CD151 Expression Is Associated with a Hyperproliferative T Cell Phenotype Lillian Seu, Christopher Tidwell, Laura Timares, Alexandra Duverger, Frederic H
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RI-Mediated Mast Cell Activation Ε of Fc Tetraspanin CD151 Is A
Tetraspanin CD151 Is a Negative Regulator of Fc εRI-Mediated Mast Cell Activation Hiam Abdala-Valencia, Paul J. Bryce, Robert P. Schleimer, Joshua B. Wechsler, Lucas F. Loffredo, Joan M. Cook-Mills, This information is current as Chia-Lin Hsu and Sergejs Berdnikovs of September 26, 2021. J Immunol 2015; 195:1377-1387; Prepublished online 1 July 2015; doi: 10.4049/jimmunol.1302874 http://www.jimmunol.org/content/195/4/1377 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2015/07/01/jimmunol.130287 Material 4.DCSupplemental http://www.jimmunol.org/ References This article cites 63 articles, 28 of which you can access for free at: http://www.jimmunol.org/content/195/4/1377.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision by guest on September 26, 2021 • No Triage! Every submission reviewed by practicing scientists • 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 © 2015 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Tetraspanin CD151 Is a Negative Regulator of Fc«RI-Mediated Mast Cell Activation Hiam Abdala-Valencia,* Paul J. -
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. -
Beta-Arrestin-Mediated Signaling in the Heart
SPECIAL ARTICLE Circ J 2008; 72: 1725–1729 Beta-Arrestin-Mediated Signaling in the Heart Priyesh A. Patel, BS; Douglas G. Tilley, PhD*; Howard A. Rockman, MD*,** Beta-arrestin is a multifunctional adapter protein well known for its role in G-protein-coupled receptor (GPCR) desensitization. Exciting new evidence indicates thatβ-arrestin is also a signaling molecule capable of initiating its own G-protein-independent signaling at GPCRs. One of the best-studiedβ-arrestin signaling pathways is the one involvingβ-arrestin-dependent activation of a mitogen-activated protein kinase cascade, the extracellular regulated kinase (ERK). ERK signaling, which is classically activated by agonist stimulation of the epidermal growth factor receptor (EGFR), can be activated by a number of GPCRs in aβ-arrestin-dependent manner. Recent work in animal models of heart failure suggests thatβ-arrestin-dependent activation of EGFR/ERK signaling by theβ-1-adrenergic receptor, and possibly the angiotensin II Type 1A receptor, are cardioprotective. Hence, a new model of signaling at cardiac GPCRs has emerged and implicates classical G-protein-mediated signaling with promoting harmful remodeling in heart failure, while concurrently linkingβ-arrestin-dependent, G-protein-inde- pendent signaling with cardioprotective effects. Based on this paradigm, a new class of drugs could be identified, termed “biased ligands”, which simultaneously block harmful G-protein signaling, while also promoting cardio- protectiveβ-arrestin-dependent signaling, leading to a potential breakthrough -
BMC Evolutionary Biology Biomed Central
BMC Evolutionary Biology BioMed Central Research article Open Access On the origins of arrestin and rhodopsin Carlos E Alvarez1,2,3 Address: 1Center for Molecular and Human Genetics, The Research Institute at Nationwide Children's Hospital, Columbus, OH, 43205, USA, 2Department of Pediatrics, The Ohio State University College of Medicine, Columbus, OH, 43210, USA and 3Novartis Institutes of BioMedical Research, CH-4002 Basel, Switzerland Email: Carlos E Alvarez - [email protected] Published: 29 July 2008 Received: 11 January 2008 Accepted: 29 July 2008 BMC Evolutionary Biology 2008, 8:222 doi:10.1186/1471-2148-8-222 This article is available from: http://www.biomedcentral.com/1471-2148/8/222 © 2008 Alvarez; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract Background: G protein coupled receptors (GPCRs) are the most numerous proteins