Immunochemical Characterisation of Erythrocyte Antigens

Total Page:16

File Type:pdf, Size:1020Kb

Immunochemical Characterisation of Erythrocyte Antigens University of Wollongong Research Online University of Wollongong Thesis Collection 1954-2016 University of Wollongong Thesis Collections 1991 Immunochemical characterisation of erythrocyte antigens Alison Michéle Jonusys University of Wollongong Follow this and additional works at: https://ro.uow.edu.au/theses University of Wollongong Copyright Warning You may print or download ONE copy of this document for the purpose of your own research or study. The University does not authorise you to copy, communicate or otherwise make available electronically to any other person any copyright material contained on this site. You are reminded of the following: This work is copyright. Apart from any use permitted under the Copyright Act 1968, no part of this work may be reproduced by any process, nor may any other exclusive right be exercised, without the permission of the author. Copyright owners are entitled to take legal action against persons who infringe their copyright. A reproduction of material that is protected by copyright may be a copyright infringement. A court may impose penalties and award damages in relation to offences and infringements relating to copyright material. Higher penalties may apply, and higher damages may be awarded, for offences and infringements involving the conversion of material into digital or electronic form. Unless otherwise indicated, the views expressed in this thesis are those of the author and do not necessarily represent the views of the University of Wollongong. Recommended Citation Jonusys, Alison Michéle, Immunochemical characterisation of erythrocyte antigens, Doctor of Philosophy thesis, Department of Biology, University of Wollongong, 1991. https://ro.uow.edu.au/theses/1067 Research Online is the open access institutional repository for the University of Wollongong. For further information contact the UOW Library: [email protected] IMMUNOCHEMICAL CHARACTERISATION OF ERYTHROCYTE ANTIGENS A thesis submitted in fulfilment of the requirements for the award of the degree DOCTOR OF PHILOSOPHY from THE UNIVERSITY OF WOLLONGONG by u n ;vers»ty of WOLLONGONG LIBRARY ALISON MICHÉLE JONUSYS, BSc (Hons) Woll. DEPARTMENT OF BIOLOGY 1991 0 1 3 7 3 5 There are many aspects of life which, when viewed retrospectively, fall into a pattern, although in their developing they seemed but a random play of accident and circumstance. Sir Macfariane Burnet, 1959. IV TABLE OF CONTENTS Declaration ii Table of Contents iv List of Figures x List of Tables xii Abbreviations xiii Acknowledgements xv Abstract xvi Chapter One : Immunochemical Characterisation of Erythrocyte Autoantigens by Natural Autoantibodies LI. Natural Autoantibodies and Autoantigens 1 1.1.1. Natural Autoantibodies 2 1.1.2. Natural Autoantibodies and Development 4 1.1.3. Natural Autoantibodies and Autoimmuninty 6 1.1.4. Autoantigens 8 1.2. The Origin and Significance of Natural Autoantibodies in the context of self-nonself discrimination 10 1.2.1. Theories of self tolerance and self recognition 10 1.2.2. Origins and Significance of Natural Autoantibodies. 15 1.3. Nature of B lymphocytes and the antibodies that recognise bromelain-treated red blood cells 1.3.1. The peritoneal cell phenomenon 18 1.3.2. Lipopolysaccharide stimulated serum 23 1.3.3. Anti-rat red blood cell serum 24 1.3.4. Ly-1+ B-cells 26 1.3.5. Antibodies and Hybridomas produced from unstimulated animals 30 1.3.6. V-genes and V-regions of natural autoantibodies 32 V. 1.4. Bromelain-treated mouse red blood cells- Characterisation of a "hidden autoantigen" 1.4.1. Regulation of the anti-BrMRBC response 35 1.4.2. Characterisation of a hidden autoantigen on autologous erythrocytes 37 1.5. Red Blood Cell Antigens. 