YBX1 and Its Interactors Derived from Unihi, Metamatched and TRRUST Databases
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
502 the Keratinocyte Growth-Differentiation Switch Intact Skin
[Frontiers in Bioscience 3, d502-508, May 15, 1998] THE KERATINOCYTE GROWTH-DIFFERENTIATION SWITCH Paolo Dotto Cutaneous Biology Research Center, Massachusetts General Hospital, Building 149, 13th Street, Charlestown, Massachusetts, 02129- 2000 Received 5/4/98 Accepted 5/8/98 TABLE OF CONTENTS 1. Abstract 2. Introduction 3. Signals which control the switch between keratinocyte growth and differentiation 4. Intermediate signalling pathways which are responsible for transduction of the differentiation signal 5. Tyrosine phosphorylation : key to regulation of keratinocyte differentiation 6. Transcription and cell cycle regulatory events connected with the onset of keratinocyte differentiation 7. References medium at low calcium concentrations (our unpublished 1. ABSTRACT observations). Growth/differentiation control of normal epithelial Besides calcium, growth/differentiation of primary cells has been relatively understudied, because of the keratinocyte cultures can be controlled by pharmacological complexities involved in their cultivation and means. In particular, treatment with the phorbol ester TPA characterization. The present review is focused on progress (12-0-tetradecanoylphorbol-13-acetate) induces growth in this area using the mouse primary keratinocyte system. arrest as well as expression of a set of differentiation This system reproduces under well defined culture markers such as involucrin, loricrin and filaggrin. However, conditions the switch between epithelial cell growth and expression of other markers induced differentiation -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated. -
Molecular Signatures in IASLC/ATS/ERS Classified Growth Patterns of Lung Adenocarcinoma
RESEARCH ARTICLE Molecular signatures in IASLC/ATS/ERS classified growth patterns of lung adenocarcinoma 1 1 1,2 1¤a Heike ZabeckID *, Hendrik Dienemann , Hans Hoffmann , Joachim Pfannschmidt , Arne Warth2,3, Philipp A. Schnabel3¤b, Thomas Muley2,4, Michael Meister2,4, Holger SuÈ ltmann2,5, Holger FroÈ hlich6, Ruprecht Kuner2,5¤c, Felix Lasitschka3 1 Department of Thoracic Surgery, Thoraxklinik, University Hospital Heidelberg, Heidelberg, Germany, 2 Translational Lung Research Centre Heidelberg (TLRC-H), German Centre for Lung Research (DZL), a1111111111 Heidelberg, Germany, 3 Institute of Pathology, University Hospital Heidelberg, Heidelberg, Germany, a1111111111 4 Translational Research Unit (STF), Thoraxklinik, University of Heidelberg, Heidelberg, Germany, 5 Cancer a1111111111 Genome Research (B063), German Cancer Research Center (DKFZ) and German Cancer Consortium a1111111111 (DKTK), Heidelberg, Germany, 6 Institute for Computer Science, c/o Bonn-Aachen International Center for a1111111111 IT, Algorithmic Bioinformatics, University of Bonn, Bonn, Germany ¤a Current address: Department of Thoracic Surgery, Lung Clinic Heckeshorn at HELIOS Hospital Emil von Behring, Berlin, Germany ¤b Current address: Institute of Pathology, Saarland University, Homburg/Saar, Germany ¤c Current address: TRONÐTranslational Oncology at the University Medical Center of Johannes OPEN ACCESS Gutenberg University, Mainz, Germany * [email protected] Citation: Zabeck H, Dienemann H, Hoffmann H, Pfannschmidt J, Warth A, Schnabel PA, et al. (2018) Molecular signatures in IASLC/ATS/ERS classified growth patterns of lung adenocarcinoma. Abstract PLoS ONE 13(10): e0206132. https://doi.org/ 10.1371/journal.pone.0206132 Editor: Stefania Crispi, Institute for Bioscience and Background Biotechnology Research, ITALY The current classification of human lung adenocarcinoma defines five different histological Received: April 4, 2018 growth patterns within the group of conventional invasive adenocarcinomas. -
Interindividual Regulation of the BCRP/ABCG2 Transporter in Term Human Placentas