in mammalian genomes, and the most common targets of clinical drugs. However, their evolution remains enigmatic. GPCRs are intimately associated with trimeric G proteins, G protein receptor kinases, and arrestins. We conducted phylogenetic studies to reconstruct the history of arrestins. Those findings, in turn, led us to investigate the origin of the photosensory GPCR rhodopsin. Results: We found that the arrestin clan is comprised of the Spo0M protein family in archaea and bacteria, and the arrestin and Vps26 families in eukaryotes. The previously known animal arrestins are members of the visual/beta subfamily, which branched from the founding "alpha" arrestins relatively recently. -
Systemic Induction of the Angiogenesis Switch by the Tetraspanin D6.1A/CO-029
Research Article Systemic Induction of the Angiogenesis Switch by the Tetraspanin D6.1A/CO-029 Sabine Gesierich,1 Igor Berezovskiy,1 Eduard Ryschich,2 and Margot Zo¨ller1,3 1Department of Tumor Progression and Immune Defence, German Cancer Research Centre; 2Department of Surgery, University of Heidelberg, Heidelberg; and 3Department of Applied Genetics, Faculty of Chemistry and Bioscience, University of Karlsruhe, Karlsruhe, Germany Abstract transcription of angiogenic factors (6, 7). Recent studies in Expression of the tetraspanin CO-029 is associated with poor knockout and transgenic mouse models have provided further prognosis in patients with gastrointestinal cancer. In a evidence that tumor angiogenesis is not only guided by the pancreatic tumor line, overexpression of the rat homologue, tumor cell itself, but is also closely tied to the tumor microenvi- ronment (8). D6.1A, induces lethally disseminated intravascular coagula- tion, suggesting D6.1A engagement in angiogenesis. D6.1A- Tetraspanins are a large family of proteins grouped according to overexpressing tumor cells induce the greatest amount of structural relatedness. The key feature of tetraspanins is their angiogenesis in vivo, and tumor cells as well as exosomes potential to associate with each other and with a multitude of derived thereof strikingly increase endothelial cell branching molecules from other protein families (9–11), the most prominent in vitro. Tumor cell–derived D6.1A stimulates angiogenic partners being integrins (12). The tetraspanin, D6.1A (rat)/CO-029 a h a h factor transcription, which includes increased matrix metal- (human), associates with 3 1 and 6 1 and, after disassembly of a h loproteinase and urokinase-type plasminogen activator se- hemidesmosomes, with 6 4. -
A Shared Pathway of Exosome Biogenesis Operates at Plasma And
bioRxiv preprint doi: https://doi.org/10.1101/545228; this version posted February 11, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. A shared pathway of exosome biogenesis operates at plasma and endosome membranes Francis K. Fordjour1, George G. Daaboul2, and Stephen J. Gould1* 1Department of Biological Chemistry Johns Hopkins University Baltimore, MD USA 2Nanoview Biosciences Boston, MA USA Corresponding author: Stephen J. Gould, Ph.D. Department of Biological Chemistry Johns Hopkins University Baltimore, MD USA Email: [email protected] Tel (01) 443 847 9918 1 bioRxiv preprint doi: https://doi.org/10.1101/545228; this version posted February 11, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Summary: This study of exosome cargo protein budding reveals that cells use a common pathway for budding exosomes from plasma and endosome membranes, providing a new mechanistic explanation for exosome heterogeneity and a rational roadmap for exosome engineering. Keywords: Protein budding, tetraspanin, endosome, plasma membrane, extracellular vesicle, CD9, CD63, CD81, SPIR, interferometry Abbreviations: EV, extracellular vesicles; IB, immunoblot; IFM, immunofluorescence microscopy; IPMC, intracellular plasma membrane-connected compartment; MVB, multivesicular body; SPIR, single-particle interferometric reflectance; SPIRI, single-particle interferometric reflectance imaging 2 bioRxiv preprint doi: https://doi.org/10.1101/545228; this version posted February 11, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. -
