Pulmonary Extranodal Marginal Zone Lymphoma That Presented

Total Page:16

File Type:pdf, Size:1020Kb

Pulmonary Extranodal Marginal Zone Lymphoma That Presented lin Journal of clinical and experimental hematopathology JC Vol. 58 No.3, 141-147, 2018 EH xp ematopathol Case report Pulmonary extranodal marginal zone lymphoma that presented with macroglobulinemia and marked plasmacytic cell proliferation carrying the t(14;18)(q32;q21)/MALT1- immunoglobulin heavy-chain fusion gene in pleural fluid Takashi Akasaka,1) Chiyuki Kishimori,2) Fumiyo Maekawa,2) Kayo Takeoka,2) 2) 3) 3) 1),2) Masahiko Hayashida, Hiroshi Gomyo, Tohru Murayama, and Hitoshi Ohno An 80-year-old man presented with the accumulation of pleural fluid in the right thoracic cavity. Serum electrophoresis revealed an M-component and immunofixation confirmed IgM/λ. The level of IgM was 1,526 mg/dL. Imaging studies showed an infil- trative condition of the ipsilateral lung parenchyma. The fluid contained abundant neoplastic cells with the morphological and immunophenotypic features of plasma cells, which expressed IgM/λ monoclonal immunoglobulins on the cell surface and in the cytoplasm. The karyotype was 48,XY,+3,add(9)(p13),+12,add(14)(q32),del(16)(q22),−18,+mar, and a series of fluores- cence in situ hybridization studies demonstrated that the add(14) chromosome represented der(14)t(14;18)(q32;q21), at which the MALT1-immunoglobulin heavy-chain (IGH) fusion gene was localized. A long-distance polymerase chain reaction ampli- fied the fragment encompassing the two genes, showing that the junction occurred at the J6 segment of IGH and 3.7-kb upstream of the MALT1 breakpoint cluster. We propose that this case represents an extreme form of the plasmacytic differenti- ation of extranodal marginal zone lymphoma that developed in the lung. Keywords: macroglobulinemia, extranodal marginal zone lymphoma, plasmacytic differentiation, t(14;18)(q32;q32)/MALT1- IGH fusion gene distinction between WM/LPL and EMZL/MALT lymphoma INTRODUCTION showing plasmacytic differentiation and associated with the Waldenström macroglobulinemia (WM) is a distinct clin- serum IgM monoclonal protein is not necessarily clear, even icopathological disease entity showing lymphoplasmacytic though >90% cases of the former disease have the MYD88 lymphoma (LPL) in bone marrow and the IgM monoclonal P265P somatic mutation.2,6 protein in serum (i.e., macroglobulinemia) at any concentra- We herein describe a patient who presented with macro- tion.1,2 WM/LPL is characterized by the proliferation of globulinemia and the accumulation of pleural fluid in the uni- small lymphocytes admixed with variable numbers of plasma lateral thoracic cavity. Neoplastic cells in the fluid showed cells and plasmacytoid lymphocytes.2 Patients with WM/ the cytomorphological and immunophenotypic features of LPL present with a number of symptoms attributable to plasma cells, indicating the differential diagnosis between tumor cell proliferation and/or an excess of macroglobulin. WM/LPL and EMZL/MALT lymphoma. Cytogenetic and However, macroglobulinemia is observed not only in WM/ molecular studies demonstrated a translocation and fusion LPL, but also a wide range of B-cell lymphoproliferative dis- gene, which was exclusively associated with the latter orders, including extranodal marginal zone lymphoma disease. (EMZL) of mucosa-associated lymphoid tissue (MALT lym- phoma).3-5 EMZL/MALT lymphoma is composed of mor- phologically heterogeneous small B cells and the plasmacytic differentiation of lymphoma cells is common.4 Thus, the Received: April 8, 2018. Revised: June 15, 2018. Accepted: July 6, 2018. J-STAGE Advance Published: August 8, 2018 DOI:10.3960/jslrt.18013 1)Department of Hematology, Tenri Hospital, Nara Japan, 2)Tenri Institute of Medical Science, Nara Japan, and 3)Hematology Division, Department of Medicine, Hyogo Cancer Center, Hyogo, Japan Corresponding author: Takashi Akasaka, MD, PhD, Department of Hematology, Tenri Hospital, 200 Mishima, Tenri, Nara 632-8552, Japan. E-mail: [email protected] Copyright © 2018 The Japanese Society for Lymphoreticular Tissue Research This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License. 