CD20 (B9E9): Sc-9984
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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. -
Tetraspanin CD53: an Overlooked Regulator of Immune Cell Function
Medical Microbiology and Immunology (2020) 209:545–552 https://doi.org/10.1007/s00430-020-00677-z REVIEW Tetraspanin CD53: an overlooked regulator of immune cell function V. E. Dunlock1 Received: 31 March 2020 / Accepted: 2 May 2020 / Published online: 21 May 2020 © The Author(s) 2020 Abstract Tetraspanins are membrane organizing proteins that play a role in organizing the cell surface through the formation of subcellular domains consisting of tetraspanins and their partner proteins. These complexes are referred to as tetraspanin enriched microdomains (TEMs) or the tetraspanin web. The formation of TEMs allows for the regulation of a variety of cellular processes such as adhesion, migration, signaling, and cell fusion. Tetraspanin CD53 is a member of the tetraspanin superfamily expressed exclusively within the immune compartment. Amongst others, B cells, CD4+ T cells, CD8+ T cells, dendritic cells, macrophages, and natural killer cells have all been found to express high levels of this protein on their sur- face. Almost three decades ago it was reported that patients who lacked CD53 sufered from an increased susceptibility to pathogens resulting in the clinical manifestation of recurrent viral, bacterial, and fungal infections. This clearly suggests a vital and non-redundant role for CD53 in immune function. Yet, despite this striking fnding, the specifc functional roles of CD53 within the immune system have remained elusive. This review aims to provide a concise overview of the published literature concerning CD53 and refect on the underappreciated role of this protein in immune cell regulation and function. Keywords Tetraspanins · Tetraspanin enriched microdomains · CD53 · Membrane organization · Immune cell signaling · Immune cell adhesion Introduction: tetraspanins in the immune surface or on intracellular membranes. -
Supplementary Table 1: Adhesion Genes Data Set
Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like, -
Human Eosinophils and Their Activation by Allergens Via Danger
Human eosinophils and their activation by allergens via danger signal receptors Elin Redvall ______________________ 2010 Department of Infectious diseases, Institute of Biomedicine, The Sahlgrenska Academy Cover illustration photo: Kerstin Andersson (Eosinophils) Abstract Human eosinophilic granulocytes are polymorphonuclear cells with a powerful arsenal of cytotoxic substances in their granules, which are mainly found in the gastrointestinal mucosa, and the respiratory and genitourinary tracts. Their physiological role is incompletely understood, although it is likely they protect the mucosal surfaces, perhaps by recognizing danger signals present on microorganisms or released from damaged tissue. We have earlier shown that eosinophils can recognize and become directly activated by aeroallergens such as house dust mite (HDM) and birch pollen. Eosinophils exposed to (HDM) release both of the cytotoxic granule proteins eosinophil peroxidase (EPO) and major basic protein, whereas birch pollen extract only triggers EPO release. Here we further investigate which receptors on eosinophils are used to signal the presence of HDM and birch pollen. Recognition was found to be mediated by the formyl peptide receptors (FPRs) FPR1 and FPR2. We also characterized the expression of this family of receptors in human eosinophils and found that they express FPR1 and FPR2, but not FPR3, similar to neutrophilic granulocytes. We also discovered that signaling through FPR1 can desensitize the eotaxin-1 receptor CCR3 rendering the cells anergic with respect to chemotaxis in response to eotaxin-1, but not regarding respiratory burst. Hence, there is cross- talk between these two receptors regarding one important effector function of eosinophils. Eosinophilic reactivity in vitro to the aeroallergens HDM, birch pollen, timothy grass pollen and cat dander did not differ between individuals with allergy and healthy individuals. -
