RBM33 Shrna Plasmid (H): Sc-89462-SH

Total Page:16

File Type:pdf, Size:1020Kb

RBM33 Shrna Plasmid (H): Sc-89462-SH SANTA CRUZ BIOTECHNOLOGY, INC. RBM33 shRNA Plasmid (h): sc-89462-SH BACKGROUND STORAGE AND RESUSPENSION Proteins containing RNA recognition motifs, including various hnRNP proteins, Store lyophilized shRNA plasmid DNA at 4° C with desiccant. Stable for are implicated in the regulation of alternative splicing and protein components at least one year from the date of shipment. Once resuspended, store at of snRNPs. The RBM (RNA-binding motif) gene family encodes proteins with 4° C for short term storage or -80° C for long term storage. Avoid repeated an RNA binding motif that have been suggested to play a role in the modula- freeze thaw cycles. tion of apoptosis. RBM33 (RNA-binding motif protein 33) is a 1,170 amino Resuspend lyophilized shRNA plasmid DNA in 200 µl of the deionized water acid protein that contains one RRM (RNA recognition motif) domain. Existing provided. Resuspension of the shRNA plasmid DNA in 200 µl of deionized as two alternatively splice isoforms, the RBM33 gene is conserved in chim- water makes a 0.1 µg/µl solution in a 10 mM Tris, 1 mM EDTA buffered panzee, cow, mouse, rat, chicken and zebrafish, and maps to human chromo- solution. some 7q36.3. Chromosome 7 is about 158 million bases long, encodes over 1000 genes and makes up about 5% of the human genome. The deletion of APPLICATIONS a portion of the q arm of chromosome 7 is associated with Williams-Beuren syndrome, a condition characterized by mild mental retardation, an unusual RBM33 shRNA Plasmid (h) is recommended for the inhibition of RBM33 comfort and friendliness with strangers and an elfin appearance. Deletions of expression in human cells. portions of the q arm of chromosome 7 are also seen in a number of myeloid disorders including cases of acute myelogenous leukemia and myelodysplasia. SUPPORT REAGENTS For optimal shRNA Plasmid transfection efficiency, Santa Cruz Biotechnology’s REFERENCES shRNA Plasmid Transfection Reagent: sc-108061 (0.2 ml) and shRNA Plasmid 1. Varani, G., et al. 1998. RNA recognition by RNP proteins during RNA pro- Transfection Medium: sc-108062 (20 ml) are recommended. Control shRNAs cessing. Annu. Rev. Biophys. Biomol. Struct. 27: 407-445. are available as 20 µg lyophilized plasmid DNA. Each encodes a scrambled shRNA sequence that will not lead to the specific degradation of any known 2. Hillier, L.W., et al. 2003. The DNA sequence of human chromosome 7. cellular mRNA. Control shRNA Plasmids include: sc-108060, sc-108065 and Nature 424: 157-164. sc-108066. 3. Scherer, S.W., et al. 2003. Human chromosome 7: DNA sequence and biology. Science 300: 767-772. RT-PCR REAGENTS 4. Maris, C., et al. 2005. The RNA recognition motif, a plastic RNA-binding Semi-quantitative RT-PCR may be performed to monitor RBM33 gene expres- platform to regulate post-transcriptional gene expression. FEBS J. 272: sion knockdown using RT-PCR Primer: RBM33 (h)-PR: sc-89462-PR (20 µl). 2118-2131. Annealing temperature for the primers should be 55-60° C and the extension temperature should be 68-72° C. 5. Sutherland, L.C., et al. 2005. RNA binding motif (RBM) proteins: a novel family of apoptosis modulators? J. Cell. Biochem. 94: 5-24. RESEARCH USE 6. Eckert, M.A., et al. 2006. The neurobiology of Williams syndrome: cascading The purchase of this product conveys to the buyer the nontransferable right influences of visual system impairment? Cell. Mol. Life Sci. 63: 1867-1875. to use the purchased amount of the product and all replicates and derivatives 7. Fukuda, T., et al. 2009. hnRNP K interacts with RNA binding motif pro- for research purposes conducted by the buyer in his laboratory only (whether tein 42 and functions in the maintenance of cellular ATP level during the buyer is an academic or for-profit entity). The buyer cannot sell or other- stress conditions. Genes Cells 14: 113-128. wise transfer (a) this product (b) its components or (c) materials made using this product or its components to a third party, or otherwise use this product CHROMOSOMAL LOCATION or its components or materials made using this product or its components for Commercial Purposes. Genetic locus: RBM33 (human) mapping to 7q36.3. PROTOCOLS PRODUCT See our web site at www.scbt.com for detailed protocols and support RBM33 shRNA Plasmid (h) is a pool of 3 target-specific lentiviral vector products. plasmids each encoding 19-25 nt (plus hairpin) shRNAs designed to knock down gene expression. Each plasmid contains a puromycin resistance gene for the selection of cells stably expressing shRNA. Each vial contains 20 µg of lyophilized shRNA plasmid DNA. Suitable for up to 20 transfections. Also see RBM33 siRNA (h): sc-89462 and RBM33 shRNA (h) Lentiviral Particles: sc-89462-V as alternate gene silencing products. Santa Cruz Biotechnology, Inc. 1.800.457.3801 831.457.3800 fax 831.457.3801 Europe +00800 4573 8000 49 6221 4503 0 www.scbt.com.