141 Akasaka T et al. condition. CASE REPORT Thoracentesis yielded exudative fluid containing abun- dant neoplastic cells with the morphological features of Case presentation plasma cells at a concentration of 6.13 × 103 cells per micro- An 80-year-old man, who had been treated in another liter (Figure 2A). These cells expressed IgM/λ monoclonal hospital for the recurrent accumulation of pleural fluid in the immunoglobulins both on the cell surface and in the cyto- right thoracic cavity for 2 years, was referred to our depart- plasm, and showed a wide range of expression levels of ment because a cytological examination of the fluid sug- CD20, CD22, CD23, CD38, and CD138. CD19 and gested lymphoma cells. On examination, breath sounds CD45RA were positive, and CD5, CD10, CD21, CD24, were decreased in the right hemithorax. There was no sur- CD56, and surface IgD were negative (Figures 2B and C). face lymphadenopathy or hepatosplenomegaly. Oxygen sat- The DNA index was 1.06 from normal diploid cells. Bone uration was 96% in room air. A chest radiograph showed marrow showed hypercellularity containing CD20-positive prominent pleural effusion (Figure 1A). His hemoglobin plasma cells, and flow cytometry revealed a lymphoplasma- level was 12.5 g/dL, white blood cell count was 6.95 × 103/ cytic population with an identical immunophenotype to that μL, and platelet count was 289 × 103/μL. Total serum pro- of pleural fluid cells. Tests for the MYD88 L265P somatic tein was 6.7 g/dL, albumin 3.2 g/dL, globulin 3.5 g/dL, lac- mutation were negative (Supplementary Figure S1). tate dehydrogenase 307 IU/L, higher than the normal range Cytogenetic studies of 124 to 222 IU/L, creatinine 0.6 mg/dL, and C-reactive pro- tein 2.25 mg/dL. Serum protein electrophoresis revealed an The G-banding of metaphase spreads obtained from a M-component migrating in the γ globulin area and immuno- short-term culture of pleural fluid cells demonstrated numeri- fixation confirmed the IgM/λ M protein. No urinary Bence cal and structural abnormalities, including a 14q+ chromo- Jones protein was detected. The level of IgG was 723 mg/ some and uncharacterized small marker chromosome; the dL, IgA was 83 mg/dL, and IgM was 1,526 mg/dL (normal karyotype according to the ISCN 2016 was 48,XY,+3,add(9) range, 33 to 183 mg/dL). Serum free light-chain κ (FLC-κ) (p13),+12,add(14)(q32),del(16)(q22),−18,+mar (Figure 3A). was 16.1 mg/L, FLC-λ was 20.5 mg/L, and the κ/λ ratio was Fluorescence in situ hybridization (FISH) of interphase 0.79. Soluble interleukin 2 receptor was 3,051 U/mL. nuclei with the MYC, BCL2, and BCL6 dual-color, break- Computed tomography (CT) of the chest revealed the apart probes detected no rearrangement of these 3 genes, accumulation of pleural fluid in the right thoracic cavity in while nuclei carried 3 hybridization signals of BCL2 and association with atelectasis of the middle and lower lobes, BCL6 (Supplementary Figure S2). The hybridization of where the marked accumulation of the tracer was demon- metaphase cells with the BCL2-IGH dual-color dual-fusion strated by 18F-fluorodeoxyglucose-positron emission tomog- probe showed that the add(14) chromosome was marked by raphy (FDG-PET) combined with CT (Figure 1B), suggest- the IGH and BCL2 probes (Figure 3B); however, these ing that the atelectatic lesion contained an infiltrative probes did not generate a fusion signal (Supplementary A B Fig. 1. Imaging studies showing pleural effusion of the right thoracic cavity and an infiltrative condition of the lung parenchyma. (A) Postero-anterior chest X-ray. (B) FDG-PET/CT. The anterior view of a maximum intensity projection image (left) and repre- sentative axial images of the thorax (right) are shown. The maximum standardized uptake value of the pulmonary lesion was 17.89. 