Monoclonal Antibody to Catenin Delta-2 - Supernatant

OriGene Technologies, Inc. OriGene Technologies GmbH 9620 Medical Center Drive, Ste 200 Schillerstr. 5 Rockville, MD 20850 32052 Herford UNITED STATES GERMANY Phone: +1-888-267-4436 Phone: +49-5221-34606-0 Fax: +1-301-340-8606 Fax: +49-5221-34606-11 [email protected] [email protected] BM5099 Monoclonal Antibody to Catenin delta-2 - Supernatant Alternate names: ARM-repeat protein, CTNND2, Delta-catenin, GT24, NPRAP, Neural plakophilin-related, Neurojungin Quantity: 5 ml Background: Delta-Catenin, is a member of the p120 catenin subfamily of catenins. Delta- Catenin/NPRAP was identified as a protein homologous to plakophilin 1 and as a protein interacting with the loop region of presenilin 1 (PS1), the gene most commonly mutated in Alzheimer's disease. Delta-Catenin/NPRAP is almost exclusively expressed in the central nervous system mainly during early brain development. Delta-Catenin/NPRAP has been shown to co- localize and interact with N-cadherin in the mouse brain and to undergo dynamic relocalization during brain development. Uniprot ID: Q9UQB3 NCBI: NP_001323.1 GeneID: 1501 Host / Isotype: Mouse / IgG1 Clone: J19 Immunogen: Synthetic peptide J6 (corresponding to aa 292-309), coupled to KLH Format: State: Liquid Culture Supernatant Applications: Immunoblotting. Immunohistochemistry on Frozen Sections. Immunohistochemistry on Paraffin Sections: Ready-to-use (only after microwave treatment). Positive Control: Murine Brain, Retina. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user. Specificity: This Monoclonal antibody reacts specifically with Neurojungin (delta-catenin,a unique 160 kD polypeptide of the plakoglobin / armadillo protein family) present in adhering type junctions in the nervous system, primarily expressed in the brain. Deltacatenin also binds to Presenilin-1, mutations of this protein are described to play a role in familial Alzheimer’s disease. No cross-reaction with other members of the Armadillo / Plakoglobin protein family. The antibody is positive with a 300 kD polypetide in Endothelia from blood vessels. Species Reactivity: Tested: Human, Bovine, Rat, Mouse, Zebrafish. Storage: Store the antibody undiluted at 2-8°C. Shelf life: one year from despatch. General Readings: 1. Paffenholz R, Kuhn C, Grund C, Stehr S, Franke WW. The arm-repeat protein NPRAP (neurojungin) is a constituent of the plaques of the outer limiting zone in the retina, defining a novel type of adhering junction. Exp Cell Res. 1999 Aug 1;250(2):452-64. PubMed PMID: 10413599. For research and in vitro use only. Not for diagnostic or therapeutic work. Material Safety Datasheets are available at www.acris-antibodies.com or on request. OG/20130513 1 / 2 BM5099: Monoclonal Antibody to Catenin delta-2 - Supernatant 2. Hatzfeld M. The p120 family of cell adhesion molecules. Eur J Cell Biol. 2005 Mar;84(2-3):205-14. PubMed PMID: 15819401. 3. Kosik KS, Donahue CP, Israely I, Liu X, Ochiishi T. Delta-catenin at the synaptic- adherens junction. Trends Cell Biol. 2005 Mar;15(3):172-8. PubMed PMID: 15752981. For research and in vitro use only. Not for diagnostic or therapeutic work. Material Safety Datasheets are available at www.acris-antibodies.com or on request. OG/20130513 2 / 2 Powered by TCPDF (www.tcpdf.org).