44 1.6. Aims of the study 47 Chapter Two: Materials and Methods 2.1. Animals 48 2.1.1. Mice 4g 2.1.2. Rabbits 4g 2.2. Antibodies and Complement 48 2.2.1. IPS stimulated serum and normal mouse serum 48 2.2.2. Monoclonal antibody culture 49 2.2.3. Quantitation of IgM form LPS serum, normal mouuse serum and mouse monoclonal antibodies 52 2.2.4. Mouse IgM Myeloma 53 2.2.5. Preparation and purification of immune rabbit serum IgG 53 2.2.6. Preparation and purification of rabbit complement 53 2.2SI. Sources of other antibodies 54 2.2.8. Preabsorbtion of primary and secondary antibodies with erythrocytes 54 2.2.9. Reduction of IgM to monomers with 2-mercaptoethanol, 2-mercaptoethylamine and dithiothreitol 54 2.3. Erythrocytes and Blood group substances 55 2.3.1. Mouse erythrocytes 55 2.3.2. Mouse erythrocyte ghosts 55 2.3.3. Erythrocytes from other species 56 2.4. Assays for Bromelain-treated Mouse Red Blood Cells 57 2.4.1. Haemolytic assays 57 2.4.2. Suspension-cellular Enzyme-linked immunoassays for erythrocytes 57 2.4.3. Direct agglutination of mouse erythrocytes (Direct Coomb's test) 58 2.4.4. Direct binding ELISA for erythrocyte ghosts 59 2.5. Blood Group Substances and Serological tests for Red Blood Cells 59 2.5.1. Preparation of Blood Group Substances 59 2.5.2. Treatment of erythrocytes with AET and periodate 60 2.6. Preparation of Affinity Columns 60 2.7. Purified antigens and Chemicals. 61 2.7.1. Purified proteins and protein assays 61 2.7.2. Buffers 62 2.8. Polyacrylamide Gel electrophoresis Techniques 63 2.8.1. SDS-PAGE 63 2.8.2. Staining methods for proteins and glycoproteins 64 2.9. Immunoblotting Techniques 68 2.9.1. Western Blotting 68 2.9.2. Lipid Blotting 69 2.10. Isoelectric Focussing and Two-dimensional Mapping of Mouse erythrocytes 2.10.1. Isoelectric focussing 70 2.10.2. Two dimensional electrophoresis of red blood cell lysates. 72 2.11. Enzyme-linked Immunoassays for carbonic anhydrase 73 2.11.1. Direct binding assays for carbonic anhydrase 73 2.11.2. Competitive inhibition assays for carbonic anhydrase 73 2.12. Murine Carbonic anhydrase 74 2.12.1. Mouse stomach carbonic anhydrase 74 2.12.2. Mouse erythrocyte carbonic anhydrase 74 2.13. Epitope analysis of carbonic anhydrase 75 2.13.1. Carbohydrate epitopes 75 2.13.2. Protein analysis 76 Chapter Three : Analysis of Red Blood Cell Membranes, Gut Material and Specific anti-BrM antibodies 3.1. Preamble 78 3.2. Preparation of red blood cell membranes 79 3.2.1. Preparation and characterisation of protein-free and protein-containing ghosts 79 3.3. Immunisation of Rabbits with BrMRBC 81 3.3.1. Preparation of immune rabbit serum. 81 3.4. Preparation of ghost affinity columns as a first step in the purification of anti-BrM antibodies 3.4.1. Testing the binding titres of LPS serum against BrM ghosts in ELISA 83 3.4.2. The preparation of BrM-ghost affinity columns and attempts to purify anti-BrMRBC antibodies from LPS serum. 87 3.4.3. Competitive ELISA assays using BrM ghosts to inhibit binding of LPS serum to BrMRBC 88 3.5. Serologiocal tests to determine the nature of mouse blood group antigens. 3.5.1. AET and periodate treatment of NMRBC and BrMRBC 89 3.5.2. Use of anti-A and anti-B typing reagents with vertebrate red blood cells 89 3.5.3. Preparation of blood group substances from mouse stomach. 90 3.6. Discussion 90 Chapter Four : Immunoblotting of Mouse Red Blood Cells 4.1. Preamble 93 4.2. Optimising Conditions for Dot Blotting 94 4.2.1. Production and characterisation of the monoclonal antibodies FUB 1 and FUB 3 94 4.2.2. Optimising conditions of blocking, washing, and levels of second antibodies in dot blots of mouse red blood cells, ghosts and blood group substances 96 4.2.3. Comparison of Different Washing and Blocking Buffers 97 4.2.4. Improvement in staining protocols for alkaline phosphatase 99 4.2.5. Optimum conditions for blotting. 