Dual Effects of Targeting S100A11 on Suppressing Cellular Metastatic
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SUPPLEMENTARY FIGURES LEGENDS Figure S1. (A) Gene
Supplementary material Gut SUPPLEMENTARY FIGURES LEGENDS Figure S1. (A) Gene Ontology enrichment analysis of biological processes in which selected TS/ONC identified by proteomic analysis are involved. Inter-connections between biological processes and genes involved are represented in B. Figure S2. mRNA expression of TSs/ONCs in constitutive hepatocytes-specific PTEN knockout mice. (A) qRT-PCR analyses of TS/ONC in liver tissues (4 controls and 5 LPTENKO mice) from 4-months-old control and constitutive hepatocyte-specific PTEN knockout (LPTENKO) mice. Cyclophilin-A was used to normalize qRT-PCR analyses. Data represent the mean+/-SD. (B) The mRNA level of TS/ONCO candidates identified in the proteomic analysis were investigated in a transcriptomic dataset from the Gene Expression Omnibus Database (GSE70681, LPTENKO 3-months old. For each candidate, Log2-Fold Change between Control and LPTENKO mice were calculated and represented in a heatmap. ***P<0.001, **P<0.01, and *P<0.05 (t-test). Figure S3. Hepatic steatosis and AKT phosphorylation in inducible hepatocytes-specific PTEN knockout mice (LIPTENKO). A. Hematoxylin/Eosin (H&E) staining of histological sections from 5-month old control and LIPTENKO mice treated with tamoxifen for 3 months. The protein level of PTEN, pAKTser473, pAKTthr308 and AKT were analyzed by Western Blot (B). Corresponding quantifications are reported in C. Data represent the mean +/- SD. *P<0.05, **P<0.01, ***P<0.001 compared with controls (t-test). Figure S4. Hepatic steatosis in ob/ob and db/db mice and analysis of TS/ONC mRNA expression in ob/ob mice. (A) Hematoxylin/Eosin (H&E) staining of histological sections from 2-month old Control, ob/ob and db/db (n=5-6 mice/group) mice. -
Rage (Receptor for Advanced Glycation End Products) in Melanoma
RAGE (RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS) IN MELANOMA PROGRESSION A Dissertation Submitted to the Graduate Faculty of the North Dakota State University of Agriculture and Applied Science By Varsha Meghnani In Partial Fulfillment for the Degree of DOCTOR OF PHILOSOPHY Major Department: Pharmaceutical Sciences May 2014 Fargo, North Dakota North Dakota State University Graduate School Title RAGE (RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS) IN MELANOMA PROGRESSION By VARSHA MEGHNANI The Supervisory Committee certifies that this disquisition complies with North Dakota State University’s regulations and meets the accepted standards for the degree of DOCTOR OF PHILOSOPHY SUPERVISORY COMMITTEE: ESTELLE LECLERC Chair BIN GUO STEPHEN O’ROURKE JANE SCHUH Approved: 5/22/2014 JAGDISH SINGH Date Department Chair ABSTRACT The Receptor for Advanced Glycation End Products (RAGE) and its ligands are expressed in multiple cancer types and are implicated in cancer progression. Our lab has previously reported higher transcript levels of RAGE and S100B in advanced staged melanoma patients. The contribution of RAGE in the pathophysiology of melanoma has not been well studied. Based on previous reports, we hypothesized that RAGE, when over-expressed in melanoma cells, promotes melanoma progression. To study the pathogenic role of RAGE in melanoma, a primary melanoma cell line, WM115, was selected and stably transfected with full length RAGE (FL_RAGE) to generate a model cell line over-expressing RAGE (WM115_RAGE). WM266, a sister cell line of WM115, originated from a metastatic tumor of the same patient was used as a metastatic control cell line in the study. After assessing the expression levels of RAGE in the transfected cells, the influence of RAGE on their cellular properties was examined. -
8296.Full.Pdf
