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Nuclear Matrix
Nuclear matrix, nuclear envelope and premature aging syndromes in a translational research perspective Pierre Cau, Claire Navarro, Karim Harhouri, Patrice Roll, Sabine Sigaudy, Elise Kaspi, Sophie Perrin, Annachiara de Sandre-Giovannoli, Nicolas Lévy To cite this version: Pierre Cau, Claire Navarro, Karim Harhouri, Patrice Roll, Sabine Sigaudy, et al.. Nuclear matrix, nuclear envelope and premature aging syndromes in a translational research perspective. Seminars in Cell and Developmental Biology, Elsevier, 2014, 29, pp.125-147. 10.1016/j.semcdb.2014.03.021. hal-01646524 HAL Id: hal-01646524 https://hal-amu.archives-ouvertes.fr/hal-01646524 Submitted on 20 Dec 2017 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Review Nuclear matrix, nuclear envelope and premature aging syndromes in a translational research perspective Pierre Cau a,b,c,∗, Claire Navarro a,b,1, Karim Harhouri a,b,1, Patrice Roll a,b,c,1,2, Sabine Sigaudy a,b,d,1,3, Elise Kaspi a,b,c,1,2, Sophie Perrin a,b,1, Annachiara De Sandre-Giovannoli a,b,d,1,3, Nicolas Lévy a,b,d,∗∗ a Aix-Marseille -
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The functional role(s) of dual intermediate filament expression in tumor cell migration and invasion. Item Type text; Dissertation-Reproduction (electronic) Authors Chu, Yi-Wen. Publisher The University of Arizona. Rights Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. Download date 02/10/2021 04:10:29 Link to Item http://hdl.handle.net/10150/186143 INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleed through, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand corner and continuing from left to right in equal sections with small overlaps. Each original is also photographed in one exposure and is included in reduced form at the back of the book. -
Lamin B2 Follows Lamin A/C- Mediated Nuclear Mechanics and Cancer Cell Invasion Efficacy
bioRxiv preprint doi: https://doi.org/10.1101/2020.04.07.028969; this version posted April 8, 2020. 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. Lamin B2 follows lamin A/C- mediated nuclear mechanics and cancer cell invasion efficacy Short running title: Nuclear lamins in tumor cell migration Marina Vortmeyer-Krause1†, Mariska te Lindert1†, Joost te Riet2†, Veronika te Boekhorst1†, Rene Marke1, Ramanil Perera1, Philipp Isermann3, Tom van Oorschot1, Monika Zwerger3, Fengwei Yang4, Martin Svoreň1, Anotida Madzvamuse 4, Jan Lammerding3, Peter Friedl1,5,6, Katarina Wolf1* †These authors contributed equally to this work. * Correspondence to: [email protected] *Address of corresponding author: Department of Cell Biology (route 283), Radboud University Medical Center, PO Box 9101, 6500 HB Nijmegen, The Netherlands; [email protected]; Orcid: http://orcid.org/0000-0003-0616-2708 Affiliations 1 Radboud University Medical Center, Department of Cell Biology, 6500 HB Nijmegen, The Netherlands 2 Radboud University Medical Center, Department of Tumor Immunology, 6500 HB Nijmegen, The Netherlands 3 Weill Institute for Cell and Molecular Biology, Meinig School of Biomedical Engineering Cornell University, Ithaca, NY 14853; USA 4 School of Mathematical and Physical Sciences, University of Sussex, Department of Mathematics, BN1 9QH, Falmer, Brighton, United Kingdom 5 David H. Koch Center for Applied Research of Genitourinary Cancers, Department of Genitourinary Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA 6 Cancer Genomics Center, 3584 CG Utrecht, The Netherlands 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.04.07.028969; this version posted April 8, 2020. -
Deficiencies in Lamin B1 and Lamin B2 Cause Neurodevelopmental Defects and Distinct Nuclear Shape Abnormalities in Neurons
