Mirna and Parkinson's Disease Protein PARK2
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Deregulated Gene Expression Pathways in Myelodysplastic Syndrome Hematopoietic Stem Cells
Leukemia (2010) 24, 756–764 & 2010 Macmillan Publishers Limited All rights reserved 0887-6924/10 $32.00 www.nature.com/leu ORIGINAL ARTICLE Deregulated gene expression pathways in myelodysplastic syndrome hematopoietic stem cells A Pellagatti1, M Cazzola2, A Giagounidis3, J Perry1, L Malcovati2, MG Della Porta2,MJa¨dersten4, S Killick5, A Verma6, CJ Norbury7, E Hellstro¨m-Lindberg4, JS Wainscoat1 and J Boultwood1 1LRF Molecular Haematology Unit, NDCLS, John Radcliffe Hospital, Oxford, UK; 2Department of Hematology Oncology, University of Pavia Medical School, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy; 3Medizinische Klinik II, St Johannes Hospital, Duisburg, Germany; 4Division of Hematology, Department of Medicine, Karolinska Institutet, Stockholm, Sweden; 5Department of Haematology, Royal Bournemouth Hospital, Bournemouth, UK; 6Albert Einstein College of Medicine, Bronx, NY, USA and 7Sir William Dunn School of Pathology, University of Oxford, Oxford, UK To gain insight into the molecular pathogenesis of the the World Health Organization.6,7 Patients with refractory myelodysplastic syndromes (MDS), we performed global gene anemia (RA) with or without ringed sideroblasts, according to expression profiling and pathway analysis on the hemato- poietic stem cells (HSC) of 183 MDS patients as compared with the the French–American–British classification, were subdivided HSC of 17 healthy controls. The most significantly deregulated based on the presence or absence of multilineage dysplasia. In pathways in MDS include interferon signaling, thrombopoietin addition, patients with RA with excess blasts (RAEB) were signaling and the Wnt pathways. Among the most signifi- subdivided into two categories, RAEB1 and RAEB2, based on the cantly deregulated gene pathways in early MDS are immuno- percentage of bone marrow blasts. -
Parkin Antibody (C-Term) Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP6402B
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 Parkin Antibody (C-term) Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP6402B Specification Parkin Antibody (C-term) - Product Information Application IF, WB, IHC-P, FC,E Primary Accession O60260 Other Accession NP_004553 Reactivity Human, Mouse Host Rabbit Clonality Polyclonal Isotype Rabbit Ig Antigen Region 387-417 Parkin Antibody (C-term) - Additional Information Gene ID 5071 Other Names E3 ubiquitin-protein ligase parkin, 632-, Confocal immunofluorescent analysis of Parkinson juvenile disease protein 2, Parkin Antibody (C-term)(Cat#AP6402b) with Parkinson disease protein 2, PARK2, PRKN NCI-H460 cell followed by Alexa Fluor 488-conjugated goat anti-rabbit lgG Target/Specificity (green).Actin filaments have been labeled This Parkin antibody is generated from with Alexa Fluor 555 phalloidin (red).DAPI rabbits immunized with a KLH conjugated was used to stain the cell nuclear (blue). synthetic peptide between 387-417 amino acids from the C-terminal region of human Parkin. Dilution IF~~1:10~50 WB~~1:1000 IHC-P~~1:50~100 FC~~1:10~50 Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. Storage Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C Park2 Antibody (C-term) (Cat. #AP6402b) in small aliquots to prevent freeze-thaw western blot analysis in K562 cell line lysates cycles. (35ug/lane).This demonstrates the Park2 antibody detected the Park2 protein (arrow). -