142 Pulmonary EMZL with t(14;18)/MALT1-IGH A C B Fig. 2. Cytomorphology and immunophenotype of lymphoma cells. (A) May-Giemsa-stained lymphoma cells in pleural fluid, showing a plasmacytic appearance. A few cells had one or more intranuclear inclusions, i.e., Dutcher bodies (right, arrows). (B and C) Flow cytometry of pleural fluid cells using antibodies against the antigens indicated. In B, cells expressed cell surface and cytoplasmic IgM/κ monoclonal immunoglobulins. In C, cells expressed variable levels of B-cell associated antigens and CD38 and CD138, but lacked myelomatous aberrant expression (e.g. CD56). Figure S2). We then performed hybridization with the and for the Eμ enhancer as well as the Cμ, Cγ, and Cα con- MALT1 dual-color, break-apart probe and found that add(14) stant genes of IGH; the MALT1 probe and IGH probes were was marked by the green-labeled telomeric probe, represent- oriented in the opposite direction (Figures 4A and B, ing 3′ MALT1, while the red-labeled centromeric MALT1 sig- Supplementary Table S1). As shown in Figure 4C, we nal was missing, and, accordingly, interphase nuclei showed obtained LD-PCR products by the MALT1-Eμ and the one green and two yellow signal pattern (Figure 3B). MALT1-Cγ primer combination, indicating Cμ to Cγ class The uncharacterized marker chromosome was marked by switching. Nucleotide sequencing of the MALT1-Eμ product unrearranged BCL2 and MALT1 probes, but not of IGH. revealed that the junction occurred at the J6 segment of IGH These cytogenetic studies indicated that the add(14) chromo- and the nucleotide position −5,399 of adenine of the ATG some represented der(14)t(14;18)(q32;q21), at which the start codon of MALT1 at the position +1, and a fragment of 9 MALT1-IGH fusion gene was localized, while the reciprocal base pairs (bp) in length was inserted at the junction (Figures der(18)t(14;18)(q32;q21) was deleted. 4A and D). As a result of translocation, the MALT1 and IGH Eμ-Cγ segments were aligned in the divergent transcriptional Amplification and sequencing of the t(14;18)(q32;q21)/ orientation.
Recommended publications
  • IDF Patient & Family Handbook
    Immune Deficiency Foundation Patient & Family Handbook for Primary Immunodeficiency Diseases This book contains general medical information which cannot be applied safely to any individual case. Medical knowledge and practice can change rapidly. Therefore, this book should not be used as a substitute for professional medical advice. FIFTH EDITION COPYRIGHT 1987, 1993, 2001, 2007, 2013 IMMUNE DEFICIENCY FOUNDATION Copyright 2013 by Immune Deficiency Foundation, USA. REPRINT 2015 Readers may redistribute this article to other individuals for non-commercial use, provided that the text, html codes, and this notice remain intact and unaltered in any way. The Immune Deficiency Foundation Patient & Family Handbook may not be resold, reprinted or redistributed for compensation of any kind without prior written permission from the Immune Deficiency Foundation. If you have any questions about permission, please contact: Immune Deficiency Foundation, 110 West Road, Suite 300, Towson, MD 21204, USA; or by telephone at 800-296-4433. Immune Deficiency Foundation Patient & Family Handbook for Primary Immunodeficency Diseases 5th Edition This publication has been made possible through a generous grant from Baxalta Incorporated Immune Deficiency Foundation 110 West Road, Suite 300 Towson, MD 21204 800-296-4433 www.primaryimmune.org [email protected] EDITORS R. Michael Blaese, MD, Executive Editor Francisco A. Bonilla, MD, PhD Immune Deficiency Foundation Boston Children’s Hospital Towson, MD Boston, MA E. Richard Stiehm, MD M. Elizabeth Younger, CPNP, PhD University of California Los Angeles Johns Hopkins Los Angeles, CA Baltimore, MD CONTRIBUTORS Mark Ballow, MD Joseph Bellanti, MD R. Michael Blaese, MD William Blouin, MSN, ARNP, CPNP State University of New York Georgetown University Hospital Immune Deficiency Foundation Miami Children’s Hospital Buffalo, NY Washington, DC Towson, MD Miami, FL Francisco A.
