aquaculture Journals Page: 1 of 331 Aquaculture Journals – Table of Contents Journal of Microbiological Methods Journal of Shellfish Research Journal of the World Aquaculture Society Letters in Applied Microbiology * Marine Biology * Marine Biotechnology * Nippon Suisan Gakkaishi Reviews in Aquaculture Trends in Biotechnology * Trends in Microbiology * * full text available Aquaculture Journals Page: 2 of 331 Aquaculture Journals – Table of Contents BibMail Information of Interest - September, 2012 Abstracts of papers presented at the XV International -
Uremic Toxicity of Advanced Glycation End Products in CKD
BRIEF REVIEW www.jasn.org Uremic Toxicity of Advanced Glycation End Products in CKD † ‡ ‡ Andréa E.M. Stinghen,* Ziad A. Massy,* Helen Vlassara, § Gary E. Striker, § and | Agnès Boullier* *Institut National de la Santé et de la Recherche Médicale (INSERM) U-1088, Jules Verne University of Picardie, Amiens, France; †Division of Nephrology, Ambroise Paré University Medical Center, Assistance Publique-Hôpitaux de Paris (APHP), University of Paris Ouest, University Versailles-Saint Quentin, Boulogne Billancourt/Paris, France; ‡Division of Experimental Diabetes and Aging, Departments of Geriatrics and Palliative Care and Medicine and §Division of Experimental Diabetes and Aging, Department of Geriatrics and Aging and Division of Nephrology, Department of Medicine, Icahn School of Medicine, New York, New York; and |Biochemistry Laboratory, Amiens University Medical Center, Amiens, France ABSTRACT Advanced glycation end products (AGEs), a heterogeneous group of compounds include the 1,2-dicarbonyl compounds formed by nonenzymatic glycation reactions between reducing sugars and amino glyoxal and methylglyoxal (MG), a highly acids, lipids, or DNA, are formed not only in the presence of hyperglycemia, but also in reactive dicarbonyl compound.7 At least diseases associated with high levels of oxidative stress, such as CKD. In chronic renal 20 different types of AGE have been de- failure, higher circulating AGE levels result from increased formation and decreased scribed: N-carboxymethyllysine (CML), renal clearance. Interactions between AGEs and -
Protein Radicals in Fungal Versatile Peroxidase
Supplemental Material can be found at: http://www.jbc.org/cgi/content/full/M808069200/DC1 THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 284, NO. 12, pp. 7986–7994, March 20, 2009 © 2009 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in the U.S.A. Protein Radicals in Fungal Versatile Peroxidase CATALYTIC TRYPTOPHAN RADICAL IN BOTH COMPOUND I AND COMPOUND II AND STUDIES ON W164Y, W164H, AND W164S VARIANTS*□S Received for publication, October 21, 2008, and in revised form, December 15, 2008 Published, JBC Papers in Press, January 21, 2009, DOI 10.1074/jbc.M808069200 Francisco J. Ruiz-Duen˜as‡1, Rebecca Pogni§2, María Morales‡3, Stefania Giansanti§4, María J. Mate‡, Antonio Romero‡, María Jesu´ s Martínez‡, Riccardo Basosi§, and Angel T. Martínez‡5 From the ‡Centro de Investigaciones Biolo´gicas (CIB), Consejo Superior de Investigaciones Científicas (CSIC), E-28040 Madrid, Spain and the §Department of Chemistry, University of Siena, 53100 Siena, Italy Lignin-degrading peroxidases, a group of biotechnologically Lignin degradation, a key step for carbon recycling in land Downloaded from interesting enzymes, oxidize high redox potential aromatics via ecosystems and a central issue for industrial use of lignocellu- an exposed protein radical. Low temperature EPR of Pleurotus losic biomass (e.g. in paper pulp manufacture and bioethanol eryngii versatile peroxidase (VP) revealed, for the first time in a production), is initiated in nature by 1-electron oxidation of the fungal peroxidase, the presence of a tryptophanyl radical in both benzenic rings of lignin by specialized high redox potential fun- the two-electron (VPI) and the one-electron (VPII) activated gal peroxidases (1–5). -
Metabolic Network-Based Stratification of Hepatocellular Carcinoma Reveals Three Distinct Tumor Subtypes
Metabolic network-based stratification of hepatocellular carcinoma reveals three distinct tumor subtypes Gholamreza Bidkhoria,b,1, Rui Benfeitasa,1, Martina Klevstigc,d, Cheng Zhanga, Jens Nielsene, Mathias Uhlena, Jan Borenc,d, and Adil Mardinoglua,b,e,2 aScience for Life Laboratory, KTH Royal Institute of Technology, SE-17121 Stockholm, Sweden; bCentre for Host-Microbiome Interactions, Dental Institute, King’s College London, SE1 9RT London, United Kingdom; cDepartment of Molecular and Clinical Medicine, University of Gothenburg, SE-41345 Gothenburg, Sweden; dThe Wallenberg Laboratory, Sahlgrenska University Hospital, SE-41345 Gothenburg, Sweden; and eDepartment of Biology and Biological Engineering, Chalmers University of Technology, SE-41296 Gothenburg, Sweden Edited by Sang Yup Lee, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea, and approved November 1, 2018 (received for review April 27, 2018) Hepatocellular carcinoma (HCC) is one of the most frequent forms of of markers associated with recurrence and poor prognosis (13–15). liver cancer, and effective treatment methods are limited due to Moreover, genome-scale metabolic models (GEMs), collections tumor heterogeneity. There is a great need for comprehensive of biochemical reactions, and associated enzymes and transporters approaches to stratify HCC patients, gain biological insights into have been successfully used to characterize the metabolism of subtypes, and ultimately identify effective therapeutic targets. We HCC, as well as identify drug targets for HCC patients (11, 16–18). stratified HCC patients and characterized each subtype using tran- For instance, HCC tumors have been stratified based on the uti- scriptomics data, genome-scale metabolic networks and network lization of acetate (11). Analysis of HCC metabolism has also led topology/controllability analysis. -
Ομεηδναλαγωγηθά Έλδπκα Ωο Πξόηππα Εθαξκνγήο Ηεο Κεζόδνπ QSAR (Quantitative Structure-Activity Relations)
ΔΘΝΗΚΟ ΚΑΗ ΚΑΠΟΓΗΣΡΗΑΚΟ ΠΑΝΔΠΗΣΖΜΗΟ ΑΘΖΝΩΝ ΥΟΛΖ ΘΔΣΗΚΩΝ ΔΠΗΣΖΜΩΝ ΣΜΖΜΑ ΥΖΜΔΗΑ ΜΔΣΑΠΣΤΥΗΑΚΟ ΠΡΟΓΡΑΜΜΑ ΠΟΤΓΧΝ «ΚΑΣΑΛΤΖ ΚΑΗ ΔΦΑΡΜΟΓΔ ΣΖ» ΔΡΔΤΝΖΣΗΚΖ ΔΡΓΑΗΑ ΓΗΠΛΧΜΑΣΟ ΔΗΓΗΚΔΤΖ Ομεηδναλαγωγηθά έλδπκα ωο πξόηππα εθαξκνγήο ηεο κεζόδνπ QSAR (Quantitative Structure-Activity relations) ΠΑΝΑΓΗΧΣΑ . ΣΕΑΝΖ ΜΖΥΑΝΗΚΟ ΣΔΥΝΟΛΟΓΗΑ ΠΔΣΡΔΛΑΗΟΤ ΚΑΗ ΦΤΗΚΟΤ ΑΔΡΗΟΤ ΑΘΖΝΑ ΝΟΔΜΒΡΗΟ 2011 ΔΡΔΤΝΖΣΗΚΖ ΔΡΓΑΗΑ ΓΗΠΛΧΜΑΣΟ ΔΗΓΗΚΔΤΖ Ομεηδναλαγσγηθά έλδπκα σο πξφηππα ηεο εθαξκνγήο ηεο κεζφδνπ QSAR (Quantitative Structrure-Activity relations) ΠΑΝΑΓΗΧΣΑ . ΣΕΑΝΖ Α.Μ.: 281604 ΔΠΗΒΛΔΠΧΝ ΚΑΘΖΓΖΣΖ: Ι. ΜΑΡΚΟΠΟΤΛΟ , Αλαπιεξσηήο Καζεγεηήο ΔΚΠΑ ΣΡΗΜΔΛΖ ΔΞΔΣΑΣΗΚΖ ΔΠΗΣΡΟΠΖ Η. ΜΑΡΚΟΠΟΤΛΟ Αλαπιεξωηεο θαζεγεηήο, Σκήκα Υεκείαο, ΔΚΠΑ Γ. ΥΑΣΕΖΝΗΚΟΛΑΟΤ Δπίθνπξνο Καζεγεηήο, Σκήκα Βηνινγίαο, ΔΚΠΑ Π. ΠΑΡΑΚΔΤΟΠΟΤΛΟΤ Λέθηνξαο, Σκήκα Υεκείαο, ΔΚΠΑ ΗΜΔΡΟΜΗΝΙΑ ΔΞΔΣΑΗ 25/11/2011 2 ΠΔΡΗΛΖΦΖ ε απηή ηε δηαηξηβή αξρηθά παξνπζηάδνληαη νη γεληθνί κεραληζκνί ελδπκηθήο θαηάιπζεο νη νπνίνη ζηε ζπλέρεηα εμεηδηθεχνληαη ζηνπο αληίζηνηρνπο κεραληζκνχο ησλ νμεηδνλαγσγηθψλ ζπζηεκάησλ ησλ θαηαιαζψλ θαη ππεξνμεηδαζψλ. Σν έλδπκν ππεξνμεηδάζε ηνπ αγξηνξάπαλνπ (horseradish peroxidase–HRP) απνηειεί ην θεληξηθφ έλδπκν αλαθνξάο ησλ αλσηέξσ κεραληζκψλ θαηάιπζεο ζηνπο νπνίνπο βαζίδεηαη θαη ε κειέηε ησλ ζρέζεσλ δνκήο-δξαζηηθφηεηαο ησλ ζπζηεκάησλ απησλ κέζσ ηεο κεζνδνινγίαο QSAR. Η εξγαζία νινθιεξψλεηαη κε ηελ αλάιπζε ησλ πεηξακαηηθψλ δεδνκέλσλ ηεο βηβιηνγξαθίαο πνπ αθνξνχλ ζηελ πξφβιεςε ησλ ηηκψλ θαη ησλ θηλεηηθψλ παξακέηξσλ δξάζεο ηεο HRP κέζσ QSAR ελψ εμάγνληαη ζπκπεξάζκαηα ηα νπνία απνδεηθλχνπλ ηφζν ηελ εθαξκνζηκφηεηα φζν θαη ηε ρξεζηκφηεηα ηεο πξνηεηλφκελεο κεζνδνινγίαο ζηα ζπζηήκαηα καο. ΘΔΜΑΣΗΚΖ ΠΔΡΗΟΥΖ: Δλδπκηθή θαηάιπζε ΛΔΞΔΗ ΚΛΔΗΓΗΑ: βηνθαηάιπζε, έλδπκα, θαηαιάζεο, ππεξνμεηδάζε ηνπ αγξηνξάπαλνπ (HRP), ζρέζεηο δνκήο-δξαζηηθφηεηαο (QSAR) 3 ABSTRACT In this essay we present the concept of enzymatic catalysis and the general methods for the investigation of this phenomenon. We concentrated on the studies of oxidoreductases and especially in catalases and peroxidases. -
12) United States Patent (10
US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S. -
Mushroom Ligninolytic Enzymes―Features and Application Of
applied sciences Review Mushroom Ligninolytic Enzymes—Features and Application of Potential Enzymes for Conversion of Lignin into Bio-Based Chemicals and Materials Seonghun Kim 1,2 1 Jeonbuk Branch Institute, Korea Research Institute of Bioscience and Biotechnology, 181 Ipsin-gil, Jeongeup 56212, Korea; [email protected]; Tel.: +82-63-570-5113 2 Department of Biosystems and Bioengineering, KRIBB School of Biotechnology, University of Science and Technology (UST), 217 Gajeong-ro, Daejeon 34113, Korea Abstract: Mushroom ligninolytic enzymes are attractive biocatalysts that can degrade lignin through oxido-reduction. Laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase are the main enzymes that depolymerize highly complex lignin structures containing aromatic or aliphatic moieties and oxidize the subunits of monolignol associated with oxidizing agents. Among these enzymes, mushroom laccases are secreted glycoproteins, belonging to a polyphenol oxidase family, which have a powerful oxidizing capability that catalyzes the modification of lignin using synthetic or natural mediators by radical mechanisms via lignin bond cleavage. The high redox potential laccase within mediators can catalyze the oxidation of a wide range of substrates and the polymeriza- tion of lignin derivatives for value-added chemicals and materials. The chemoenzymatic process using mushroom laccases has been applied effectively for lignin utilization and the degradation of recalcitrant chemicals as an eco-friendly technology. Laccase-mediated grafting