Defining Functional Interactions During Biogenesis of Epithelial Junctions
ARTICLE Received 11 Dec 2015 | Accepted 13 Oct 2016 | Published 6 Dec 2016 | Updated 5 Jan 2017 DOI: 10.1038/ncomms13542 OPEN Defining functional interactions during biogenesis of epithelial junctions J.C. Erasmus1,*, S. Bruche1,*,w, L. Pizarro1,2,*, N. Maimari1,3,*, T. Poggioli1,w, C. Tomlinson4,J.Lees5, I. Zalivina1,w, A. Wheeler1,w, A. Alberts6, A. Russo2 & V.M.M. Braga1 In spite of extensive recent progress, a comprehensive understanding of how actin cytoskeleton remodelling supports stable junctions remains to be established. Here we design a platform that integrates actin functions with optimized phenotypic clustering and identify new cytoskeletal proteins, their functional hierarchy and pathways that modulate E-cadherin adhesion. Depletion of EEF1A, an actin bundling protein, increases E-cadherin levels at junctions without a corresponding reinforcement of cell–cell contacts. This unexpected result reflects a more dynamic and mobile junctional actin in EEF1A-depleted cells. A partner for EEF1A in cadherin contact maintenance is the formin DIAPH2, which interacts with EEF1A. In contrast, depletion of either the endocytic regulator TRIP10 or the Rho GTPase activator VAV2 reduces E-cadherin levels at junctions. TRIP10 binds to and requires VAV2 function for its junctional localization. Overall, we present new conceptual insights on junction stabilization, which integrate known and novel pathways with impact for epithelial morphogenesis, homeostasis and diseases. 1 National Heart and Lung Institute, Faculty of Medicine, Imperial College London, London SW7 2AZ, UK. 2 Computing Department, Imperial College London, London SW7 2AZ, UK. 3 Bioengineering Department, Faculty of Engineering, Imperial College London, London SW7 2AZ, UK. 4 Department of Surgery & Cancer, Faculty of Medicine, Imperial College London, London SW7 2AZ, UK. -
Diminished Dosage of 22Q11 Genes Disrupts Neurogenesis and Cortical Development in a Mouse Model of 22Q11 Deletion/Digeorge Syndrome
Diminished dosage of 22q11 genes disrupts neurogenesis and cortical development in a mouse model of 22q11 deletion/DiGeorge syndrome Daniel W. Meechana, Eric S. Tuckera, Thomas M. Maynarda, and Anthony-Samuel LaMantiaa,b,1 aDepartment of Cell and Molecular Physiology and bNeuroscience Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599 Edited by Pasko Rakic, Yale University School of Medicine, New Haven, CT, and approved July 22, 2009 (received for review May 28, 2009) The 22q11 deletion (or DiGeorge) syndrome (22q11DS), the result of flect changes in cortical neurogenesis. We focused on two a 1.5- to 3-megabase hemizygous deletion on human chromosome 22, distinct classes of cortical progenitors: basal progenitors–transit results in dramatically increased susceptibility for ‘‘diseases of cortical amplifying progenitors in the cortical subventricular zone connectivity’’ thought to arise during development, including schizo- (SVZ)–and apical progenitors–self-renewing radial glial stem phrenia and autism. We show that diminished dosage of the genes cells present in the cortical VZ. Each class can be recognized deleted in the 1.5-megabase 22q11 minimal critical deleted region in with combinations of proliferative and molecular markers (Fig. a mouse model of 22q11DS specifically compromises neurogenesis 1). We found reduced frequency of mitotic basal progenitors, and subsequent differentiation in the cerebral cortex. Proliferation of identified by phosphohistone 3 labeling (PH3; a G2/M-phase basal, but not apical, progenitors is disrupted, and subsequently, the cell-cycle marker) as well as SVZ location, throughout the frequency of layer 2/3, but not layer 5/6, projection neurons is altered. -