DMD Fast Forward. Published on January 31, 2018 as DOI: 10.1124/dmd.117.079228 This article has not been copyedited and formatted. The final version may differ from this version. DMD #79228 Title Page Interindividual Regulation of the BCRP/ABCG2 Transporter in Term Human Placentas Kristin M Bircsak, Jamie E Moscovitz, Xia Wen, Faith Archer, Poi Yu Sofia Yuen, Moiz Mohammed, Naureen Memon, Barry I Weinberger, Laura M Saba, Anna M Vetrano, Lauren M Aleksunes Downloaded from Department of Pharmacology and Toxicology, Rutgers, The State University of New Jersey, Ernest Mario School of Pharmacy, Piscataway, NJ, USA (K.M.B., J.E.M., X.W., L.M.A.), dmd.aspetjournals.org Department of Pediatrics, Rutgers University Robert Wood Johnson Medical School, New Brunswick, NJ, USA (F.A., P.Y.S.Y, M.M., N.M., A.M.V.), Hofstra Northwell School of Medicine, Cohen Children’s Medical Center of New York, New Hyde Park, NY, USA (B.I.W.), at ASPET Journals on October 2, 2021 Department of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado, Aurora, CO, USA (L.S.), Environmental and Occupational Health Sciences Institute, Rutgers, The State University of New Jersey, Piscataway, NJ, USA (L.M.A.), Lipid Center, Rutgers, The State University of New Jersey, Piscataway, NJ, USA (L.M.A.) 1 DMD Fast Forward. Published on January 31, 2018 as DOI: 10.1124/dmd.117.079228 This article has not been copyedited and formatted. The final version may differ from this version. DMD #79228 Running Title Page Running title: Interindividual -
Nuclear PTEN Safeguards Pre-Mrna Splicing to Link Golgi Apparatus for Its Tumor Suppressive Role
ARTICLE DOI: 10.1038/s41467-018-04760-1 OPEN Nuclear PTEN safeguards pre-mRNA splicing to link Golgi apparatus for its tumor suppressive role Shao-Ming Shen1, Yan Ji2, Cheng Zhang1, Shuang-Shu Dong2, Shuo Yang1, Zhong Xiong1, Meng-Kai Ge1, Yun Yu1, Li Xia1, Meng Guo1, Jin-Ke Cheng3, Jun-Ling Liu1,3, Jian-Xiu Yu1,3 & Guo-Qiang Chen1 Dysregulation of pre-mRNA alternative splicing (AS) is closely associated with cancers. However, the relationships between the AS and classic oncogenes/tumor suppressors are 1234567890():,; largely unknown. Here we show that the deletion of tumor suppressor PTEN alters pre-mRNA splicing in a phosphatase-independent manner, and identify 262 PTEN-regulated AS events in 293T cells by RNA sequencing, which are associated with significant worse outcome of cancer patients. Based on these findings, we report that nuclear PTEN interacts with the splicing machinery, spliceosome, to regulate its assembly and pre-mRNA splicing. We also identify a new exon 2b in GOLGA2 transcript and the exon exclusion contributes to PTEN knockdown-induced tumorigenesis by promoting dramatic Golgi extension and secretion, and PTEN depletion significantly sensitizes cancer cells to secretion inhibitors brefeldin A and golgicide A. Our results suggest that Golgi secretion inhibitors alone or in combination with PI3K/Akt kinase inhibitors may be therapeutically useful for PTEN-deficient cancers. 1 Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine (SJTU-SM), Shanghai 200025, China. 2 Institute of Health Sciences, Shanghai Institutes for Biological Sciences of Chinese Academy of Sciences and SJTU-SM, Shanghai 200025, China. -
Identification of Cigarette Smoke Condensate-Modulated Hiv-1-Associated Host Factors Using a Targeted Transcriptomic Approach
Journal of HIV/AIDS & Infectious Diseases Research Open Access Identification of Cigarette Smoke Condensate-Modulated Hiv-1-Associated Host Factors Using A Targeted Transcriptomic Approach Janaki Purushe and Mario PS Chin* Department of Microbiology and Immunology, Center for Substance Abuse Research, Temple University School of Medicine, 3440 N. Broad Street, Philadelphia, PA 19140 *Corresponding author: Mario PS Chin, Department of Microbiology and Immunology, Center for Substance Abuse Research, Temple University School of Medicine, 3440 N. Broad Street, Philadelphia; E-mail: mpschin@ temple.edu Received