Copy Link

Recommended publications

Genes in Eyecare Geneseyedoc 3 W.M
Genes in Eyecare geneseyedoc 3 W.M. Lyle and T.D. Williams 15 Mar 04 This information has been gathered from several sources; however, the principal source is V. A. McKusick’s Mendelian Inheritance in Man on CD-ROM. Baltimore, Johns Hopkins University Press, 1998. Other sources include McKusick’s, Mendelian Inheritance in Man. Catalogs of Human Genes and Genetic Disorders. Baltimore. Johns Hopkins University Press 1998 (12th edition). http://www.ncbi.nlm.nih.gov/Omim See also S.P.Daiger, L.S. Sullivan, and B.J.F. Rossiter Ret Net http://www.sph.uth.tmc.edu/Retnet disease.htm/. Also E.I. Traboulsi’s, Genetic Diseases of the Eye, New York, Oxford University Press, 1998. And Genetics in Primary Eyecare and Clinical Medicine by M.R. Seashore and R.S.Wappner, Appleton and Lange 1996. M. Ridley’s book Genome published in 2000 by Perennial provides additional information. Ridley estimates that we have 60,000 to 80,000 genes. See also R.M. Henig’s book The Monk in the Garden: The Lost and Found Genius of Gregor Mendel, published by Houghton Mifflin in 2001 which tells about the Father of Genetics. The 3rd edition of F. H. Roy’s book Ocular Syndromes and Systemic Diseases published by Lippincott Williams & Wilkins in 2002 facilitates differential diagnosis. Additional information is provided in D. Pavan-Langston’s Manual of Ocular Diagnosis and Therapy (5th edition) published by Lippincott Williams & Wilkins in 2002. M.A. Foote wrote Basic Human Genetics for Medical Writers in the AMWA Journal 2002;17:7-17. A compilation such as this might suggest that one gene = one disease.
[Show full text]
Differential Stromal Reprogramming in Benign and Malignant Naturally Occurring Canine Mammary Tumours Identifies Disease-Promoting Stromal Components
bioRxiv preprint doi: https://doi.org/10.1101/783621; this version posted September 26, 2019. 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. Differential stromal reprogramming in benign and malignant naturally occurring canine mammary tumours identifies disease-promoting stromal components Parisa Amini 1,a, Sina Nassiri 2,a, Alexandra Malbon 3,4 and Enni Markkanen 1,* 1 Institute of Veterinary Pharmacology and Toxicology, Vetsuisse Faculty, University of Zürich, Zürich, Switzerland 2 Bioinformatics Core Facility, SIB Swiss Institute of Bioinformatics, Lausanne, Switzerland 3 Institute of Veterinary Pathology, Vetsuisse Faculty, University of Zürich, Zürich, Switzerland 4 current address: The Royal (Dick) School of Veterinary Studies and The Roslin Institute Easter Bush Campus, Midlothian, EH25 9RG a these authors contributed equally to the manuscript * Correspondence: [email protected]; ORCID: 0000-0001-7780-8233 Keywords Laser-capture microdissection, canine mammary carcinoma, canine mammary adenoma, breast cancer, tumour stroma, tumour microenvironment Summary statement: RNasequencing-based analysis of stromal reprogramming between benign and malignant naturally occurring canine mammary tumours identifies potential molecular drivers in cancer-associated stroma that support tumour growth and malignancy. Abstract The importance of cancer-associated stroma (CaS) for initiation and progression of cancer is well accepted. However, as stromal changes in benign forms of naturally occurring tumours are poorly understood, it remains unclear how CaS from benign and malignant tumours compare. Spontaneous canine mammary tumours are viewed as excellent models of human mammary carcinomas (mCa).