Expression of the Tetraspanins CD9, CD37, CD63, and CD151 in Merkel Cell Carcinoma: Strong Evidence for a Posttranscriptional Fine-Tuning of CD9 Gene Expression
Modern Pathology (2010) 23, 751–762 & 2010 USCAP, Inc. All rights reserved 0893-3952/10 $32.00 751 Expression of the tetraspanins CD9, CD37, CD63, and CD151 in Merkel cell carcinoma: strong evidence for a posttranscriptional fine-tuning of CD9 gene expression Markus Woegerbauer1, Dietmar Thurnher1, Roland Houben2, Johannes Pammer3, Philipp Kloimstein1, Gregor Heiduschka1, Peter Petzelbauer4 and Boban M Erovic1 1Department of Otorhinolaryngology, Head and Neck Surgery, Medical University of Vienna, Vienna, Austria; 2Department of Dermatology, Medical University of Wuerzburg, Germany; 3Department of Clinical Pathology, Medical University of Vienna, Vienna, Austria and 4Department of Dermatology, Medical University of Vienna, Vienna, Austria Tetraspanins including CD9, CD37, CD63, and CD151 are linked to cellular adhesion, cell differentiation, migration, carcinogenesis, and tumor progression. The aim of the study was to detect, quantify, and evaluate the prognostic value of these tetraspanins in Merkel cell carcinoma and to study the regulation of CD9 mRNA expression in Merkel cell carcinoma cell lines in detail. Immunohistochemical staining of 28 Merkel cell carcinoma specimens from 25 patients showed a significant correlation of CD9 (P ¼ 0.03) and CD151 (P ¼ 0.043) expression to overall survival. CD9 and CD63 expression correlated significantly to patients’ disease-free interval (P ¼ 0.017 and P ¼ 0.058). Of primary Merkel cell carcinoma tumors, 42% were CD9 positive in contrast to only 21% of the subcutaneous in-transit metastases. Characterization of the 50 untranslated region (UTR) of the CD9 mRNA from two cultured Merkel cell carcinoma cell lines revealed the presence of two major RNA species differing only in the length of their 50 termini (183 versus 102 nucleotides). -
Kruppel-Like Factor 9 Inhibits Glioblastoma Stemness
KRUPPEL-LIKE FACTOR 9 INHIBITS GLIOBLASTOMA STEMNESS THROUGH GLOBAL TRANSCRIPTION REPRESSION AND INHIBITION OF INTEGRIN ALPHA 6 AND CD151 By Jessica Tilghman A dissertation submitted to Johns Hopkins University in conformity with the requirements for the degree of Doctor of Philosophy Baltimore, Maryland October, 2015 Abstract Glioblastoma (GBM) stem cells (GSCs) represent tumor-propagating cells with stem-like characteristics (stemness) that contribute disproportionately to GBM drug resistance and tumor recurrence. Understanding the mechanisms supporting GSC stemness is important for developing novel strategies that target tumor propagation to inhibit cancer progression and improve patient survival. Krüppel-like factor 9 (KLF9) has emerged as a regulator of cell differentiation, neural development, and oncogenesis; however, the molecular basis for KLF9’s diverse contextual functions has been unclear. We establish for the first time a genome-wide map of KLF9-regulated targets in human glioblastoma stem-like cells, and show that KLF9 functions as a transcriptional repressor and thereby regulates multiple signaling pathways involved in oncogenesis and regulation of cancer stem-like phenotype. A detailed analysis of two novel KLF9 targets suggests that KLF9 inhibits glioma cell stemness by repressing expression of integrin α6 and CD151. The expression of one candidate KLF9 target gene ITGA6 coding for integrin α6 was verified to be downregulated by KLF9 in GSCs. ITGA6 transcription repression by KLF9 altered GBM neurosphere cell behavior as evidenced by reduced cell adhesion to and migration through membrane coated with the integrin α6 ligand laminin. Forced expression of integrin α6 partially rescued GBM neurosphere cells from the differentiating and adhesion/migration-inhibiting effects of KLF9. -