Inflammation-Induced Chondrocyte Hypertrophy Is Driven by Receptor for Advanced Glycation End Products This information is current as Denise L. Cecil, Kristen Johnson, John Rediske, Martin of September 28, 2021. Lotz, Ann Marie Schmidt and Robert Terkeltaub J Immunol 2005; 175:8296-8302; ; doi: 10.4049/jimmunol.175.12.8296 http://www.jimmunol.org/content/175/12/8296 Downloaded from References This article cites 43 articles, 13 of which you can access for free at: http://www.jimmunol.org/content/175/12/8296.full#ref-list-1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 28, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2005 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Inflammation-Induced Chondrocyte Hypertrophy Is Driven by Receptor for Advanced Glycation End Products1 Denise L. Cecil,* Kristen Johnson,* John Rediske,‡ Martin Lotz,§ Ann Marie Schmidt,† and Robert Terkeltaub2* The multiligand receptor for advanced glycation end products (RAGE) mediates certain chronic vascular and neurologic degen- erative diseases accompanied by low-grade inflammation. -
(Rage) in Progression of Pancreatic Cancer
The Texas Medical Center Library DigitalCommons@TMC The University of Texas MD Anderson Cancer Center UTHealth Graduate School of The University of Texas MD Anderson Cancer Biomedical Sciences Dissertations and Theses Center UTHealth Graduate School of (Open Access) Biomedical Sciences 8-2017 INVOLVEMENT OF THE RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS (RAGE) IN PROGRESSION OF PANCREATIC CANCER Nancy Azizian MS Follow this and additional works at: https://digitalcommons.library.tmc.edu/utgsbs_dissertations Part of the Biology Commons, and the Medicine and Health Sciences Commons Recommended Citation Azizian, Nancy MS, "INVOLVEMENT OF THE RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS (RAGE) IN PROGRESSION OF PANCREATIC CANCER" (2017). The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences Dissertations and Theses (Open Access). 748. https://digitalcommons.library.tmc.edu/utgsbs_dissertations/748 This Dissertation (PhD) is brought to you for free and open access by the The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences at DigitalCommons@TMC. It has been accepted for inclusion in The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences Dissertations and Theses (Open Access) by an authorized administrator of DigitalCommons@TMC. For more information, please contact [email protected]. INVOLVEMENT OF THE RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS (RAGE) IN PROGRESSION OF PANCREATIC CANCER by Nancy -
Tudor Staphylococcal Nuclease Drives Chemoresistance of Non-Small Cell
www.impactjournals.com/oncotarget/ Oncotarget, Vol. 6, No. 14 Tudor staphylococcal nuclease drives chemoresistance of non-small cell lung carcinoma cells by regulating S100A11 Anna Zagryazhskaya1, Olga Surova1,2, Nadeem S. Akbar1, Giulia Allavena1,3, Katarina Gyuraszova1,4, Irina B. Zborovskaya5,6, Elena M. Tchevkina5,6, Boris Zhivotovsky1,6 1Institute of Environmental Medicine, Division of Toxicology, Stockholm, Sweden 2Ludwig Institute for Cancer Research Ltd, Karolinska Institutet, Stockholm, Sweden 3Department of Molecular and Developmental Medicine, University of Siena, Siena, Italy 4Institute of Biology and Ecology, Faculty of Science, Pavol Jozef Šafárik University in Košice, Košice, Slovakia 5NN Blokhin Russian Cancer Research Center, Moscow, Russia 6Faculty of Fundamental Medicine, ML Lomonosov State University, Moscow, Russia Correspondence to: Boris Zhivotovsky, e-mail: [email protected] Keywords: tudor staphylococcal nuclease, S100A11, phospholipase A2, non-small cell lung cancer, apoptosis Received: December 19, 2014 Accepted: March 07, 2015 Published: March 26, 2015 ABSTRACT Lung cancer is the leading cause of cancer-related deaths worldwide. Non-small cell lung cancer (NSCLC), the major lung cancer subtype, is characterized by high resistance to chemotherapy. Here we demonstrate that Tudor staphylococcal nuclease (SND1 or TSN) is overexpressed in NSCLC cell lines and tissues, and is important for maintaining NSCLC chemoresistance. Downregulation of TSN by RNAi in NSCLC cells led to strong potentiation of cell death in response to cisplatin. Silencing of TSN was accompanied by a significant decrease in S100A11 expression at both mRNA and protein level. Downregulation of S100A11 by RNAi resulted in enhanced sensitivity of NSCLC cells to cisplatin, oxaliplatin and 5-fluouracil. AACOCF3, a phospholipase A2 (PLA2) inhibitor, strongly abrogated chemosensitization upon silencing of S100A11 suggesting that PLA2 inhibition by S100A11 governs the chemoresistance of NSCLC. -