[Show full text]
A Unique and Specific Interaction Between Αt-Catenin and Plakophilin
2126 Research Article A unique and specific interaction between ␣T-catenin and plakophilin-2 in the area composita, the mixed-type junctional structure of cardiac intercalated discs Steven Goossens1,2,*, Barbara Janssens1,2,*,‡, Stefan Bonné1,2,§, Riet De Rycke1,2, Filip Braet1,2,¶, Jolanda van Hengel1,2 and Frans van Roy1,2,** 1Department for Molecular Biomedical Research, VIB and 2Department of Molecular Biology, Ghent University, B-9052 Ghent, Belgium *These authors contributed equally to this work ‡Present address: Wiley-VCH, Boschstrasse 12, D-69469 Weinheim, Germany §Present address: Diabetes Research Center, Brussels Free University (VUB), Laarbeeklaan 103, B-1090 Brussels, Belgium ¶Present address: Australian Key Centre for Microscopy and Microanalysis, The University of Sydney, NSW 2006, Australia **Author for correspondence (e-mail: [email protected]) Accepted 24 April 2007 Journal of Cell Science 120, 2126-2136 Published by The Company of Biologists 2007 doi:10.1242/jcs.004713 Summary Alpha-catenins play key functional roles in cadherin- desmosomal proteins in the heart localize not only to the catenin cell-cell adhesion complexes. We previously desmosomes in the intercalated discs but also at adhering reported on ␣T-catenin, a novel member of the ␣-catenin junctions with hybrid composition. We found that in the protein family. ␣T-catenin is expressed predominantly in latter junctions, endogenous plakophilin-2 colocalizes with cardiomyocytes, where it colocalizes with ␣E-catenin at the ␣T-catenin. By providing an extra link between the intercalated discs. Whether ␣T- and ␣E-catenin have cadherin-catenin complex and intermediate filaments, the specific or synergistic functions remains unknown. In this binding of ␣T-catenin to plakophilin-2 is proposed to be a study we used the yeast two-hybrid approach to identify means of modulating and strengthening cell-cell adhesion specific functions of ␣T-catenin.
[Show full text]
Improved Memory and Reduced Anxiety in Δ-Catenin Transgenic Mice T Taeyong Ryua,1, Hyung Joon Parkb,1, Hangun Kimc, Young-Chang Choa, Byeong C
Experimental Neurology 318 (2019) 22–31 Contents lists available at ScienceDirect Experimental Neurology journal homepage: www.elsevier.com/locate/yexnr Research Paper Improved memory and reduced anxiety in δ-catenin transgenic mice T Taeyong Ryua,1, Hyung Joon Parkb,1, Hangun Kimc, Young-Chang Choa, Byeong C. Kimd, ⁎ ⁎⁎ Jihoon Jod, Young-Woo Seoe, Won-Seok Choib, , Kwonseop Kima, a College of Pharmacy and Research Institute for Drug Development, Chonnam National University, Gwangju 61186, Republic of Korea b School of Biological Sciences and Technology, College of Natural Sciences, College of Medicine, Chonnam National University, Gwangju 61186, Republic of Korea c College of Pharmacy and Research Institute of Life and Pharmaceutical Sciences, Sunchon National University, Sunchon 57922, Republic of Korea d Department of Neurology, Chonnam National University Medical School, Gwnagju 61469, Republic of Korea e Korea Basic Science Institute, Gwangju Center, Gwangju 61186, Republic of Korea ARTICLE INFO ABSTRACT Keywords: δ-Catenin is abundant in the brain and affects its synaptic plasticity. Furthermore, loss of δ-catenin is related to δ-Catenin the deficits of learning and memory, mental retardation (cri-du-chat syndrome), and autism. A few studies about N-cadherin δ-catenin deficiency mice were performed. However, the effect of δ-catenin overexpression in the brain has not Glutamate receptor been investigated as yet. Therefore we generated a δ-catenin overexpressing mouse model. To generate a Memory transgenic mouse model overexpressing δ-catenin in the brain, δ-catenin plasmid having a Thy-1 promotor was Sociability microinjected in C57BL/6 mice. Our results showed δ-catenin transgenic mice expressed higher levels of N- Anxiety cadherin, β-catenin, and p120-catenin than did wild type mice.
