RT² Profiler PCR Array (96-Well Format and 384-Well [4 X 96] Format)
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Stem Cell Factor Is Selectively Secreted by Arterial Endothelial Cells in Bone Marrow
ARTICLE DOI: 10.1038/s41467-018-04726-3 OPEN Stem cell factor is selectively secreted by arterial endothelial cells in bone marrow Chunliang Xu1,2, Xin Gao1,2, Qiaozhi Wei1,2, Fumio Nakahara 1,2, Samuel E. Zimmerman3,4, Jessica Mar3,4 & Paul S. Frenette 1,2,5 Endothelial cells (ECs) contribute to haematopoietic stem cell (HSC) maintenance in bone marrow, but the differential contributions of EC subtypes remain unknown, owing to the lack 1234567890():,; of methods to separate with high purity arterial endothelial cells (AECs) from sinusoidal endothelial cells (SECs). Here we show that the combination of podoplanin (PDPN) and Sca-1 expression distinguishes AECs (CD45− Ter119− Sca-1bright PDPN−) from SECs (CD45− Ter119− Sca-1dim PDPN+). PDPN can be substituted for antibodies against the adhesion molecules ICAM1 or E-selectin. Unexpectedly, prospective isolation reveals that AECs secrete nearly all detectable EC-derived stem cell factors (SCF). Genetic deletion of Scf in AECs, but not SECs, significantly reduced functional HSCs. Lineage-tracing analyses suggest that AECs and SECs self-regenerate independently after severe genotoxic insults, indicating the per- sistence of, and recovery from, radio-resistant pre-specified EC precursors. AEC-derived SCF also promotes HSC recovery after myeloablation. These results thus uncover heterogeneity in the contribution of ECs in stem cell niches. 1 The Ruth L. and David S. Gottesman Institute for Stem Cell and Regenerative Medicine Research, Albert Einstein College of Medicine, New York, NY 10461, USA. 2 Department of Cell Biology, Albert Einstein College of Medicine, New York, NY 10461, USA. 3 Department of Systems and Computational Biology, Albert Einstein College of Medicine, New York, NY 10461, USA. -
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. -
Altered Integrin Alpha 6 Expression As a Rescue for Muscle Fiber Detachment in Zebrafish (Danio Rerio)
The University of Maine DigitalCommons@UMaine Honors College Spring 2014 Altered Integrin Alpha 6 Expression As A Rescue For Muscle Fiber Detachment In Zebrafish (Danio Rerio) Rose E. McGlauflin Follow this and additional works at: https://digitalcommons.library.umaine.edu/honors Part of the Animal Diseases Commons, and the Musculoskeletal Diseases Commons Recommended Citation McGlauflin, Rose E., Alter" ed Integrin Alpha 6 Expression As A Rescue For Muscle Fiber Detachment In Zebrafish (Danio Rerio)" (2014). Honors College. 140. https://digitalcommons.library.umaine.edu/honors/140 This Honors Thesis is brought to you for free and open access by DigitalCommons@UMaine. It has been accepted for inclusion in Honors College by an authorized administrator of DigitalCommons@UMaine. For more information, please contact [email protected]. ALTERED INTEGRIN ALPHA 6 EXPRESSION AS A RESCUE FOR MUSCLE FIBER DETACHMENT IN ZEBRAFISH (DANIO RERIO) by Rose E. McGlauflin A Thesis Submitted in Partial Fulfillment of the Requirements for a Degree with Honors (Biology) The Honors College University of Maine May 2014 Advisory Committee: Clarissa A. Henry, Ph.D., Associate Professor of Biological Sciences, Advisor Mary S. Tyler, Ph.D., Professor of Zoology Mary Astumian, Henry Lab Manager Michelle Smith, Ph.D., Assistant Professor of Biological Sciences Mark Haggerty, Ph.D., Honors Preceptor for Civic Engagement Abstract Cells adhere to their extracellular matrix by way of integrins, transmembrane molecules that attach the cytoskeleton to the extracellular basement membrane (one kind of extracellular matrix). In some muscular dystrophies, specific integrins are disrupted and muscle fibers detach from the myotendenous junction and degenerate. This integrin disruption causes a constant cycle of regeneration and degeneration, which greatly harms the tissue over time. -
