Immunohematology
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Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse
Welcome to More Choice CD Marker Handbook For more information, please visit: Human bdbiosciences.com/eu/go/humancdmarkers Mouse bdbiosciences.com/eu/go/mousecdmarkers Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse CD3 CD3 CD (cluster of differentiation) molecules are cell surface markers T Cell CD4 CD4 useful for the identification and characterization of leukocytes. The CD CD8 CD8 nomenclature was developed and is maintained through the HLDA (Human Leukocyte Differentiation Antigens) workshop started in 1982. CD45R/B220 CD19 CD19 The goal is to provide standardization of monoclonal antibodies to B Cell CD20 CD22 (B cell activation marker) human antigens across laboratories. To characterize or “workshop” the antibodies, multiple laboratories carry out blind analyses of antibodies. These results independently validate antibody specificity. CD11c CD11c Dendritic Cell CD123 CD123 While the CD nomenclature has been developed for use with human antigens, it is applied to corresponding mouse antigens as well as antigens from other species. However, the mouse and other species NK Cell CD56 CD335 (NKp46) antibodies are not tested by HLDA. Human CD markers were reviewed by the HLDA. New CD markers Stem Cell/ CD34 CD34 were established at the HLDA9 meeting held in Barcelona in 2010. For Precursor hematopoetic stem cell only hematopoetic stem cell only additional information and CD markers please visit www.hcdm.org. Macrophage/ CD14 CD11b/ Mac-1 Monocyte CD33 Ly-71 (F4/80) CD66b Granulocyte CD66b Gr-1/Ly6G Ly6C CD41 CD41 CD61 (Integrin b3) CD61 Platelet CD9 CD62 CD62P (activated platelets) CD235a CD235a Erythrocyte Ter-119 CD146 MECA-32 CD106 CD146 Endothelial Cell CD31 CD62E (activated endothelial cells) Epithelial Cell CD236 CD326 (EPCAM1) For Research Use Only. -
The Membrane Complement Regulatory Protein CD59 and Its Association with Rheumatoid Arthritis and Systemic Lupus Erythematosus
Current Medicine Research and Practice 9 (2019) 182e188 Contents lists available at ScienceDirect Current Medicine Research and Practice journal homepage: www.elsevier.com/locate/cmrp Review Article The membrane complement regulatory protein CD59 and its association with rheumatoid arthritis and systemic lupus erythematosus * Nibhriti Das a, Devyani Anand a, Bintili Biswas b, Deepa Kumari c, Monika Gandhi c, a Department of Biochemistry, All India Institute of Medical Sciences, New Delhi 110029, India b Department of Zoology, Ramjas College, University of Delhi, India c University School of Biotechnology, Guru Gobind Singh Indraprastha University, India article info abstract Article history: The complement cascade consisting of about 50 soluble and cell surface proteins is activated in auto- Received 8 May 2019 immune inflammatory disorders. This contributes to the pathological manifestations in these diseases. In Accepted 30 July 2019 normal health, the soluble and membrane complement regulatory proteins protect the host against Available online 5 August 2019 complement-mediated self-tissue injury by controlling the extent of complement activation within the desired limits for the host's benefit. CD59 is a membrane complement regulatory protein that inhibits the Keywords: formation of the terminal complement complex or membrane attack complex (C5b6789n) which is CD59 generated on complement activation by any of the three pathways, namely, the classical, alternative, and RA SLE the mannose-binding lectin pathway. Animal experiments and human studies have suggested impor- Pathophysiology tance of membrane complement proteins including CD59 in the pathophysiology of rheumatoid arthritis Disease marker (RA) and systemic lupus erythematosus (SLE). Here is a brief review on CD59 and its distribution, structure, functions, and association with RA and SLE starting with a brief introduction on the com- plement system, its activation, the biological functions, and relations of membrane complement regu- latory proteins, especially CD59, with RA and SLE. -
Supplementary Material Contents