[Show full text]
Multivariate Gene Expression Analysis Reveals Functional Connectivity
BMC Systems Biology BioMed Central Research article Open Access Multivariate gene expression analysis reveals functional connectivity changes between normal/tumoral prostates André Fujita*1, Luciana Rodrigues Gomes2, João Ricardo Sato3, Rui Yamaguchi1, Carlos Eduardo Thomaz4, Mari Cleide Sogayar2 and Satoru Miyano1 Address: 1Human Genome Center, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo, 108-8639, Japan, 2Chemistry Institute, University of São Paulo, Av. Lineu Prestes, 748, São Paulo-SP, 05508-900, Brazil, 3Mathematics, Computation and Cognition Center, Universidade Federal do ABC, Rua Santa Adélia, 166 – Santo André, 09210-170, Brazil and 4Department of Electrical Engineering, Centro Universitário da FEI, Av. Humberto de Alencar Castelo Branco, 3972 – São Bernardo do Campo, 09850-901, Brazil Email: André Fujita* - [email protected] ; Luciana Rodrigues Gomes - [email protected]; João [email protected]; Rui Yamaguchi - [email protected]; Carlos Eduardo Thomaz - [email protected]; Mari Cleide Sogayar - [email protected]; Satoru Miyano - [email protected] * Corresponding author Published: 5 December 2008 Received: 29 August 2008 Accepted: 5 December 2008 BMC Systems Biology 2008, 2:106 doi:10.1186/1752-0509-2-106 This article is available from: http://www.biomedcentral.com/1752-0509/2/106 © 2008 Fujita et al; 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: Prostate cancer is a leading cause of death in the male population, therefore, a comprehensive study about the genes and the molecular networks involved in the tumoral prostate process becomes necessary.
[Show full text]
Viewed in Poste and Fidler, 1980) (See Fig
UNIVERSITY OF CINCINNATI _____________December 6 , 20 _____ 00 I,________________________________Randall Glenn Marsh ______________, hereby submit this as part of the requirements for the degree of: ________________________Doctorate of Philosophy (Ph.D.) ________________________ in: ________________________Cell and Molecular Biology ________________________ It is entitled: ________________________Characterization of a new role for plakoglobin________________________ in ________________________suppressing epithelial cell translocation________________________ ________________________________________________ ________________________________________________ Approved by: ________________________Dr. Robert Brackenbury, Ph.D. (Chair) ________________________Dr. Wallace Ip, Ph.D. ________________________Dr. Randal Morris, Ph.D. ________________________Dr. James Greenberg, M.D. ________________________ CHARACTERIZATION OF A NEW ROLE FOR PLAKOGLOBIN IN SUPPRESSING EPITHELIAL CELL TRANSLOCATION A dissertation submitted to the Division of Research and Advanced Studies of the University of Cincinnati in partial fulfillment of the requirements for the degree of DOCTORATE OF PHILOSOPHY (Ph.D.) in the Department of Cell Biology, Neurobiology, and Anatomy of the College of Medicine 2000 by Randall Glenn Marsh B.Sc., University of Alberta, 1989 M.Sc., University of Alberta, 1992 Committee Chair: Dr. Robert Brackenbury, Ph.D. ii ABSTRACT Despite advances in the treatment of cancer patients, spread, or metastasis, of tumor cells remains a major cause of
[Show full text]
Regulation of the Intermediate Filament Protein Nestin at Rodent Neuromuscular Junctions by Innervation and Activity
5948 • The Journal of Neuroscience, May 30, 2007 • 27(22):5948–5957 Development/Plasticity/Repair Regulation of the Intermediate Filament Protein Nestin at Rodent Neuromuscular Junctions by Innervation and Activity Hyuno Kang,1 Le Tian,1 Young-Jin Son,1 Yi Zuo,1 Diane Procaccino,1 Flora Love,1 Christopher Hayworth,1 Joshua Trachtenberg,1 Michelle Mikesh,1 Lee Sutton,1 Olga Ponomareva,1 John Mignone,2 Grigori Enikolopov,2 Mendell Rimer,1 and Wesley Thompson1 1Section of Neurobiology, Institute of Neuroscience, and Institute for Cell and Molecular Biology, University of Texas, Austin, Texas 78712, and 2Cold Spring Harbor Laboratories, Cold Spring Harbor, New York 11724 The intermediate filament nestin is localized postsynaptically at rodent neuromuscular junctions. The protein forms a filamentous network beneath and between the synaptic gutters, surrounds myofiber nuclei, and is associated with Z-discs adjacent to the junction. In situ hybridization shows that nestin mRNA is synthesized selectively by