Recommended publications
  • Epigenome-Wide Exploratory Study of Monozygotic Twins Suggests Differentially Methylated Regions to Associate with Hand Grip Strength
    Biogerontology (2019) 20:627–647 https://doi.org/10.1007/s10522-019-09818-1 (0123456789().,-volV)( 0123456789().,-volV) RESEARCH ARTICLE Epigenome-wide exploratory study of monozygotic twins suggests differentially methylated regions to associate with hand grip strength Mette Soerensen . Weilong Li . Birgit Debrabant . Marianne Nygaard . Jonas Mengel-From . Morten Frost . Kaare Christensen . Lene Christiansen . Qihua Tan Received: 15 April 2019 / Accepted: 24 June 2019 / Published online: 28 June 2019 Ó The Author(s) 2019 Abstract Hand grip strength is a measure of mus- significant CpG sites or pathways were found, how- cular strength and is used to study age-related loss of ever two of the suggestive top CpG sites were mapped physical capacity. In order to explore the biological to the COL6A1 and CACNA1B genes, known to be mechanisms that influence hand grip strength varia- related to muscular dysfunction. By investigating tion, an epigenome-wide association study (EWAS) of genomic regions using the comb-p algorithm, several hand grip strength in 672 middle-aged and elderly differentially methylated regions in regulatory monozygotic twins (age 55–90 years) was performed, domains were identified as significantly associated to using both individual and twin pair level analyses, the hand grip strength, and pathway analyses of these latter controlling the influence of genetic variation. regions revealed significant pathways related to the Moreover, as measurements of hand grip strength immune system, autoimmune disorders, including performed over 8 years were available in the elderly diabetes type 1 and viral myocarditis, as well as twins (age 73–90 at intake), a longitudinal EWAS was negative regulation of cell differentiation.
    [Show full text]
  • Dissecting the Genomic Complexity Underlying Medulloblastoma
    LETTER doi:10.1038/nature11284 Dissecting the genomic complexity underlying medulloblastoma A list of authors and their affiliations appears at the end of the paper Medulloblastoma is an aggressively growing tumour, arising in Some cases probably went through even higher polyploidy states the cerebellum or medulla/brain stem. It is the most common before reaching an approximately 4n baseline (for example malignant brain tumour in children, and shows tremendous bio- ICGC_MB45, displaying 4n chromosomes with 4:0 or 3:1 allele ratios; logical and clinical heterogeneity1. Despite recent treatment Supplementary Fig. 2). Across the discovery set, tetraploidy was most advances, approximately 40% of children experience tumour commonly observed in Group 3 (7 out of 13, 54%) and Group 4 recurrence, and 30% will die from their disease. Those who survive tumours (8 out of 20, 40%), followed by SHH (4 out of 14, 29%) and often have a significantly reduced quality of life. Four tumour WNT tumours (1 out of 7, 14%). Interestingly, the four tetraploid SHH subgroups with distinct clinical, biological and genetic profiles tumours all harboured TP53 mutations and also displayed chromo- are currently identified2,3. WNT tumours, showing activated thripsis6. Tetraploid Group 3 and 4 tumours showed significantly wingless pathway signalling, carry a favourable prognosis under more large-scale copy number alterations compared with diploid cases current treatment regimens4. SHH tumours show hedgehog (median 10 changes per tumour in tetraploid versus 4 per tumour in pathway activation, and have an intermediate prognosis2. Group 3 diploid cases, P 5 0.008, two-tailed Mann–Whitney U-test; Supplemen- and 4 tumours are molecularly less well characterized, and also tary Fig.