Date: July 18, 2013, Accepted Date: September 13, 2013, Published Date: September 15, 2013 Citation: Mario PS Chin (2013) Identification of Cigarette Smoke Condensate-Modulated Hiv-1-Associated Host Factors Us- ing A Targeted Transcriptomic Approach. J HIV AIDS Infect Dis 1: 1-7. Abstract Tobacco use has been correlated with increased HIV-1 infection. In vitro characterization of alveolar macrophages obtained from uninfected cigarette smokers showed an increased susceptibility to HIV-1 infection when compared with cell from non-smokers. We showed that Cigarette Smoke Condensate (CSC) enhances HIV-1 infection in primary CD4+ cells. The underlying mechanisms of how CSC affects HIV-1 replication are unclear. The traditional approach that studies the specific cellular processes that are modulated by CSC and examines the resulting effects on viral replication has generated incon- clusive results. Indeed, CSC has a pleiotropic effect on cell expression and transcriptomic studies have shown that CSC can modulate the expression of a large number of genes. This global transcriptomic approach generates a large number of unreg- ulated and downregulated genes, prohibiting the specific functional analysis of genes that are related to viral replication. -
Sp1 Transcription Factor: a Long-Standing Target in Cancer Chemotherapy
Sp1 transcription factor: A long-standing target in cancer chemotherapy Carolina Vizcaíno, Sylvia Mansilla and José Portugal* Instituto de Biología Molecular de Barcelona, CSIC, Parc Científic de Barcelona, E-08028 Barcelona, Spain *to whom correspondence should be addressed: Dr. José Portugal, Instituto de Biología Molecular de Barcelona, CSIC, Parc Científic de Barcelona, Baldiri Reixac, 10; E-08028 Barcelona, Spain. Phone: +34 93 403 4959, FAX: +34 93 403 4979, E-mail: [email protected] 1 ABSTRACT Sp1 (Specificity protein 1) is a well-known member of a family of transcription factors that also includes Sp2, Sp3 and Sp4, which are implicated in an ample variety of essential biological processes and have been proven important in cell growth, differentiation, apoptosis and carcinogenesis. Sp1 activates the transcription of many cellular genes that contain putative CG- rich Sp-binding sites in their promoters. Sp1 and Sp3 proteins bind to similar, if not the same, DNA tracts and compete for binding, thus they can enhance or repress gene expression. Evidences exist that the Sp-family of proteins regulates the expression of genes that play pivotal roles in cell proliferation and metastasis of various tumors. In patients with a variety of cancers, high levels of Sp1 protein are considered a negative prognostic factor. A plethora of compounds can interfere with the trans-activating activities of Sp1 and other Sp proteins on gene expression. Several pathways are involved in the down-regulation of Sp proteins by compounds with different mechanisms of action, which include not only the direct interference with the binding of Sp proteins to their putative DNA binding sites, but also promoting the degradation of Sp protein factors. -
Interindividual Regulation of the BCRP/ABCG2 Transporter in Term Human Placentas
DMD Fast Forward. Published on January 31, 2018 as DOI: 10.1124/dmd.117.079228 This article has not been copyedited and formatted. The final version may differ from this version. DMD #79228 Title Page Interindividual Regulation of the BCRP/ABCG2 Transporter in Term Human Placentas Kristin M Bircsak, Jamie E Moscovitz, Xia Wen, Faith Archer, Poi Yu Sofia Yuen, Moiz Mohammed, Naureen Memon, Barry I Weinberger, Laura M Saba, Anna M Vetrano, Lauren M Aleksunes Downloaded from Department of Pharmacology and Toxicology, Rutgers, The State University of New Jersey, Ernest Mario School of Pharmacy, Piscataway, NJ, USA (K.M.B., J.E.M., X.W., L.M.A.), dmd.aspetjournals.org Department of Pediatrics, Rutgers University Robert Wood Johnson Medical School, New Brunswick, NJ, USA (F.A., P.Y.S.Y, M.M., N.M., A.M.V.), Hofstra Northwell School of