High RAD54B Expression: an Independent Predictor of Postoperative Distant Recurrence in Colorectal Cancer Patients
www.impactjournals.com/oncotarget/ Oncotarget, Vol. 6, No. 25 High RAD54B expression: an independent predictor of postoperative distant recurrence in colorectal cancer patients Yuzo Nagai1, Yoko Yamamoto1, Takaaki Yasuhara2, Keisuke Hata1, Takeshi Nishikawa1, Toshiaki Tanaka1, Junichiro Tanaka1, Tomomichi Kiyomatsu1, Kazushige Kawai1, Hiroaki Nozawa1, Shinsuke Kazama1, Hironori Yamaguchi1, Soichiro Ishihara1, Eiji Sunami1, Takeharu Yamanaka3, Kiyoshi Miyagawa2 and Toshiaki Watanabe1 1 Department of Surgical Oncology, Faculty of Medicine, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan 2 Laboratory of Molecular Radiology, Center for Disease Biology and Integrative Medicine, Graduate School of Medicine, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan 3 Department of Biostatistics, Graduate School of Medicine, Yokohama City University, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, Japan Correspondence to: Toshiaki Watanabe, email: [email protected] Keywords: RAD54B, colorectal cancer, homologous recombination, prognosis, distant recurrence Received: April 21, 2015 Accepted: May 09, 2015 Published: May 20, 2015 This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ABSTRACT We recently reported a specific mechanism that RAD54B, an important factor in homologous recombination, promotes genomic instability via the degradation of p53 protein in vitro. However, clinical significance of RAD54B in colorectal cancer (CRC) remains unclear. Thus we analyzed RAD54B gene expression in CRC patients. Using the training set (n = 123), the optimal cut-off value for stratification was determined, and validated in another cohort (n = 89). Kaplan–Meier plots showed that distant recurrence free survival was significantly lesser in high RAD54B expression group compared with that of low expression group in both training (P = 0.0013) and validation (P = 0.024) set. -
RAD51AP1 Compensates for the Loss of RAD54 in Homology-Directed DNA Repair
bioRxiv preprint doi: https://doi.org/10.1101/2021.07.15.452469; this version posted July 15, 2021. 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-NC-ND 4.0 International license. RAD51AP1 compensates for the loss of RAD54 in homology-directed DNA repair Platon Selemenakis1,2, Neelam Sharma1, Youngho Kwon3, Mollie Uhrig1, Patrick Sung3 and Claudia Wiese1* 1 Environmental and Radiological Health Sciences, Colorado State University, Fort Collins, Colorado, 80523, USA 2 Cell and Molecular Biology Graduate Program, Colorado State University, Fort Collins, Colorado, 80523, USA 3 Department of Biochemistry and Structural Biology, University of Texas Health San Antonio, San Antonio, Texas 78229, USA * To whom correspondence should be addressed: C.W. (email: [email protected]) 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.07.15.452469; this version posted July 15, 2021. 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-NC-ND 4.0 International license. Abstract Homology-directed repair (HDR) is a complex DNA damage repair pathway and an attractive target of inhibition in anti-cancer therapy. To develop the most efficient inhibitors of HDR in cells, it is critical to identify compensatory sub-pathways. In this study, we describe the synthetic interaction between RAD51AP1 and RAD54, two structurally unrelated proteins that function downstream of RAD51 in HDR. -
Structure of the SWI2/SNF2 Chromatin-Remodeling Domain of Eukaryotic Rad54