99 4.3. SDS-PAGE and Immunoblotting of Mouse Erythrocytes 108 4.3.1. SDS-PAGE of mouse erythrocytes 108 4.3.2. Western Blot experiments with mouse erythrocytes 112 4.3.3. Isoelectric focussing and two dimensional maps of whole mouse red blood cells to further characterise the immunoreactive bands 113 4.3.4. Determination of the involvement of carbonic anhydrase in the BrMRBC epitope. 120 4.4. Lipid immunoblotting 121 4.5. Discussion 124 Chapter Five: Characterisation of carbonic anhydrase from murine stomach, and from erythrocytes of different species, and determinantion of carbonic anhydrase epitopes recognised by LPS serum and FUB 1. 5.1. A brief introduction to carbonic anhydrase 130 5.2. Natural autoantibodies recognise native and denatured forms of carbonic anhydrase 134 5.3. Attempts to inhibit the binding of antibodies to BrMRBC with various forms of carbonic anhydrase 142 5.4. Mouse stomach carbonic anhydrase. 153 5.5. Murine IgM anti-BrMRBC natural autoantibodies recognise erythrocytes from different species 160 5.6. Defining the epitopes of carbonic anhydrase recognised by IgM natural autoantibodies 167 5.7. Discussion 177 Chapter Six General Discussion and Conclusions 182 References 192 Publications X. List of Figures Figure 3.1. Titration of LPS stimulated serum against BrM-ghosts in a suspension c-ELIS A. 85 Figure 4.1. Initial dot blot experiment to determine the binding patterns of LPS serum, FUB 1 and FUB 3 against red blood cells, ghosts and gut material. 98 Figure 4.2. Comparison of 1% bovine serum albumin and 1% gelatin as blocking agents, and PBS versus PBS-Tween 20 in dot blotting. 100 Figure 4.3 Dot blotting experiment to test the patterns of binding of LPS serum and FUB 1 that have been preabsorbed with BrMRBC or NMRBC 102 Figure 4.4 Suspension c-ELIS A to test the antibodies used in the prev­ ious experiment for titres against BrMRBC and NMRBC using either 1% gelatin or 1% BS A as blocking and diluting agents.
Recommended publications
  • Medical Immunology.Pdf
    Page i Introduction to Medical Immunology Fourth Edition Edited by Gabriel Virella Medical University of South Carolina Charleston, South Carolina MARCEL DEKKER, INC. NEW YORK • BASEL • HONG KONG Page ii Library of Congress Cataloging-in-Publication Data Introduction to medical immunology / edited by Gabriel Virella. — 4th ed. p. cm. Includes bibliographical references and index. ISBN 0-8247-9897-X (hardcover : alk. paper) 1. Clinical immunology. 2. Immunology. I. Virella, Gabriel. [DNLM: 1. Immunity. 2. Immunologic Diseases. QW 504 I6286 1997] RC582.I59 1997 616.07'9—dc21 DNLM/DLC for Library of Congress 97-22373 CIP The publisher offers discounts on this book when ordered in bulk quantities. For more information, write to Special Sales/Professional Marketing at the address below. This book is printed on acid-free paper. Copyright © 1998 by MARCEL DEKKER, INC. All Rights Reserved. Neither this book nor any part may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, microfilming, and recording, or by any information storage and retrieval system, without permission in writing from the publisher. MARCEL DEKKER, INC. 270 Madison Avenue, New York, New York 10016 http://www.dekker.com Current printing (last digit): 10 9 8 7 6 5 4 3 2 1 PRINTED IN THE UNITED STATES OF AMERICA Page iii PREFACE Ten years after the publication of the first edition of Introduction to Medical Immunology, the ideal immunology textbook continues to be a very elusive target. The discipline continues to grow at a brisk pace, and the concepts tend to become obsolete as quickly as we put them in writing.