Molecular Profile of Tumor-Specific CD8+ T Cell Hypofunction in a Transplantable Murine Cancer Model
Downloaded from http://www.jimmunol.org/ by guest on September 25, 2021 T + is online at: average * The Journal of Immunology , 34 of which you can access for free at: 2016; 197:1477-1488; Prepublished online 1 July from submission to initial decision 4 weeks from acceptance to publication 2016; doi: 10.4049/jimmunol.1600589 http://www.jimmunol.org/content/197/4/1477 Molecular Profile of Tumor-Specific CD8 Cell Hypofunction in a Transplantable Murine Cancer Model Katherine A. Waugh, Sonia M. Leach, Brandon L. Moore, Tullia C. Bruno, Jonathan D. Buhrman and Jill E. Slansky J Immunol cites 95 articles Submit online. Every submission reviewed by practicing scientists ? is published twice each month by Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts http://jimmunol.org/subscription Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html http://www.jimmunol.org/content/suppl/2016/07/01/jimmunol.160058 9.DCSupplemental This article http://www.jimmunol.org/content/197/4/1477.full#ref-list-1 Information about subscribing to The JI No Triage! Fast Publication! Rapid Reviews! 30 days* Why • • • Material References Permissions Email Alerts Subscription Supplementary The Journal of Immunology The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2016 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. This information is current as of September 25, 2021. The Journal of Immunology Molecular Profile of Tumor-Specific CD8+ T Cell Hypofunction in a Transplantable Murine Cancer Model Katherine A. -
ARVC-Variants.Pdf
Updated gene list responsible for ARVC/D pathology Subtype Gene Location Reference ARVC1 TGFB3 14q24.3 Beffagna G, Occhi G, Nava A, et al. Regulatory mutations in transforming growth factor-beta3 gene cause arrhythmogenic right ventricular cardiomyopathy type 1. Cardiovasc Res. 2005;65:366–73. ARVC2 RYR2 1q43 Tiso N, Stephan DA, Nava A, et al. Identification of mutations in the cardiac ryanodine receptor gene in families affected with arrhythmogenic right ventricular cardiomyopathy type 2 (ARVD2). Hum Mol Genet. 2001;10:189–94. ARVC3 Unknown 14q12-q22 Severini GM, Krajinovic M, Pinamonti B, et al. A new locus for arrhythmogenic right ventricular dysplasia on the long arm of chromosome 14. Genomics. 1996;31:193–200. ARVC4 TTN 2q32.1-q32.3 Taylor M, Graw S, Sinagra G, et al. Genetic variation in titin in arrhythmogenic right ventricular cardiomyopathy-overlap syndromes. Circulation. 2011;124:876–85. ARVC5 TMEM43 3p25.1 Merner ND, Hodgkinson KA, Haywood AF, et al. Arrhythmogenic right ventricular cardiomyopathy type 5 is a fully penetrant, lethal arrhythmic disorder caused by a missense mutation in the TMEM43 gene. Am J Hum Genet. 2008;82:809–21. ARVC6 Unknown 10p14-p12 Li D, Ahmad F, Gardner MJ, et al. The locus of a novel gene responsible for arrhythmogenic right- ventricular dysplasia characterized by early onset and high penetrance maps to chromosome 10p12-p14. Am J Hum Genet. 2000;66:148–56. ARVC7 DES 2q35 Klauke B, Kossmann S, Gaertner A, et al. De novo desmin-mutation N116S is associated with arrhythmogenic right ventricular cardiomyopathy. Hum Mol Genet. 2010;19:4595–607. -
Propranolol-Mediated Attenuation of MMP-9 Excretion in Infants with Hemangiomas
Supplementary Online Content Thaivalappil S, Bauman N, Saieg A, Movius E, Brown KJ, Preciado D. Propranolol-mediated attenuation of MMP-9 excretion in infants with hemangiomas. JAMA Otolaryngol Head Neck Surg. doi:10.1001/jamaoto.2013.4773 eTable. List of All of the Proteins Identified by Proteomics This supplementary material has been provided by the authors to give readers additional information about their work. © 2013 American Medical Association. All rights reserved. Downloaded From: https://jamanetwork.com/ on 10/01/2021 eTable. List of All of the Proteins Identified by Proteomics Protein Name Prop 12 mo/4 Pred 12 mo/4 Δ Prop to Pred mo mo Myeloperoxidase OS=Homo sapiens GN=MPO 26.00 143.00 ‐117.00 Lactotransferrin OS=Homo sapiens