synaptic myonuclei. Although weak immunoreactivity is present in myelinating Schwann cells that wrap the preterminal axon, nestin is not detected in the terminal Schwann cells (tSCs) that cover the nerve terminal branches. However, after denervation of muscle, nestin is upregulated in tSCs and in SCs within the nerve distal to the lesion site. In contrast, immunoreactivity is strongly downregulated in the muscle fiber. Transgenic mice in which the nestin neural enhancer drives expression of a green fluorescent protein (GFP) reporter show that the regulation in SCs is transcriptional. However, the postsynaptic expression occurs through enhancer elements distinct from those responsible for regulation in SCs. Application of botuli- num toxin shows that the upregulation in tSCs and the loss of immunoreactivity in muscle fibers occurs with blockade of transmitter release.
[Show full text]
Download The
The Role of DHHC5-Mediated Palmitoylation of δ-Catenin in Cadherin Stability and Synapse Plasticity by Gian Stefano Brigidi B.Sc., McGill University, 2007 A THESIS SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY in THE FACULTY OF GRADUATE AND POSTDOCTORAL STUDIES (Neuroscience) THE UNIVERSITY OF BRITISH COLUMBIA (Vancouver) December 2014 © Gian Stefano Brigidi, 2014 Abstract Synapses of the Central Nervous System are specialized junctions of cell-cell contact that transmit signals from one neuron to another in a rapid and efficient manner. Synapses are highly plastic structures that can be continually modified in response to fluctuations in neuronal activity. Changes in the number, size, and protein composition of synapses have been observed following alterations in neuronal activity in vitro and following the learning of specific tasks in vivo. Thus, elucidating the molecular mechanisms underlying activity-mediated trafficking of proteins to and from synaptic compartments is essential for our understanding of brain function. Previous work has demonstrated a requirement for the cadherin-adhesion complex in activity-induced enhancements in synapse strength, however the molecular mechanisms that translate synaptic activation into enhanced cadherin-based adhesion and synapse strengthening remain unknown. This dissertation discusses work that unravels how synaptic activity coordinates the enhancement of cadherin surface stabilization, enlargement of dendritic spines, and increased surface insertion of AMPA receptors. This work demonstrates that increased synaptic activity enhances the palmitoylation of a brain-specific component of the cadherin-adhesion complex, δ-catenin, which in turn causes δ-catenin to traffic toward the synaptic membrane in spines where it associates with and stabilizes surface N-cadherin.
[Show full text]
Ankyrin-G-190 Palmitoylation Mediates Dendrite and Spine Morphogenesis and Is Altered in Response to Lithium
bioRxiv preprint doi: https://doi.org/10.1101/620708; this version posted May 2, 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. Ankyrin-G-190 palmitoylation mediates dendrite and spine morphogenesis and is altered in response to lithium Nicolas H. Piguel, Ph.D. 1,7 Sehyoun Yoon, Ph.D. 1,7 Francesca I. DeSimone, Ph.D. 2 Shaun S. Sanders, Ph.D. 2 Ruoqi Gao, Ph.D. 1 Katherine E. Horan, B.A 1 Leonardo E. Dionisio, B.A 1 , Jacob C. Garza 3 Tracey L. Petryshen, Ph.D.3 Gareth M. Thomas, Ph.D.4 Katharine R. Smith, Ph.D.5 and Peter Penzes, Ph.D.1,6,7* 1 Department of Physiology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611 2 Shriners Hospitals Pediatric Research Center, Lewis Katz School of Medicine at Temple University, Philadelphia, PA 19140 3 Psychiatric and Neurodevelopmental Genetics Unit, Department of Psychiatry and Center for Genomic Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, MA 4 Shriners Hospitals Pediatric Research Center and Department of Anatomy and Cell Biology, Lewis Katz School of Medicine at Temple University, Philadelphia, PA 19140 5 Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045 6 Department of Psychiatry and Behavioral Sciences, Northwestern University Feinberg School of Medicine, Chicago, IL 60611 7 Northwestern University Center for Autism and Neurodevelopment, Chicago, IL 60611 *Corresponding author: Department of Physiology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611; Tel: 312-503-5379; [email protected] bioRxiv preprint doi: https://doi.org/10.1101/620708; this version posted May 2, 2019.