Supplementary Material Contents Immune modulating proteins identified from exosomal samples.....................................................................2 Figure S1: Overlap between exosomal and soluble proteomes.................................................................................... 4 Bacterial strains:..............................................................................................................................................4 Figure S2: Variability between subjects of effects of exosomes on BL21-lux growth.................................................... 5 Figure S3: Early effects of exosomes on growth of BL21 E. coli .................................................................................... 5 Figure S4: Exosomal Lysis............................................................................................................................................ 6 Figure S5: Effect of pH on exosomal action.................................................................................................................. 7 Figure S6: Effect of exosomes on growth of UPEC (pH = 6.5) suspended in exosome-depleted urine supernatant ....... 8 Effective exosomal concentration....................................................................................................................8 Figure S7: Sample constitution for luminometry experiments..................................................................................... 8 Figure S8: Determining effective concentration ......................................................................................................... -
Anti-Glycophorin a Antibody (Biotin) Product Number: AC12-0684-07
Anti-Glycophorin A Antibody (Biotin) Product Number: AC12-0684-07 Overview Host Species: Rabbit Clonality: Monoclonal (GYPA/1725R) Purity: Antibody is purified by Protein A. The antibody is then conjugated to biotin, also known as vitamin B7, vitamin H, or coenzyme R, which is a small molecule which has an extremely high affinity for avidin and streptavidin. Isotype: IgG Conjugate: Biotin Immunogen Type: Anti-glycophorin a antibody was raised against recombinant full-length human glycophorin A protein. Physical Characteristics Amount: 0.05 mg Concentration: 1 mg/ml Volume: 0.05 ml Buffer: Antibody is purified by Protein A. Prepared in 10mM PBS at 1.0mg/ml. Storage: Biotin conjugated antibody can be stored at 4?C for up to 18 months. For longer storage the conjugate can be stored at -20?C after adding 50% glycerol. Specificity Species Reactivity: Human Specificity: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation. Target Information Accession Number(s): Swissprot: P02724 (Human) -
ABH Secretor and Lewis Subtype Status Peter J
Metabolic and Immunologic Consequences of ABH Secretor and Lewis Subtype Status Peter J. D’Adamo, ND, and Gregory S. Kelly, ND Abstract Determining ABH secretor phenotype and/or Lewis (Le) blood group status can be useful to the metabolically-oriented clinician. For example, differences in ABH secretor status drastically alter the carbohydrates present in body fluids and secretions; this can have profound influence on microbial attachment and persistence. Lewis typing is one genetic marker which might help identify subpopulations of individuals genetically prone to insulin resistance, autoimmunity, and heart disease. Understanding the clinical significance of ABH secretor status and the Lewis blood groups can provide insight into seemingly unrelated aspects of physiology, including variations in intestinal alkaline phosphatase activity, propensities toward blood clotting, reliability of some tumor markers, the composition of breast milk, and several generalized aspects of the immune function. Since the relevance of ABH blood group antigens as tumor markers and parasitic/bacterial/viral receptors and their association with immunologically important proteins is now well established, the prime biologic role for ABH blood group antigens may well be independent and unrelated to the erythrocyte. (Altern Med Rev 2001;6(4):390-405) Functional and Genetic Factors Involved in ABH Secretion The term “ABH secretor,” as used in blood banking, refers to secretion of ABO blood group antigens in fluids such as saliva, sweat, tears, semen, and serum. A person who is an ABH secretor will secrete antigens according to their blood group; for example, a group O individual will secrete H antigen, a group A individual will secrete A and H antigens, etc. -
New Methods for Characterization of N-Type Glycosylation of Proteins by Integration of LC-MS/MS and NMR