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 6,191,108 B1 Rodkey Et Al
    USOO619 1108B1 (12) United States Patent (10) Patent No.: US 6,191,108 B1 Rodkey et al. (45) Date of Patent: Feb. 20, 2001 (54) RH BLOOD GROUPANTIGEN Moore et al., “Evaluation of monoclonal anti-Rh antibodies COMPOSITIONS AND METHODS OF USE as reagents for blood grouping and for the identification of (76) Inventors: L. Scott Rodkey, 6234 Yarwell, red cell membrane components associated with Rh antigen Houston, TX (US) 77096; Marwan A. activity,” Revue Francaise de Transfusion et Immuno-hé Yared; Kenneth J. Moise, Jr., both of matologie, 31(2):141-144, 1988. 4234 Tennyson, Houston, TX (US) 77005 Paradis et al., “Protective Effect of the Membrane Skeleton (*) Notice: Under 35 U.S.C. 154(b), the term of this on the Immunologic Reactivity of the Human Red Cell patent shall be extended for 0 days. Rho(D) Antigen,” J. Immunol., 137:240–244, 1986. Plapp et al., “Partial Purification of Rh(D) Antigen from Rh (21) Appl. No.: 09/164,789 Positive and Negative Erythrocytes,” Proc. Natl. Acad. Sci. (22) Filed: Oct. 1, 1998 USA, 76:2964-2968, 1979. Related U.S. Application Data Yokoi et al. “Isolation and Purification of Rh(D) Antigen of Human Erythrocyte Membrane and Its Serological Prop 62) DivisiVision off application No.NO. 08/715,173,f3, filedilled On Sep. 17If, 1996, now Pat. No. 5,840,585. erty,’” J. Exp. Med., 141:143–154, 1983. (51) Int. Cl." ..................................................... A61K 38/00 Foreign Search Report dated Dec. 2, 1997. (52) U.S. Cl. ............................................... 514/12; 530/380 (58) Field of Search ................................ 514/12; 530/380 Oellerich M., “Enzyme-Immunoassay: A Review,” J.
    [Show full text]
  • A Review: the Duffy Blood Group System
    A review: the Duffy blood group system K.M. BEATTIE In 1950, two reports described an antibody that had neuraminidase. On the other hand, Fy3, Fy4, and Fy5 been found during the investigation of a hemolytic are not affected. Reactionswith purified trypsin show transfusion reaction in the serum of a 43-year-old man that the Fysup(a) antigen is unaffected and Fy sup(b) is only slightly suffering from hemophilia. 1,2 After the unidentified reduced in strength; Fy3 and Fy6 are slightly enhanced. antibody had been separated from the anti-D, anti-A, The trypsin most commonly used by blood bankers and anti-Bin his serum, it was tested against the blood is a crude preparation that is contaminated with chymo- of 205 unrelated English adults; 64.9 percent were ,agglu- trypsin; therefore, results obtained with that product tinated. With the permission of the patient, the new would approximate those resulting from chymotrypsin blood group system was named Duffy The antigen was treatment. designated as Fysup(a), the gene responsible for it, Fy sup(a), and Inactivation of Fy determinants is such that they are its hypothetical allele, Fysup(b). Anti-Fysup(b) was reported the no longer capable of adsorbing their antithetical anti- following year in the serum of a German woman who bodies. This is not due to the removal of sialic acid but had been pregnant three times but not transfused.sup(3) probably represents proteolytic action on cell membrane Four years later, Fy(a-b-) was reported to be the proteins. Fy(a-b-) red cells are not sialic acid deficient most common phenotype in American blacks.sup(4) and their electrophoretic mobility is normal.