At Elevated Temperatures, Heat Shock Protein Genes Show Altered Ratios Of
EXPERIMENTAL AND THERAPEUTIC MEDICINE 22: 900, 2021 At elevated temperatures, heat shock protein genes show altered ratios of different RNAs and expression of new RNAs, including several novel HSPB1 mRNAs encoding HSP27 protein isoforms XIA GAO1,2, KEYIN ZHANG1,2, HAIYAN ZHOU3, LUCAS ZELLMER4, CHENGFU YUAN5, HAI HUANG6 and DEZHONG JOSHUA LIAO2,6 1Department of Pathology, Guizhou Medical University Hospital; 2Key Lab of Endemic and Ethnic Diseases of The Ministry of Education of China in Guizhou Medical University; 3Clinical Research Center, Guizhou Medical University Hospital, Guiyang, Guizhou 550004, P.R. China; 4Masonic Cancer Center, University of Minnesota, Minneapolis, MN 55455, USA; 5Department of Biochemistry, China Three Gorges University, Yichang, Hubei 443002; 6Center for Clinical Laboratories, Guizhou Medical University Hospital, Guiyang, Guizhou 550004, P.R. China Received December 16, 2020; Accepted May 10, 2021 DOI: 10.3892/etm.2021.10332 Abstract. Heat shock proteins (HSP) serve as chaperones genes may engender multiple protein isoforms. These results to maintain the physiological conformation and function of collectively suggested that, besides increasing their expres‑ numerous cellular proteins when the ambient temperature is sion, certain HSP and associated genes also use alternative increased. To determine how accurate the general assumption transcription start sites to produce multiple RNA transcripts that HSP gene expression is increased in febrile situations is, and use alternative splicing of a transcript to produce multiple the RNA levels of the HSF1 (heat shock transcription factor 1) mature RNAs, as important mechanisms for responding to an gene and certain HSP genes were determined in three cell increased ambient temperature in vitro. lines cultured at 37˚C or 39˚C for three days. -
Genome-Wide Association Study of Diabetic Kidney Disease Highlights Biology Involved in Glomerular Basement Membrane Collagen
CLINICAL RESEARCH www.jasn.org Genome-Wide Association Study of Diabetic Kidney Disease Highlights Biology Involved in Glomerular Basement Membrane Collagen Rany M. Salem ,1 Jennifer N. Todd,2,3,4 Niina Sandholm ,5,6,7 Joanne B. Cole ,2,3,4 Wei-Min Chen,8 Darrell Andrews,9 Marcus G. Pezzolesi,10 Paul M. McKeigue,11 Linda T. Hiraki,12 Chengxiang Qiu,13 Viji Nair,14 Chen Di Liao,12 Jing Jing Cao,12 Erkka Valo ,5,6,7 Suna Onengut-Gumuscu,8 Adam M. Smiles,15 Stuart J. McGurnaghan,16 Jani K. Haukka,5,6,7 Valma Harjutsalo,5,6,7,17 Eoin P. Brennan,9 Natalie van Zuydam,18,19 Emma Ahlqvist,20 Ross Doyle,9 Tarunveer S. Ahluwalia ,21 Maria Lajer,21 Maria F. Hughes,9 Jihwan Park,13 Jan Skupien,15 Athina Spiliopoulou,11 Andrew Liu,22 Rajasree Menon,14,23 Carine M. Boustany-Kari,24 Hyun M. Kang,23,25 Robert G. Nelson,26 Ronald Klein,27 Barbara E. Klein,27 Kristine E. Lee ,27 Xiaoyu Gao,28 Michael Mauer,29 Silvia Maestroni,30 Maria Luiza Caramori,29 Ian H. de Boer ,31 Rachel G. Miller,32 Jingchuan Guo ,32 Andrew P. Boright,12 David Tregouet,33,34 Beata Gyorgy,33,34 Janet K. Snell-Bergeon,35 David M. Maahs,36 Shelley B. Bull ,37 Angelo J. Canty,38 Colin N.A. Palmer,39 Lars Stechemesser,40 Bernhard Paulweber,40 Raimund Weitgasser,40,41 Jelizaveta Sokolovska,42 Vita Rovıte,43 Valdis Pırags, 42,44 Edita Prakapiene,45 Lina Radzeviciene,46 Rasa Verkauskiene,46 Nicolae Mircea Panduru,6,47 Leif C. -