[Show full text]
Mapping Transmembrane Binding Partners for E-Cadherin Ectodomains
SUPPLEMENTARY INFORMATION TITLE: Mapping transmembrane binding partners for E-cadherin ectodomains. AUTHORS: Omer Shafraz 1, Bin Xie 2, Soichiro Yamada 1, Sanjeevi Sivasankar 1, 2, * AFFILIATION: 1 Department of Biomedical Engineering, 2 Biophysics Graduate Group, University of California, Davis, CA 95616. *CORRESPONDING AUTHOR: Sanjeevi Sivasankar, Tel: (530)-754-0840, Email: [email protected] Figure S1: Western blots a. EC-BioID, WT and Ecad-KO cell lysates stained for Ecad and tubulin. b. HRP-streptavidin staining of biotinylated proteins eluted from streptavidin coated magnetic beads incubated with cell lysates of EC-BioID with (+) and without (-) exogenous biotin. c. C-BioID, WT and Ecad-KO cell lysates stained for Ecad and tubulin. d. HRP-streptavidin staining of biotinylated proteins eluted from streptavidin coated magnetic beads incubated with cell lysates of C-BioID with (+) and without (-) exogenous biotin. (+) Biotin (-) Biotin Sample 1 Sample 2 Sample 3 Sample 4 Sample 1 Sample 2 Sample 3 Sample 4 Percent Percent Percent Percent Percent Percent Percent Percent Gene ID Coverage Coverage Coverage Coverage Coverage Coverage Coverage Coverage CDH1 29.6 31.4 41.1 36.5 10.8 6.7 28.8 29.1 DSG2 26 14.6 45 37 0.8 1.9 1.6 18.7 CXADR 30.2 26.2 32.7 27.1 0.0 0.0 0.0 6.9 EFNB1 24.3 30.6 24 30.3 0.0 0.0 0.0 0.0 ITGA2 16.5 22.2 30.1 33.4 1.1 1.1 5.2 7.2 CDH3 21.8 9.7 20.6 25.3 1.3 1.3 0.0 0.0 ITGB1 11.8 16.7 23.9 20.3 0.0 2.9 8.5 5.8 DSC3 9.7 7.5 11.5 13.3 0.0 0.0 2.6 0.0 EPHA2 23.2 31.6 31.6 30.5 0.8 0.0 0.0 5.7 ITGB4 21.8 27.8 33.1 30.7 0.0 1.2 3.9 4.4 ITGB3 23.5 22.2 26.8 24.7 0.0 0.0 5.2 9.1 CDH6 22.8 18.1 28.6 24.3 0.0 0.0 0.0 9.1 CDH17 8.8 12.4 20.7 18.4 0.0 0.0 0.0 0.0 ITGB6 12.7 10.4 14 17.1 0.0 0.0 0.0 1.7 EPHB4 11.4 8.1 14.2 16.3 0.0 0.0 0.0 0.0 ITGB8 5 10 15 17.6 0.0 0.0 0.0 0.0 ITGB5 6.2 9.5 15.2 13.8 0.0 0.0 0.0 0.0 EPHB2 8.5 4.8 9.8 12.1 0.0 0.0 0.0 0.0 CDH24 5.9 7.2 8.3 9 0.0 0.0 0.0 0.0 Table S1: EC-BioID transmembrane protein hits.
[Show full text]
Supplementary Data
Supplemental Material Materials and Methods Immunohistochemistry Primary antibodies used for validation studies include: mouse anti-desmoglein-3 (Cat. # 32-6300, Invitrogen, CA, USA; 1:25), rabbit anti-cytokeratin 4 (Cat. # ab11215, Abcam, Cambridge, MA, USA; 1:100), mouse anti-cytokeratin 16 (Cat. # ab8741, Abcam; 1:25), rabbit anti-desmoplakin antibody (Cat. # ab14418, Abcam; 1:200), mouse anti-vimentin (Cat. # M7020, Dako, Carpinteria, CA, USA; 1:100). Secondary antibodies conjugated with biotin (Vector, Burlingame, CA, USA) were used, diluted to 1:400. Tissues slides containing archival FFPE sections, or tissue micro arrays (TMA) consisting of 508 HNSCC and controls, were dewaxed in SafeClear II (Fisher Scientific, Pittsburgh, PA, USA) hydrated through graded alcohols, immersed in 3% hydrogen peroxide in PBS for 30 min to quench the endogenous peroxidase, and processed for antigen retrieval and immunostaining with the appropriate primary antibodies and biotinylated secondary antibodies as described (1), followed by the avidin-biotin complex method (Vector Stain Elite, ABC kit; Vector). Slides were washed and developed in 3,3'- diaminobenzidine (Sigma FASTDAB tablet; Sigma Chemical) under microscopic control, and counterstained with Mayer's hematoxylin. For each stained TMA the number of positive cells in each core was visually evaluated and the results expressed as a percentage of stained cells/ total number of cells. According to their immunoreactivity the tissues array cores were divided according to tumor differentiation, where the percentage of stained cells in the three tumor classes were scored as more than 5% and less than 25% of the cells stained, 26 to 50%, 51 to 75% or, 75 to 100%.
[Show full text]
Diverse Functions of P120ctn in Tumors ⁎ Jolanda Van Hengel, Frans Van Roy
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Biochimica et Biophysica Acta 1773 (2007) 78–88 www.elsevier.com/locate/bbamcr Review Diverse functions of p120ctn in tumors ⁎ Jolanda van Hengel, Frans van Roy Molecular Cell Biology Unit, Department for Molecular Biomedical Research, VIB-Ghent University, Technologiepark 927, B-9052 Gent (Zwijnaarde), Belgium Received 31 May 2006; received in revised form 22 August 2006; accepted 23 August 2006 Available online 30 August 2006 Abstract p120ctn is a member of the Armadillo protein family. It stabilizes the cadherin–catenin adhesion complex at the plasma membrane, but also has additional roles in the cytoplasm and nucleus. Extensive alternative mRNA splicing and multiple phosphorylation sites generate additional complexity. Evidence is emerging that complete loss, downregulation or mislocalization of p120ctn correlates with progression of different types of human tumors. It remains to be determined whether a causal relationship exists between specific isoform expression, subcellular localization or selective phosphorylation of p120ctn on the one hand and tumor prognosis on the other. © 2006 Elsevier B.V. All rights reserved. Keywords: Cancer progression; EMT; Cell–cell adhesion; Armadillo; Catenin; Cadherin; Rho GTPase 1. Introduction: cadherins and catenins in cancer metastatic development must be followed by a reverse process, MET, at the site of secondary sites [12]. For instance, E-cadherin Cell–cell interactions, which are mediated by adhesion mole- expression is dynamically and reversibly modulated during cules, play vital roles in developmental morphogenesis, tissue progression of ductal breast carcinoma [13]. Reduced E-cadherin remodeling and carcinogenesis.
[Show full text]