    [Show full text]
  • Rbgp-An-International-Study.Pdf
    IMMUNOHEMATOLOGY Recombinant blood group proteins facilitate the detection of alloantibodies to high-prevalence antigens and reveal underlying antibodies: results of an international study Axel Seltsam,1 Franz Wagner,1 Mark Lambert,2 Tom Bullock,3 Nicole Thornton,3 Erwin A. Scharberg,4 Daniela Grueger,5 Clemens Schneeweiss,5 and Rainer Blasczyk6 n current blood transfusion practice, red blood cell BACKGROUND: Alloantibodies to high-prevalence red (RBC) antibodies are identified using panels of blood cell (RBC) antigens are not easily identified by human RBCs pretyped for the most common blood routine serologic techniques. This multicenter study was group antigens. The specificity of a given antibody is conducted to test the effectiveness of recombinant Iidentified based on the pattern of reactivity observed blood group proteins (rBGPs) at regional and interna- when serum is tested with the cell panel. Since many anti- tional RBC reference laboratories. gens are expressed on RBCs, antibody identification in STUDY DESIGN AND METHODS: Single or mixed RBC-based assays relies on nonreactivity of an antibody soluble rBGPs (Lu, Yt, Kn, JMH, Sc, Rg, Ch, Do, and with panel cells lacking the corresponding antigen. This Cr) were assessed for their ability to inhibit the reactiv- method of antibody identification is challenged if autoan- ity of antibodies to specific antigens. Initially, the effect tibodies, multiple antibodies, or antibodies to high- of rBGPs was validated by testing panels of well- prevalence antigens are present. In such cases, rare characterized patient serum samples containing antisera and cells as well as specially trained personnel antibodies to high-prevalence antigens in the hemagglu- not available to routine laboratories are required for tination inhibition assay.
    [Show full text]
  • Antigens to Detect Or Inhibit Antibodies to Knops (Kn) Blood Group System Antigens
    PRODUCTION OF SOLUBLE RECOMBINANT COMPLEMENT RECEPTOR 1 (CR1) ANTIGENS TO DETECT OR INHIBIT ANTIBODIES TO KNOPS (KN) BLOOD GROUP SYSTEM ANTIGENS WENDY ETHERIDGE A thesis submitted in partial fulfilment of the requirements of the University of the West of England, Bristol for the Professional Doctorate in Biomedical Science Faculty of Applied Sciences, University of the West of England, Bristol October 2014 ABSTRACT The purpose of this study was to produce a reagent to use in investigation of antibodies directed against the Knops blood group system antigens. A novel reagent based on sr-proteins was produced and used in a new test to inhibit these antibodies. Current investigation of patients with alloantibodies directed against Knops blood group system antigens can be a difficult, time-consuming process and the provision of blood for transfusion of these patients can often be delayed. This is because these antibodies are hard to identify and the most commonly found anti-Knops antibodies react with most reagent or donor cells that they are tested with because the corresponding Knops antigens are found at high frequency in most populations. The presence of Knops related antibodies can mask underlying antibodies that are clinically significant. The Knops antigens are carried on Complement Receptor 1 (CR1) located on the red blood cell membrane. Two DNA constructs encoding different parts of CR1 termed long homologous repeat (LHR) C and D were used to transfect human embryonic kidney (HEK293) cells. The cells were grown in different culture systems. Cell culture supernatant containing soluble recombinant (sr)-LHRC or sr-LHR-D was harvested and purified by affinity gel chromatography.
