A Balanced Transcription Between Telomerase and the Telomeric DNA
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Regulates Cellular Telomerase Activity by Methylation of TERT Promoter
www.impactjournals.com/oncotarget/ Oncotarget, 2017, Vol. 8, (No. 5), pp: 7977-7988 Research Paper Tianshengyuan-1 (TSY-1) regulates cellular Telomerase activity by methylation of TERT promoter Weibo Yu1, Xiaotian Qin2, Yusheng Jin1, Yawei Li2, Chintda Santiskulvong3, Victor Vu1, Gang Zeng4,5, Zuofeng Zhang6, Michelle Chow1, Jianyu Rao1,5 1Department of Pathology and Laboratory Medicine, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA 2Beijing Boyuantaihe Biological Technology Co., Ltd., Beijing, China 3Genomics Core, Cedars-Sinai Medical Center, Los Angeles, CA, USA 4Department of Urology, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA 5Jonsson Comprehensive Cancer Center, University of California at Los Angeles, Los Angeles, CA, USA 6Department of Epidemiology, School of Public Health, University of California at Los Angeles, Los Angeles, CA, USA Correspondence to: Jianyu Rao, email: [email protected] Keywords: TSY-1, hematopoietic cells, Telomerase, TERT, methylation Received: September 08, 2016 Accepted: November 24, 2016 Published: December 15, 2016 ABSTRACT Telomere and Telomerase have recently been explored as anti-aging and anti- cancer drug targets with only limited success. Previously we showed that the Chinese herbal medicine Tianshengyuan-1 (TSY-1), an agent used to treat bone marrow deficiency, has a profound effect on stimulating Telomerase activity in hematopoietic cells. Here, the mechanism of TSY-1 on cellular Telomerase activity was further investigated using HL60, a promyelocytic leukemia cell line, normal peripheral blood mononuclear cells, and CD34+ hematopoietic stem cells derived from umbilical cord blood. TSY-1 increases Telomerase activity in normal peripheral blood mononuclear cells and CD34+ hematopoietic stem cells with innately low Telomerase activity but decreases Telomerase activity in HL60 cells with high intrinsic Telomerase activity, both in a dose-response manner. -
NBN Gene Analysis and It's Impact on Breast Cancer
Journal of Medical Systems (2019) 43: 270 https://doi.org/10.1007/s10916-019-1328-z IMAGE & SIGNAL PROCESSING NBN Gene Analysis and it’s Impact on Breast Cancer P. Nithya1 & A. ChandraSekar1 Received: 8 March 2019 /Accepted: 7 May 2019 /Published online: 5 July 2019 # Springer Science+Business Media, LLC, part of Springer Nature 2019 Abstract Single Nucleotide Polymorphism (SNP) researches have become essential in finding out the congenital relationship of structural deviations with quantitative traits, heritable diseases and physical responsiveness to different medicines. NBN is a protein coding gene (Breast Cancer); Nibrin is used to fix and rebuild the body from damages caused because of strand breaks (both singular and double) associated with protein nibrin. NBN gene was retrieved from dbSNP/NCBI database and investigated using computational SNP analysis tools. The encrypted region in SNPs (exonal SNPs) were analyzed using software tools, SIFT, Provean, Polyphen, INPS, SNAP and Phd-SNP. The 3’ends of SNPs in un-translated region were also investigated to determine the impact of binding. The association of NBN gene polymorphism leads to several diseases was studied. Four SNPs were predicted to be highly damaged in coding regions which are responsible for the diseases such as, Aplastic Anemia, Nijmegan breakage syndrome, Microsephaly normal intelligence, immune deficiency and hereditary cancer predisposing syndrome (clivar). The present study will be helpful in finding the suitable drugs in future for various diseases especially for breast cancer. Keywords NBN . Single nucleotide polymorphism . Double strand breaks . nsSNP . Associated diseases Introduction NBN has a more complex structure due to its interaction with large proteins formed from the ATM gene which is NBN (Nibrin) is a protein coding gene, it is also known as highly essential in identifying damaged strands of DNA NBS1, Cell cycle regulatory Protein P95, is situated on and facilitating their repair [1]. -
Anti-TERF2 / Trf2 Antibody (ARG59099)
Product datasheet [email protected] ARG59099 Package: 50 μg anti-TERF2 / Trf2 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes TERF2 / Trf2 Tested Reactivity Hu, Rat Tested Application IHC-P, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name TERF2 / Trf2 Antigen Species Human Immunogen Recombinant protein corresponding to A81-K287 of Human TERF2 / Trf2. Conjugation Un-conjugated Alternate Names Telomeric DNA-binding protein; TRF2; TTAGGG repeat-binding factor 2; TRBF2; Telomeric repeat- binding factor 2 Application Instructions Application table Application Dilution IHC-P 0.5 - 1 µg/ml WB 0.1 - 0.5 µg/ml Application Note IHC-P: Antigen Retrieval: By heat mediation. * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Calculated Mw 60 kDa Properties Form Liquid Purification Affinity purification with immunogen. Buffer 0.9% NaCl, 0.2% Na2HPO4, 0.05% Sodium azide and 5% BSA. Preservative 0.05% Sodium azide Stabilizer 5% BSA Concentration 0.5 mg/ml Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C or below. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. www.arigobio.com 1/3 Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol TERF2 Gene Full Name telomeric repeat binding factor 2 Background This gene encodes a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. -
TRF2-Mediated ORC Recruitment Underlies Telomere Stability Upon DNA Replication Stress
bioRxiv preprint doi: https://doi.org/10.1101/2021.02.08.430303; this version posted February 8, 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 4.0 International license. 1 TRF2-mediated ORC recruitment underlies telomere stability upon DNA replication stress 2 3 Mitsunori Higa,1 Yukihiro Matsuda,1 Jumpei Yamada,1 Nozomi Sugimoto,1 Kazumasa Yoshida,1,* and 4 Masatoshi Fujita1,* 5 6 1Department of Cellular Biochemistry, Graduate SChool of PharmaCeutiCal SCiences, Kyushu 7 University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan 8 9 *Correspondence to: Kazumasa Yoshida, Department of Cellular Biochemistry, Graduate SChool of 10 PharmaCeutiCal SCiences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan; 11 Tel: +81-92-642-6635; Fax: +81-92-642-6635; E-mail: [email protected] 12 13 *Correspondence to: Masatoshi Fujita, Department of Cellular Biochemistry, Graduate SChool of 14 PharmaCeutiCal SCiences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan; 15 Tel: +81-92-642-6635; Fax: +81-92-642-6635; E-mail: [email protected] 16 17 Keywords: MCM /ORC / RepliCation stress / Telomere / TRF2 18 Running title: TRF2-ORC ensures telomere stability 19 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.02.08.430303; this version posted February 8, 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. -
Abnormal Function of Telomere Protein TRF2 Induces Cell Mutation and the Effects of Environmental Tumor‑Promoting Factors (Review)
ONCOLOGY REPORTS 46: 184, 2021 Abnormal function of telomere protein TRF2 induces cell mutation and the effects of environmental tumor‑promoting factors (Review) ZHENGYI WANG1‑3 and XIAOYING WU4 1Good Clinical Practice Center, Sichuan Academy of Medical Sciences and Sichuan Provincial People's Hospital, Chengdu, Sichuan 610071; 2Institute of Laboratory Animals of Sichuan Academy of Medical Sciences and Sichuan Provincial People's Hospital; 3Yinglongwan Laboratory Animal Research Institute, Zhonghe Community, High‑Tech Zone, Chengdu, Sichuan 610212; 4Ministry of Education and Training, Chengdu Second People's Hospital, Chengdu, Sichuan 610000, P.R. China Received March 24, 2021; Accepted June 14, 2021 DOI: 10.3892/or.2021.8135 Abstract. Recent studies have found that somatic gene muta‑ microenvironment, and maintains the stemness characteris‑ tions and environmental tumor‑promoting factors are both tics of tumor cells. TRF2 levels are abnormally elevated by a indispensable for tumor formation. Telomeric repeat‑binding variety of tumor control proteins, which are more conducive factor (TRF)2 is the core component of the telomere shelterin to the protection of telomeres and the survival of tumor cells. complex, which plays an important role in chromosome In brief, the various regulatory mechanisms which tumor cells stability and the maintenance of normal cell physiological rely on to survive are organically integrated around TRF2, states. In recent years, TRF2 and its role in tumor forma‑ forming a regulatory network, which is conducive to the tion have gradually become a research hot topic, which has optimization of the survival direction of heterogeneous tumor promoted in‑depth discussions into tumorigenesis and treat‑ cells, and promotes their survival and adaptability. -
Overexpression of TP53, TP53I3 and BIRC5, Alterations of Gene Regulation of Apoptosis and Aging of Human Immune Cells in a Remote Period After Radiation Exposure
КЛІНІЧНІ ДОСЛІДЖЕННЯ ISSN 23048336. Проблеми радіаційної медицини та радіобіології = Problems of radiation medicine and radiobiology. 2016. Вип. 21. UDC I. N. Ilienko✉, D. A. Bazyka State Institution «National Research Center for Radiation Medicine of the National Academy of Medical Sciences of Ukraine», Melnykov str., 53, Kyiv, 04050, Ukraine Overexpression of TP53, TP53I3 and BIRC5, alterations of gene regulation of apoptosis and aging of human immune cells in a remote period after radiation exposure Objective. To identify a contributive role of changes in gene regulation of apoptosis and telomere length at tran& scriptional and translational levels to the formation of radiation&induced effects in immune system. Patients and Methods. Study groups included 310 Chornobyl (Chornobyl) cleanup workers (dose of external expo& sure (360.82 ± 32.3) mSv; age 58.9 ± 0.6 (M ± SD) years) and control (n = 77; age (52.9 ± 0.64) (M ± SD) years). Expression of CD95, phosphatidylserine receptors, bcl2 and p53 proteins was studied by flow cytometry; the relative expression (RQ) of BAX, BIRC5, FASLG, MADD, MAPK14, TP53, TP53I3, TERT, TERF1, TERF2 genes was performed using 7900 HT Fast RT&PCR System and TagMan technology. Relative telomere length (RTL) was quantified by flow&FISH assay. Results. Dose&dependent deregulation of apoptosis was shown at transcriptional level (TP53, TP53 I3, BAX, BIRC5, FASL genes) and translational level (bcl&2 and p53 proteins) with blocking entry to apoptosis, dose&dependent activation of anti&apoptotic proteins and TP53&mediated expression of genes&inhibitors of apoptosis. After exposure below 100 mSv a decrease in TERT gene RQ was associated with shortened telomeres, after exposure to doses over 500 mSv the TERT RQ and RTL increase were associated with imbalance in TERF1 and TERF2 genes expression. -
Anti-TERF2 / Trf2 Antibody (ARG59098)
Product datasheet [email protected] ARG59098 Package: 100 μl anti-TERF2 / Trf2 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes TERF2 / Trf2 Tested Reactivity Hu, Ms Tested Application WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name TERF2 / Trf2 Antigen Species Human Immunogen Recombinant protein of Human TERF2 / Trf2. Conjugation Un-conjugated Alternate Names Telomeric DNA-binding protein; TRF2; TTAGGG repeat-binding factor 2; TRBF2; Telomeric repeat- binding factor 2 Application Instructions Application table Application Dilution WB 1:500 - 1:2000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control Jurkat Calculated Mw 60 kDa Observed Size 70kDa Properties Form Liquid Purification Affinity purified. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol. Preservative 0.02% Sodium azide Stabilizer 50% Glycerol Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol TERF2 Gene Full Name telomeric repeat binding factor 2 Background This gene encodes a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. This protein is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. -
Clinically Annotated Breast, Ovarian and Pancreatic Cancer
www.nature.com/scientificreports OPEN MetaGxData: Clinically Annotated Breast, Ovarian and Pancreatic Cancer Datasets and their Use in Received: 19 November 2018 Accepted: 31 May 2019 Generating a Multi-Cancer Gene Published: xx xx xxxx Signature Deena M. A. Gendoo 1, Michael Zon2,4, Vandana Sandhu2, Venkata S. K. Manem2,3,5, Natchar Ratanasirigulchai2, Gregory M. Chen2, Levi Waldron 6 & Benjamin Haibe- Kains2,3,7,8,9 A wealth of transcriptomic and clinical data on solid tumours are under-utilized due to unharmonized data storage and format. We have developed the MetaGxData package compendium, which includes manually-curated and standardized clinical, pathological, survival, and treatment metadata across breast, ovarian, and pancreatic cancer data. MetaGxData is the largest compendium of curated transcriptomic data for these cancer types to date, spanning 86 datasets and encompassing 15,249 samples. Open access to standardized metadata across cancer types promotes use of their transcriptomic and clinical data in a variety of cross-tumour analyses, including identifcation of common biomarkers, and assessing the validity of prognostic signatures. Here, we demonstrate that MetaGxData is a fexible framework that facilitates meta-analyses by using it to identify common prognostic genes in ovarian and breast cancer. Furthermore, we use the data compendium to create the frst gene signature that is prognostic in a meta-analysis across 3 cancer types. These fndings demonstrate the potential of MetaGxData to serve as an important resource in oncology research, and provide a foundation for future development of cancer-specifc compendia. Ovarian, breast and pancreatic cancers are among the leading causes of cancer deaths among women, and recent studies have identifed biological and molecular commonalities between them1–4. -
An R2R3-Type MYB Transcription Factor MYB103 Is Involved in Phosphate Remobilization in Arabidopsis Thaliana
An R2R3-type MYB transcription factor MYB103 is involved in phosphate remobilization in Arabidopsis thaliana Fangwei Yu Jiangsu Academy of Agricultural Sciences Shenyun Wang Jiangsu Academy of Agricultural Sciences Wei Zhang Jiangsu Academy of Agricultural Sciences Hong Wang Jiangsu Academy of Agricultural Sciences Li Yu Jiangsu Academy of Agricultural Sciences Zhangjun Fei Boyce Thompson Institute Jianbin Li ( [email protected] ) Jiangsu Academy of Agricultural Sciences https://orcid.org/0000-0002-0592-5112 Research article Keywords: Arabidopsis, Cell wall, Ethylene, Phosphorus (P), MYB103 Posted Date: October 30th, 2019 DOI: https://doi.org/10.21203/rs.2.16579/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/18 Abstract Background The MYB transcription factor (MYB TF) family has been reported to be involved in the regulation of biotic and abiotic stresses in plants. However, the involvement of MYB TF in phosphate remobilization under phosphate deciency remains largely unexplored. Results Here, we showed that an R2R3 type MYB transcription factor, MYB103, was involved in the tolerance to P deciency in Arabidopsis thaliana . AtMYB103 was induced by P deciency, and loss function of AtMYB103 signicantly enhanced sensitivity to P deciency, as root and shoot biomass and soluble P content in the myb103 mutant were signicantly lower than those in wild-type (WT) plants under the P-decient condition. Furthermore, the expression of Pi deciency -responsive genes was more profound in myb103 than in WT. In addition, AtMYB103 may also be involved in the cell wall-based P reutilization, as less P was released from the cell wall in myb103 than in WT, which was in company with a reduction of the ethylene production. -
The Shelterin Complex and Hematopoiesis
The shelterin complex and hematopoiesis Morgan Jones, … , Catherine E. Keegan, Ivan Maillard J Clin Invest. 2016;126(5):1621-1629. https://doi.org/10.1172/JCI84547. Review Mammalian chromosomes terminate in stretches of repetitive telomeric DNA that act as buffers to avoid loss of essential genetic information during end-replication. A multiprotein complex known as shelterin prevents recognition of telomeric sequences as sites of DNA damage. Telomere erosion contributes to human diseases ranging from BM failure to premature aging syndromes and cancer. The role of shelterin telomere protection is less understood. Mutations in genes encoding the shelterin proteins TRF1-interacting nuclear factor 2 (TIN2) and adrenocortical dysplasia homolog (ACD) were identified in dyskeratosis congenita, a syndrome characterized by somatic stem cell dysfunction in multiple organs leading to BM failure and other pleiotropic manifestations. Here, we