M BoC | ARTICLE Deficiencies in lamin B1 and lamin B2 cause neurodevelopmental defects and distinct nuclear shape abnormalities in neurons Catherine Coffiniera, Hea-Jin Jungb, Chika Nobumoria, Sandy Changa, Yiping Tua, Richard H. Barnes IIa, Yuko Yoshinagac, Pieter J. de Jongc, Laurent Vergnesd, Karen Reued, Loren G. Fonga, and Stephen G. Younga,d aDepartment of Medicine and bMolecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095; cChildren’s Hospital Oakland Research Institute, Oakland, CA 94609; dDepartment of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095 ABSTRACT Neuronal migration is essential for the development of the mammalian brain. Monitoring Editor Here, we document severe defects in neuronal migration and reduced numbers of neurons in Thomas Michael Magin lamin B1–deficient mice. Lamin B1 deficiency resulted in striking abnormalities in the nuclear University of Leipzig shape of cortical neurons; many neurons contained a solitary nuclear bleb and exhibited an Received: Jun 13, 2011 asymmetric distribution of lamin B2. In contrast, lamin B2 deficiency led to increased numbers Revised: Sep 9, 2011 of neurons with elongated nuclei. We used conditional alleles for Lmnb1 and Lmnb2 to create Accepted: Sep 23, 2011 forebrain-specific knockout mice. The forebrain-specificLmnb1- and Lmnb2-knockout models had a small forebrain with disorganized layering of neurons and nuclear shape abnormalities, similar to abnormalities identified in the conventional knockout mice. A more severe pheno- type, complete atrophy of the cortex, was observed in forebrain-specific Lmnb1/Lmnb2 double-knockout mice. This study demonstrates that both lamin B1 and lamin B2 are essential for brain development, with lamin B1 being required for the integrity of the nuclear lamina, and lamin B2 being important for resistance to nuclear elongation in neurons. -
Proteomic Expression Profile in Human Temporomandibular Joint
diagnostics Article Proteomic Expression Profile in Human Temporomandibular Joint Dysfunction Andrea Duarte Doetzer 1,*, Roberto Hirochi Herai 1 , Marília Afonso Rabelo Buzalaf 2 and Paula Cristina Trevilatto 1 1 Graduate Program in Health Sciences, School of Medicine, Pontifícia Universidade Católica do Paraná (PUCPR), Curitiba 80215-901, Brazil; [email protected] (R.H.H.); [email protected] (P.C.T.) 2 Department of Biological Sciences, Bauru School of Dentistry, University of São Paulo, Bauru 17012-901, Brazil; [email protected] * Correspondence: [email protected]; Tel.: +55-41-991-864-747 Abstract: Temporomandibular joint dysfunction (TMD) is a multifactorial condition that impairs human’s health and quality of life. Its etiology is still a challenge due to its complex development and the great number of different conditions it comprises. One of the most common forms of TMD is anterior disc displacement without reduction (DDWoR) and other TMDs with distinct origins are condylar hyperplasia (CH) and mandibular dislocation (MD). Thus, the aim of this study is to identify the protein expression profile of synovial fluid and the temporomandibular joint disc of patients diagnosed with DDWoR, CH and MD. Synovial fluid and a fraction of the temporomandibular joint disc were collected from nine patients diagnosed with DDWoR (n = 3), CH (n = 4) and MD (n = 2). Samples were subjected to label-free nLC-MS/MS for proteomic data extraction, and then bioinformatics analysis were conducted for protein identification and functional annotation. The three Citation: Doetzer, A.D.; Herai, R.H.; TMD conditions showed different protein expression profiles, and novel proteins were identified Buzalaf, M.A.R.; Trevilatto, P.C. -
Irreversible Modifications of Chromatin and the Nuclear Lamina: a Review Inside the Nuclear Origin of Alzheimer's Disease