    [Show full text]
  • FACT-JACIE International Standards for HEMATOPOIETIC CELLULAR THERAPY Product Collection, Processing, and Administration SEVENTH EDITION 7.0
    FACT-JACIE International Standards for HEMATOPOIETIC CELLULAR THERAPY Product Collection, Processing, and Administration SEVENTH EDITION 7.0 INTERNATIONAL STANDARDS FOR HEMATOPOIETIC CELLULAR THERAPY PRODUCT COLLECTION, PROCESSING, AND ADMINISTRATION Seventh Edition Version 7.0 March 2018 NOTICE These Standards are designed to provide minimum guidelines for programs, facilities, and individuals performing cellular therapy or providing support services for such procedures. These Standards are not intended to establish best practices or include all procedures and practices that a program, facility, or individual should implement if the standard of practice in the community or applicable governmental laws or regulations establish additional requirements. Each program, facility, and individual should analyze its practices and procedures to determine whether additional standards apply. Compliance with these Standards is not an exclusive means of complying with the standard of care in the industry or community or with local, national, or international laws or regulations. The Foundation for the Accreditation of Cellular Therapy and the Joint Accreditation Committee – ISCT and EBMT expressly disclaim any responsibility for setting maximum standards and further expressly disclaim any responsibility, liability, or duty to member programs, directors, staff, or program donors or patients for any such liability arising out of injury or loss to any person by the failure of member programs, directors, or staff to adhere to the Standards or related
    [Show full text]
  • AN IMMUNOCHEMICAL INVESTIGATION of the Wr* and Wrb BLOOD GROUP ANTIGENS
    AN IMMUNOCHEMICAL INVESTIGATION OF THE Wr* AND Wrb BLOOD GROUP ANTIGENS. SUSAN MARGARET RING A thesis submitted for the degree of Doctor of Philosophy. Department of Genetics. University College London. August 1992. ProQuest Number: 10608858 All rights reserved INFORMATION TO ALL USERS The quality of this reproduction is dependent upon the quality of the copy submitted. In the unlikely event that the author did not send a com plete manuscript and there are missing pages, these will be noted. Also, if material had to be removed, a note will indicate the deletion. uest ProQuest 10608858 Published by ProQuest LLC(2017). Copyright of the Dissertation is held by the Author. All rights reserved. This work is protected against unauthorized copying under Title 17, United States C ode Microform Edition © ProQuest LLC. ProQuest LLC. 789 East Eisenhower Parkway P.O. Box 1346 Ann Arbor, Ml 48106- 1346 ABSTRACT This thesis describes the production of a monoclonal antibody to the low incidence blood group antigen Wr3 which is thought to be allelic to Wr*5 (a high frequency antigen known to be associated with glycophorin A and band 3). The main approach was to immunise mice with Wr(a+) red cells and select appropriate antibodies by screening them against a panel of red cells by haemagglutination. One anti-Wr3 antibody (BGU1-WR) was found from the 1074 hybridomas screened. BGU1-WR belongs to immunoglobulin subclass IgGl and has an affinity constant of 1.82x10^. This antibody and a previously described anti-Wr*5 monoclonal antibody was used to investigate the nature of the antigens.
    [Show full text]
  • EMP3 Enhances Erythroid Proliferation and Causes the MAM-Negative Phenotype ✉ Nicole Thornton 1,11 , Vanja Karamatic Crew 1,11, Louise Tilley1,11, Carole A
    ARTICLE https://doi.org/10.1038/s41467-020-17060-4 OPEN Disruption of the tumour-associated EMP3 enhances erythroid proliferation and causes the MAM-negative phenotype ✉ Nicole Thornton 1,11 , Vanja Karamatic Crew 1,11, Louise Tilley1,11, Carole A. Green2, Chwen Ling Tay1, Rebecca E. Griffiths 2, Belinda K. Singleton2, Frances Spring2, Piers Walser1, Abdul Ghani Alattar 3, Benjamin Jones1, Rosalind Laundy1, Jill R. Storry 3,4, Mattias Möller 3, Lorna Wall 5, Richard Charlewood 5, Connie M. Westhoff6, Christine Lomas-Francis6, Vered Yahalom7, Ute Feick8, Axel Seltsam9, Beate Mayer 10, Martin L. Olsson 3,4,12 & David J. Anstee2,12 1234567890():,; The clinically important MAM blood group antigen is present on haematopoietic cells of all humans except rare MAM-negative individuals. Its molecular basis is unknown. By whole- exome sequencing we identify EMP3, encoding epithelial membrane protein 3 (EMP3), as a candidate gene, then demonstrate inactivating mutations in ten known MAM-negative individuals. We show that EMP3, a purported tumour suppressor in various solid tumours, is expressed in erythroid cells. Disruption of EMP3 by CRISPR/Cas9 gene editing in an immortalised human erythroid cell line (BEL-A2) abolishes MAM expression. We find EMP3 to associate with, and stabilise, CD44 in the plasma membrane. Furthermore, cultured ery- throid progenitor cells from MAM-negative individuals show markedly increased proliferation and higher reticulocyte yields, suggesting an important regulatory role for EMP3 in ery- thropoiesis and control of cell production. Our data establish MAM as a new blood group system and demonstrate an interaction of EMP3 with the cell surface signalling molecule CD44.