This Is the Accepted Version of the Author's Manuscript. Reis SD, Pinho BR, Oliveira JMA "Modulation of Molecular Chapero
This is the Accepted Version of the Author’s Manuscript. Reis SD, Pinho BR, Oliveira JMA "Modulation of molecular chaperones in Huntington’s disease and other polyglutamine disorders". Molecular Neurobiology. September 2016 DOI: 10.1007/s12035-016-0120-z Link to Publisher: https://link.springer.com/article/10.1007%2Fs12035-016-0120-z Links to Full Text (RedCube, shared via Springer Nature) – View Only http://rdcu.be/kwjE 1 ! Title page Modulation of molecular chaperones in Huntington’s disease and other polyglutamine disorders Sara D. Reis, Brígida R. Pinho, Jorge M. A. Oliveira* REQUIMTE/LAQV, Department of Drug Sciences, Pharmacology Lab, Faculty of Pharmacy, University of Porto, Porto, Portugal *Corresponding author: Jorge M. Ascenção Oliveira Tel. +351 220428610 Email: [email protected] Acknowledgements This work was supported by Fundação para a Ciência e a Tecnologia (FCT): Strategic award UID/QUI/50006/2013, and by the research grant PTDC/NEU-NMC/0412/2014 (PI: JMAO), co- financed by the European Union (FEDER, QREN, COMPETE) – POCI-01-0145-FEDER- 016577. SDR acknowledges FCT for her PhD Grant (PD/BD/113567/2015). BRP acknowledges FCT for her PostDoc Grant (SFRH/BPD/102259/2014). We thank Ana Isabel Duarte (PhD, U. Coimbra) and Maria Clara Quintas (PhD, U. Porto) for reading and commenting the initial manuscript draft. 2 ! Abstract Polyglutamine expansion mutations in specific proteins underlie the pathogenesis of a group of progressive neurodegenerative disorders, including Huntington’s disease, spinal and bulbar muscular atrophy, dentatorubral-pallidoluysian atrophy, and several spinocerebellar ataxias. The different mutant proteins share ubiquitous expression and abnormal proteostasis, with misfolding and aggregation, but nevertheless evoke distinct patterns of neurodegeneration. -
Downloaded the “Top Edge” Version
bioRxiv preprint doi: https://doi.org/10.1101/855338; this version posted December 6, 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 4.0 International license. 1 Drosophila models of pathogenic copy-number variant genes show global and 2 non-neuronal defects during development 3 Short title: Non-neuronal defects of fly homologs of CNV genes 4 Tanzeen Yusuff1,4, Matthew Jensen1,4, Sneha Yennawar1,4, Lucilla Pizzo1, Siddharth 5 Karthikeyan1, Dagny J. Gould1, Avik Sarker1, Yurika Matsui1,2, Janani Iyer1, Zhi-Chun Lai1,2, 6 and Santhosh Girirajan1,3* 7 8 1. Department of Biochemistry and Molecular Biology, Pennsylvania State University, 9 University Park, PA 16802 10 2. Department of Biology, Pennsylvania State University, University Park, PA 16802 11 3. Department of Anthropology, Pennsylvania State University, University Park, PA 16802 12 4 contributed equally to work 13 14 *Correspondence: 15 Santhosh Girirajan, MBBS, PhD 16 205A Life Sciences Building 17 Pennsylvania State University 18 University Park, PA 16802 19 E-mail: [email protected] 20 Phone: 814-865-0674 21 1 bioRxiv preprint doi: https://doi.org/10.1101/855338; this version posted December 6, 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 4.0 International license. 22 ABSTRACT 23 While rare pathogenic copy-number variants (CNVs) are associated with both neuronal and non- 24 neuronal phenotypes, functional studies evaluating these regions have focused on the molecular 25 basis of neuronal defects. -