ARTICLES Structure of the SWI2/SNF2 chromatin-remodeling domain of eukaryotic Rad54 Nicolas H Thomä1, Bryan K Czyzewski1,2, Andrei A Alexeev3, Alexander V Mazin4, Stephen C Kowalczykowski3 & Nikola P Pavletich1,2 SWI2/SNF2 chromatin-remodeling proteins mediate the mobilization of nucleosomes and other DNA-associated proteins. SWI2/SNF2 proteins contain sequence motifs characteristic of SF2 helicases but do not have helicase activity. Instead, they couple ATP hydrolysis with the generation of superhelical torsion in DNA. The structure of the nucleosome-remodeling domain of zebrafish Rad54, a protein http://www.nature.com/nsmb involved in Rad51-mediated homologous recombination, reveals that the core of the SWI2/SNF2 enzymes consist of two ␣/-lobes similar to SF2 helicases. The Rad54 helicase lobes contain insertions that form two helical domains, one within each lobe. These insertions contain SWI2/SNF2-specific sequence motifs likely to be central to SWI2/SNF2 function. A broad cleft formed by the two lobes and flanked by the helical insertions contains residues conserved in SWI2/SNF2 proteins and motifs implicated in DNA-binding by SF2 helicases. The Rad54 structure suggests that SWI2/SNF2 proteins use a mechanism analogous to helicases to translocate on dsDNA. Cellular processes such as transcription, replication, DNA repair and breaks by Rad51-mediated homologous recombination15–20. Like other recombination require direct access to DNA. This process is facilitated SWI2/SNF2 remodeling enzymes, Rad54 can translocate on DNA, gen- by the SWI2/SNF2 family of ATPases, which detach DNA from histones erate superhelical torsion and enhance the accessibility to nucleosomal and other bound proteins1,2. The SWI2/SNF2 chromatin remodeling DNA18,19,21. -
The Pseudopeptide HB-19 Binds to Cell Surface Nucleolin and Inhibits Angiogenesis
VASCULAR CELL OPEN ACCESS | RESEARCH The pseudopeptide HB-19 binds to cell surface nucleolin and inhibits angiogenesis Charalampos Birmpas, 1 Jean Paul Briand, 2 Josẻ Courty, 3 Panagiotis Katsoris, 1, d, @ @ corresponding author, & equal contributor Vascular Cell. 2012; 4(1):21 | © Birmpas et al Received: 24 July 2012 | Accepted: 30 November 2012 | Published: 24 December 2012 Vascular Cell ISSN: 2045-824X DOI: https://doi.org/10.1186/2045-824X-4-21 Author information 1. Department of Biology - University of Patras; Patras, Greece 2. CNRS, Université Paris Est Créteil; Créteil Cedex, France 3. CNRS, Institut de Biologie Moléculaire et Cellulaire; Strasbourg, France [d] [email protected] Abstract Background Nucleolin is a protein over-expressed on the surface of tumor and endothelial cells. Recent studies have underlined the involvement of cell surface nucleolin in tumor growth and angiogenesis. This cell surface molecule serves as a receptor for various ligands implicated in pathophysiological processes such as growth factors, cell adhesion molecules like integrins, selectins or laminin-1, lipoproteins and viruses (HIV and coxsackie B). HB-19 is a synthetic multimeric pseudopeptide that binds cell surface expressed nucleolin and inhibits both tumor growth and angiogenesis. Methodology/principal findings In the present work, we further investigated the biological actions of pseudopeptide HB-19 on HUVECs. In a previous work, we have shown that HB-19 inhibits the in vivo angiogenesis on the chicken embryo CAM assay. We now provide evidence that HB-19 inhibits the in vitro adhesion, migration and proliferation of HUVECs without inducing their apoptosis. The above biological actions seem to be regulated by SRC, ERK1/2, AKT and FAK kinases as we found that HB-19 inhibits their activation in HUVECs. -
Werner Syndrome Protein Participates in a Complex with RAD51, RAD54
Erratum Werner syndrome protein participates in a complex with RAD51, RAD54, RAD54B and ATR in response to ICL-induced replication arrest Marit Otterlei, Per Bruheim, Byungchan Ahn, Wendy Bussen, Parimal Karmakar, Kathy Baynton and Vilhelm A. Bohr Journal of Cell Science 119, 5215 (2006) doi:10.1242/jcs.03359 There was an error in the first e-press version of the article published in J. Cell Sci. 119, 5137-5146. The first e-press version of this article gave the page range as 5114-5123, whereas it should have been 5137-5146. We apologise for this mistake. Research Article 5137 Werner syndrome protein participates in a complex with RAD51, RAD54, RAD54B and ATR in response to ICL-induced replication arrest Marit Otterlei1,2,*, Per Bruheim1,3,§, Byungchan Ahn1,4,§, Wendy Bussen5, Parimal Karmakar1,6, Kathy