    [Show full text]
  • ANZSBT Oral Abstracts Annual Scientific Meeting October 2003 - Christchurch, New Zealand
    ANZSBT Oral Abstracts Annual Scientific Meeting October 2003 - Christchurch, New Zealand ANZSBT ORAL ABSTRACTS FROM The HSANZ/ANZSBT/ASTH Annual Scientific Meeting October 2003 Christchurch, New Zealand ANZSBT Oral Abstracts Annual Scientific Meeting October 2003 - Christchurch, New Zealand 6 Do Blood Group Antigens Play A Biological Role? Garratty G American Red Cross Blood Services, and University of California, Los Angeles, CA There have been thousands of publications purporting to show an association of blood group antigens (BGAs) and disease. Most of these are statistical associations of ABO with various conditions. The first report was as early as 1917. Many of these studies were small and/or not repeatable, but some were large studies and/or the results have been duplicated by many investigators. Although some of the associations seem more akin to astrology than science, others appear now to have a scientific rationale. Some areas of interest have been: BGA associations with 1) malignancy (e.g., BGAs as tumor antigens and adhesion molecules enhancing metastatic potential; 2) receptors for parasites (e.g., malaria/Duffy), bacteria (e.g., E. coli/P, H. pylori/ABH, Le); viruses (e.g., Parvovirus B19/P, HIV/ABO, Le); 3) coagulation (e.g., bleeding/O↑, thrombosis/A↑, Factor VIII/A↑, vW factor/A↑; immunological ligands (e.g., complement/Bg, Ch, Kn, McC, Yk, Cr; adhesion molecules/s-Lex, Lu, Inb (CD44); cytokines/Duffy; integrins/LW). Most of these associations relate to cells other than RBCs, but BGAs may perhaps sometimes play a role as functional molecules in the RBC membrane. Rare null phenotypes sometimes have abnormally shaped RBCs (e.g., Rhnull/stomatocytes; McLeod syndrome (Kell)/acanthocytes; Leach phenotype (Gerbich)/elliptocytes).
    [Show full text]
  • 1971 to 1980 Lister Annual Report and Accounts
    THE LISTER INSTITUTE OF PREVENTIVE MEDICINE Balance Sheet and Accounts 31 DECEMBER 1971 CHELSEA BRIDGE ROAD . LONDON, S.W.I. 23 MAY, 1971 The Governing Body Professor A. NEUBERGER, CBE, md, frcp, frc path, frs, Chairman R. A. McNEILE, mbe, Hon. Treasurer Professor D. A. K. BLACK, M sc, md, frcp Professor D. G. EVANS, cbe, d sc, frc path, frs C. E. GUINNESS Professor HENRY HARRIS, mb, d phil, frs The Rt Hon the EARL OF IVEAGH Professor Sir EWART JONES, D sc, frs Dr. A. F. B. STANDFAST, sc d Clerk to the Governors ... S. A. WHITE, ACCA Financial Report of the Governing Body The Governing Body presents the accounts accounts. These include further payments of the Institute for the year ended on account of the new wing at Chelsea, the 31st December 1971. cost of which is expected to be about 1. Results £400,000. The Governors have transferred to Capital Fund a further £25,000 from the The General Fund Income and Expendi­ Sinking Fund, first set up in 1901 for the ture Account shows the Income for the year replacement and repair of buildings, towards as £405,796 compared with £344,136 in the cost of this new wing. 1970. Expenditure amounted to £545,583 against £495,405 last year. The deficit for 5. Interests in Land the year is £139,787 compared with a deficit The market value of the Institute’s pro­ of £151,269 in 1970. The capital fund has perties is now in excess of the amount at been reduced by the year’s deficit of which they are included in the Balance £139,787.