Supplementary Material DNA Methylation in Inflammatory Pathways Modifies the Association Between BMI and Adult-Onset Non- Atopic
Supplementary Material DNA Methylation in Inflammatory Pathways Modifies the Association between BMI and Adult-Onset Non- Atopic Asthma Ayoung Jeong 1,2, Medea Imboden 1,2, Akram Ghantous 3, Alexei Novoloaca 3, Anne-Elie Carsin 4,5,6, Manolis Kogevinas 4,5,6, Christian Schindler 1,2, Gianfranco Lovison 7, Zdenko Herceg 3, Cyrille Cuenin 3, Roel Vermeulen 8, Deborah Jarvis 9, André F. S. Amaral 9, Florian Kronenberg 10, Paolo Vineis 11,12 and Nicole Probst-Hensch 1,2,* 1 Swiss Tropical and Public Health Institute, 4051 Basel, Switzerland; [email protected] (A.J.); [email protected] (M.I.); [email protected] (C.S.) 2 Department of Public Health, University of Basel, 4001 Basel, Switzerland 3 International Agency for Research on Cancer, 69372 Lyon, France; [email protected] (A.G.); [email protected] (A.N.); [email protected] (Z.H.); [email protected] (C.C.) 4 ISGlobal, Barcelona Institute for Global Health, 08003 Barcelona, Spain; [email protected] (A.-E.C.); [email protected] (M.K.) 5 Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain 6 CIBER Epidemiología y Salud Pública (CIBERESP), 08005 Barcelona, Spain 7 Department of Economics, Business and Statistics, University of Palermo, 90128 Palermo, Italy; [email protected] 8 Environmental Epidemiology Division, Utrecht University, Institute for Risk Assessment Sciences, 3584CM Utrecht, Netherlands; [email protected] 9 Population Health and Occupational Disease, National Heart and Lung Institute, Imperial College, SW3 6LR London, UK; [email protected] (D.J.); [email protected] (A.F.S.A.) 10 Division of Genetic Epidemiology, Medical University of Innsbruck, 6020 Innsbruck, Austria; [email protected] 11 MRC-PHE Centre for Environment and Health, School of Public Health, Imperial College London, W2 1PG London, UK; [email protected] 12 Italian Institute for Genomic Medicine (IIGM), 10126 Turin, Italy * Correspondence: [email protected]; Tel.: +41-61-284-8378 Int. -
Antioxidant Enzymes and Heat Shock Protein Genes from Liposcelis Bostrychophila Are Involved in Stress Defense Upon Heat Shock
insects Article Antioxidant Enzymes and Heat Shock Protein Genes from Liposcelis bostrychophila Are Involved in Stress Defense upon Heat Shock Ze Qing Miao 1,2, Yan Qing Tu 1,2, Peng Yu Guo 1, Wang He 1,2, Tian Xing Jing 1,2, Jin Jun Wang 1,2 and Dan Dan Wei 1,2,* 1 Key Laboratory of Entomology and Pest Control Engineering, College of Plant Protection, Southwest University, Chongqing 400715, China; [email protected] (Z.Q.M.); [email protected] (Y.Q.T.); [email protected] (P.Y.G.); [email protected] (W.H.); [email protected] (T.X.J.); [email protected] (J.J.W.) 2 Academy of Agricultural Sciences, Southwest University, Chongqing 400715, China * Correspondence: [email protected]; Tel.: +86-23-68250653; Fax: +86-23-68251269 Received: 2 November 2020; Accepted: 26 November 2020; Published: 27 November 2020 Simple Summary: Liposcelis bostrychophila is one of the most serious pests of stored commodities among the psocids. Controlling psocids mainly relies on chemical insecticides and heat stress. In fact, L. bostrychophila has developed high levels of resistance or tolerance to heat treatment in grain storage systems. In this study, we evaluated the changes in malondialdehyde (MDA) concentration after different high temperatures. The result showed that MDA is increased slightly overall, but a drastic increase is detected at 42.5 ◦C for exposure of different times. To further explore the principles of L. bostrychophila in response to heat stress, we tested the changes of superoxide dismutase (SOD), catalase (CAT), peroxidases (POD) and glutathione-S-transferases (GST) activities under different heat treatments and identified four inducible LbHsp70 genes and one LbHsp110 gene. -