Medicine, Cohen Children’s Medical Center of New York, New Hyde Park, NY, USA (B.I.W.), at ASPET Journals on October 1, 2021 Department of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado, Aurora, CO, USA (L.S.), Environmental and Occupational Health Sciences Institute, Rutgers, The State University of New Jersey, Piscataway, NJ, USA (L.M.A.), Lipid Center, Rutgers, The State University of New Jersey, Piscataway, NJ, USA (L.M.A.) 1 DMD Fast Forward. Published on January 31, 2018 as DOI: 10.1124/dmd.117.079228 This article has not been copyedited and formatted. The final version may differ from this version. DMD #79228 Running Title Page Running title: Interindividual -
The Alter Retina: Alternative Splicing of Retinal Genes in Health and Disease
International Journal of Molecular Sciences Review The Alter Retina: Alternative Splicing of Retinal Genes in Health and Disease Izarbe Aísa-Marín 1,2 , Rocío García-Arroyo 1,3 , Serena Mirra 1,2 and Gemma Marfany 1,2,3,* 1 Departament of Genetics, Microbiology and Statistics, Avda. Diagonal 643, Universitat de Barcelona, 08028 Barcelona, Spain; [email protected] (I.A.-M.); [email protected] (R.G.-A.); [email protected] (S.M.) 2 Centro de Investigación Biomédica en Red Enfermedades Raras (CIBERER), Instituto de Salud Carlos III (ISCIII), Universitat de Barcelona, 08028 Barcelona, Spain 3 Institute of Biomedicine (IBUB, IBUB-IRSJD), Universitat de Barcelona, 08028 Barcelona, Spain * Correspondence: [email protected] Abstract: Alternative splicing of mRNA is an essential mechanism to regulate and increase the diversity of the transcriptome and proteome. Alternative splicing frequently occurs in a tissue- or time-specific manner, contributing to differential gene expression between cell types during development. Neural tissues present extremely complex splicing programs and display the highest number of alternative splicing events. As an extension of the central nervous system, the retina constitutes an excellent system to illustrate the high diversity of neural transcripts. The retina expresses retinal specific splicing factors and produces a large number of alternative transcripts, including exclusive tissue-specific exons, which require an exquisite regulation. In fact, a current challenge in the genetic diagnosis of inherited retinal diseases stems from the lack of information regarding alternative splicing of retinal genes, as a considerable percentage of mutations alter splicing Citation: Aísa-Marín, I.; or the relative production of alternative transcripts. Modulation of alternative splicing in the retina García-Arroyo, R.; Mirra, S.; Marfany, is also instrumental in the design of novel therapeutic approaches for retinal dystrophies, since it G. -
Supplementary Table 1A. Genes Significantly Altered in A4573 ESFT
Supplementary Table 1A. Genes significantly altered in A4573 ESFT cells following BMI-1knockdown genesymbol genedescription siControl siBMI1 FC Direction P-value AASS aminoadipate-semialdehyde synthase | tetra-peptide repeat homeobox-like6.68 7.24 1.5 Up 0.007 ABCA2 ATP-binding cassette, sub-family A (ABC1), member 2 | neural5.44 proliferation,6.3 differentiation1.8 and Upcontrol, 1 0.006 ABHD4 abhydrolase domain containing 4 7.51 6.69 1.8 Down 0.002 ACACA acetyl-Coenzyme A carboxylase alpha | peroxiredoxin 5 | similar6.2 to High mobility7.26 group2.1 protein UpB1 (High mobility0.009 group protein 1) (HMG-1) (Amphoterin) (Heparin-binding protein p30) | Coenzyme A synthase ACAD9 acyl-Coenzyme A dehydrogenase family, member 9 9.25 8.59 1.6 Down 0.008 ACBD3 acyl-Coenzyme A binding domain containing 3 7.89 8.53 1.6 Up 0.008 ACCN2 amiloride-sensitive cation channel 2, neuronal 5.47 6.28 1.8 Up 0.005 ACIN1 apoptotic chromatin condensation inducer 1 7.15 7.79 1.6 Up 0.008 ACPL2 acid phosphatase-like 2 6.04 7.6 2.9 Up 0.000 ACSL4 acyl-CoA synthetase long-chain family member 4 6.72 5.8 1.9 Down 0.001 ACTA2 actin, alpha 2, smooth muscle, aorta 9.18 8.44 1.7 Down 0.003 ACYP1 acylphosphatase 1, erythrocyte (common) type 7.09 7.66 1.5 Up 0.009 ADA adenosine deaminase 6.34 7.1 1.7 Up 0.009 ADAL adenosine deaminase-like 7.88 6.89 2.0 Down 0.006 ADAMTS1 ADAM metallopeptidase with thrombospondin type 1 motif, 1 6.57 7.65 2.1 Up 0.000 ADARB1 adenosine deaminase, RNA-specific, B1 (RED1 homolog rat) 6.49 7.13 1.6 Up 0.008 ADCY9 adenylate cyclase 9 6.5 7.18 -