    [Show full text]
  • Marilyn Jo Telen, MD Primary Academic Appointment
    CURRICULUM VITAE Name: Marilyn Jo Telen, M.D. Primary academic appointment: Professor (with tenure) Department of Medicine Division of Hematology Secondary appointment: Associate Professor Department of Pathology Present academic rank and title: Wellcome Professor of Medicine Division of Hematology Associate Professor of Pathology Assoc. Med. Director, Transfusion Service Director, Duke Comprehensive Sickle Cell Center Medical licensure: Diplomate of National Boards Medical licensure, North Carolina Specialty certification and dates: Diplomate, American Board of Internal Medicine, 1980 Diplomate, ABIM Subspecialty of Hematology, 1984 Citizenship: U.S.A. Education: Place Date Degree G.W. Hewlett High Sch. Hewlett, NY 1961-1965 Regents diploma Vassar College Poughkeepsie, NY 1965-1969 A.B., cum laude New York University New York, NY 1973-1977 M.D. Honors: Matthew Vassar Scholar; Esso Foundation Premedical Scholarship; American Society for Clinical Investigation; Association of American Physicians; Fellow of the American Association for the Advancement of Science; Almita S. R. Woods Award, State of North Carolina Department of Health and Human Services 2004; Duke Medical Alumni Distinguished Faculty Award 2008; Fulbright Scholar (Russia) 2010; Petteway- Shepherd Award, NCABB 2011; American Clinical and Climatological Assocation; 2014 Duke University Research Mentoring Award for Translational Research. Marilyn J. Telen, M.D. Professional training and academic career: Intern in Medicine, Department of Medicine, State University of New York
    [Show full text]
  • Journal of Blood Group Serology and Education Volume 3, No
    American Red Cross Journal of Blood Group Serology and Education Volume 3, No. 1, 1987 CONTENTS SOME NEW Rh ANTIGENS Rh43 TO Rh47 Some New Rb Antigens: Rh43 to Rh47 Peter D. Issitt, Nancy S. Gutgsell Peter D. Issitt, Nancy S. Gutgsell 1 Stimulation of Antibody Following sup(51)Chromium Survival Studies Introduction Susan S Esty, Tracy Wahl, Julie Zawisza In 1962, Rosenfield et al sup(1) reviewed the serology of the Rh blood group Delores Mallory, Richard J Davey 6 system and introduced a numerical terminology. Numbers for the anti- An Example of Mild Hemolytic Disease of the Newborn Caused by gens Rhl to Rh21 were assigned in the text of that report, Rh22 to Rh25 Anti-Cob were listed in an addendum printed as part of the paper. A number of Nancy B. Steffey, Mary A. Lieb 9 reports of new Rh antigens were reviewed by Allen and Rosenfieldsup(2) in Book Review Red Cell Antigens and 1972; in that paper the numbers Rh26 to Rh33 were assigned. In a later Antibodies review, sup(3) time on Rh genetics, Rh34 was named. The term Rh35 seems Mary H. McGinniss 10 this first to have been used in two textbooks published in 1975.sup(4,5) When COMMUNICATIONS: Letter From the Editor 11 we sup(6) described the first examples of anti-Rh39 in 1979, we took the op- ISBT Announcement 11 portunity to update the numerical Rh terminology from Rh36 to Rh39. Instructions for Submitting Articles 11 The next three Rh antigens to be discovered were assigned numbers by Classified Ads 12 the authors first describing them.
    [Show full text]