Baynton7 and Vilhelm A. Bohr1 1Laboratory of Molecular Gerontology, National Institute on Aging, NIH, 5600 Nathan Shock Dr., Baltimore, MD 21224, USA 2Department of Cancer Research and Molecular Medicine, Laboratory Centre, Faculty of Medicine, Norwegian University of Science and Technology, Erling Skjalgsons gt. 1, N-7006 Trondheim, Norway 3Department of Biotechnology, Norwegian University of Science and Technology, N-7491 Trondheim, Norway 4Department of Life Sciences, University of Ulsan, Ulsan 680-749, Korea 5Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar St, SHM-C130, New Haven, CT 06515, USA 6Department of Life Science and Biotechnology, Jadavpur University, Kolkata-700 032, WB, -
Role of Rad54, Rad54b and Snm1 in DNA Damage Repair
Role of Rad54, Rad54B and Snm1 in DNA Damage Repair De rol van Rad54, Rad54B en Snm1 in herstel van schade aan DNA Proefschrift Ter verkrijging van de graad van doctor aan de Erasmus Universiteit Rotterdam op gezag van de Rector Magnificus Prof.dr.ir. J.H. van Bemmel en volgens besluit van het College voor Promoties. De openbare verdediging zal plaatsvinden op woensdag 8 oktober 2003 om 9.45 uur door Joanna Wesoty Geboren te Poznan, Polen Promotiecommissie Promotoren: Prof.dr. R. Kanaar Prof.dr. J.H.J. Hoeijmakers Overige !eden: Prof.dr. J.A. Grootegoed Dr. G.T.J. van der Horst Prof.dr.ir. A.A. van Zeeland The work presented in this thesis was performed at the Department of Cell Biology and Genetics of Erasmus MC in Rotterdam from 1998 to 2003. The research and the printing of the thesis were financially supported by the Dutch Cancer Society. Dziadkowi i Jasiowi Contents list of abbreviations 6 Scope of the thesis 7 Chapter 1 11 DNA double-strand breaks: significance, generation, repair and link to cellular processes 1. Generation of DSBs, their significance and repair 11 2. Homologous recombination and non-homologous end joining - interplay and contribution to repair of DBSs 13 3. Biochemistry of homologous recombination 15 4. DSBs in meiosis 23 5. Non-homologous end joining 26 6. DNA rearrangements in the immune system 27 7. lnterstrand cross-links and homologous recombination 33 8. Perspective 34 Chapter 2 37 Analysis of mouse Rad54 expression and its implications for homologous recombination Chapter 3 57 Sublethal damage recovery -
The RAD51-Stimulatory Compound RS-1 Can Exploit the RAD51 Overexpression That Exists in Cancer Cells and Tumors
Author Manuscript Published OnlineFirst on April 21, 2014; DOI: 10.1158/0008-5472.CAN-13-3220 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. The RAD51-stimulatory compound RS-1 can exploit the RAD51 overexpression that exists in cancer cells and tumors Jennifer M Mason1,2, Hillary L. Logan1,2, Brian Budke1, Megan Wu1, Michal Pawlowski3, Ralph R. Weichselbaum1,4, Alan P. Kozikowski3, Douglas K. Bishop1,5,6, and Philip P. Connell1,6 1Department of Radiation and Cellular Oncology, 4Ludwig Center for Metastasis Research, 5Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 3Department of Medicinal Chemistry and Pharmacognosy, Drug Discovery Program, University of Illinois at Chicago, Chicago, IL 2These authors contributed equally 6These authors contributed equally Precis: We developed a novel therapeutic strategy that exploits the high levels of RAD51 overexpression that occur in human cancers, using the RAD51-stimulatory compound RS-1 to form genotoxic RAD51 protein complexes on undamaged chromatin. Key Words: DNA repair, Homologous recombination, RAD51, RS-1 Conflicts of interest: The authors disclose no potential conflicts of interest Running Title: RAD51-stimulatory compound kills malignant cells Correspondence should be directed to: Philip P. Connell MD Dep. of Radiation and Cellular Oncology University of Chicago 5758 S. Maryland Ave, MC 9006 Chicago, IL 60637 Phone: (773) 834-8119 Fax: (773) 702-0610 email: [email protected] 1 Downloaded from cancerres.aacrjournals.org on October 2, 2021. © 2014 American Association for Cancer Research. Author Manuscript Published OnlineFirst on April 21, 2014; DOI: 10.1158/0008-5472.CAN-13-3220 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited.