Integrin Expression in the Mouse Vestibular System
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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. -
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. -
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, -
Integrin Alpha 2 Antibody
Product Datasheet Integrin alpha 2 Antibody Catalog No: #49071 Package Size: #49071-1 50ul #49071-2 100ul Orders: [email protected] Support: [email protected] Description Product Name Integrin alpha 2 Antibody Host Species Rabbit Clonality Monoclonal Clone No. SN0752 Purification ProA affinity purified Applications WB, ICC/IF, IHC, IP, FC Species Reactivity Hu, Ms, Rt Immunogen Description recombinant protein Other Names BR antibody CD 49b antibody CD49 antigen like family member B antibody CD49 antigen-like family member B antibody CD49b antibody CD49b antigen antibody Collagen receptor antibody DX5 antibody Glycoprotein Ia deficiency included antibody GP Ia antibody GP Ia deficiency, included antibody GPIa antibody HPA 5 included antibody HPA5 included antibody Human platelet alloantigen system 5 antibody Integrin alpha 2 antibody Integrin alpha-2 antibody Integrin, alpha 2 (CD49B alpha 2 subunit of VLA 2 receptor) antibody ITA2_HUMAN antibody ITGA2 antibody Platelet alloantigen Br(a), included antibody Platelet antigen Br antibody Platelet glycoprotein GPIa antibody Platelet glycoprotein Ia antibody Platelet glycoprotein Ia/IIa antibody Platelet membrane glycoprotein Ia antibody Platelet receptor for collagen, deficiency of, included antibody Very late activation protein 2 receptor alpha 2 subunit antibody VLA 2 alpha chain antibody VLA 2 antibody VLA 2 subunit alpha antibody VLA-2 subunit alpha antibody VLA2 antibody VLA2 receptor alpha 2 subunit antibody VLAA2 antibody Accession No. Swiss-Prot#:P17301 Calculated MW 150 kDa Formulation 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide. Storage Store at -20°C Application Details WB: 1:1,000-5,000 IHC: 1:50-1:200 ICC: 1:100-1:500 FC: 1:50-1:100 Images Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 1 Western blot analysis of ITGA2 on A431 cells lysates using anti-ITGA2 antibody at 1/1,000 dilution. -
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. -
Integrins: Roles in Cancer Development and As Treatment Targets
British Journal of Cancer (2004) 90, 561 – 565 & 2004 Cancer Research UK All rights reserved 0007 – 0920/04 $25.00 www.bjcancer.com Minireview Integrins: roles in cancer development and as treatment targets 1 ,1,2 H Jin and J Varner* 1John and Rebecca Moores Comprehensive Cancer Center, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0912, USA; 2Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0912, USA The integrin family of cell adhesion proteins promotes the attachment and migration of cells on the surrounding extracellular matrix (ECM). Through signals transduced upon integrin ligation by ECM proteins or immunoglobulin superfamily molecules, this family of proteins plays key roles in regulating tumour growth and metastasis as well as tumour angiogenesis. Several integrins play key roles in promoting tumour angiogenesis and tumour metastasis. Antagonists of several integrins (a5b1, avb3 and avb5) are now under evaluation in clinical trials to determine their potential as therapeutics for cancer and other diseases. British Journal of Cancer (2004) 90, 561 – 565. doi:10.1038/sj.bjc.6601576 www.bjcancer.com & 2004 Cancer Research UK Keywords: angiogenesis; metastasis; apoptosis; integrin a5b1; integrin avb3 During the last 10 years, novel insights into the mechanisms sequences (e.g., integrin a4b1 recognises EILDV and REDV in that regulate cell survival as well as cell migration and invasion alternatively spliced CS-1 fibronectin). Inhibitors of integrin have led to the development of novel integrin-based therapeutics function include function-blocking monoclonal antibodies, pep- for the treatment of cancer. Several integrins play important tide antagonists and small molecule peptide mimetics matrix roles in promoting cell proliferation, migration and survival (reviewed in Hynes, 1992; Cheresh, 1993). -
Cell Adhesion and Angiogenesis
Cell adhesion and angiogenesis. J Bischoff J Clin Invest. 1997;99(3):373-376. https://doi.org/10.1172/JCI119168. Perspective Find the latest version: https://jci.me/119168/pdf Perspectives Series: Cell Adhesion in Vascular Biology Cell Adhesion and Angiogenesis Joyce Bischoff Department of Surgery, Children’s Hospital and Harvard Medical School, Children’s Hospital, Boston, Massachusetts 02115 Introduction and postcapillary venules (3). Thus, the formation of a new mi- Angiogenesis is the growth of new capillary blood vessels from crovessel requires a number of interactions that must be coor- preexisting capillaries and postcapillary venules. This process dinated in a spatially and temporally specified manner. These is critical for normal growth and development and in protec- adhesion events are likely mediated by endothelial cell adhe- tive responses such as wound healing and inflammation. In sion molecules and ECM molecules that provide instructions healthy adults, angiogenesis does not normally occur except in to the endothelial cells as they migrate into the perivascular certain phases of the female reproductive cycle. However, ab- space and assemble into new vessels with surrounding peri- errant angiogenesis can occur in a variety of pathologic set- cytes. tings. These include the neovascularization of solid tumors, the Cell adhesion and endothelial cell growth growth of vessels into the retina in diabetic retinopathy, and the unwanted vessel growth in chronic inflammatory diseases. Adhesion of endothelial cells to ECM and attainment of an The hypothesis that angiogenic diseases, in particular tumor appropriate cellular shape has been known for many years to growth and metastases, may be alleviated by inhibiting the an- be crucial for endothelial cell growth, differentiation, and sur- giogenic responses (1) has prompted many to investigate the vival. -
Integrin Α2β1 in Nonactivated Conformation Can Induce Focal
www.nature.com/scientificreports OPEN Integrin α2β1 in nonactivated conformation can induce focal adhesion kinase signaling Received: 17 February 2017 Maria Salmela1, Johanna Jokinen1,2, Silja Tiitta1, Pekka Rappu1, R. Holland Cheng 2 & Jyrki Accepted: 2 May 2017 Heino1 Published: xx xx xxxx Conformational activation of integrins is generally required for ligand binding and cellular signalling. However, we have previously reported that the nonactivated conformation of α2β1 integrin can also bind to large ligands, such as human echovirus 1. In this study, we show that the interaction between the nonactivated integrin and a ligand resulted in the activation of focal adhesion kinase (FAK) in a protein kinase C dependent manner. A loss-of-function mutation, α2E336A, in the α2-integrin did not prevent the activation of FAK, nor did EDTA-mediated inactivation of the integrin. Full FAK activation was observed, since phosphorylation was not only confirmed in residue Y397, but also in residues Y576/7. Furthermore, initiation of downstream signaling by paxillin phosphorylation in residue Y118 was evident, even though this activation was transient by nature, probably due to the lack of talin involvement in FAK activation and the absence of vinculin in the adhesion complexes formed by the nonactivated integrins. Altogether these results indicate that the nonactivated integrins can induce cellular signaling, but the outcome of the signaling differs from conventional integrin signaling. The well-established model of integrin function stresses the importance of the conformational change from a nonactivated, bent conformation to an active, extended state prior to ligand binding and outside-in signaling1. Despite the fact that the conformational activation of integrins is often required for ligand binding, nonactivated integrins may have specific biological functions as well. -
Laminin-Binding Integrin A7,1: Functional Characterization and Expression in Normal and Malignant Melanocytes
CELL REGULATION, Vol. 2, 805-817, October 1991 Laminin-binding integrin a7,1: functional characterization and expression in normal and malignant melanocytes Randall H. Kramer,*t$ Mai P. Vu,* increased attachment to laminin exhibit much Yao-Fen Cheng,* Daniel M. Ramos,* higher metastatic potential in lung colonization Rupert Timpl,§ and Nahid Waleh 11 assays (reviewed in Liotta et aL, 1986). Fur- *Departments of Stomatology and Anatomy thermore, the presence of intact laminin will en- and the tCardiovascular Research Institute hance lung colonization (Barsky et aL., 1984). University of California These results and others strongly suggest that San Francisco, California 94143 melanoma cells interact with laminin-rich base- §Max-Planck-lnstitut fur Biochemie ment membrane and that this interaction facil- Martinsried, Germany itates their vascular arrest and colonization of IISRI International distant sites. Menlo Park, California 94025 During tissue invasion, metastatic melanoma cells interact with different types of extracellular matrix, including the interstitium and basement A novel integrin, a,#,, that specifically binds with membranes. It is expected, then, that these high affinity to laminin has been identified on mel- malignant cells will express surface adhesion anoma cells. This complex was purified from both receptors with diverse ligand specificities human and murine melanoma cells by laminin-af- (Ruoslahti and Giancotti, 1989). The integrin finity chromatography, and the a7 subunit was re- family of adhesion receptors consists of a large covered after gel electrophoresis. N-terminal amino number of heterodimer receptors that appear acid sequence analysis of the a7 subunit from both to mediate many of the cell-extracellular matrix human and mouse cells verifies that this integrin interactions for melanoma and other cell types is distinct from other a chains in the #I family, al- (Hynes, 1987; Ruoslahti and Pierschbacher, though strikingly similar to the as subunit. -
Integrin Activity 7Β , and 3Β , 2 Β Chemoattractant-Stimulated Differential Regulation Of
Differential Regulation of Chemoattractant-Stimulated β2, β3, and β7 Integrin Activity This information is current as Chanchal Sadhu, Boris Masinovsky and Donald E. Staunton of September 26, 2021. J Immunol 1998; 160:5622-5628; ; http://www.jimmunol.org/content/160/11/5622 Downloaded from References This article cites 24 articles, 11 of which you can access for free at: http://www.jimmunol.org/content/160/11/5622.full#ref-list-1 Why The JI? Submit online. http://www.jimmunol.org/ • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average by guest on September 26, 2021 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 © 1998 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. b b Differential Regulation of Chemoattractant-Stimulated 2, 3, b and 7 Integrin Activity Chanchal Sadhu,1 Boris Masinovsky, and Donald E. Staunton Leukocyte adhesion to endothelium and extravasation are dynamic processes that require activation of integrins. Chemoattrac- tants such as IL-8 and FMLP are potent activators of leukocyte integrins. To compare the chemoattractant-stimulated activation a b a b a b of three integrins, 4 7, L 2, and V 3, in the same cellular context, we expressed an IL-8 receptor (IL-8RA) and FMLP receptor a b a b (FPR) in the lymphoid cell line JY. -