DOCSLIB.ORG

Links Among Neuronal Nitric Oxide Synthase, Oxidative Stress, and Asymmetric Dimethylarginine (Adma)

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Links Among Neuronal Nitric Oxide Synthase, Oxidative Stress, and Asymmetric Dimethylarginine (Adma) NITRIC OXIDE DEFICIENCY IN CHRONIC KIDNEY DISEASE: LINKS AMONG NEURONAL NITRIC OXIDE SYNTHASE, OXIDATIVE STRESS, AND ASYMMETRIC DIMETHYLARGININE (ADMA) By YOU-LIN TAIN A DISSERTATION PRESENTED TO THE GRADUATE SCHOOL OF THE UNIVERSITY OF FLORIDA IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY UNIVERSITY OF FLORIDA 2007 1 © 2007 You-Lin Tain 2 This dissertation is dedication to my family for their constant love 3 ACKNOWLEDGMENTS This dissertation would not have been possible without the support of many people. Many thanks go to my adviser: Dr. Chris Baylis gave me the chance to work on many projects and also gave me numerous valuable comments for my manuscripts. I would like to thank my committee members for their guidance and valuable comments: Dr. Richard Johnson, Dr. Mohan Raizada, and Dr. Mark Segal. I thanks also go to the Chang Gung Memorial Hospital for awarding me a fellowship, providing me with the financial means to complete this dissertation. I am grateful to many persons who shared their technical assistance and experience, especially Dr. Verlander and Dr. Chang (University of Florida), Dr. Muller and Dr. Szabo (Semmelweis University, Hungary), Dr. Griendling and Dr. Dikalova (Emory University), and Dr. Merchant and Dr. Klein (University of Louisville). Next, I would like to thank all of the members of Dr. Baylis lab, both past and present, with whom I have been fortunate enough to work: Dr. Aaron Erdely, Gerry Freshour, Kevin Engels, Lennie Samsell, Dr. Sarah Knight, Dr. Cheryl Smith, Dr. Jenny Sasser, Harold Snellen, Bruce Cunningham, Gin-Fu Chen, and Natasha Moningka. I will miss all of them. Finally, thanks go to my wife, CN, and numerous friends who endured this long process with me, always offering support and love. 4 TABLE OF CONTENTS page ACKNOWLEDGMENTS ...............................................................................................................4 LIST OF TABLES...........................................................................................................................8 LIST OF FIGURES .........................................................................................................................9 ABSTRACT...................................................................................................................................12 CHAPTER 1 INTRODUCTION ..................................................................................................................14 Overview.................................................................................................................................14 Chronic Kidney Disease Is a Global Challenge ..............................................................14 Nitric Oxide Deficiency Is a Common Mechanism of CKD Progression.......................14 Neuronal Nitric Oxide Synthase.............................................................................................15 Role of Renal Cortical Neuronal Nitric Oxide Synthase in Chronic Kidney Disease Progression...................................................................................................................15 Neuronal Nitric Oxide Synthase Isoforms in the Kidney................................................16 Regulation of Neuronal Nitric Oxide Synthase Expression............................................17 Oxidative Stress and Asymmetric Dimethylarginine .............................................................18 Role of Oxidative Stress in Chronic Kidney Disease......................................................18 Role of Asymmetric Dimethylarginine in Chronic Kidney Disease...............................18 Objective.................................................................................................................................20 2 GENERAL METHODS .........................................................................................................25 Animal Models .......................................................................................................................25 Ablation/infarction Model...............................................................................................25 5/6 Nephrectomy Model..................................................................................................25 Renal Transplantation Model ..........................................................................................25 Tissue Harvest .................................................................................................................26 Biochemical Analysis .............................................................................................................26 Nitric Oxide Assay ..........................................................................................................26 Nitric Oxide Synthase Activity .......................................................................................27 Pathology.........................................................................................................................27 Western Blot....................................................................................................................28 Electronic Spin Resonance..............................................................................................29 Reverse Transcription Polymerase Chain Reaction ........................................................29 5 3 IDENTIFICATION OF NEURONAL NITRIC OXIDE SYNTHASE ISOFORMS IN THE KIDNEY ........................................................................................................................31 Introduction.............................................................................................................................31 Materials and Methods ...........................................................................................................31 Results.....................................................................................................................................34 Discussion...............................................................................................................................36 4 RENAL CORTEX NEURONAL NITRIC OXIDE SYNTHASE IN KIDNEY TRANSPLANTS ....................................................................................................................44 Introduction.............................................................................................................................44 Materials and Methods ...........................................................................................................45 Results.....................................................................................................................................47 Discussion...............................................................................................................................49 5 DETERMINATION OF DIMETHYLARGININE DIMETHYLAMINOHYDROLASE ACTIVITY IN THE KIDNEY ...............................................................................................61 Introduction.............................................................................................................................61 Materials and Methods ...........................................................................................................61 Optimization of Homogenization Buffers .......................................................................62 Optimization of Deproteinization....................................................................................63 Tests for Other Pathways That Could Alter Citrulline Concentration ............................63 Comparison of Citrulline Assay and Asymmetric Dimethylarginine Degradation by High Performance Liquid Chromatography ................................................................64 Statistical Analysis ..........................................................................................................65 Results.....................................................................................................................................65 Optimization of Citrulline Assay.....................................................................................65 Effect of Urea on Citrulline Assay ..................................................................................65 Comparison of Dimethylarginine Dimethylaminohydrolase Activity Measured by Citrulline Accumulation with Asymmetric Dimethylarginine Consumption..............66 Tests for Other Pathways That Could Alter Citrulline Concentration ............................66 Discussion...............................................................................................................................66 6 VITAMIN E REDUCES GLOMERULOCLEROSIS, RESTORES RENAL NEURONAL NITRIC OXIDE SYNTHASE, AND SUPPRESSES OXIDATIVE STRESS IN THE 5/6 NEPHRECTOMIZED RAT................................................................78 Introduction.............................................................................................................................78 Materials and Methods ...........................................................................................................79 Results.....................................................................................................................................80 Discussion...............................................................................................................................82
Load more

Recommended publications
  • DDAH I (C-19): Sc-26068
    SANTA CRUZ BIOTECHNOLOGY, INC. DDAH I (C-19): sc-26068 The Power to Question BACKGROUND APPLICATIONS DDAH, a dimethylarginine dimethylaminohydrolase, hydrolyzes dimethyl DDAH I (C-19) is recommended for detection of DDAH I of mouse, rat and arginine (ADMA) and monomethyl arginine (MMA), both inhibitors of nitric human origin by Western Blotting (starting dilution 1:200, dilution range oxide synthases, and may be involved in in vivo modulation of nitric oxide 1:100-1:1000) and immunofluorescence (starting dilution 1:50, dilution production. Impairment of DDAH causes ADMA accumulation and a reduc- range 1:50-1:500). tion in cGMP generation. DDAH II, the predominant DDAH isoform in endothelial cells, facilitates the induction of nitric oxide synthesis by all- RECOMMENDED SECONDARY REAGENTS trans-Retinoic acid (atRA). DDAH proteins are highly expressed in colon, kid- To ensure optimal results, the following support (secondary) reagents are ney, stomach and liver tissues. recommended: 1) Western Blotting: use donkey anti-goat IgG-HRP: sc-2020 (dilution range: 1:2000-1:100,000) or Cruz Marker™ compatible donkey anti- REFERENCES goat IgG-HRP: sc-2033 (dilution range: 1:2000-1:5000), Cruz Marker™ 1. Nakagomi, S., et al. 1999. Dimethylarginine dimethylaminohydrolase Molecular Weight Standards: sc-2035, TBS Blotto A Blocking Reagent: (DDAH) as a nerve-injury-associated molecule: mRNA localization in the sc-2333 and Western Blotting Luminol Reagent: sc-2048. 2) Immunofluores- rat brain and its coincident up-regulation with neuronal NO synthase cence: use donkey anti-goat IgG-FITC: sc-2024 (dilution range: 1:100-1:400) (nNOS) in axotomized motoneurons. Eur. J.
    [Show full text]
  • Association Between the Gut Microbiota and Blood Pressure in a Population Cohort of 6953 Individuals
    Journal of the American Heart Association ORIGINAL RESEARCH Association Between the Gut Microbiota and Blood Pressure in a Population Cohort of 6953 Individuals Joonatan Palmu , MD; Aaro Salosensaari , MSc; Aki S. Havulinna , DSc (Tech); Susan Cheng , MD, MPH; Michael Inouye, PhD; Mohit Jain, MD, PhD; Rodolfo A. Salido , BSc; Karenina Sanders , BSc; Caitriona Brennan, BSc; Gregory C. Humphrey, BSc; Jon G. Sanders , PhD; Erkki Vartiainen , MD, PhD; Tiina Laatikainen , MD, PhD; Pekka Jousilahti, MD, PhD; Veikko Salomaa , MD, PhD; Rob Knight , PhD; Leo Lahti , DSc (Tech); Teemu J. Niiranen , MD, PhD BACKGROUND: Several small-scale animal studies have suggested that gut microbiota and blood pressure (BP) are linked. However, results from human studies remain scarce and conflicting. We wanted to elucidate the multivariable-adjusted as- sociation between gut metagenome and BP in a large, representative, well-phenotyped population sample. We performed a focused analysis to examine the previously reported inverse associations between sodium intake and Lactobacillus abun- dance and between Lactobacillus abundance and BP. METHODS AND RESULTS: We studied a population sample of 6953 Finns aged 25 to 74 years (mean age, 49.2±12.9 years; 54.9% women). The participants underwent a health examination, which included BP measurement, stool collection, and 24-hour urine sampling (N=829). Gut microbiota was analyzed using shallow shotgun metagenome sequencing. In age- and sex-adjusted models, the α (within-sample) and β (between-sample) diversities of taxonomic composition were strongly re- lated to BP indexes (P<0.001 for most). In multivariable-adjusted models, β diversity was only associated with diastolic BP (P=0.032).
    [Show full text]
  • Circuits Regulating Superoxide and Nitric Oxide
    antioxidants Article Circuits Regulating Superoxide and Nitric Oxide Production and Neutralization in Different Cell Types: Expression of Participating Genes and Changes Induced by Ionizing Radiation 1,2, 1,2, 1 1,2, Patryk Bil y, Sylwia Ciesielska y, Roman Jaksik and Joanna Rzeszowska-Wolny * 1 Department of Systems Biology and Engineering, Faculty of Automatic Control, Electronics and Computer Science, Silesian University of Technology, 44-100 Gliwice, Poland; [email protected] (P.B.); [email protected] (S.C.); [email protected] (R.J.) 2 Biotechnology Centre, Silesian University of Technology, 44-100 Gliwice, Poland * Correspondence: [email protected] These authors contributed equally. y Received: 30 June 2020; Accepted: 29 July 2020; Published: 3 August 2020 Abstract: Superoxide radicals, together with nitric oxide (NO), determine the oxidative status of cells, which use different pathways to control their levels in response to stressing conditions. Using gene expression data available in the Cancer Cell Line Encyclopedia and microarray results, we compared the expression of genes engaged in pathways controlling reactive oxygen species and NO production, neutralization, and changes in response to the exposure of cells to ionizing radiation (IR) in human cancer cell lines originating from different tissues. The expression of NADPH oxidases and NO synthases that participate in superoxide radical and NO production was low in all cell types. Superoxide dismutase, glutathione peroxidase, thioredoxin, and peroxiredoxins participating in radical neutralization showed high expression in nearly all cell types. Some enzymes that may indirectly influence superoxide radical and NO levels showed tissue-specific expression and differences in response to IR.
    [Show full text]
  • Copyright by Yun Wang 2010
    Copyright by Yun Wang 2010 The Dissertation Committee for Yun Wang Certifies that this is the approved version of the following dissertation: Controlling Nitric Oxide (NO) Overproduction: Nω, Nω- Dimethylarginine Dimethylaminohydrolase (DDAH) as a Novel Drug Target Committee: Walter L. Fast, Supervisor Christian P. Whitman Jon D. Robertus George Georgiou Sean M. Kerwin Controlling Nitric Oxide (NO) Overproduction: Nω, Nω- Dimethylarginine Dimethylaminohydrolase (DDAH) as a Novel Drug Target by Yun Wang, B.S.; M.S. Dissertation Presented to the Faculty of the Graduate School of The University of Texas at Austin in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy The University of Texas at Austin August, 2010 Dedication To all people who have given me generous help when I am in Austin, including professors, colleagues and friends. To my beloved parents in P.R.China, who always motivate me to pursue my dream. Acknowledgements First and foremost, I would like to thank my supervisor, Dr. Walt Fast, for his generous support and for giving me an opportunity to work in his lab four years ago at the University of Texas at Austin. Walt gives me lots of freedom to explore scientific problems and provides a wonderful working environment along with my lovely colleagues. He always gives me useful directions when I meet difficulties. I appreciate every scientific conversation with him. They were especially important to me during the beginning of my Ph.D. study. I wouldn’t have accomplished as much as today without his help. In addition, I’d like to thank colleagues in Fast lab for their generous help during these years.
    [Show full text]
  • (10) Patent No.: US 8119385 B2
    US008119385B2 (12) United States Patent (10) Patent No.: US 8,119,385 B2 Mathur et al. (45) Date of Patent: Feb. 21, 2012 (54) NUCLEICACIDS AND PROTEINS AND (52) U.S. Cl. ........................................ 435/212:530/350 METHODS FOR MAKING AND USING THEMI (58) Field of Classification Search ........................ None (75) Inventors: Eric J. Mathur, San Diego, CA (US); See application file for complete search history. Cathy Chang, San Diego, CA (US) (56) References Cited (73) Assignee: BP Corporation North America Inc., Houston, TX (US) OTHER PUBLICATIONS c Mount, Bioinformatics, Cold Spring Harbor Press, Cold Spring Har (*) Notice: Subject to any disclaimer, the term of this bor New York, 2001, pp. 382-393.* patent is extended or adjusted under 35 Spencer et al., “Whole-Genome Sequence Variation among Multiple U.S.C. 154(b) by 689 days. Isolates of Pseudomonas aeruginosa” J. Bacteriol. (2003) 185: 1316 1325. (21) Appl. No.: 11/817,403 Database Sequence GenBank Accession No. BZ569932 Dec. 17. 1-1. 2002. (22) PCT Fled: Mar. 3, 2006 Omiecinski et al., “Epoxide Hydrolase-Polymorphism and role in (86). PCT No.: PCT/US2OO6/OOT642 toxicology” Toxicol. Lett. (2000) 1.12: 365-370. S371 (c)(1), * cited by examiner (2), (4) Date: May 7, 2008 Primary Examiner — James Martinell (87) PCT Pub. No.: WO2006/096527 (74) Attorney, Agent, or Firm — Kalim S. Fuzail PCT Pub. Date: Sep. 14, 2006 (57) ABSTRACT (65) Prior Publication Data The invention provides polypeptides, including enzymes, structural proteins and binding proteins, polynucleotides US 201O/OO11456A1 Jan. 14, 2010 encoding these polypeptides, and methods of making and using these polynucleotides and polypeptides.
    [Show full text]
  • The Microbiota-Produced N-Formyl Peptide Fmlf Promotes Obesity-Induced Glucose
    Page 1 of 230 Diabetes Title: The microbiota-produced N-formyl peptide fMLF promotes obesity-induced glucose intolerance Joshua Wollam1, Matthew Riopel1, Yong-Jiang Xu1,2, Andrew M. F. Johnson1, Jachelle M. Ofrecio1, Wei Ying1, Dalila El Ouarrat1, Luisa S. Chan3, Andrew W. Han3, Nadir A. Mahmood3, Caitlin N. Ryan3, Yun Sok Lee1, Jeramie D. Watrous1,2, Mahendra D. Chordia4, Dongfeng Pan4, Mohit Jain1,2, Jerrold M. Olefsky1 * Affiliations: 1 Division of Endocrinology & Metabolism, Department of Medicine, University of California, San Diego, La Jolla, California, USA. 2 Department of Pharmacology, University of California, San Diego, La Jolla, California, USA. 3 Second Genome, Inc., South San Francisco, California, USA. 4 Department of Radiology and Medical Imaging, University of Virginia, Charlottesville, VA, USA. * Correspondence to: 858-534-2230, [email protected] Word Count: 4749 Figures: 6 Supplemental Figures: 11 Supplemental Tables: 5 1 Diabetes Publish Ahead of Print, published online April 22, 2019 Diabetes Page 2 of 230 ABSTRACT The composition of the gastrointestinal (GI) microbiota and associated metabolites changes dramatically with diet and the development of obesity. Although many correlations have been described, specific mechanistic links between these changes and glucose homeostasis remain to be defined. Here we show that blood and intestinal levels of the microbiota-produced N-formyl peptide, formyl-methionyl-leucyl-phenylalanine (fMLF), are elevated in high fat diet (HFD)- induced obese mice. Genetic or pharmacological inhibition of the N-formyl peptide receptor Fpr1 leads to increased insulin levels and improved glucose tolerance, dependent upon glucagon- like peptide-1 (GLP-1). Obese Fpr1-knockout (Fpr1-KO) mice also display an altered microbiome, exemplifying the dynamic relationship between host metabolism and microbiota.
    [Show full text]
  • The Role of Nitric Oxide in the Pathogenesis of Brain Lesions During the Development of Alzheimer's Disease
    in vivo 18: 325-334 (2004) Review The Role of Nitric Oxide in the Pathogenesis of Brain Lesions During the Development of Alzheimer’s Disease DILARA SEYIDOVA1,2, ALI ALIYEV1,2, NIZAMI RZAYEV1,2, MARK OBRENOVICH2, BRUCE T. LAMB3, MARK A. SMITH2, JACK C. DE LA TORRE2, GEORGE PERRY2 and GJUMRAKCH ALIEV1,2 1Microscopy Research Center, 2Institute of Pathology and 3Department of Genetics, School of Medicine, Case Western Reserve University, 2085 Adelbert Road, Cleveland, Ohio, 44106, U.S.A. Abstract. Nitric oxide (NO) is a key bioregulatory active regulated by diverse signaling pathways (65). NO also molecule in the cardiovascular, immune and nervous systems, inhibits enzymes in target cells and can interact with oxygen- synthesized through converting L-arginine to L-citrulline by derived radicals or free oxygen species (ROS) to produce NO synthase (NOS). Research exploration supports the theory other toxic substances. Thus, NO also plays a role in that this molecule appears to be one of the key factors for the immunological host defense and in the pathophysiology of disruption of normal brain homeostasis, which causes the certain clinical conditions (55). development of brain lesions and pathology such as in The role of NO in brain homeostasis has been extensively Alzheimer’s disease (AD). Especially the vascular content of reviewed more recently (34). Experiments demonstrate that NO activity appears to be a major contributor to this pathology NO exerts several actions in the cerebral cortex. NO before the overexpression of NOS activity in other brain production is mediated by neuronal activity through at least cellular compartments develop. We theorize that two pathways: ¡-metylD-aspartate (NMDA) receptors and pharmacological intervention using NO donors and/or NO alpha-amino-3-hydroxy-5-metyl-4-isoxazoleproprionic acid suppressors should delay or minimize brain lesion development (AMPA) receptors.
    [Show full text]
  • (DDAH): Discovery, Synthesis and Development
    molecules Review Inhibitors of the Hydrolytic Enzyme Dimethylarginine Dimethylaminohydrolase (DDAH): Discovery, Synthesis and Development Rhys B. Murphy †, Sara Tommasi †, Benjamin C. Lewis and Arduino A. Mangoni * Department of Clinical Pharmacology, School of Medicine, Flinders University, Bedford Park, Adelaide 5042, Australia; rhys.murphy@flinders.edu.au (R.B.M.); sara.tommasi@flinders.edu.au (S.T.); ben.lewis@flinders.edu.au (B.C.L.) * Correspondence: arduino.mangoni@flinders.edu.au; Tel.: +61-8-8204-7495; Fax: +61-8-8204-5114 † These authors contributed equally to this work. Academic Editors: Jean Jacques Vanden Eynde and Sylvain Rault Received: 9 February 2016; Accepted: 4 May 2016; Published: 11 May 2016 Abstract: Dimethylarginine dimethylaminohydrolase (DDAH) is a highly conserved hydrolytic enzyme found in numerous species, including bacteria, rodents, and humans. In humans, the DDAH-1 isoform is known to metabolize endogenous asymmetric dimethylarginine (ADMA) and monomethyl arginine (L-NMMA), with ADMA proposed to be a putative marker of cardiovascular disease. Current literature reports identify the DDAH family of enzymes as a potential therapeutic target in the regulation of nitric oxide (NO) production, mediated via its biochemical interaction with the nitric oxide synthase (NOS) family of enzymes. Increased DDAH expression and NO production have been linked to multiple pathological conditions, specifically, cancer, neurodegenerative disorders, and septic shock. As such, the discovery, chemical synthesis, and development of DDAH inhibitors as potential drug candidates represent a growing field of interest. This review article summarizes the current knowledge on DDAH inhibition and the derived pharmacokinetic parameters of the main DDAH inhibitors reported in the literature. Furthermore, current methods of development and chemical synthetic pathways are discussed.
    [Show full text]
  • Datasheet Blank Template
    SAN TA C RUZ BI OTEC HNOL OG Y, INC . DDAH II (C-19): sc-26071 BACKGROUND RECOMMENDED SECONDARY REAGENTS DDAH, a dimethylarginine dimethylaminohydrolase, hydrolyzes dimethyl To ensure optimal results, the following support (secondary) reagents are arginine (ADMA) and monomethyl arginine (MMA), both inhibitors of nitric recommended: 1) Western Blotting: use donkey anti-goat IgG-HRP: sc-2020 oxide synthases, and may be involved in in vivo modulation of nitric oxide (dilution range: 1:2000-1:100,000) or Cruz Marker™ compatible donkey production. Impairment of DDAH causes ADMA accumulation and a reduction anti- goat IgG-HRP: sc-2033 (dilution range: 1:2000-1:5000), Cruz Marker™ in cGMP generation. DDAH II, the predominant DDAH isoform in endothelial Molecular Weight Standards: sc-2035, TBS Blotto A Blocking Reagent: cells, facilitates the induction of nitric oxide synthesis by all- trans -retinoic sc-2333 and Western Blotting Luminol Reagent: sc-2048. 2) Immunoprecip- acid (atRA). DDAH proteins are highly expressed in colon, kidney, stomach itation: use Protein A/G PLUS-Agarose: sc-2003 (0.5 ml agarose/2.0 ml). and liver tissues. 3) Immunofluorescence: use donkey anti-goat IgG-FITC: sc-2024 (dilution range: 1:100-1:400) or donkey anti-goat IgG-TR: sc-2783 (dilution range: REFERENCES 1:100-1:400) with UltraCruz™ Mounting Medium: sc-24941. 1. Nakagomi, S., et al. 1999. Dimethylarginine dimethylaminohydrolase (DDAH) as a nerve-injury-associated molecule: mRNA localization in the DATA rat brain and its coincident upregulation with neuronal NO synthase AB (nNOS) in axotomized motoneurons. Eur. J. Neurosci. 11: 2160-2166. 132 K 2.
    [Show full text]
  • Kidney V-Atpase-Rich Cell Proteome Database
    A comprehensive list of the proteins that are expressed in V-ATPase-rich cells harvested from the kidneys based on the isolation by enzymatic digestion and fluorescence-activated cell sorting (FACS) from transgenic B1-EGFP mice, which express EGFP under the control of the promoter of the V-ATPase-B1 subunit. In these mice, type A and B intercalated cells and connecting segment principal cells of the kidney express EGFP. The protein identification was performed by LC-MS/MS using an LTQ tandem mass spectrometer (Thermo Fisher Scientific). For questions or comments please contact Sylvie Breton ([email protected]) or Mark A. Knepper ([email protected]).
    [Show full text]
  • 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.
    [Show full text]
  • Protein T1 C1 Accession No. Description
    Protein T1 C1 Accession No. Description SW:143B_HUMAN + + P31946 14-3-3 protein beta/alpha (protein kinase c inhibitor protein-1) (kcip-1) (protein 1054). 14-3-3 protein epsilon (mitochondrial import stimulation factor l subunit) (protein SW:143E_HUMAN + + P42655 P29360 Q63631 kinase c inhibitor protein-1) (kcip-1) (14-3-3e). SW:143S_HUMAN + - P31947 14-3-3 protein sigma (stratifin) (epithelial cell marker protein 1). SW:143T_HUMAN + - P27348 14-3-3 protein tau (14-3-3 protein theta) (14-3-3 protein t-cell) (hs1 protein). 14-3-3 protein zeta/delta (protein kinase c inhibitor protein-1) (kcip-1) (factor SW:143Z_HUMAN + + P29312 P29213 activating exoenzyme s) (fas). P01889 Q29638 Q29681 Q29854 Q29861 Q31613 hla class i histocompatibility antigen, b-7 alpha chain precursor (mhc class i antigen SW:1B07_HUMAN + - Q9GIX1 Q9TP95 b*7). hla class i histocompatibility antigen, b-14 alpha chain precursor (mhc class i antigen SW:1B14_HUMAN + - P30462 O02862 P30463 b*14). P30479 O19595 Q29848 hla class i histocompatibility antigen, b-41 alpha chain precursor (mhc class i antigen SW:1B41_HUMAN + - Q9MY79 Q9MY94 b*41) (bw-41). hla class i histocompatibility antigen, b-42 alpha chain precursor (mhc class i antigen SW:1B42_HUMAN + - P30480 P79555 b*42). P30488 O19615 O19624 O19641 O19783 O46702 hla class i histocompatibility antigen, b-50 alpha chain precursor (mhc class i antigen SW:1B50_HUMAN + - O78172 Q9TQG1 b*50) (bw-50) (b-21). hla class i histocompatibility antigen, b-54 alpha chain precursor (mhc class i antigen SW:1B54_HUMAN + - P30492 Q9TPQ9 b*54) (bw-54) (bw-22). P30495 O19758 P30496 hla class i histocompatibility antigen, b-56 alpha chain precursor (mhc class i antigen SW:1B56_HUMAN - + P79490 Q9GIM3 Q9GJ17 b*56) (bw-56) (bw-22).
    [Show full text]