    [Show full text]
  • CD29 Identifies IFN-Γ–Producing Human CD8+ T Cells With
    + CD29 identifies IFN-γ–producing human CD8 T cells with an increased cytotoxic potential Benoît P. Nicoleta,b, Aurélie Guislaina,b, Floris P. J. van Alphenc, Raquel Gomez-Eerlandd, Ton N. M. Schumacherd, Maartje van den Biggelaarc,e, and Monika C. Wolkersa,b,1 aDepartment of Hematopoiesis, Sanquin Research, 1066 CX Amsterdam, The Netherlands; bLandsteiner Laboratory, Oncode Institute, Amsterdam University Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands; cDepartment of Research Facilities, Sanquin Research, 1066 CX Amsterdam, The Netherlands; dDivision of Molecular Oncology and Immunology, Oncode Institute, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; and eDepartment of Molecular and Cellular Haemostasis, Sanquin Research, 1066 CX Amsterdam, The Netherlands Edited by Anjana Rao, La Jolla Institute for Allergy and Immunology, La Jolla, CA, and approved February 12, 2020 (received for review August 12, 2019) Cytotoxic CD8+ T cells can effectively kill target cells by producing therefore developed a protocol that allowed for efficient iso- cytokines, chemokines, and granzymes. Expression of these effector lation of RNA and protein from fluorescence-activated cell molecules is however highly divergent, and tools that identify and sorting (FACS)-sorted fixed T cells after intracellular cytokine + preselect CD8 T cells with a cytotoxic expression profile are lacking. staining. With this top-down approach, we performed an un- + Human CD8 T cells can be divided into IFN-γ– and IL-2–producing biased RNA-sequencing (RNA-seq) and mass spectrometry cells. Unbiased transcriptomics and proteomics analysis on cytokine- γ– – + + (MS) analyses on IFN- and IL-2 producing primary human producing fixed CD8 T cells revealed that IL-2 cells produce helper + + + CD8 Tcells.
    [Show full text]
  • WO 2019/079361 Al 25 April 2019 (25.04.2019) W 1P O PCT
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date WO 2019/079361 Al 25 April 2019 (25.04.2019) W 1P O PCT (51) International Patent Classification: CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, C12Q 1/68 (2018.01) A61P 31/18 (2006.01) DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, C12Q 1/70 (2006.01) HR, HU, ID, IL, IN, IR, IS, JO, JP, KE, KG, KH, KN, KP, KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, (21) International Application Number: MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, PCT/US2018/056167 OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, (22) International Filing Date: SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, 16 October 2018 (16. 10.2018) TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (25) Filing Language: English (84) Designated States (unless otherwise indicated, for every kind of regional protection available): ARIPO (BW, GH, (26) Publication Language: English GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, TZ, (30) Priority Data: UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, 62/573,025 16 October 2017 (16. 10.2017) US TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, EE, ES, FI, FR, GB, GR, HR, HU, ΓΕ , IS, IT, LT, LU, LV, (71) Applicant: MASSACHUSETTS INSTITUTE OF MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, SM, TECHNOLOGY [US/US]; 77 Massachusetts Avenue, TR), OAPI (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, GW, Cambridge, Massachusetts 02139 (US).
    [Show full text]
  • An Integrated Approach to Comprehensively Map the Molecular Context of Proteins
    bioRxiv preprint doi: https://doi.org/10.1101/264788; this version posted February 13, 2018. 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. Liu et al. An integrated approach to comprehensively map the molecular context of proteins Xiaonan Liu1,2, Kari Salokas1,2, Fitsum Tamene1,2,3 and Markku Varjosalo1,2,3* 1Institute of Biotechnology, University of Helsinki, Helsinki 00014, Finland 2Helsinki Institute of Life Science, University of Helsinki, Helsinki 00014, Finland 3Proteomics Unit, University of Helsinki, Helsinki 00014, Finland *Corresponding author Abstract: Protein-protein interactions underlie almost all cellular functions. The comprehensive mapping of these complex cellular networks of stable and transient associations has been made available by affi nity purifi cation mass spectrometry (AP-MS) and more recently by proximity based labelling methods such as BioID. Due the advancements in both methods and MS instrumentation, an in-depth analysis of the whole human proteome is at grasps. In order to facilitate this, we designed and optimized an integrated approach utilizing MAC-tag combining both AP-MS and BioID in a single construct. We systematically applied this approach to 18 subcellular localization markers and generated a molecular context database, which can be used to defi ne molecular locations for any protein of interest. In addition, we show that by combining the AP-MS and BioID results we can also obtain interaction distances within a complex. Taken together, our combined strategy off ers comprehensive approach for mapping physical and functional protein interactions. Introduction: Majority of proteins do not function in isolation geting the endogenous bait protein, allowing and their interactions with other proteins defi ne purifi cation of the bait protein together with the their cellular functions.