Combination Immunotherapy with Anti-CD20 and Anti-HLA-DR Monoclonal Antibodies Induces Synergistic Anti-Lymphoma Effects in Human Lymphoma Cell Lines
UC Davis UC Davis Previously Published Works Title Combination immunotherapy with anti-CD20 and anti-HLA-DR monoclonal antibodies induces synergistic anti-lymphoma effects in human lymphoma cell lines Permalink https://escholarship.org/uc/item/8pk1f4nx Journal Leukemia & Lymphoma, 48(5) ISSN 1042-8194 Authors Tobin, Evan Denardo, Gerald Zhang, Nan et al. Publication Date 2007-05-01 Peer reviewed eScholarship.org Powered by the California Digital Library University of California Rituximab & ChLym-1 Combined Immunotherapy Combination Immunotherapy with Anti-CD20 and Anti-HLA-DR Monoclonal Antibodies Induces Synergistic Anti-lymphoma Effects in Human Lymphoma Cell Lines Evan Tobin1, Gerald DeNardo1, Nan Zhang2, Alan L. Epstein2, Cathy Liu1 & Sally DeNardo1 1 Department of Internal Medicine, University of California Davis, CA, USA 2 Department of Pathology, University of Southern California Keck School of Medicine, Los Angeles, CA, USA Running Title: Rituximab & ChLym-1 Combined Immunotherapy Keywords: Lymphoma; immunotherapy; rituximab; Lym-1; CD20; HLA-DR 1Address for correspondence: Gerald L. DeNardo, M.D. Division of Hematology and Oncology 1508 Alhambra Blvd., No. 3100 Sacramento, CA 95816 Telephone (916) 734-3787 Fax (916) 703-5014 E-mail: [email protected] 1 Rituximab & ChLym-1 Combined Immunotherapy ABSTRACT Rituximab is effective in about one half of patients with indolent lymphoma. Even these patients relapse and develop rituximab resistance. To increase potency and circumvent resistance, the anti-lymphoma effects of rituximab, an anti-CD20 MAb1, combined with chLym-12, an anti- HLA-DR MAb, were assessed in human lymphoma cell lines by examining growth inhibition and cell death, apoptosis induction, ADCC3 and CDC4. There were additive effects in all assays and synergism in cell lines, such as B35M, which displayed resistance to either MAb alone. -
Aberrant Expression of Tetraspanin Molecules in B-Cell Chronic Lymphoproliferative Disorders and Its Correlation with Normal B-Cell Maturation
Leukemia (2005) 19, 1376–1383 & 2005 Nature Publishing Group All rights reserved 0887-6924/05 $30.00 www.nature.com/leu Aberrant expression of tetraspanin molecules in B-cell chronic lymphoproliferative disorders and its correlation with normal B-cell maturation S Barrena1,2, J Almeida1,2, M Yunta1,ALo´pez1,2, N Ferna´ndez-Mosteirı´n3, M Giralt3, M Romero4, L Perdiguer5, M Delgado1, A Orfao1,2 and PA Lazo1 1Instituto de Biologı´a Molecular y Celular del Ca´ncer, Centro de Investigacio´n del Ca´ncer, Consejo Superior de Investigaciones Cientı´ficas-Universidad de Salamanca, Salamanca, Spain; 2Servicio de Citometrı´a, Universidad de Salamanca and Hospital Universitario de Salamanca, Salamanca, Spain; 3Servicio de Hematologı´a, Hospital Universitario Miguel Servet, Zaragoza, Spain; 4Hematologı´a-hemoterapia, Hospital Universitario Rı´o Hortega, Valladolid, Spain; and 5Servicio de Hematologı´a, Hospital de Alcan˜iz, Teruel, Spain Tetraspanin proteins form signaling complexes between them On the cell surface, tetraspanin antigens are present either as and with other membrane proteins and modulate cell adhesion free molecules or through interaction with other proteins.25,26 and migration properties. The surface expression of several tetraspanin antigens (CD9, CD37, CD53, CD63, and CD81), and These interacting proteins include other tetraspanins, integri- F 22,27–30F their interacting proteins (CD19, CD21, and HLA-DR) were ns particularly those with the b1 subunit HLA class II 31–33 34,35 analyzed during normal B-cell maturation and compared to a moleculesFeg HLA DR -, CD19, the T-cell recep- group of 67 B-cell neoplasias. Three patterns of tetraspanin tor36,37 and several other members of the immunoglobulin expression were identified in normal B cells. -
Tetraspanin CD53 Promotes Lymphocyte Recirculation by Stabilizing L-Selectin Surface Expression
iScience ll OPEN ACCESS Article Tetraspanin CD53 Promotes Lymphocyte Recirculation by Stabilizing L-Selectin Surface Expression Maria C. Demaria, Louisa Yeung, Rens Peeters, ..., Annemiek van Spriel, Michael J. Hickey, Mark D. Wright [email protected] HIGHLIGHTS CD53 is essential for lymph node cellularity as À/À Cd53 lymph nodes lack TandBcells CD53 is essential for lymphocyte homing to lymph nodes CD53 stabilizes L-selectin cell surface expression and may restrain shedding Impaired lymphocyte homing leads to diminished immune À À responses in Cd53 / mice Demaria et al., iScience 23, 101104 May 22, 2020 ª 2020 The Author(s). https://doi.org/10.1016/ j.isci.2020.101104 iScience ll OPEN ACCESS Article Tetraspanin CD53 Promotes Lymphocyte Recirculation by Stabilizing L-Selectin Surface Expression Maria C. Demaria,1 Louisa Yeung,1,2 Rens Peeters,3 Janet L. Wee,1,2 Masa Mihaljcic,1 Eleanor L. Jones,1 Zeyad Nasa,1 Frank Alderuccio,1 Pamela Hall,2 Brodie C. Smith,2 Katrina J. Binger,4 Gunther Hammerling,5 Hang Fai Kwok,6 Andrew Newman,7 Ann Ager,7 Annemiek van Spriel,3 Michael J. Hickey,2 and Mark D. Wright1,8,* SUMMARY Tetraspanins regulate key processes in immune cells; however, the function of the leukocyte-restricted tetraspanin CD53 is unknown. Here we show that CD53 is essential for lymphocyte recirculation. Lymph nodes of Cd53À/À mice were smaller than those of wild-type mice due to a marked reduction in B cells and a 50% decrease in T cells. This reduced cellularity reflected an inability of Cd53À/À B and T cells to effi- ciently home to lymph nodes, due to the near absence of L-selectin from Cd53À/À B cells and reduced stability of L-selectin on Cd53À/À T cells. -
Complexes of Tetraspanins with Integrins: More Than Meets the Eye
COMMENTARY 4143 Complexes of tetraspanins with integrins: more than meets the eye Fedor Berditchevski CRC Institute for Cancer Studies, The University of Birmingham, Edgbaston, Birmingham, B15 2TA, UK Author for correspondence (e-mail: [email protected]) Journal of Cell Science 114, 4143-4151 (2001) © The Company of Biologists Ltd Summary The transmembrane proteins of the tetraspanin membrane, integrin-tetraspanin signalling complexes superfamily are implicated in a diverse range of biological are partitioned into specific microdomains proximal to phenomena, including cell motility, metastasis, cell cholesterol-rich lipid rafts. A substantial fraction of proliferation and differentiation. The tetraspanins are tetraspanins colocalise with integrins in various associated with adhesion receptors of the integrin family intracellular vesicular compartments. It is proposed that and regulate integrin-dependent cell migration. In cells tetraspanins can influence cell migration by one of the attached to the extracellular matrix, the integrin- following mechanisms: (1) modulation of integrin tetraspanin adhesion complexes are clustered into a distinct signalling; (2) compartmentalisation of integrins on the cell type of adhesion structure at the cell periphery. Various surface; or (3) direction of intracellular trafficking and tetraspanins are associated with phosphatidylinositol 4- recycling of integrins. kinase and protein kinase C isoforms, and they may facilitate assembly of signalling complexes by tethering these enzymes to integrin heterodimers. At the plasma Key words: Tetraspanin, Integrin, Migration, Signalling Introduction relatively well conserved among tetraspanins (Fig. 1). A Tetraspanins (also referred to as tetraspans or TM4SF proteins) combination of all the above features distinguishes tetraspanins are a family of widely expressed four-transmembrane-domain from a diverse group of proteins that have four transmembrane proteins. -
Human CD Marker Chart Reviewed by HLDA1 Bdbiosciences.Com/Cdmarkers
BD Biosciences Human CD Marker Chart Reviewed by HLDA1 bdbiosciences.com/cdmarkers 23-12399-01 CD Alternative Name Ligands & Associated Molecules T Cell B Cell Dendritic Cell NK Cell Stem Cell/Precursor Macrophage/Monocyte Granulocyte Platelet Erythrocyte Endothelial Cell Epithelial Cell CD Alternative Name Ligands & Associated Molecules T Cell B Cell Dendritic Cell NK Cell Stem Cell/Precursor Macrophage/Monocyte Granulocyte Platelet Erythrocyte Endothelial Cell Epithelial Cell CD Alternative Name Ligands & Associated Molecules T Cell B Cell Dendritic Cell NK Cell Stem Cell/Precursor Macrophage/Monocyte Granulocyte Platelet Erythrocyte Endothelial Cell Epithelial Cell CD1a R4, T6, Leu6, HTA1 b-2-Microglobulin, CD74 + + + – + – – – CD93 C1QR1,C1qRP, MXRA4, C1qR(P), Dj737e23.1, GR11 – – – – – + + – – + – CD220 Insulin receptor (INSR), IR Insulin, IGF-2 + + + + + + + + + Insulin-like growth factor 1 receptor (IGF1R), IGF-1R, type I IGF receptor (IGF-IR), CD1b R1, T6m Leu6 b-2-Microglobulin + + + – + – – – CD94 KLRD1, Kp43 HLA class I, NKG2-A, p39 + – + – – – – – – CD221 Insulin-like growth factor 1 (IGF-I), IGF-II, Insulin JTK13 + + + + + + + + + CD1c M241, R7, T6, Leu6, BDCA1 b-2-Microglobulin + + + – + – – – CD178, FASLG, APO-1, FAS, TNFRSF6, CD95L, APT1LG1, APT1, FAS1, FASTM, CD95 CD178 (Fas ligand) + + + + + – – IGF-II, TGF-b latency-associated peptide (LAP), Proliferin, Prorenin, Plasminogen, ALPS1A, TNFSF6, FASL Cation-independent mannose-6-phosphate receptor (M6P-R, CIM6PR, CIMPR, CI- CD1d R3G1, R3 b-2-Microglobulin, MHC II CD222 Leukemia -
Of Small Intestine Harboring Driver Gene Mutations: a Case Report and a Literature Review
1161 Case Report A rare multiple primary sarcomatoid carcinoma (SCA) of small intestine harboring driver gene mutations: a case report and a literature review Zhu Zhu1#, Xinyi Liu2#, Wenliang Li1, Zhengqi Wen1, Xiang Ji1, Ruize Zhou1, Xiaoyu Tuo3, Yaru Chen2, Xian Gong2, Guifeng Liu2, Yanqing Zhou2, Shifu Chen2, Lele Song2#^, Jian Huang1 1Department of Oncology, First Affiliated Hospital of Kunming Medical University, Kunming, China; 2HaploX Biotechnology, Shenzhen, China; 3Department of Pathology, First Affiliated Hospital of Kunming Medical University, Kunming, China #These authors contributed equally to this work. Correspondence to: Jian Huang. Department of Oncology, First Affiliated Hospital of Kunming Medical University, No. 295, Xichang Road, Kunming 560032, Yunnan Province, China. Email: [email protected]; Lele Song. HaploX Biotechnology, 8th floor, Auto Electric Power Building, Songpingshan Road, Nanshan District, Shenzhen 518057, Guangdong Province, China. Email: [email protected]. Abstract: Primary sarcomatoid carcinoma (SCA) is a type of rare tumor consisting of both malignant epithelial and mesenchymal components. Only 32 cases of SCA of the small bowel have been reported in the literature to date. Due to its rarity and complexity, this cancer has not been genetically studied and its diagnosis and treatment remain difficult. Here we report a 54-year-old male underwent emergency surgical resection in the small intestine due to severe obstruction and was diagnosed with multiple SCA based on postoperative pathological examination. Over 100 polypoid tumors scattered along his whole jejunum and proximal ileum. Chemotherapy (IFO+Epirubicin) was performed after surgery while the patient died two months after the surgery due to severe malnutrition. Whole-exome sequencing was performed for the tumor tissue with normal tissue as the control. -
Table Def 26O608
Table 5: Genes found to be regulated by Thymosin alpha 1 in PBMCs from HIV infected patients (1) Gene Gene Bank SuperArray Access number fold change Cytokine , Chemokines and receptors UP CCL2 Chemokine (C-C motif) ligand 2 (MCP-1/ MCAF) NM_002982 2,56 CCL3 Chemokine (C-C motif) ligand 3 (MIP-1 alpha) NM_002983 1,96 CCL3L1 Chemokine (C-C motif) ligand 3-like 1 (LD78 beta) NM_021006 1,97 CCL4L1 Chemokine (C-C motif) ligand 4-like 1 NM_001001435 2,73 CCL5 Chemokine (C-C motif) ligand 5 (Rantes) NM_002985 3,21 CCL18 Chemokine (C-C motif) ligand 18 (pulmonary and activation-regulated) (MIP-4/PARC) NM_002988 2,03 CCL22 Chemokine (C-C motif) ligand 22 (MDC) NM_002990 1,56 IL8 Interleukin 8 NM_000584 1,66 TRAP1 TNF receptor-associated protein 1 NM_016292 1,51 VEGFB Vascular endothelial growth factor B NM_003377 3,13 CCR1 Chemokine (C-C motif) receptor 1 NM_001295 2,38 CCR7 Chemokine (C-C motif) receptor 7 NM_001838 2,21 CCRL2 Chemokine (C-C motif) receptor-like 2 NM_003965 2,35 IL4R Interleukin 4 receptor NM_000418 1,66 IL6R Interleukin 6 receptor NM_000565 1,9 IL10RA Interleukin 10 receptor, alpha NM_001558 1,56 IL10RB Interleukin 10 receptor, beta NM_000628 1,93 DOWN CCL1 (I-309) Chemokine (C-C motif) ligand 1 NM_002981 0,02 CCL11 Chemokine (C-C motif) ligand 11 (Eotaxin) NM_002986 0,15 CMTM1 (CKLF) CKLF-like MARVEL transmembrane domain containing 1 NM_181269 0,11 CXCL1 Chemokine (C-X-C motif) ligand 1 (melanoma growth stimulating activity, alpha) NM_001511 0,61 IFNA1 Interferon, alpha 1 NM_024013 0,45 IFNA 2 Interferon, alpha 2 NM_000605 0,04 -
Fang Et Al Supplementary Data S1
Supplementary Data S1. List of genes differentially expressed in human hepatoma HepG2 cells binding HCV-LPs versus control cells assessed as described in Materials and Methods ) ld o f - x ( D e I e m c k a n n a N e b e r e n n f e e if G G D Genes with up-regulated expression in human hepatoma cells binding HCV-LPs vs. control cells AF002672 Homo sapiens breast cancer suppressor candidate 1 (bcsc-1) mRNA_ complete cds /chromosome=11 /cytoband=11q23 5,9 X16667 Human HOX2G mRNA from the Hox2 locus /cytoband=17q21-q22 3,6 AF104942 Homo sapiens ABC transporter MOAT-C (MOAT-C) mRNA_ complete cds /chromosome=3 /cytoband=3q27 3,3 IMAGp958H12346 IMAGp958H12346 3,1 AF047042 Homo sapiens citrate synthase mRNA_ complete cds /chromosome=2 /cytoband=12p11-qter 3,1 T47961 Human hematopoietic progenitor kinase (HPK1) mRNA_ complete cds 2,9 T57079 Human IgG Fc receptor I gene 2,8 Y10696 H.sapiens INE1 mRNA /chromosome=4 2,7 M13955 Human mesothelial keratin K7 (type II) mRNA_ 3 end /chromosome=12 /cytoband=12q12-q21 2,6 X04506 Human mRNA for apolipoprotein B-100 /chromosome=2 /cytoband=2p24-p23 2,6 M33987 Human carbonic anhydrase I (CAI) mRNA_ complete cds /chromosome=8 /cytoband=8q13-q22.1 2,5 M12529 Human apolipoprotein E mRNA_ complete cds /chromosome=19 /cytoband=19q13.2 2,5 D87291 Human mRNA for inward rectifier potassium channel_ complete cds /chromosome=21 /cytoband=21q22.2 2,5 M55914 Human c-myc binding protein (MBP-1) mRNA_ complete cds /chromosome=1 /cytoband=1pter-p35 2,5 T64149 Homo sapiens FIGF gene_ promoter exon 1 and joined CDS 2,4 D30655