Revista Mexicana de Neurociencia REVIEW ARTICLE Irreversible modifications of chromatin and the nuclear lamina: A review inside the nuclear origin of Alzheimer’s disease Laura Gil1¶, Gabriela Capdeville2*¶, Ildefonso Rodríguez-Leyva3, Sandra A. Niño4, and María E. Jiménez-Capdeville4 1Departamento de Genética, Escuela de Medicina, Universidad “Alfonso X el Sabio”, Madrid, España; 2Escuela de Medicina, Universidad Panamericana, Mexico City; 3Servicio de Neurología, Hospital Central “Ignacio Morones Prieto”, San Luis Potosí; 4Departamento de Bioquímica, Facultad de Medicina, Universidad Autónoma de San Luis Potosí, San Luis Potosí, Mexico ¶These authors contributed equally in this study. Abstract Dementia is a public health problem with an extraordinary increase in recent years. Alzheimer’s disease (AD) is the most common cause of dementia. This disease has been considered a consequence of cytoplasmic and extracellular accumula- tions of Tau protein and β- amyloid, respectively. Nevertheless, a nuclear origin of AD has recently emerged. Both Tau protein and the nuclear lamin protect the nuclear and chromatin organization for proper gene expression throughout neuronal life. Accumulation of DNA damage, mainly as a result of aging, drives post-mitotic neurons to initiate DNA repair by entering the cell cycle. The complexity of the nucleus-cytoskeleton prevents neurons from dividing and condemns them to a state of hyperdiploidy ending in neuronal death, after transiently prolonging their life. In AD, hippocampal neurons survive their fatal fate by triggering an aberrant structural and functional transformation of the nucleus. Lamin A expression and Tau protein transfer to the cytoplasm results in loss of the protector role of nuclear Tau and the subsequent global chromatin disorgani- zation. -
Nuclear Envelope Protein MAN1 Regulates Clock Through BMAL1
RESEARCH ARTICLE elifesciences.org Nuclear envelope protein MAN1 regulates clock through BMAL1 Shu-Ting Lin1†, Luoying Zhang1†, Xiaoyan Lin1†‡, Linda Chen Zhang1, Valentina Elizabeth Garcia1, Chen-Wei Tsai1, Louis Ptáček1,2, Ying-Hui Fu1* 1Department of Neurology, University of California, San Francisco, San Francisco, United States; 2Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, United States Abstract Circadian clocks serve as internal pacemakers that influence many basic homeostatic processes; consequently, the expression and function of their components are tightly regulated by intricate networks of feedback loops that fine-tune circadian processes. Our knowledge of these components and pathways is far from exhaustive. In recent decades, the nuclear envelope has emerged as a global gene regulatory machine, although its role in circadian regulation has not been explored. We report that transcription of the core clock component BMAL1 is positively modulated by the inner nuclear membrane protein MAN1, which directly binds the BMAL1 promoter and enhances its transcription. Our results establish a novel connection between the nuclear periphery and circadian rhythmicity, therefore bridging two global regulatory systems that modulate all aspects of bodily functions. DOI: 10.7554/eLife.02981.001 *For correspondence: ying-hui. [email protected] Introduction † These authors contributed Most organisms, ranging from cyanobacteria to humans, are governed by their circadian rhythms: equally to this work endogenous and self-sustained oscillations with a period of roughly 24 hr, which manifest in diverse Present address: ‡Neurogenetics metabolic, physiological, and behavioral processes (Ueda et al., 2005). This internal pacemaker is Branch, National Institute of charged with two important roles: to perpetuate its own rhythms and to regulate the expression of Neurological Disorders and genes that are under circadian control. -
Akt1-Associated Actomyosin Remodelling Is Required for Nuclear Lamina Dispersal and Nuclear Shrinkage in Epidermal Terminal Differentiation
bioRxiv preprint doi: https://doi.org/10.1101/868034; this version posted December 8, 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. Akt1-associated actomyosin remodelling is required for nuclear lamina dispersal and nuclear shrinkage in epidermal terminal differentiation Clare Rogerson1, Duncan Wotherspoon1, Ryan F L O’Shaughnessy1* 1 Centre for Cell Biology and Cutaneous Research, Blizard Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, London, UK *Corresponding author: Ryan O’Shaughnessy Centre for Cell Biology and Cutaneous Research, Blizard Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, London E1 2AT, UK [email protected] Abstract Keratinocyte cornification and epidermal barrier formation are tightly controlled processes, which require complete degradation of intracellular organelles, including removal of keratinocyte nuclei. Keratinocyte nuclear destruction requires Akt1-dependent phosphorylation and degradation of the nuclear lamina protein, Lamin A/C, essential for nuclear integrity. However, the molecular mechanisms that result in complete nuclear removal and their regulation are not well defined. Post-confluent cultures of rat epidermal keratinocytes (REKs) undergo spontaneous and complete differentiation, allowing visualisation and perturbation of the differentiation process in vitro. We demonstrate that there is dispersal of phosphorylated Lamin A/C to structures throughout the cytoplasm in differentiating keratinocytes. We show that the dispersal of phosphorylated Lamin A/C is Akt1-dependent and these structures are specific for the removal of Lamin A/C from the nuclear lamina; nuclear contents and Lamin B were not present in these structures. -
Keratin Remodelling in Stress Tan Tong San National
KERATIN REMODELLING IN STRESS TAN TONG SAN NATIONAL UNIVERSITY OF SINGAPORE 2012 i KERATIN REMODELLING IN STRESS TAN TONG SAN (B. Sc. (Hons.), NUS) A THESIS SUBMITTED FOR THE DEGREE OF DOCTOR OF PHILOSOPHY NUS Graduate School for Integrative Sciences and Engineering NATIONAL UNIVERSITY OF SINGAPORE 2012 ii iii ACKNOWLEDGEMENTS I would like to express my deepest gratitude to my supervisor, Prof. Birgit Lane, for her guidance and mentorship, and for giving me the opportunity, independence and resources to conduct my research. Her depth of knowledge and passion for scientific discovery have been a great source of inspiration and motivation for me throughout these four years of PhD endeavour, and will continue to be in the future. I would also like to thank my thesis advisory committee, Prof. Michael Raghunath and A/Prof. Edward Manser, for their critical feedback along the way. My sincere thanks and appreciation also go to John Common, for his insightful comments and suggestions throughout the course of this project. I would also like to acknowledge Ildiko for initiating the keratin phosphorylation project. Special thanks also go to Cedric, Chida, Darren, Gopi, Nama, John Lim, Delina, Chye Ling, Huijia and Declan, for their help in research techniques. I am most fortunate to be part of the EBL lab, a stimulating and lively place to work in. Thanks go to Kenneth, Zhou Fan, Paula, Chai Ling, Christine, Yi Zhen, Rosita, Vivien and Giorgiana, fellow students who join me in the pursuit of a doctorate. Appreciation is also extended to Iskandar, Jun Xian, Carol, Anita, Yi Ling, Ting Ting and other lab members for their support and help. -
Lamin B1 Is Required for Mature Neuron-Specific Gene Expression
ARTICLE Received 4 Jul 2016 | Accepted 28 Feb 2017 | Published 20 Apr 2017 DOI: 10.1038/ncomms15098 OPEN Lamin B1 is required for mature neuron-specific gene expression during olfactory sensory neuron differentiation Crystal M. Gigante1,2, Michele Dibattista3,4, Frederick N. Dong1, Xiaobin Zheng2, Sibiao Yue2, Stephen G. Young5, Johannes Reisert3, Yixian Zheng2 & Haiqing Zhao1 B-type lamins are major constituents of the nuclear lamina in all metazoan cells, yet have specific roles in the development of certain cell types. Although they are speculated to regulate gene expression in developmental contexts, a direct link between B-type lamins and developmental gene expression in an in vivo system is currently lacking. Here, we identify lamin B1 as a key regulator of gene expression required for the formation of functional olfactory sensory neurons. By using targeted knockout in olfactory epithelial stem cells in adult mice, we show that lamin B1 deficient neurons exhibit attenuated response to odour stimulation. This deficit can be explained by decreased expression of genes involved in mature neuron function, along with increased expression of genes atypical of the olfactory lineage. These results support that the broadly expressed lamin B1 regulates expression of a subset of genes involved in the differentiation of a specific cell type. 1 Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218, USA. 2 Department of Embryology, Carnegie Institution for Science, Baltimore, Maryland 21218, USA. 3 Monell Chemical Senses Center, Philadelphia, Pennsylvania 19104, USA. 4 Department of Basic Medical Sciences, Neuroscience and Sensory Organs, University of Bari ‘A. Moro’, Bari 70121, Italy. 