    [Show full text]
  • CD29 Identifies IFN-Γ–Producing Human CD8+ T Cells with an Increased Cytotoxic Potential
    + CD29 identifies IFN-γ–producing human CD8 T cells with an increased cytotoxic potential Benoît P. Nicoleta,b, Aurélie Guislaina,b, Floris P. J. van Alphenc, Raquel Gomez-Eerlandd, Ton N. M. Schumacherd, Maartje van den Biggelaarc,e, and Monika C. Wolkersa,b,1 aDepartment of Hematopoiesis, Sanquin Research, 1066 CX Amsterdam, The Netherlands; bLandsteiner Laboratory, Oncode Institute, Amsterdam University Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands; cDepartment of Research Facilities, Sanquin Research, 1066 CX Amsterdam, The Netherlands; dDivision of Molecular Oncology and Immunology, Oncode Institute, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; and eDepartment of Molecular and Cellular Haemostasis, Sanquin Research, 1066 CX Amsterdam, The Netherlands Edited by Anjana Rao, La Jolla Institute for Allergy and Immunology, La Jolla, CA, and approved February 12, 2020 (received for review August 12, 2019) Cytotoxic CD8+ T cells can effectively kill target cells by producing therefore developed a protocol that allowed for efficient iso- cytokines, chemokines, and granzymes. Expression of these effector lation of RNA and protein from fluorescence-activated cell molecules is however highly divergent, and tools that identify and sorting (FACS)-sorted fixed T cells after intracellular cytokine + preselect CD8 T cells with a cytotoxic expression profile are lacking. staining. With this top-down approach, we performed an un- + Human CD8 T cells can be divided into IFN-γ– and IL-2–producing biased RNA-sequencing (RNA-seq) and mass spectrometry cells. Unbiased transcriptomics and proteomics analysis on cytokine- γ– – + + (MS) analyses on IFN- and IL-2 producing primary human producing fixed CD8 T cells revealed that IL-2 cells produce helper + + + CD8 Tcells.
    [Show full text]
  • Protein-Protein Interaction Network Alignment and Evolution
    Protein-Protein Interaction Network Alignment and Evolution by Brian Man-Kin Law A thesis submitted in conformity with the requirements for the degree of Doctor of Philosophy Computer Science University of Toronto © Copyright by Brian Law 2019 Protein-Protein Interaction Network Alignment and Evolution Brian Law Doctor of Philosophy Computer Science University of Toronto 2019 Abstract Network alignment is an emerging analysis method enabled by the rapid large-scale collection of protein-protein interaction data for many different species. As sequence alignment did for gene evolution, network alignment will hopefully provide new insights into network evolution and serve as a new bioinformatic tool for making biological inferences across species. Using new SH3 binding data from Saccharomyces cerevisiae , Caenorhabditis elegans , and Homo sapiens , I construct new interface-interaction networks and devise a new network alignment method for these networks. With appropriate parameterization, this method is highly successful at generating alignments that reflect known protein orthology information and contain high network topology overlap. However, close examination of the optimal parameterization reveals a heavy reliance on protein sequence similarity and fungibility of other data features, including network topology data, an observation that may also pertain to protein-protein interaction network alignment. Closer examination of interactomic data, along with established orthology data, reveals that protein-protein interaction conservation is quite low across multiple species, suggesting that the high network topology overlap achieved by contemporary network aligners is ill-advised if biological relevance of results is desired. Further consideration of gene duplication and protein ii binding sites reveal additional PPI evolution phenomena further reducing the network topology overlap expected in network alignments, casting doubt on the utility of network alignment metrics solely based on network topology.