GN=LTF 114.00 205.50 ‐91.50 Matrix metalloproteinase‐9 OS=Homo sapiens GN=MMP9 5.00 36.00 ‐31.00 Neutrophil elastase OS=Homo sapiens GN=ELANE 24.00 48.00 ‐24.00 Bleomycin hydrolase OS=Homo sapiens GN=BLMH 3.00 25.00 ‐22.00 CAP7_HUMAN Azurocidin OS=Homo sapiens GN=AZU1 PE=1 SV=3 4.00 26.00 ‐22.00 S10A8_HUMAN Protein S100‐A8 OS=Homo sapiens GN=S100A8 PE=1 14.67 30.50 ‐15.83 SV=1 IL1F9_HUMAN Interleukin‐1 family member 9 OS=Homo sapiens 1.00 15.00 ‐14.00 GN=IL1F9 PE=1 SV=1 MUC5B_HUMAN Mucin‐5B OS=Homo sapiens GN=MUC5B PE=1 SV=3 2.00 14.00 ‐12.00 MUC4_HUMAN Mucin‐4 OS=Homo sapiens GN=MUC4 PE=1 SV=3 1.00 12.00 ‐11.00 HRG_HUMAN Histidine‐rich glycoprotein OS=Homo sapiens GN=HRG 1.00 12.00 ‐11.00 PE=1 SV=1 TKT_HUMAN Transketolase OS=Homo sapiens GN=TKT PE=1 SV=3 17.00 28.00 ‐11.00 CATG_HUMAN Cathepsin G OS=Homo -
Goat Anti-JAM2 / JAMB / CD322 Antibody Peptide-Affinity Purified Goat Antibody Catalog # Af1576a
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 Goat Anti-JAM2 / JAMB / CD322 Antibody Peptide-affinity purified goat antibody Catalog # AF1576a Specification Goat Anti-JAM2 / JAMB / CD322 Antibody - Product Information Application WB Primary Accession P57087 Other Accession NP_067042, 58494, 67374 (mouse), 619374 (rat) Reactivity Human Predicted Mouse, Rat, Dog, Cow Host Goat Clonality Polyclonal Concentration 100ug/200ul Isotype IgG Calculated MW 33207 Goat Anti-JAM2 / JAMB / CD322 Antibody - AF1576a (0.5 µg/ml) staining of Human Additional Information Heart lysate (35 µg protein in RIPA buffer) with (B) and without (A) blocking with the Gene ID 58494 immunising peptide. Primary incubation was 1 hour. Detected by chemiluminescence. Other Names Junctional adhesion molecule B, JAM-B, Junctional adhesion molecule 2, JAM-2, Goat Anti-JAM2 / JAMB / CD322 Antibody - Vascular endothelial junction-associated Background molecule, VE-JAM, CD322, JAM2, C21orf43, VEJAM Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial Format cell sheets, forming continuous seals around 0.5 mg IgG/ml in Tris saline (20mM Tris cells and serving as a physical barrier to pH7.3, 150mM NaCl), 0.02% sodium azide, prevent solutes and water from passing freely with 0.5% bovine serum albumin through the paracellular space. The protein encoded by this immunoglobulin superfamily Storage gene member is localized in the tight junctions Maintain refrigerated at 2-8°C for up to 6 between high endothelial cells. It acts as an months. For long term storage store at adhesive ligand for interacting with a variety of -20°C in small aliquots to prevent immune cell types and may play a role in freeze-thaw cycles. -
2335 Roles of Molecules Involved in Epithelial/Mesenchymal Transition
[Frontiers in Bioscience 13, 2335-2355, January 1, 2008] Roles of molecules involved in epithelial/mesenchymal transition during angiogenesis Giulio Ghersi Dipartimento di Biologia Cellulare e dello Sviluppo, Universita di Palermo, Italy TABLE OF CONTENTS 1. Abstract 2. Introduction 3. Extracellular matrix 3.1. ECM and integrins 3.2. Basal lamina components 4. Cadherins. 4.1. Cadherins in angiogenesis 5. Integrins. 5.1. Integrins in angiogenesis 6. Focal adhesion molecules 7. Proteolytic enzymes 7.1. Proteolytic enzymes inhibitors 7.2. Proteolytic enzymes in angiogenesis 8. Perspective 9. Acknowledgements 10. References 1.ABSTRACT 2. INTRODUCTION Formation of vessels requires “epithelial- Growth of new blood vessels (angiogenesis) mesenchymal” transition of endothelial cells, with several plays a key role in several physiological processes, such modifications at the level of endothelial cell plasma as vascular remodeling during embryogenesis and membranes. These processes are associated with wound healing tissue repair in the adult; as well as redistribution of cell-cell and cell-substrate adhesion pathological processes, including rheumatoid arthritis, molecules, cross talk between external ECM and internal diabetic retinopathy, psoriasis, hemangiomas, and cytoskeleton through focal adhesion molecules and the cancer (1). Vessel formation entails the “epithelial- expression of several proteolytic enzymes, including matrix mesenchymal” transition of endothelial cells (ECs) “in metalloproteases and serine proteases. These enzymes with vivo”; a similar phenotypic exchange can be induced “in their degradative action on ECM components, generate vitro” by growing ECs to low cell density, or in “wound molecules acting as activators and/or inhibitors of healing” experiments or perturbing cell adhesion and angiogenesis. The purpose of this review is to provide an associated molecule functions. -