    [Show full text]
  • Λ-Light Chain and Igg-Heavy Chain Constant Regions
    Detection of new allotypic variants of bovine antibody -light chain and IgG-heavy chain constant regions Dissertation To obtain the Ph.D. degree In the International Ph. D. Program for Agricultural Sciences in Goettingen (IPAG) At the Faculty of Agricultural Sciences, Georg-August-University Goettingen, Germany Presented by Dalia Mohamed Hemdan Aboelhassan born in Cairo, Egypt Göttingen, 2012 D7 Referent: Prof. Dr. Dr. Claus-Peter Czerny Co-referent: Prof. Dr. Sven König Date of dissertation: 03.02.2012 Contents I Contents Abbreviations 1 INTRODUCTION ................................................................................................................ 1 2 REVIEW OF LITERATURE .............................................................................................. 2 2.1 IMMUNOGLOBULIN (IG) ........................................................................................................... 2 2.2 BOVINE IMMUNOGLOBULINS ................................................................................................... 5 2.3 BOVINE IMMUNOGLOBULIN HEAVY CHAINS .......................................................................... 6 2.3.1 Bovine immunoglobulin M (IgM) ................................................................................... 6 2.3.2 Bovine immunoglobulin D (IgD) .................................................................................... 7 2.3.3 Bovine immunoglobulin E (IgE) ..................................................................................... 8 2.3.4 Bovine immunoglobulin
    [Show full text]
  • Absence of Surface Igd Does Not Impair Naive B Cell Homeostasis and Memory B Cell
    bioRxiv preprint doi: https://doi.org/10.1101/332361; this version posted May 28, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Absence of surface IgD does not impair naive B cell homeostasis and memory B cell formation in humans J. Nechvatalova,1,2 S.J.W. Bartol,3 Z. Chovancova,1,2 L. Boon,4 M. Vlkova,1,2 M.C. van Zelm3,5* 1Dept. Clinical Immunology and Allergology, St Anne´s University Hospital in Brno, the Czech Republic 2Faculty of Medicine, Masaryk University, Brno, the Czech Republic 3Dept. Immunology, Erasmus MC, University Medical Center, Rotterdam, the Netherlands 4Bioceros B.V., Utrecht, the Netherlands 5Dept. Immunology and Pathology, Central Clinical School, Monash University and The Alfred Hospital, Melbourne, VIC, Australia One Sentence Summary: Human B cells with a genetic defect in IGHD develop normally in vivo, and do not have a competitive disadvantage to IgD-expressing B cells for developing into memory B cells. * Address correspondence to: Menno C. van Zelm, Department of Immunology and Pathology, Central Clinical School, Monash University, Level 6 Burnet Centre, 89 Commercial Rd, Melbourne VIC 3004, Australia; Email: [email protected] Conflict of interest: The authors have declared that no conflict of interest exists. Key words: IgD; B cell; inherited gene defect; antibody; memory; immunodeficiency; auto- immunity; surface immunoglobulin 1 bioRxiv preprint doi: https://doi.org/10.1101/332361; this version posted May 28, 2018.
    [Show full text]
  • Immunoglobulin Heavy) Marie-Paule Lefranc IMGT, LIGM, IGH, UPR CNRS 1142, 141 Rue De La Cardonille, 34396 Montpellier Cedex 5, France (MPL)
    Atlas of Genetics and Cytogenetics in Oncology and Haematology OPEN ACCESS JOURNAL AT INIST-CNRS Gene Section Review IGH@ (Immunoglobulin Heavy) Marie-Paule Lefranc IMGT, LIGM, IGH, UPR CNRS 1142, 141 rue de la Cardonille, 34396 Montpellier Cedex 5, France (MPL) Published in Atlas Database: September 2003 Online updated version: http://AtlasGeneticsOncology.org/Genes/IgHID40.html DOI: 10.4267/2042/38013 This article is an update of : Lefranc MP. IGH (immunoglobulin heavy). Atlas Genet Cytogenet Oncol Haematol.2000;4(3):107-110. This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 France Licence. © 2003 Atlas of Genetics and Cytogenetics in Oncology and Haematology depending from the haplotypes, 27 IGHD segments Identity belonging to 7 subgroups, 9 IGHJ segments, and 11 Other names: IGH (Immunoglobulin Heavy) IGHC genes. HGNC (Hugo): IGH@ Eighty-two to 88 IGHV genes belong to 7 subgroups, whereas 41 pseudogenes, which are too divergent to be Location: 14q32.33 assigned to subgroups, have been assigned to 4 clans. Note Seven non-mapped IGHV genes have been described The human IGH locus is located on the chromo-some as insertion/deletion polymorphism but have not yet 14 at band 14q32.33, at the telomeric extremity of the been precisely located. long arm; the orientation of the locus has been The most 5' IGHV genes occupy a position very close determined by the analysis of translocations, involving to the chromosome 14q telomere whereas the IGHC the IGH locus, in leukemia and lymphoma. genes are in a more centromeric position. The potentiel genomic IGH repertoire is more limited since it comprises 38-46 functional IGHV genes belonging to 6 or 7 subgroups depending from the haplotypes 23 IGHD, 6 IGHJ, and 9 IGHC genes.
    [Show full text]
  • Ig Light Chain Precedes Heavy Chain Gene Rearrangement During Development of B Cells in Swine
    Ig Light Chain Precedes Heavy Chain Gene Rearrangement during Development of B Cells in Swine This information is current as Marek Sinkora, Jana Sinkorova and Katerina Stepanova of September 27, 2021. J Immunol 2017; 198:1543-1552; Prepublished online 9 January 2017; doi: 10.4049/jimmunol.1601035 http://www.jimmunol.org/content/198/4/1543 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2017/01/06/jimmunol.160103 Material 5.DCSupplemental References This article cites 43 articles, 20 of which you can access for free at: http://www.jimmunol.org/ http://www.jimmunol.org/content/198/4/1543.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists by guest on September 27, 2021 • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2017 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Ig Light Chain Precedes Heavy Chain Gene Rearrangement during Development of B Cells in Swine Marek Sinkora, Jana Sinkorova, and Katerina Stepanova The current mammalian paradigm states that 1) rearrangements in the IgH locus precede those in IgL loci, 2) IgLl genes rearrange only when IgLk genes are consumed, and 3) the surrogate L chain is necessary for selection of productive IgH gene rearrange- ments.
    [Show full text]
  • The Diagnostic Significance of Immunoglobulin Light Chain Gene Expression Signatures by Gene Expression Profiling for B-Cell Lymphoma
    Research Article Remedy Open Access Published: 26 Jul, 2016 The Diagnostic Significance of Immunoglobulin Light Chain Gene Expression Signatures by Gene Expression Profiling for B-Cell Lymphoma James Z. Huang1*, Rita M. Braziel2, Guang Fan2, Louis M. Staudt3 and Wing C. Chan4 1Departments of Pathology and Laboratory Medicine, Oakland University William Beaumont School of Medicine, USA 2Departments of Pathology, Oregon Health & Science University, USA 3Metabolism Branch, Division of Clinical Sciences, National Institutes of Health, USA 4Departments of Pathology, City of Hope National Medical Center, USA Abstract Gene expression profiling (GEP) has been shown to have great potential to become a powerful diagnostic tool for lymphoma classification. However, it is not clear whether the expression pattern of immunoglobulin light chain genes defined by GEP can be used as a diagnostic signature to differentiate B-cell lymphoma from B-cell hyperplasia. To assess the difference in expression signatures of kappa and lambda genes among samples from reactive tonsils, normal peripheral bloods, chronic lymphocytic leukemias (CLL), follicular lymphomas (FL) and diffuse large B-cell lymphomas (DLBCL), GEP data available from the Lymphoma/Leukemia Molecular Profiling Project (LLMPP) were reanalyzed. A normal reference range of kappa and lambda light chain gene expression was defined by analysis of polyclonal B-cells from normal peripheral bloods and tonsils. Restricted light chain gene expression was detected in 100% (11/11) of CLL, in 83% (5/6) of FL, and 67% (198 of 296) of DLBCL. Our findings provide the evidence for the concept that immunoglobulin OPEN ACCESS light chain restriction can be determined at the gene transcription level by GEP microarray in most *Correspondence: of B-cell malignancies.
    [Show full text]
  • Insights Into the Function of Igd
    Developmental and Comparative Immunology 35 (2011) 1309–1316 Contents lists available at ScienceDirect Developmental and Comparative Immunology journal homepage: www.elsevier.com/locate/dci Insights into the function of IgD Eva-Stina Edholm, Eva Bengten, Melanie Wilson ∗ University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216, United States article info abstract Article history: IgD, previously thought to be a recent addition to the immunoglobulin classes, has long been consid- Available online 15 March 2011 ered an enigmatic molecule. For example, it was debated if IgD had a specific function other than as an antigen receptor co-expressed with IgM on naive B cells and if it had an important role in mammalian Keywords: immunity. However, during the past decade extensive sequencing of vertebrate genomes has shown that Teleosts IgD homologs are present in all vertebrate taxa, except for birds. Moreover, recent functional studies Immunoglobulin indicate that IgD likely performs a unique role in vertebrate immune responses. The goal of this review is IgD to summarize the IgD gene organization and structural data, which demonstrate that IgD has an ancient Alternative splicing B cells origin, and discuss the findings in catfish and humans that provide insight into the possible function of this elusive immunoglobulin isotype. © 2011 Elsevier Ltd. All rights reserved. 1. Introduction (Gambon-Deza et al., 2010), and Atlantic salmon, Salmo salar (Tadiso et al., 2010). However, PCR and genomic sequencing stud- It is well
    [Show full text]
  • Genetic Diversity of IGHM and IGHE in the Leporids Revealed Different
    animals Article Genetic Diversity of IGHM and IGHE in the Leporids Revealed Different Patterns of Diversity in the Two European Rabbit Subspecies (O. cuniculus algirus and O. c. cuniculus) Ana Pinheiro 1,*, Tereza Almeida 1,2 and Pedro J. Esteves 1,2,3 1 CIBIO Centro de Investigação em Biodiversidade e Recursos Genéticos, InBio Laboratório Associado, Universidade do Porto, Campus Agrário de Vairão, 4485-661 Vairão, Portugal; [email protected] (T.A.); [email protected] (P.J.E.) 2 Departamento de Biologia, Faculdade de Ciências, Universidade do Porto, 4169-007 Porto, Portugal 3 CESPU, Instituto de Investigação e Formação Avançada em Ciências e Tecnologias da Saúde, 4585-116 Gandra PRD, Portugal * Correspondence: [email protected]; Tel.: +00351-252-660-411 Received: 7 October 2019; Accepted: 8 November 2019; Published: 12 November 2019 Simple Summary: The study of European rabbit immunoglobulin genes has contributed decisively to the current knowledge on antibody structure and diversification. The European rabbit has also been increasingly used as an animal model for the study of many human diseases, such as syphilis, tuberculosis, and AIDS. As such, the study of its immune system genes is of crucial relevance, but the study of rabbit immunoglobulins has focused only on the IgG and IgA antibodies. In this study, we added to the knowledge of the rabbit immune system by investigating the genetic diversity of two antibodies, IgM and IgE, in wild and domestic rabbits as well as other rabbit close species. With the data obtained in this study, we showed a high similarity between the different rabbit close species studied and we pointed out important genetic differences in the wild and domestic rabbits.
    [Show full text]
  • University of Groningen Influenza Vaccination-Induced B Cell
    University of Groningen Influenza vaccination-induced B cell response in monoclonal gammopathy of undetermined significance (MGUS) Tete, Sarah IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2014 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Tete, S. (2014). Influenza vaccination-induced B cell response in monoclonal gammopathy of undetermined significance (MGUS). [S.n.]. Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license. More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne- amendment. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 02-10-2021 CHAPTER Monoclonal paraprotein influences baseline B cell repertoire diversity and pertubates influenza vaccination-induced 5 B cell response Sarah M.
    [Show full text]
  • 36-2559: Anti-Igm (Immunoglobulin Mu Heavy Chain) (B-Cell Marker) Monoclonal Antibody(Clone: IGHM/3135R)
    9853 Pacific Heights Blvd. Suite D. San Diego, CA 92121, USA Tel: 858-263-4982 Email: [email protected] 36-2559: Anti-IgM (Immunoglobulin Mu Heavy Chain) (B-Cell Marker) Monoclonal Antibody(Clone: IGHM/3135R) Clonality : Monoclonal Clone Name : IGHM/3135R Application : IHC Reactivity : Human Gene : IGHM Gene ID : 3507 Uniprot ID : P01871; P20769 Alternative Name : AGM1; IGHM; Constant Region of Heavy Chain of IgM; Ig Mu Chain C Region Isotype : Rabbit IgG Immunogen Information : Recombinant full-length human IGHM protein Description Recognizes a protein of 75kDa, identified as mu heavy chain of human immunoglobulins. It does not cross-react with alpha (IgA), gamma (IgG), epsilon (IgE), or delta (IgD), heavy chains, T-cells, monocytes, granulocytes, or erythrocytes. Monomeric IgM is expressed as a membrane bound antibody on the surface of B cells and as a pentamer when secreted by plasma cells. IgM antibody is prominent in early immune responses to most antigens. Aberrant levels are associated with immune deficiency states, hereditary deficiencies, myeloma, Waldenstrom's macroglobulinemia, chronic infection and hepatocellular disease. This MAb is useful in the identification of leukemias, plasmacytomas, and certain non-Hodgkin's lymphomas. The most common feature of these malignancies is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant. Product Info Amount : 20 µg / 100 µg 200 µg/ml of Ab Purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with Content : 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml.
    [Show full text]
  • The Expression Pattern of the Pre-B Cell Receptor Components Correlates with Cellular Stage and Clinical Outcome in Acute Lymphoblastic Leukemia
    RESEARCH ARTICLE The Expression Pattern of the Pre-B Cell Receptor Components Correlates with Cellular Stage and Clinical Outcome in Acute Lymphoblastic Leukemia Dongfeng Chen1, Junxiong Zheng1, Natalija Gerasimcik1, Kristina Lagerstedt1, Helene Sjögren2, Jonas Abrahamsson3, Linda Fogelstrand2,4, Inga-Lill Mårtensson1* a11111 1 Department of Rheumatology and Inflammation Research, Institute of Medicine, University of Gothenburg, Gothenburg, Sweden, 2 Department of Clinical Chemistry, Sahlgrenska University Hospital, Gothenburg, Sweden, 3 Queen Silvia Children’s Hospital, Gothenburg, Sweden, 4 Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden * [email protected] OPEN ACCESS Abstract Citation: Chen D, Zheng J, Gerasimcik N, Lagerstedt K, Sjögren H, Abrahamsson J, et al. (2016) The Precursor-B cell receptor (pre-BCR) signaling represents a crucial checkpoint at the pre-B Expression Pattern of the Pre-B Cell Receptor cell stage. Aberrant pre-BCR signaling is considered as a key factor for B-cell precursor Components Correlates with Cellular Stage and acute lymphoblastic leukemia (BCP-ALL) development. BCP-ALL are believed to be Clinical Outcome in Acute Lymphoblastic Leukemia. PLoS ONE 11(9): e0162638. doi:10.1371/journal. arrested at the pre-BCR checkpoint independent of pre-BCR expression. However, the cel- pone.0162638 lular stage at which BCP-ALL are arrested and whether this relates to expression of the pre- Editor: Connie J Eaves, B.C. Cancer Agency, BCR components (IGHM, IGLL1 and VPREB1) is still unclear. Here, we show differential CANADA protein expression and copy number variation (CNV) patterns of the pre-BCR components Received: June 27, 2016 in pediatric BCP-ALL.
    [Show full text]
  • Monoclonal Antibody(Clone: IGHM/3776R)
    9853 Pacific Heights Blvd. Suite D. San Diego, CA 92121, USA Tel: 858-263-4982 Email: [email protected] 36-2560: Anti-IgM (Immunoglobulin Mu Heavy Chain) (B-Cell Marker) Monoclonal Antibody(Clone: IGHM/3776R) Clonality : Monoclonal Clone Name : IGHM/3776R Application : IHC Reactivity : Human Gene : IGHM Gene ID : 3507 Uniprot ID : P01871; P20769 Alternative Name : AGM1; IGHM; Constant Region of Heavy Chain of IgM; Ig Mu Chain C Region Isotype : Rabbit IgG Immunogen Information : Recombinant full-length human IGHM protein Description Recognizes a protein of 75kDa, identified as mu heavy chain of human immunoglobulins. It does not cross-react with alpha (IgA), gamma (IgG), epsilon (IgE), or delta (IgD), heavy chains, T-cells, monocytes, granulocytes, or erythrocytes. This MAb is useful in the identification of leukemias, plasmacytomas, and certain non-Hodgkin s lymphomas. The most common feature of these malignancies is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant. Product Info Amount : 20 µg / 100 µg 200 µg/ml of Ab Purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with Content : 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml. Antibody with azide - store at 2 to 8°C. Antibody without azide - store at -20 to -80°C. Antibody is Storage condition : stable for 24 months. Non-hazardous. Application Note Immunohistochemistry (Formalin-fixed) (0.5-1.0µg/ml for 30 minutes at RT)(Staining of formalin-fixed tissues is enhanced by boiling tissue sections in 10mM Tris with 1mM EDTA, pH 9.0 for 10-20 min followed by cooling at RT for 20 minutes)Optimal dilution for a specific application should be determined.
    [Show full text]