    [Show full text]
  • WO 2013/064702 A2 10 May 2013 (10.05.2013) P O P C T
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date WO 2013/064702 A2 10 May 2013 (10.05.2013) P O P C T (51) International Patent Classification: AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, C12Q 1/68 (2006.01) BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (21) International Application Number: HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, PCT/EP2012/071868 KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, (22) International Filing Date: ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, 5 November 20 12 (05 .11.20 12) NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, (25) Filing Language: English TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, (26) Publication Language: English ZM, ZW. (30) Priority Data: (84) Designated States (unless otherwise indicated, for every 1118985.9 3 November 201 1 (03. 11.201 1) GB kind of regional protection available): ARIPO (BW, GH, 13/339,63 1 29 December 201 1 (29. 12.201 1) US GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, (71) Applicant: DIAGENIC ASA [NO/NO]; Grenseveien 92, TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, N-0663 Oslo (NO).
    [Show full text]
  • The Circular Rnome of Primary Breast Cancer
    Downloaded from genome.cshlp.org on September 28, 2021 - Published by Cold Spring Harbor Laboratory Press Research The circular RNome of primary breast cancer Marcel Smid,1 Saskia M. Wilting,1 Katharina Uhr,1 F. Germán Rodríguez-González,1 Vanja de Weerd,1 Wendy J.C. Prager-Van der Smissen,1 Michelle van der Vlugt-Daane,1 Anne van Galen,1 Serena Nik-Zainal,2,3 Adam Butler,2 Sancha Martin,2 Helen R. Davies,2 Johan Staaf,4 Marc J. van de Vijver,5 Andrea L. Richardson,6,7 Gaëten MacGrogan,8 Roberto Salgado,9,10 Gert G.G.M. van den Eynden,10,11 Colin A. Purdie,12 Alastair M. Thompson,12 Carlos Caldas,13 Paul N. Span,14 Fred C.G.J. Sweep,15 Peter T. Simpson,16 Sunil R. Lakhani,16,17 Steven Van Laere,18 Christine Desmedt,9 Angelo Paradiso,19 Jorunn Eyfjord,20 Annegien Broeks,21 Anne Vincent-Salomon,22 Andrew P. Futreal,23 Stian Knappskog,24,25 Tari King,26 Alain Viari,27,28 Anne-Lise Børresen-Dale,29,30 Hendrik G. Stunnenberg,31 Mike Stratton,2 John A. Foekens,1 Anieta M. Sieuwerts,1 and John W.M. Martens1 1Erasmus MC Cancer Institute and Cancer Genomics Netherlands, University Medical Center Rotterdam, Department of Medical Oncology, 3015GD Rotterdam, the Netherlands; 2Wellcome Trust Sanger Institute, Hinxton, Cambridge CB10 1SA, United Kingdom; 3East Anglian Medical Genetics Service, Cambridge University Hospitals NHS Foundation Trust, Cambridge CB2 9NB, United Kingdom; 4Division of Oncology and Pathology, Department of Clinical Sciences Lund, Lund University, SE-223 81 Lund, Sweden; 5Department of Pathology, Academic Medical Center, 1105AZ
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2016/0264934 A1 GALLOURAKIS Et Al
    US 20160264934A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2016/0264934 A1 GALLOURAKIS et al. (43) Pub. Date: Sep. 15, 2016 (54) METHODS FOR MODULATING AND Publication Classification ASSAYING MI6AIN STEM CELL POPULATIONS (51) Int. Cl. CI2N5/0735 (2006.01) (71) Applicants: THE GENERAL, HOSPITAL AOIN I/02 (2006.01) CORPORATION, Boston, MA (US); CI2O I/68 (2006.01) The Regents of the University of GOIN 33/573 (2006.01) California, Oakland, CA (US) CI2N 5/077 (2006.01) CI2N5/0793 (2006.01) (72) Inventors: Cosmas GIALLOURAKIS, Boston, (52) U.S. Cl. MA (US); Alan C. MULLEN, CPC ............ CI2N5/0606 (2013.01); CI2N5/0657 Brookline, MA (US); Yi XING, (2013.01); C12N5/0619 (2013.01); C12O Torrance, CA (US) I/6888 (2013.01); G0IN33/573 (2013.01); A0IN I/0226 (2013.01); C12N 2501/72 (73) Assignees: THE GENERAL, HOSPITAL (2013.01); C12N 2506/02 (2013.01); C12O CORPORATION, Boston, MA (US); 2600/158 (2013.01); C12Y 201/01062 The Regents of the University of (2013.01); C12Y 201/01 (2013.01) California, Oakland, CA (US) (57) ABSTRACT (21) Appl. No.: 15/067,780 The present invention generally relates to methods, assays and kits to maintain a human stem cell population in an (22) Filed: Mar 11, 2016 undifferentiated state by inhibiting the expression or function of METTL3 and/or METTL4, and mA fingerprint methods, assays, arrays and kits to assess the cell state of a human stem Related U.S. Application Data cell population by assessing mA levels (e.g. mA peak inten (60) Provisional application No.
    [Show full text]
  • The Tip of the Iceberg: RNA-Binding Proteins with Prion-Like Domains in Neurodegenerative Disease
    BRES-42024; No. of pages: 20; 4C: 7, 8, 10, 12, 13 BRAIN RESEARCH XX (2012) XXX– XXX Available online at www.sciencedirect.com www.elsevier.com/locate/brainres Review The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease Oliver D. Kinga,⁎, Aaron D. Gitlerb,⁎⁎, James Shorterc,⁎⁎⁎ aBoston Biomedical Research Institute, 64 Grove St., Watertown, MA 02472, USA bDepartment of Genetics, Stanford University School of Medicine, 300 Pasteur Drive, M322 Alway Building, Stanford, CA 94305-5120, USA cDepartment of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 805b Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, PA 19104, USA ARTICLE INFO ABSTRACT Article history: Prions are self-templating protein conformers that are naturally transmitted between individ- Accepted 7 January 2012 uals and promote phenotypic change. In yeast, prion-encoded phenotypes can be beneficial, neutral or deleterious depending upon genetic background and environmental conditions. A dis- Keywords: tinctive and portable ‘prion domain’ enriched in asparagine, glutamine, tyrosine and glycine res- Prion idues unifies the majority of yeast prion proteins. Deletion of this domain precludes RNA-binding protein prionogenesis and appending this domain to reporter proteins can confer prionogenicity. An al- TDP-43 gorithm designed to detect prion domains has successfully identified 19 domains that can confer FUS prion behavior. Scouring the human genome with this algorithm enriches a select group of RNA- TAF15 binding proteins harboring a canonical RNA recognition motif (RRM) and a putative prion do- EWSR1 main. Indeed, of 210 human RRM-bearing proteins, 29 have a putative prion domain, and 12 of Amyotrophic lateral sclerosis these are in the top 60 prion candidates in the entire genome.
    [Show full text]
  • (Passenger Strand of Mir-99A-Duplex) in Head and Neck Squamous Cell Carcinoma
    cells Article Regulation of Oncogenic Targets by miR-99a-3p (Passenger Strand of miR-99a-Duplex) in Head and Neck Squamous Cell Carcinoma 1, 1,2, 1 3 Reona Okada y, Keiichi Koshizuka y, Yasutaka Yamada , Shogo Moriya , Naoko Kikkawa 1,2, Takashi Kinoshita 2, Toyoyuki Hanazawa 2 and Naohiko Seki 1,* 1 Department of Functional Genomics, Chiba University Graduate School of Medicine, Chiba 260-8670, Japan; [email protected] (R.O.); [email protected] (K.K.); [email protected] (Y.Y.); [email protected] (N.K.) 2 Department of Otorhinolaryngology/Head and Neck Surgery, Chiba University Graduate School of Medicine, Chiba 260-8670, Japan; [email protected] (T.K.); [email protected] (T.H.) 3 Department of Biochemistry and Genetics, Chiba University Graduate School of Medicine, Chiba 260-8670, Japan; [email protected] * Correspondence: [email protected]; Tel.: +81-43-226-2971; Fax: +81-43-227-3442 These authors contributed equally to this work. y Received: 3 November 2019; Accepted: 27 November 2019; Published: 28 November 2019 Abstract: To identify novel oncogenic targets in head and neck squamous cell carcinoma (HNSCC), we have analyzed antitumor microRNAs (miRNAs) and their controlled molecular networks in HNSCC cells. Based on our miRNA signature in HNSCC, both strands of the miR-99a-duplex (miR-99a-5p: the guide strand, and miR-99a-3p: the passenger strand) are downregulated in cancer tissues. Moreover, low expression of miR-99a-5p and miR-99a-3p significantly predicts poor prognosis in HNSCC, and these miRNAs regulate cancer cell migration and invasion.
    [Show full text]