New Methods for Characterization of N-type Glycosylation of Proteins by Integration of LC-MS/MS and NMR Thesis Submitted in fulfillment of the requirements of the degree Doctor rer. nat. at the Department of Chemistry, Faculty of Sciences, University of Hamburg by Alena Wiegandt from Hamburg Hamburg, 2016 This thesis was prepared at the Institute for Organic Chemistry from October 2012 to July 2016 (managing director: Prof. Dr. C.B.W. Stark). I would like to thank Prof. Dr. Bernd Meyer for his continuous and motivating support during the work on my PhD thesis. I would like to thank Prof. Dr. Dr. h. c. mult. Wittko Francke for being the second reviewer of this thesis. 1st Reviewer: Prof. Dr. Bernd Meyer 2nd Reviewer: Prof. Dr. Dr. h.c. mult. Wittko Francke Date of defense: 07.04.2017 OUTLINE Outline ABBREVIATIONS ..................................................................................................................... VIII 1 SUMMARY ............................................................................................................................ 1 2 ZUSAMMENFASSUNG .......................................................................................................... 4 3 INTRODUCTION ................................................................................................................... 7 3.1 Glycosylation of Proteins - Biosynthesis, Structures, Functions .................................... 8 3.2 Glycans in Human Diseases ......................................................................................... -
A Comprehensive Review of Our Current Understanding of Red Blood Cell (RBC) Glycoproteins
membranes Review A Comprehensive Review of Our Current Understanding of Red Blood Cell (RBC) Glycoproteins Takahiko Aoki Laboratory of Quality in Marine Products, Graduate School of Bioresources, Mie University, 1577 Kurima Machiya-cho, Mie, Tsu 514-8507, Japan; [email protected]; Tel.: +81-59-231-9569; Fax: +81-59-231-9557 Received: 18 August 2017; Accepted: 24 September 2017; Published: 29 September 2017 Abstract: Human red blood cells (RBC), which are the cells most commonly used in the study of biological membranes, have some glycoproteins in their cell membrane. These membrane proteins are band 3 and glycophorins A–D, and some substoichiometric glycoproteins (e.g., CD44, CD47, Lu, Kell, Duffy). The oligosaccharide that band 3 contains has one N-linked oligosaccharide, and glycophorins possess mostly O-linked oligosaccharides. The end of the O-linked oligosaccharide is linked to sialic acid. In humans, this sialic acid is N-acetylneuraminic acid (NeuAc). Another sialic acid, N-glycolylneuraminic acid (NeuGc) is present in red blood cells of non-human origin. While the biological function of band 3 is well known as an anion exchanger, it has been suggested that the oligosaccharide of band 3 does not affect the anion transport function. Although band 3 has been studied in detail, the physiological functions of glycophorins remain unclear. This review mainly describes the sialo-oligosaccharide structures of band 3 and glycophorins, followed by a discussion of the physiological functions that have been reported in the literature to date. Moreover, other glycoproteins in red blood cell membranes of non-human origin are described, and the physiological function of glycophorin in carp red blood cell membranes is discussed with respect to its bacteriostatic activity. -
Platelet Proteome Reveals Specific Proteins Associated with Platelet Activation and the Hypercoagulable State in Β-Thalassmia/H
www.nature.com/scientificreports OPEN Platelet proteome reveals specifc proteins associated with platelet activation and the hypercoagulable Received: 24 October 2018 Accepted: 29 March 2019 state in β-thalassmia/HbE patients Published: xx xx xxxx Puangpaka Chanpeng1, Saovaros Svasti2, Kittiphong Paiboonsukwong2, Duncan R. Smith 3 & Kamonlak Leecharoenkiat1 A hypercoagulable state leading to a high risk of a thrombotic event is one of the most common complications observed in β-thalassemia/HbE disease, particularly in patients who have undergone a splenectomy. However, the hypercoagulable state, as well as the molecular mechanism of this aspect of the pathogenesis of β-thalassemia/HbE, remains poorly understood. To address this issue, ffteen