Ab207227 Sp1/Sp3 Transcription Factor Assay Kit (Colorimetric)
ab207227 Sp1/Sp3 Transcription Factor Assay Kit (Colorimetric) Instructions for use: For quantitative measurement of Sp1/Sp3 Activation in human, mouse and rat nuclear extracts. This product is for research use only and is not intended for diagnostic use. Version 2 Last Updated 24 August 2017 Table of Contents INTRODUCTION 1 1. BACKGROUND 1 2. ASSAY SUMMARY 3 GENERAL INFORMATION 4 3. PRECAUTIONS 4 4. STORAGE AND STABILITY 4 5. LIMITATIONS 5 6. MATERIALS SUPPLIED 5 7. MATERIALS REQUIRED, NOT SUPPLIED 6 8. TECHNICAL HINTS 7 ASSAY PREPARATION 8 9. REAGENT PREPARATION 8 10. SAMPLE PREPARATION 14 ASSAY PROCEDURE 16 11. ASSAY PROCEDURE 16 DATA ANALYSIS 18 12. TYPICAL DATA 18 RESOURCES 19 13. QUICK ASSAY PROCEDURE 19 14. TROUBLESHOOTING 20 15. INTERFERENCES 21 16. NOTES 22 INTRODUCTION INTRODUCTION 1. BACKGROUND Sp1/Sp3 Transcription Factor Assay Kit (Colorimetric) (ab207227) is a high throughput assay to quantify Sp1/Sp3 activation. This assay combines a quick ELISA format with a sensitive and specific non- radioactive assay for transcription factor activation. A specific double stranded DNA sequence containing the Sp1/Sp3 consensus binding site (5’ – GGGGCGGGG – 3’) has been immobilized onto a 96-well plate. Active Sp1/Sp3 present in the nuclear extract specifically binds to the oligonucleotide. Sp1/Sp3 is detected by a primary antibody that recognizes an epitope of Sp1/Sp3 accessible only when the protein is activated and bound to its target DNA. An HRP- conjugated secondary antibody provides sensitive colorimetric readout at OD 450 nm. This product detects human, mouse and rat Sp1/Sp3. Key performance and benefits: Assay time: 3.5 hours (cell extracts preparation not included). -
Mrna Editing, Processing and Quality Control in Caenorhabditis Elegans
| WORMBOOK mRNA Editing, Processing and Quality Control in Caenorhabditis elegans Joshua A. Arribere,*,1 Hidehito Kuroyanagi,†,1 and Heather A. Hundley‡,1 *Department of MCD Biology, UC Santa Cruz, California 95064, †Laboratory of Gene Expression, Medical Research Institute, Tokyo Medical and Dental University, Tokyo 113-8510, Japan, and ‡Medical Sciences Program, Indiana University School of Medicine-Bloomington, Indiana 47405 ABSTRACT While DNA serves as the blueprint of life, the distinct functions of each cell are determined by the dynamic expression of genes from the static genome. The amount and specific sequences of RNAs expressed in a given cell involves a number of regulated processes including RNA synthesis (transcription), processing, splicing, modification, polyadenylation, stability, translation, and degradation. As errors during mRNA production can create gene products that are deleterious to the organism, quality control mechanisms exist to survey and remove errors in mRNA expression and processing. Here, we will provide an overview of mRNA processing and quality control mechanisms that occur in Caenorhabditis elegans, with a focus on those that occur on protein-coding genes after transcription initiation. In addition, we will describe the genetic and technical approaches that have allowed studies in C. elegans to reveal important mechanistic insight into these processes. KEYWORDS Caenorhabditis elegans; splicing; RNA editing; RNA modification; polyadenylation; quality control; WormBook TABLE OF CONTENTS Abstract 531 RNA Editing and Modification 533 Adenosine-to-inosine RNA editing 533 The C. elegans A-to-I editing machinery 534 RNA editing in space and time 535 ADARs regulate the levels and fates of endogenous dsRNA 537 Are other modifications present in C.