GADD45A Recombinant Protein Cat

Total Page:16

File Type:pdf, Size:1020Kb

GADD45A Recombinant Protein Cat GADD45A Recombinant Protein Cat. No.: 92-028 GADD45A Recombinant Protein Specifications SPECIES: Human SOURCE SPECIES: E. coli SEQUENCE: Met1-Arg165 FUSION TAG: N-6 His tag TESTED APPLICATIONS: APPLICATIONS: This recombinant protein can be used for biological assays. For research use only. PREDICTED MOLECULAR 20.5 kD WEIGHT: Properties Greater than 95% as determined by reducing SDS-PAGE. PURITY: Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. PHYSICAL STATE: Lyophilized Lyophilized from a 0.2 um filtered solution of 20mM PB, 150mM NaCl, pH 7.2. It is not BUFFER: recommended to reconstitute to a concentration less than 100 ug/ml. Dissolve the lyophilized protein in ddH2O. September 27, 2021 1 https://www.prosci-inc.com/gadd45a-recombinant-protein-92-028.html Lyophilized protein should be stored at -20˚C, though stable at room temperature for 3 weeks. STORAGE CONDITIONS: Reconstituted protein solution can be stored at 4-7˚C for 2-7 days. Aliquots of reconstituted samples are stable at -20˚C for 3 months. Additional Info OFFICIAL SYMBOL: GADD45A Growth Arrest and DNA Damage-Inducible Protein GADD45 Alpha, DNA Damage-Inducible ALTERNATE NAMES: Transcript 1 Protein, DDIT-1, GADD45A, DDIT1, GADD45 ACCESSION NO.: P24522 GENE ID: 1647 Background and References Growth Arrest and DNA Damage-Inducible Protein GADD45 alpha (GADD45A) is a member of the GADD45 family. GADD45A can be induced by UV irradiation, X-rays, growth arrest and alkylating agents, of which can be mediated by some kinases other BACKGROUND: than PKC. GADD45A can interact with MAPK14, GADD45GIP1, PCNA. In T-cells, GADD45A functions as a regulator of p38 MAPKs by inhibiting p88 phosphorylation and activity. GADD45A may affect PCNA interaction with some cell division protein kinase complexes, stimulating DNA excision repair in vitro and inhibits entry of cells into S phase. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 27, 2021 2 https://www.prosci-inc.com/gadd45a-recombinant-protein-92-028.html.
Recommended publications
  • DNA Damage Activates a Spatially Distinct Late Cytoplasmic Cell-Cycle Checkpoint Network Controlled by MK2-Mediated RNA Stabilization
    DNA Damage Activates a Spatially Distinct Late Cytoplasmic Cell-Cycle Checkpoint Network Controlled by MK2-Mediated RNA Stabilization The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Reinhardt, H. Christian, Pia Hasskamp, Ingolf Schmedding, Sandra Morandell, Marcel A.T.M. van Vugt, XiaoZhe Wang, Rune Linding, et al. “DNA Damage Activates a Spatially Distinct Late Cytoplasmic Cell-Cycle Checkpoint Network Controlled by MK2-Mediated RNA Stabilization.” Molecular Cell 40, no. 1 (October 2010): 34–49.© 2010 Elsevier Inc. As Published http://dx.doi.org/10.1016/j.molcel.2010.09.018 Publisher Elsevier B.V. Version Final published version Citable link http://hdl.handle.net/1721.1/85107 Terms of Use Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. Molecular Cell Article DNA Damage Activates a Spatially Distinct Late Cytoplasmic Cell-Cycle Checkpoint Network Controlled by MK2-Mediated RNA Stabilization H. Christian Reinhardt,1,6,7,8 Pia Hasskamp,1,10,11 Ingolf Schmedding,1,10,11 Sandra Morandell,1 Marcel A.T.M. van Vugt,5 XiaoZhe Wang,9 Rune Linding,4 Shao-En Ong,2 David Weaver,9 Steven A. Carr,2 and Michael B. Yaffe1,2,3,* 1David H. Koch Institute for Integrative Cancer Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02132, USA 2Broad Institute of MIT and Harvard, Cambridge, MA 02132, USA 3Center for Cell Decision Processes,