non-splenectomized β-thalassemia/HbE patients, 8 splenectomized β-thalassemia/HbE patients and 20 healthy volunteers were recruited to this study. Platelet activation and hypercoagulable parameters including levels of CD62P and prothrombin fragment 1 + 2 were analyzed by fow cytometry and ELISA, respectively. A proteomic analysis was conducted to compare the platelet proteome between patients and normal subjects, and the results were validated by western blot analysis. The β-thalassemia/ HbE patients showed signifcantly higher levels of CD62P and prothrombin fragment 1 + 2 than normal subjects. The levels of platelet activation and hypercoagulation found in patients were strongly associated with splenectomy status. The platelet proteome analysis revealed 19 diferential spots which were identifed to be 19 platelet proteins, which included 10 cytoskeleton proteins, thrombin generation related proteins, and antioxidant enzymes. Our fndings highlight markers of coagulation activation and molecular pathways known to be associated with the pathogenesis of platelet activation, the hypercoagulable state, and consequently with the thrombosis observed in β-thalassemia/HbE patients. -
Resolving the Distinct Stages in Erythroid Differentiation Based on Dynamic Changes in Membrane Protein Expression During Erythropoiesis
Resolving the distinct stages in erythroid differentiation based on dynamic changes in membrane protein expression during erythropoiesis Ke Chena,1, Jing Liua,1, Susanne Heckb, Joel A. Chasisc, Xiuli Ana,d,2, and Narla Mohandasa aRed Cell Physiology Laboratory, bFlow Cytometry Core, New York Blood Center, New York, NY 10065; cLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; and dDepartment of Biophysics, Peking University Health Science Center, Beijing 100191, China Communicated by Joseph F. Hoffman, Yale University School of Medicine, New Haven, CT, August 18, 2009 (received for review June 25, 2009) Erythropoiesis is the process by which nucleated erythroid progeni- results in loss of cohesion between the bilayer and the skeletal tors proliferate and differentiate to generate, every second, millions network, leading to membrane loss by vesiculation. This diminution of nonnucleated red cells with their unique discoid shape and mem- in surface area reduces red cell life span with consequent anemia. brane material properties. Here we examined the time course of A number of additional transmembrane proteins, including CD44 appearance of individual membrane protein components during and Lu, have been characterized, although their structural organi- murine erythropoiesis to throw new light on our understanding of zation in the membrane has not been fully defined. the evolution of the unique features of the red cell membrane. We Some transmembrane proteins exhibit multiple functions. Band found that the accumulation of all of the major transmembrane and 3 serves as an anion exchanger, while Rh/RhAG are probably gas all skeletal proteins of the mature red blood cell, except actin, accrued transporters (8, 9), and Duffy functions as a chemokine receptor progressively during terminal erythroid differentiation. -
Blood Group Have Increased Susceptibility to Symptomatic \(Vibrio\) \(Cholerae\) O1 Infection
Individuals with Le(a+b−) Blood Group have Increased Susceptibility to Symptomatic \(Vibrio\) \(cholerae\) O1 Infection The Harvard community has made this article openly available. Please share how this access benefits you. Your story matters Citation Arifuzzaman, Mohammad, Tanvir Ahmed, Mohammad Arif Rahman, Fahima Chowdhury, Rasheduzzaman Rashu, Ashraful I. Khan, Regina C. LaRocque, et al. 2011. Individuals with Le(a+b−) blood group have increased susceptibility to symptomatic \(Vibrio\) \(cholerae\) O1 infection. PLoS Neglected Tropical Diseases 5(12): e1413. Published Version doi:10.1371/journal.pntd.0001413 Citable link http://nrs.harvard.edu/urn-3:HUL.InstRepos:9369412 Terms of Use This article was downloaded from Harvard University’s DASH repository, and is made available under the terms and conditions applicable to Other Posted Material, as set forth at http:// nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of- use#LAA Individuals with Le(a+b2) Blood Group Have Increased Susceptibility to Symptomatic Vibrio cholerae O1 Infection Mohammad Arifuzzaman1,2, Tanvir Ahmed1, Mohammad Arif Rahman1, Fahima Chowdhury1, Rasheduzzaman Rashu1, Ashraful I. Khan1, Regina C. LaRocque2,3, Jason B. Harris2,4, Taufiqur Rahman Bhuiyan1, Edward T. Ryan2,3,5, Stephen B. Calderwood2,3,6., Firdausi Qadri1*. 1 Centre for Vaccine Sciences, International Centre for Diarrhoeal Disease Research Bangladesh (ICDDR,B), Dhaka, Bangladesh, 2 Division of Infectious Diseases, Massachusetts General Hospital, Boston, Massachusetts, United States of America, -