5 Department of Medicine, Molecular Biology Institute and Department of Human Genetics, University of California, Los Angeles, California 90095, USA. -
Proteomic Analysis Identifies Oxidative Stress Induction by Adaphostin Luke H
Cancer Therapy: Preclinical Proteomic Analysis Identifies Oxidative Stress Induction by Adaphostin Luke H. Stockwin,1Maja A. Bumke,1Sherry X. Yu,1Simon P. Webb,2 Jack R. Collins,2 Melinda G. Hollingshead,3 and Dianne L. Newton1 Abstract Purpose: Activities distinct from inhibition of Bcr/abl have led to adaphostin (NSC 680410) being described as ‘‘a drug in search of a mechanism.’’ In this study, proteomic analysis of adaphostin- treated myeloid leukemia cell lines was used to further elucidate a mechanism of action. Experimental Design: HL60 and K562 cells treated with adaphostin for 6, 12, or 24 h were analyzed using two-dimensional PAGE. Differentially expressed spots were excised, digested with trypsin, and analyzed by liquid chromatography ^ tandem mass spectrometry.The contribu- tion of the redox-active hydroquinone group in adaphostin was also examined by carrying out proteomic analysis of HL60 cells treated with a simple hydroquinone (1,4-dihydroxybenzene) or H2O2. Results: Analysis of adaphostin-treated cells identified 49 differentially expressed proteins, the majority being implicated in the response to oxidative stress (e.g., CALM, ERP29, GSTP1,PDIA1) or induction of apoptosis (e.g., LAMA, FLNA, TPR, GDIS). Interestingly, modulation of these proteins was almost fully prevented by inclusion of an antioxidant, N-acetylcysteine. Validation of the proteomic data confirmed GSTP1as an adaphostin resistance gene. Subsequent analysis of HL60 cells treated with1,4-dihydroxybenzene or H2O2 showed similar increases in intracellular peroxides and an almost identical proteomic profiles to that of adaphostin treatment. Western blotting of a panel of cell lines identified Cu/Zn superoxide dismutase (SOD) as correlating with adaphostin resistance. -
Proquest Dissertations
NOTE TO USERS This reproduction is the best copy available. UMI' nm u Ottawa L'Universite canadienne Canada's university TTTTT FACULTE DES ETUDES SUPERIEURES l^s FACULTY OF GRADUATE AND ET POSTOCTORALES u Ottawa POSDOCTORAL STUDIES L'Universite canadienne Canada's university Elmira Ahmady AUTEUR DE LA THESE / AUTHOR OF THESIS M.Sc. (Biochemistry) GRADE/DEGREE Department of Biochemistry, Microbiology and Immunology FACiX7E7EcaE7b^ The Functional Role of A-type Lamin Interacting Transcription Factor (LITF) During Skeletal Myogenesis TITRE DE LA THESE / TITLE OF THESIS Patrick Burgon ._____._______^ Bernard Jasmin Robin Parks Gary W. Slater Le Doyen de la Faculte des etudes superieures et postdoctorales / Dean of the Faculty of Graduate and Postdoctoral Studies The Functional Role of A-type Lamin Interacting Transcription Factor (LITF) during Skeletal Myogenesis Elmira Ahmady, BSc. Thesis submitted to the Faculty of Graduate and Postdoctoral Studies, in partial fulfillment of the requirements for the M.Sc. degree in Biochemistry Department of Biochemistry, Microbiology and Immunology Faculty of Medicine University of Ottawa © Elmira Ahmady, Ottawa, Canada, 2009 Library and Archives Bibliotheque et 1*1 Canada Archives Canada Published Heritage Direction du Branch Patrimoine de I'edition 395 Wellington Street 395, rue Wellington Ottawa ON K1A0N4 OttawaONK1A0N4 Canada Canada Your file Votre reference ISBN: 978-0-494-65551-1 Our file Notre reference ISBN: 978-0-494-65551-1 NOTICE: AVIS: The author has granted a non L'auteur a accorde une licence