    [Show full text]
  • Expression Profiling of KLF4
    Expression Profiling of KLF4 AJCR0000006 Supplemental Data Figure S1. Snapshot of enriched gene sets identified by GSEA in Klf4-null MEFs. Figure S2. Snapshot of enriched gene sets identified by GSEA in wild type MEFs. 98 Am J Cancer Res 2011;1(1):85-97 Table S1: Functional Annotation Clustering of Genes Up-Regulated in Klf4 -Null MEFs ILLUMINA_ID Gene Symbol Gene Name (Description) P -value Fold-Change Cell Cycle 8.00E-03 ILMN_1217331 Mcm6 MINICHROMOSOME MAINTENANCE DEFICIENT 6 40.36 ILMN_2723931 E2f6 E2F TRANSCRIPTION FACTOR 6 26.8 ILMN_2724570 Mapk12 MITOGEN-ACTIVATED PROTEIN KINASE 12 22.19 ILMN_1218470 Cdk2 CYCLIN-DEPENDENT KINASE 2 9.32 ILMN_1234909 Tipin TIMELESS INTERACTING PROTEIN 5.3 ILMN_1212692 Mapk13 SAPK/ERK/KINASE 4 4.96 ILMN_2666690 Cul7 CULLIN 7 2.23 ILMN_2681776 Mapk6 MITOGEN ACTIVATED PROTEIN KINASE 4 2.11 ILMN_2652909 Ddit3 DNA-DAMAGE INDUCIBLE TRANSCRIPT 3 2.07 ILMN_2742152 Gadd45a GROWTH ARREST AND DNA-DAMAGE-INDUCIBLE 45 ALPHA 1.92 ILMN_1212787 Pttg1 PITUITARY TUMOR-TRANSFORMING 1 1.8 ILMN_1216721 Cdk5 CYCLIN-DEPENDENT KINASE 5 1.78 ILMN_1227009 Gas2l1 GROWTH ARREST-SPECIFIC 2 LIKE 1 1.74 ILMN_2663009 Rassf5 RAS ASSOCIATION (RALGDS/AF-6) DOMAIN FAMILY 5 1.64 ILMN_1220454 Anapc13 ANAPHASE PROMOTING COMPLEX SUBUNIT 13 1.61 ILMN_1216213 Incenp INNER CENTROMERE PROTEIN 1.56 ILMN_1256301 Rcc2 REGULATOR OF CHROMOSOME CONDENSATION 2 1.53 Extracellular Matrix 5.80E-06 ILMN_2735184 Col18a1 PROCOLLAGEN, TYPE XVIII, ALPHA 1 51.5 ILMN_1223997 Crtap CARTILAGE ASSOCIATED PROTEIN 32.74 ILMN_2753809 Mmp3 MATRIX METALLOPEPTIDASE
    [Show full text]
  • Gadd45a Regulates B-Catenin Distribution and Maintains Cell–Cell Adhesion/ Contact
    Oncogene (2007) 26, 6396–6405 & 2007 Nature Publishing Group All rights reserved 0950-9232/07 $30.00 www.nature.com/onc ORIGINAL ARTICLE Gadd45a regulates b-catenin distribution and maintains cell–cell adhesion/ contact JJi1, R Liu1, T Tong, Y Song, S Jin, M Wu and Q Zhan State Key Laboratory of Molecular Oncology, Cancer Institute, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, PR China Gadd45a,a growth arrest and DNA-damage gene,plays 1999;Jin et al., 2000;Tong et al., 2005). Gadd45a important roles in the control of cell cycle checkpoints, also plays roles in negative regulation of cell malig- DNA repair and apoptosis. We show here that Gadd45a is nancy. Mouse embryonic fibroblasts (MEFs) derived involved in the control of cell contact inhibition and cell– from Gadd45a-null mice exhibited genomic instability, cell adhesion. Gadd45a can serve as an adapter to enhance single oncogene-mediated transformation, loss of nor- the interaction between b-catenin and Caveolin-1,and in mal cellular senescence, increased cellular proliferation, turn induces b-catenin translocation to cell membrane for centrosome amplification and reduced DNA repair maintaining cell–cell adhesion/contact inhibition. This is (Hollander et al., 1999;Smith et al., 2000). Gadd45a- coupled with reduction of b-catenin in cytoplasm and null mice have an increased frequency of tumorigenesis nucleus following Gadd45a induction,which is reflected by by ionizing radiation (IR), ultraviolet radiation (UVR) the downregulation of cyclin D1,one of the b-catenin and dimethylbenzanthracene (DMBA), although these targeted genes. Additionally,Gadd45a facilitates ultra- mice do not develop spontaneous tumors (Hollander violet radiation-induced degradation of cytoplasmic and et al., 1999, 2001;Hildesheim et al., 2002).
    [Show full text]
  • DNA Excision Repair Proteins and Gadd45 As Molecular Players for Active DNA Demethylation
    Cell Cycle ISSN: 1538-4101 (Print) 1551-4005 (Online) Journal homepage: http://www.tandfonline.com/loi/kccy20 DNA excision repair proteins and Gadd45 as molecular players for active DNA demethylation Dengke K. Ma, Junjie U. Guo, Guo-li Ming & Hongjun Song To cite this article: Dengke K. Ma, Junjie U. Guo, Guo-li Ming & Hongjun Song (2009) DNA excision repair proteins and Gadd45 as molecular players for active DNA demethylation, Cell Cycle, 8:10, 1526-1531, DOI: 10.4161/cc.8.10.8500 To link to this article: http://dx.doi.org/10.4161/cc.8.10.8500 Published online: 15 May 2009. Submit your article to this journal Article views: 135 View related articles Citing articles: 92 View citing articles Full Terms & Conditions of access and use can be found at http://www.tandfonline.com/action/journalInformation?journalCode=kccy20 Download by: [University of Pennsylvania] Date: 27 April 2017, At: 12:48 [Cell Cycle 8:10, 1526-1531; 15 May 2009]; ©2009 Landes Bioscience Perspective DNA excision repair proteins and Gadd45 as molecular players for active DNA demethylation Dengke K. Ma,1,2,* Junjie U. Guo,1,3 Guo-li Ming1-3 and Hongjun Song1-3 1Institute for Cell Engineering; 2Department of Neurology; and 3The Solomon Snyder Department of Neuroscience; Johns Hopkins University School of Medicine; Baltimore, MD USA Abbreviations: DNMT, DNA methyltransferases; PGCs, primordial germ cells; MBD, methyl-CpG binding protein; NER, nucleotide excision repair; BER, base excision repair; AP, apurinic/apyrimidinic; SAM, S-adenosyl methionine Key words: DNA demethylation, Gadd45, Gadd45a, Gadd45b, Gadd45g, 5-methylcytosine, deaminase, glycosylase, base excision repair, nucleotide excision repair DNA cytosine methylation represents an intrinsic modifica- silencing of gene activity or parasitic genetic elements (Fig.
    [Show full text]
  • Gadd45a Levels in Human Breast Cancer Are Hormone Receptor Dependent Jennifer S Tront1, Alliric Willis2, Yajue Huang3, Barbara Hoffman1,4 and Dan a Liebermann1,4*
    Tront et al. Journal of Translational Medicine 2013, 11:131 http://www.translational-medicine.com/content/11/1/131 RESEARCH Open Access Gadd45a levels in human breast cancer are hormone receptor dependent Jennifer S Tront1, Alliric Willis2, Yajue Huang3, Barbara Hoffman1,4 and Dan A Liebermann1,4* Abstract Background: Gadd45a is a member of the Gadd45 family of genes that are known stress sensors. Gadd45a has been shown to serve as an effector in oncogenic stress in breast carcinogenesis in murine models. The present study was aimed at clarifying the expression of Gadd45a in human breast cancer and its correlation with clinicopathologic features. Methods: The expression levels of Gadd45a in breast tissue samples of female breast surgery cases were examined by immunohistochemistry (IHC) using a Gadd45a antibody. Percent staining was determined and statistical analyses were applied to determine prognostic correlations. Results: 56 female breast surgery cases were studied: Normal (11), Luminal A (9), Luminal B (11), HER2+ (10), Triple Negative (15). There was a highly significant difference in percent Gadd45a staining between groups [Mean]: Normal 16.3%; Luminal A 65.3%; Luminal B 80.7%; HER2+ 40.5%; TN 32%, P < 0.001, ANOVA. Gadd45a IHC levels for Normal cases found 82% negative/low. Luminal A breast cancer cases were found to be 67% high. Luminal B breast cancers were 100% high. Her2+ cases were 50% negative/low. Triple Negative cases were 67% negative/low. This difference in distribution of Gadd45a levels across breast cancer receptor subtypes was significant, P = 0.0009. Conclusions: Gadd45a levels are significantly associated with hormone receptor status in human breast cancer.
    [Show full text]
  • The Functional Diversity of Aurora Kinases: a Comprehensive Review
    Willems et al. Cell Div (2018) 13:7 https://doi.org/10.1186/s13008-018-0040-6 Cell Division REVIEW Open Access The functional diversity of Aurora kinases: a comprehensive review Estelle Willems1, Matthias Dedobbeleer1, Marina Digregorio1, Arnaud Lombard1,2, Paul Noel Lumapat1,3 and Bernard Rogister1,3* Abstract Aurora kinases are serine/threonine kinases essential for the onset and progression of mitosis. Aurora members share a similar protein structure and kinase activity, but exhibit distinct cellular and subcellular localization. AurA favors the G2/M transition by promoting centrosome maturation and mitotic spindle assembly. AurB and AurC are chromo- some-passenger complex proteins, crucial for chromosome binding to kinetochores and segregation of chromo- somes. Cellular distribution of AurB is ubiquitous, while AurC expression is mainly restricted to meiotically-active germ cells. In human tumors, all Aurora kinase members play oncogenic roles related to their mitotic activity and promote cancer cell survival and proliferation. Furthermore, AurA plays tumor-promoting roles unrelated to mitosis, includ- ing tumor stemness, epithelial-to-mesenchymal transition and invasion. In this review, we aim to understand the functional interplay of Aurora kinases in various types of human cells, including tumor cells. The understanding of the functional diversity of Aurora kinases could help to evaluate their relevance as potential therapeutic targets in cancer. Keywords: Aurora kinase, Mitosis, Cancer Mitosis poles move apart to separate the two sets of sister chro- In physiological conditions, mitosis is induced by activa- matids. Te movements of the sister chromatids and tion of the Cyclin B1-CDK1 complex, which controls the spindle poles are both mediated through kinetochore and transition of the G2/M checkpoint.
    [Show full text]
  • Title Tap73-Mediated the Activation of C-Jun N-Terminal Kinase Enhances
    CORE Metadata, citation and similar papers at core.ac.uk Provided by HKU Scholars Hub TAp73-mediated the activation of C-jun N-terminal kinase Title enhances cellular chemosensitivity to cisplatin in ovarian cancer cells Author(s) Zhang, P; Liu, SS; Ngan, HYS Citation PLoS One, 2012, v. 7 n. 8, article no. e42985 Issued Date 2012 URL http://hdl.handle.net/10722/173380 Rights Creative Commons: Attribution 3.0 Hong Kong License TAp73-Mediated the Activation of C-Jun N-Terminal Kinase Enhances Cellular Chemosensitivity to Cisplatin in Ovarian Cancer Cells Pingde Zhang, Stephanie Si Liu, Hextan Yuen Sheung Ngan* Department of Obstetrics and Gynecology, LKS Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, People’s Republic of China Abstract P73, one member of the tumor suppressor p53 family, shares highly structural and functional similarity to p53. Like p53, the transcriptionally active TAp73 can mediate cellular response to chemotherapeutic agents in human cancer cells by up- regulating the expressions of its pro-apoptotic target genes such as PUMA, Bax, NOXA. Here, we demonstrated a novel molecular mechanism for TAp73-mediated apoptosis in response to cisplatin in ovarian cancer cells, and that was irrespective of p53 status. We found that TAp73 acted as an activator of the c-Jun N-terminal kinase (JNK) signaling pathway by up-regulating the expression of its target growth arrest and DNA-damage-inducible protein GADD45 alpha (GADD45a) and subsequently activating mitogen-activated protein kinase kinase-4 (MKK4). Inhibition of JNK activity by a specific inhibitor or small interfering RNA (siRNA) significantly abrogated TAp73-mediated apoptosis induced by cisplatin.
    [Show full text]
  • Inactivation of Gadd45a Sensitizes Epithelial Cancer Cells to Ionizing Radiation in Vivo Resulting in Prolonged Survival
    Research Article Inactivation of gadd45a Sensitizes Epithelial Cancer Cells to Ionizing Radiation In vivo Resulting in Prolonged Survival Xiangdong Lu,1 Chunyu Yang,1 Reginald Hill,1 Chaoyin Yin,1 M. Christine Hollander,2 Albert J. Fornace, Jr.,3 and Terry Van Dyke1 1Lineberger Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina; 2Division of Basic Science, National Cancer Institute, NIH, Bethesda, Maryland; and 3Lombardi Cancer Center, Georgetown University, Washington, District of Columbia Abstract For example, gadd45a deficiency causes defective UV-induced nucleotide excision repair (4). Gadd45a participates in the proper Ionizing radiation (IR) therapy is one of the most commonly used treatments for cancer patients. The responses of tumor control of the G2-M checkpoint in response to UV radiation and of cells to IR are often tissue specific and depend on pathway the S-phase checkpoint under multiple conditions of nutrient aberrations present in the tumor. Identifying molecules and deprivation (5–7). Gadd45a-null mouse embryonic fibroblast cells mechanisms that sensitize tumor cells to IR provides new exhibit increasedaneuploidyaccompaniedwith abnormal centro- potential therapeutic strategies for cancer treatment. In this mere amplification; when exposedto IR, gadd45a knockout mice also study, we used two genetically engineered mouse carcinoma show increasedlymphomagenesis comparedwith control mice (8). models, brain choroid plexus carcinoma (CPC) and prostate, Interestingly, in vivo studies have shown that gadd45a inactivation to test the effect of inactivating gadd45a, a DNA damage also causes abnormal p38 mitogen-activatedprotein kinase phos- response p53 target gene, on tumor responses to IR. We show phorylation, T-cell hyperproliferation, anda lupus-like autoimmune disease in mice (9, 10).
    [Show full text]
  • DNA Damage Response Induced by Etoposide Promotes Steroidogenesis Via GADD45A in Cultured Adrenal Cells
    www.nature.com/scientificreports OPEN DNA damage response induced by Etoposide promotes steroidogenesis via GADD45A in Received: 29 August 2017 Accepted: 12 June 2018 cultured adrenal cells Published: xx xx xxxx Mimi Tamamori-Adachi1, Akane Koga1,2, Takao Susa1, Hiroko Fujii1,3, Masao Tsuchiya2, Hiroko Okinaga4, Harumi Hisaki1, Masayoshi Iizuka1, Shigetaka Kitajima5 & Tomoki Okazaki1 Glucocorticoid production is regulated by adrenocorticotropic hormone (ACTH) via the cyclic adenosine monophosphate (cAMP)/protein kinase A (PKA) pathway in the adrenal cortex, but the changes in steroidogenesis associated with aging are unknown. In this study, we show that cell-autonomous steroidogenesis is induced by non-ACTH- mediated genotoxic stress in human adrenocortical H295R cells. Low-dose etoposide (EP) was used to induce DNA damage as a genotoxic stress, leading to cellular senescence. We found that steroidogenesis was promoted in cells stained with γH2AX, a marker of DNA damaged cells. Among stress-associated and p53-inducible genes, the expression of GADD45A and steroidogenesis-related genes was signifcantly upregulated. Immunofuorescence analysis revealed that GADD45A accumulated in the nuclei. Metabolite assay using cultured media showed that EP-treated cells were induced to produce and secrete considerable amounts of glucocorticoid. Knockdown of GADD45A using small interfering RNA markedly inhibited the EP-induced upregulation of steroidogenesis-related gene expression, and glucocorticoid production. A p38MAPK inhibitor, but not a PKA inhibitor, suppressed EP-stimulated steroidogenesis. These results suggest that DNA damage itself promotes steroidogenesis via one or more unprecedented non-ACTH-mediated pathway. Specifcally, GADD45A plays a crucial role in the steroidogenic processes triggered by EP-stimulated genotoxic stress. Our study sheds new light on an alternate mechanism of steroidogenesis in the adrenal cortex.
    [Show full text]
  • A Novel Nupr1-Aurora Kinase a Pathway Provides Protection Against Metabolic Stress-Mediated Autophagic-Associated Cell Death
    Author Manuscript Published OnlineFirst on August 16, 2012; DOI: 10.1158/1078-0432.CCR-12-0026 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. A novel Nupr1-Aurora kinase A pathway provides protection against metabolic stress-mediated autophagic-associated cell death Tewfik Hamidi1, Carla E Cano1, Daniel Grasso1, Maria Noé Garcia1, Maria José Sandi1, Ezequiel L Calvo2, Jean-Charles Dagorn1, Gwen Lomberk3, Raul Urrutia3, Sandro Goruppi4, Arkaitz Carracedo5,6, Guillermo Velasco7,8, Juan L Iovanna1. 1INSERM U.624, Stress Cellulaire, Parc Scientifique et Technologique de Luminy, Marseille, France; 2Molecular Endocrinology and Oncology Research Center, CHUL Research Center, Quebec, Canada; 3Laboratory of Epigenetics and Chromatin Dynamics, Gastroenterology Research Unit, Departments of Biochemistry and Molecular Biology, Biophysics, and Medicine, Mayo Clinic, Rochester, USA; 4MCRI, Tufts Medical Center and Department of Medicine, Tufts University School of Medicine, Boston, USA; 5CIC bioGUNE, Bizkaia technology park, Derio, Spain; 6IKERBASQUE, Basque Foundation for Science; 7Department of Biochemistry and Molecular Biology I, School of Biology, Complutense University, Madrid, Spain; 8Instituto de Investigación Sanitaria del Hospital Clínico San Carlos (IdISSC), Madrid, Spain Short title: Nupr1-Aurora kinase A pathway The authors declare no conflicts of interest Corresponding author: Juan L Iovanna, INSERM U.624, Stress Cellulaire, 163 Avenue de Luminy, CP 915, 13288 Marseille cedex 9, France. Tel (33) 491 828803. Fax (33) 491 826083. e-mail: [email protected] 1 Downloaded from clincancerres.aacrjournals.org on September 26, 2021. © 2012 American Association for Cancer Research. Author Manuscript Published OnlineFirst on August 16, 2012; DOI: 10.1158/1078-0432.CCR-12-0026 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited.
    [Show full text]
  • Mutations in the RAS-BRAF-MAPK-ERK Pathway
    Chronic Lymphocytic Leukemia SUPPLEMENTARY APPENDIX Mutations in the RAS-BRAF-MAPK-ERK pathway define a specific subgroup of patients with adverse clinical features and provide new therapeutic options in chronic lymphocytic leukemia Neus Giménez, 1,2 * Alejandra Martínez-Trillos, 1,3 * Arnau Montraveta, 1 Mónica Lopez-Guerra, 1,4 Laia Rosich, 1 Ferran Nadeu, 1 Juan G. Valero, 1 Marta Aymerich, 1,4 Laura Magnano, 1,4 Maria Rozman, 1,4 Estella Matutes, 4 Julio Delgado, 1,3 Tycho Baumann, 1,3 Eva Gine, 1,3 Marcos González, 5 Miguel Alcoceba, 5 M. José Terol, 6 Blanca Navarro, 6 Enrique Colado, 7 Angel R. Payer, 7 Xose S. Puente, 8 Carlos López-Otín, 8 Armando Lopez-Guillermo, 1,3 Elias Campo, 1,4 Dolors Colomer 1,4 ** and Neus Villamor 1,4 ** 1Institut d’Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), CIBERONC, Barcelona; 2Anaxomics Biotech, Barcelona; 3Hematol - ogy Department and 4Hematopathology Unit, Hospital Clinic, Barcelona; 5Hematology Department, University Hospital- IBSAL, and In - stitute of Molecular and Cellular Biology of Cancer, University of Salamanca, CIBERONC; 6Hematology Department, Hospital Clínico Universitario, Valencia: 7Hematology Department, Hospital Universitario Central de Asturias, Oviedo, and 8Departamento de Bio - química y Biología Molecular, Instituto Universitario de Oncología, Universidad de Oviedo, CIBERONC, Spain. *NG and AM-T contributed equally to the study. **DC and NV share senior authorship of the manuscript. ©2019 Ferrata Storti Foundation. This is an open-access paper. doi:10.3324/haematol. 2018.196931 Received: May 1, 2018. Accepted: September 26, 2018. Pre-published: September 27, 2018. Correspondence: DOLORS COLOMER [email protected] Supplemental data METHODS Primary CLL cells Cells were isolated from peripheral blood (PB) samples by Ficoll-Paque sedimentation (GE-Healthcare, Chicago, IL, USA).
    [Show full text]
  • NAC-1, a Potential Stem Cell Pluripotency Factor, Contributes to Paclitaxel Resistance in Ovarian Cancer Through Inactivating Gadd45 Pathway
    Oncogene (2009) 28, 1941–1948 & 2009 Macmillan Publishers Limited All rights reserved 0950-9232/09 $32.00 www.nature.com/onc ORIGINAL ARTICLE NAC-1, a potential stem cell pluripotency factor, contributes to paclitaxel resistance in ovarian cancer through inactivating Gadd45 pathway N Jinawath1, C Vasoontara1, K-L Yap1, MM Thiaville1, K Nakayama2, T-L Wang1 andI-M Shih 1 1Departments of Pathology, Oncology, and Gynecology and Obstetrics, Johns Hopkins Medical Institutions, Baltimore, MD, USA and 2Department of Gynecology and Obstetrics, Shimane University, Izumo, Japan Nucleus accumbens-1 (Nac1 or NAC-1) belongs to the 22 430 new cases and15 280 deathsin 2007 (Jemal et al., BTB/POZ (Pox virus and Zinc finger/Bric-a-brac Tram- 2007). Unlike other histological types of ovarian track Broad complex) transcription factor family and is a epithelial tumors, high-grade serous carcinoma is the novel protein that potentially participates in self-renewal most aggressive andmost rapidly growing neoplasm, and pluripotency in embryonic stem cells. In human andhas a 5-year survival rate below 30%. Patients with cancer, NAC-1 is upregulated in several types of high-grade serous carcinomas always present their neoplasms, but particularly in recurrent chemoresistant diseases at the advanced stages. These patients routinely ovarian carcinomas, suggesting a biological role for NAC- receive cytoreduction surgery followed by a combined 1 in the development of drug resistance in ovarian cancer. carboplatin/paclitaxel chemotherapy regimen. Despite We have assessed this possibility and shown a correlation initial responsiveness to the chemotherapeutic drugs, between NAC-1 expression and ex vivo paclitaxel most patients eventually develop chemoresistant tumors resistance in ovarian serous carcinoma tissues and cell andsuccumb to their diseases.Therefore, treatment lines.
    [Show full text]