Concentration of an Integral Membrane Protein, CD43
Concentration of an Integral Membrane Protein, CD43 (Leukosialin, Sialophofin), in the Cleavage Furrow through the Interaction of Its Cytoplasmic Domain with Actin-based Cytoskeletons Shigenobu Yonemura,* Akira Nagafuchi,* Naruki Sato,** and Shoichiro Tsukita*r * Laboratory of Cell Biology, Department of Information Physiology,National Institute for Physiological Sciences, Okazaki, Aichi 444, Japan; and *Department of Physiological Sciences, School of Life Science, The Graduate University of Advanced Studies, Myodaiji-cho, Okazaki, Aichi 444, Japan Abstract. In leukocytes such as thymocytes and consisting of the extracellular domain of mouse Downloaded from http://rupress.org/jcb/article-pdf/120/2/437/1256004/437.pdf by guest on 24 September 2021 basophilic leukemia cells, a glycosilated integral mem- E-cadherin and the transmembrane/cytoplasmic do- brane protein called CIM3 (leukosialin or sialopho- main of rat CD43, and introduced it into mouse L rin), which is defective in patients with Wiskott- fibroblasts lacking both endogenous CD43 and Aldrich syndrome, was highly concentrated in the E-cadherin. In dividing transfectants, the chimeric cleavage furrow during cytokinesis. Not only at the molecules were concentrated in the cleavage furrow mitotic phase but also at interphase, CIM3 was pre- together with ERM, and both proteins were precisely cisely colocalized with ezrin-radixin-moesin family colocalized throughout the cell cycle. Furthermore, members (ERM), which were previously reported to using this transfection system, we narrowed down the play an important role in the plasma membrane-actin domain responsible for the CD43-concentration in the filament association in general. At the electron micro- cleavage furrow. Based on these findings, we conclude scopic level, throughout the cell cycle, both CIM3 and that CD43 is concentrated in the cleavage furrow ERM were tightly associated with microvilli, provid- through the direct or indirect interaction of its cyto- ing membrane attachment sites for actin filaments. -
CD System of Surface Molecules
THE CD SYSTEM OF LEUKOCYTE APPENDIX 4A SURFACE MOLECULES Monoclonal Antibodies to Human Cell Surface Antigens APPENDIX 4A Alice Beare,1 Hannes Stockinger,2 Heddy Zola,1 and Ian Nicholson1 1Women’s and Children’s Health Research Institute, Women’s and Children’s Hospital, Adelaide, Australia 2Institute of Immunology, University of Vienna, Vienna ABSTRACT Many of the leukocyte cell surface molecules are known by “CD” numbers. In this Appendix, a short introduction describes the history and the use of CD nomenclature and provides a few key references to enable access to the wider literature. This is followed by a table that lists all human molecules with approved CD names, tabulating alternative names, key structural features, cellular expression, major known functions, and usefulness of the molecules or antibodies against them in research or clinical applications. Curr. Protoc. Immunol. 80:A.4A.1-A.4A.73. C 2008 by John Wiley & Sons, Inc. Keywords: CD nomenclature r HLDA r HCDM r leukocyte marker r human leukocyte differentiation r antigens INTRODUCTION During the last 25 years, large numbers of monoclonal antibodies (MAbs) have been pro- duced that have facilitated the purification and functional characterization of a plethora of leukocyte surface molecules. The antibodies have been even more useful as markers for cell populations, allowing the counting, separation, and functional study of numer- ous subsets of cells of the immune system. A series of international workshops were instrumental in coordinating this development through multi-laboratory “blind” studies of thousands of antibodies. These HLDA (Human Leukocyte Differentiation Antigens) Workshops have, up until now, defined 500 different entities and assigned them cluster of differentiation (CD) designations.