Reading Through the Building Blocks of the Genome: Exonic Variation in PD
UNIVERSITY OF CATANIA INTERNATIONAL PhD PROGRAM IN NEUROSCIENCE XXIX Cycle VALENTINA LA COGNATA READING THROUGH THE BUILDING BLOCKS OF THE GENOME: EXONIC VARIATION IN PARKINSON'S DISEASE PhD Thesis Coordinator: Supervisors: Prof. Salvatore Salomone Prof. Velia D’Agata Dr. Sebastiano Cavallaro January 2017 Copyright © V. La Cognata, 2017 All rights reserved. No part of this book may be reproduced, stored in a retrieval system or transmitted in any form or by any means, without prior permission of the author. The copyright of the published papers remains with the publishers. SUMMARY Abstract ...................................................................................................... 5 Chapter 1 .................................................................................................... 7 PARKINSON’S DISEASE ....................................................................................................... 9 HAS EXONIC VARIATION A ROLE IN PD? ............................................................................12 AIMS OF THE PhD WORK ...................................................................................................13 Chapter 2 .................................................................................................. 15 ABSTRACT ........................................................................................................................17 INTRODUCTION ................................................................................................................18 CNVs: A PREVALENT -
Nº Ref Uniprot Proteína Péptidos Identificados Por MS/MS 1 P01024
Document downloaded from http://www.elsevier.es, day 26/09/2021. This copy is for personal use. Any transmission of this document by any media or format is strictly prohibited. Nº Ref Uniprot Proteína Péptidos identificados 1 P01024 CO3_HUMAN Complement C3 OS=Homo sapiens GN=C3 PE=1 SV=2 por 162MS/MS 2 P02751 FINC_HUMAN Fibronectin OS=Homo sapiens GN=FN1 PE=1 SV=4 131 3 P01023 A2MG_HUMAN Alpha-2-macroglobulin OS=Homo sapiens GN=A2M PE=1 SV=3 128 4 P0C0L4 CO4A_HUMAN Complement C4-A OS=Homo sapiens GN=C4A PE=1 SV=1 95 5 P04275 VWF_HUMAN von Willebrand factor OS=Homo sapiens GN=VWF PE=1 SV=4 81 6 P02675 FIBB_HUMAN Fibrinogen beta chain OS=Homo sapiens GN=FGB PE=1 SV=2 78 7 P01031 CO5_HUMAN Complement C5 OS=Homo sapiens GN=C5 PE=1 SV=4 66 8 P02768 ALBU_HUMAN Serum albumin OS=Homo sapiens GN=ALB PE=1 SV=2 66 9 P00450 CERU_HUMAN Ceruloplasmin OS=Homo sapiens GN=CP PE=1 SV=1 64 10 P02671 FIBA_HUMAN Fibrinogen alpha chain OS=Homo sapiens GN=FGA PE=1 SV=2 58 11 P08603 CFAH_HUMAN Complement factor H OS=Homo sapiens GN=CFH PE=1 SV=4 56 12 P02787 TRFE_HUMAN Serotransferrin OS=Homo sapiens GN=TF PE=1 SV=3 54 13 P00747 PLMN_HUMAN Plasminogen OS=Homo sapiens GN=PLG PE=1 SV=2 48 14 P02679 FIBG_HUMAN Fibrinogen gamma chain OS=Homo sapiens GN=FGG PE=1 SV=3 47 15 P01871 IGHM_HUMAN Ig mu chain C region OS=Homo sapiens GN=IGHM PE=1 SV=3 41 16 P04003 C4BPA_HUMAN C4b-binding protein alpha chain OS=Homo sapiens GN=C4BPA PE=1 SV=2 37 17 Q9Y6R7 FCGBP_HUMAN IgGFc-binding protein OS=Homo sapiens GN=FCGBP PE=1 SV=3 30 18 O43866 CD5L_HUMAN CD5 antigen-like OS=Homo