P190a Rhogap Induces CDH1 Expression and Cooperates with E-Cadherin to Activate LATS Kinases and Suppress Tumor Cell Growth
p190A RhoGAP induces CDH1 expression and cooperates with E-cadherin to activate LATS kinases and suppress tumor cell growth Ouyang, Hanyue; Luong, Phi; Frödin, Morten; Hansen, Steen H. Published in: Oncogene DOI: 10.1038/s41388-020-1385-2 Publication date: 2020 Document version Publisher's PDF, also known as Version of record Document license: CC BY Citation for published version (APA): Ouyang, H., Luong, P., Frödin, M., & Hansen, S. H. (2020). p190A RhoGAP induces CDH1 expression and cooperates with E-cadherin to activate LATS kinases and suppress tumor cell growth. Oncogene, 39(33), 5570- 5587. https://doi.org/10.1038/s41388-020-1385-2 Download date: 05. okt.. 2021 Oncogene (2020) 39:5570–5587 https://doi.org/10.1038/s41388-020-1385-2 ARTICLE p190A RhoGAP induces CDH1 expression and cooperates with E-cadherin to activate LATS kinases and suppress tumor cell growth 1 1 2 1 Hanyue Ouyang ● Phi Luong ● Morten Frödin ● Steen H. Hansen Received: 26 March 2020 / Revised: 9 June 2020 / Accepted: 29 June 2020 / Published online: 8 July 2020 © The Author(s) 2020. This article is published with open access Abstract The ARHGAP35 gene encoding p190A RhoGAP (p190A) is significantly altered by both mutation and allelic deletion in human cancer, but the functional implications of such alterations are not known. Here, we demonstrate for the first time that p190A is a tumor suppressor using a xenograft mouse model with carcinoma cells harboring defined ARHGAP35 alterations. In vitro, restoration of p190A expression in carcinoma cells promotes contact inhibition of proliferation (CIP) through activation of LATS kinases and phosphorylation of the proto-oncogenic transcriptional co-activator YAP. -
Orally Administered Glucosylceramide Improves the Skin Barrier Function by Upregulating Genes Associated with the Tight Junction and Cornified Envelope Formation
110215 (251) Biosci. Biotechnol. Biochem., 75 (8), 110215-1–8, 2011 Orally Administered Glucosylceramide Improves the Skin Barrier Function by Upregulating Genes Associated with the Tight Junction and Cornified Envelope Formation y Ritsuro IDETA, Tomohiro SAKUTA, Yusuke NAKANO, and Taro UCHIYAMA Shiseido Functional Food Research and Development Center, 2-12-1 Fukuura, Kanazawa-ku, Yokohama 236-8643, Japan Received March 18, 2011; Accepted May 9, 2011; Online Publication, August 7, 2011 [doi:10.1271/bbb.110215] Dietary glucosylceramide improves the skin barrier mammalian skin barrier function through their role as function. We used a microarray system to analyze the intracellular lipids.6) The skin barrier is essential for mRNA expression in SDS-treated dorsal skin of the protecting against physical stimuli, thermal challenge, hairless mouse to elucidate the molecular mechanisms ultraviolet light (UV), chemical substances and micro- involved. The transepidermal water loss of mouse skin organisms, as well as for preventing water loss.7) The was increased by the SDS treatment, this increase being barrier function is mainly localized in the stratum significantly reduced by a prior oral administration of corneum (SC) which is formed in the outermost layer of glucosylceramides. The microarray-evaluated mRNA the epidermis and consists of the cornified envelope expressionAdvance ratio showed a statistically significant View in- (CE) and intercellular multilamellar lipids. CE forms crease in the expression of genes related to the cornified a highly durable and flexible barrier8) comprising a envelope and tight junction formation when compared 15-nm-thick structure composed of such insoluble with all genes in the glucosylceramide-fed/SDS-treated proteins as involucrin, loricrin, and small proline-rich mouse skin. -
The Schizosaccharomyces Pombe Cdt2 Gene, a Target of G1-S Phase-Specific Transcription Factor Complex DSC1, Is Required for Mito
Copyright 2003 by the Genetics Society of America The Schizosaccharomyces pombe cdt2؉ Gene, a Target of G1-S Phase-Specific Transcription Factor Complex DSC1, Is Required for Mitotic and Premeiotic DNA Replication Shu-hei Yoshida,* Hiba Al-Amodi,† Taro Nakamura,* Christopher J. McInerny† and Chikashi Shimoda*,1 *Department of Biology, Graduate School of Science, Osaka City University, Osaka 558-8585, Japan and †Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, United Kingdom Manuscript received November 16, 2002 Accepted for publication March 24, 2003 ABSTRACT We have defined five sev genes by genetic analysis of Schizosaccharomyces pombe mutants, which are defective in both proliferation and sporulation. sev1 ϩ/cdt2 ϩ was transcribed during the G1-S phase of the mitotic cell cycle, as well as during the premeiotic S phase. The mitotic expression of cdt2 ϩ was regulated by the MCB-DSC1 system. A mutant of a component of DSC1 affected cdt2 ϩ expression in vivo, and a cdt2 ϩ promoter fragment containing MCB motifs bound DSC1 in vitro. Cdt2 protein also accumulated in S phase and localized to the nucleus. cdt2 null mutants grew slowly at 30Њ and were unable to grow at 19Њ. These cdt2 mutants were also medially sensitive to hydroxyurea, camptothecin, and 4-nitroquinoline- 1-oxide and were synthetically lethal in combination with DNA replication checkpoint mutations. Flow cytometry analysis and pulsed-field gel electrophoresis revealed that S-phase progression was severely retarded in cdt2 mutants, especially at low temperatures. Under sporulation conditions, premeiotic DNA replication was impaired with meiosis I blocked. -
Similarities and Differences in Extracellular Vesicle Profiles
biomedicines Article Similarities and Differences in Extracellular Vesicle Profiles between Ischaemic Stroke and Myocardial Infarction Laura Otero-Ortega 1,† , Elisa Alonso-López 1,† , María Pérez-Mato 1,†, Fernando Laso-García 1,† , Mari Carmen Gómez-de Frutos 1 , Luke Diekhorst 1 , María Laura García-Bermejo 2, Elisa Conde-Moreno 2 , Blanca Fuentes 1, María Alonso de Leciñana 1 , Eduardo Armada 3, Lorena Buiza-Palomino 4, Exuperio Díez-Tejedor 1,‡ and María Gutiérrez-Fernández 1,*,‡ 1 Neurological Sciences and Cerebrovascular Research Laboratory, Department of Neurology and Stroke Centre, Neuroscience Area of IdiPAZ, Hospital La Paz Institute for Health Research–IdiPAZ, La Paz University Hospital, Universidad Autónoma de Madrid, 28046 Madrid, Spain; [email protected] (L.O.-O.); [email protected] (E.A.-L.); [email protected] (M.P.-M.); [email protected] (F.L.-G.); [email protected] (M.C.G.-d.F.); [email protected] (L.D.); [email protected] (B.F.); [email protected] (M.A.d.L.); [email protected] (E.D.-T.) 2 Biomarkers and Therapeutic Targets Unit, Instituto Ramón y Cajal de Investigación Sanitaria (IRYCIS), 28034 Madrid, Spain; [email protected] (M.L.G.-B.); [email protected] (E.C.-M.) 3 Acute Cardiac Care Unit, Cardiology Department, IdiPAZ Health Research Institute, 28046 Madrid, Spain; [email protected] 4 Clinical Analysis Department, La Paz University Hospital, 28046 Madrid, Spain; [email protected] * Correspondence: [email protected]; Tel.: +34-91-207-1028 † These authors share first author position. ‡ These authors contributed equally to this work. Citation: Otero-Ortega, L.; Abstract: Extracellular vesicles (EVs) are involved in intercellular signalling through the transfer of Alonso-López, E.; Pérez-Mato, M.; molecules during physiological and pathological conditions, such as ischaemic disease.