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. -
Tetraspanin CD151 Plays a Key Role in Skin Squamous Cell Carcinoma
Oncogene (2013) 32, 1772–1783 & 2013 Macmillan Publishers Limited All rights reserved 0950-9232/13 www.nature.com/onc ORIGINAL ARTICLE Tetraspanin CD151 plays a key role in skin squamous cell carcinoma QLi1, XH Yang2,FXu1, C Sharma1, H-X Wang1, K Knoblich1, I Rabinovitz3, SR Granter4 and ME Hemler1 Here we provide the first evidence that tetraspanin CD151 can support de novo carcinogenesis. During two-stage mouse skin chemical carcinogenesis, CD151 reduces tumor lag time and increases incidence, multiplicity, size and progression to malignant squamous cell carcinoma (SCC), while supporting both cell survival during tumor initiation and cell proliferation during the promotion phase. In human skin SCC, CD151 expression is selectively elevated compared with other skin cancer types. CD151 support of keratinocyte survival and proliferation may depend on activation of transcription factor STAT3 (signal transducers and activators of transcription), a regulator of cell proliferation and apoptosis. CD151 also supports protein kinase C (PKC)a–a6b4 integrin association and PKC-dependent b4 S1424 phosphorylation, while regulating a6b4 distribution. CD151–PKCa effects on integrin b4 phosphorylation and subcellular localization are consistent with epithelial disruption to a less polarized, more invasive state. CD151 ablation, while minimally affecting normal cell and normal mouse functions, markedly sensitized mouse skin and epidermoid cells to chemicals/drugs including 7,12-dimethylbenz[a]anthracene (mutagen) and camptothecin (topoisomerase inhibitor), as well as to agents targeting epidermal growth factor receptor, PKC, Jak2/Tyk2 and STAT3. Hence, CD151 ‘co-targeting’ may be therapeutically beneficial. These findings not only support CD151 as a potential tumor target, but also should apply to other cancers utilizing CD151/laminin-binding integrin complexes. -
Novel CD37, Humanized CD37 and Bi-Specific Humanized CD37-CD19
cancers Article Novel CD37, Humanized CD37 and Bi-Specific Humanized CD37-CD19 CAR-T Cells Specifically Target Lymphoma Vita Golubovskaya 1,*, Hua Zhou 1, Feng Li 1,2, Michael Valentine 1, Jinying Sun 1, Robert Berahovich 1, Shirley Xu 1, Milton Quintanilla 1, Man Cheong Ma 1, John Sienkiewicz 1, Yanwei Huang 1 and Lijun Wu 1,3,* 1 Promab Biotechnologies, 2600 Hilltop Drive, Richmond, CA 94806, USA; [email protected] (H.Z.); [email protected] (F.L.); [email protected] (M.V.); [email protected] (J.S.); [email protected] (R.B.); [email protected] (S.X.); [email protected] (M.Q.); [email protected] (M.C.M.); [email protected] (J.S.); [email protected] (Y.H.) 2 Biology and Environmental Science College, Hunan University of Arts and Science, Changde 415000, China 3 Forevertek Biotechnology, Janshan Road, Changsha Hi-Tech Industrial Development Zone, Changsha 410205, China * Correspondence: [email protected] (V.G.); [email protected] (L.W.); Tel.: +510-974-0697 (V.G.) Simple Summary: Chimeric antigen receptor (CAR) T cell therapy represents a major advancement in cancer treatment. Recently, FDA approved CAR-T cells directed against the CD19 protein for treatment of leukemia and lymphoma. In spite of impressive clinical responses with CD19-CAR-T cells, some patients demonstrate disease relapse due to either antigen loss, cancer heterogeneity or other mechanisms. Novel CAR-T cells and targets are important for the field. This report describes Citation: Golubovskaya, V.; Zhou, novel CD37, humanized CD37 and bispecific humanized CD37-CD19-CAR-T cells targeting both H.; Li, F.; Valentine, M.; Sun, J.; CD37 and CD19.