introduce the biochemical features and in vivo effects of individual shelterin proteins, discuss shelterin functions in hematopoiesis, and review emerging knowledge implicating the shelterin complex in hematological disorders. Find the latest version: https://jci.me/84547/pdf The Journal of Clinical Investigation REVIEW The shelterin complex and hematopoiesis Morgan Jones,1,2 Kamlesh Bisht,3 Sharon A. Savage,4 Jayakrishnan Nandakumar,3 Catherine E. Keegan,5,6 and Ivan Maillard7,8,9 1Graduate Program in Cellular and Molecular Biology, 2Medical Scientist Training Program, and 3Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan, USA. 4Clinical Genetics Branch, Division of Cancer Epidemiology and Genetics, National Cancer Institute, Bethesda, Maryland, USA. 5Department of Human Genetics, 6Department of Pediatrics, 7Life Sciences Institute, 8Division of Hematology-Oncology, Department of Internal Medicine, and 9Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, Michigan, USA. -
(AS) Alternative Splicing Variants and TERF2 in Osteosarcoma
Research EUR. J. ONCOL.; Vol. 21, n. 4, pp. 227-237, 2016 © Mattioli 1885 Expression of TERT (AS) alternative splicing variants and TERF2 in osteosarcoma Indhira Dias Oliveira1,2, Antonio Sergio Petrilli1, Carla Renata Pacheco Donato Macedo1, Maria Teresa de Seixas Alves1,3, Reinaldo de Jesus Garcia Filho1,4, Silvia Regina Caminada Toledo1,2 1 Pediatric Oncology Institute/GRAACC, Department of Pediatrics, Federal University of São Paulo, São Paulo, SP, Brazil; 2 Department of Morphology and Genetics, Division of Genetics, Federal University of São Paulo, São Paulo, SP, Brazil; 3De- partment of Pathology, Federal University of São Paulo, São Paulo, SP, Brazil; 4Department of Orthopedics and Traumatology, Federal University of São Paulo, São Paulo, SP, Brazil Summary. Background: Osteosarcoma (OS) is the most common malignant bone tumor in children and ado- lescents. Mechanisms of telomere maintenance (TMM) are central features of the tumor cells to maintaining their proliferative capacity. Aim: In this study, we investigated the expression of TERT (telomerase reverse transcriptase) alternative splicing (AS) variants, TERC (telomerase RNA component), TERF1 (telomeric repeat binding factor 1) and TERF2 (telomeric repeat binding factor 2) and quantified telomerase enzyme activity in samples of OS, correlating with clinical and pathological aspects. Methods: A total of 70 fragments of OS tumor samples and 10 normal bone samples (NB) were used for the analysis of gene expression by nested RT-PCR (reverse transcriptase-polymerase chain reaction) and qPCR (quantitative real time PCR). For the quantification of telomerase by TRAP assay we used 20 OS samples and two NB samples. Results: We observed the expression of TERT in 44% of the tumors and full length (FL) isoform in only 4%. -
Characterization of Telomeric Repeat-Containing RNA (TERRA) Localization and Protein
bioRxiv preprint doi: https://doi.org/10.1101/362632; this version posted July 5, 2018. 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. 1 1 Characterization of Telomeric Repeat-Containing RNA (TERRA) localization and protein 2 interactions in Primordial Germ Cells of the mouse 3 4 Running tittle: Characterization of TERRA in mouse PGCs 5 6 Summary sentence: TERRA transcription and interacting proteins during PGC development are 7 regulated in a dynamic fashion that is dependent on gestational age and sex 8 9 Keywords: TERRA, Primordial Germ Cells, Long non-coding RNA, Telomeres, SFPQ, NONO 10 11 Miguel A. Brieño-Enríquez2, Stefannie L. Moak, Anyul Abud-Flores1, and Paula E. Cohen2 12 Department of Biomedical Sciences and Center for Reproductive Genomics, Cornell University, Ithaca, 13 New York 14853, United States of America 14 1 Current Address: Facultad de Medicina de la, Universidad Autónoma de San Luis Potosí, San Luis 15 Potosí, México 16 2 Corresponding authors: [email protected] and [email protected] 17 18 19 20 21 Research reported in this publication was supported in part by the Eunice Kennedy Shriver National Institute of Child Health & Human 22 Development of the National Institutes of Health under Award Number K99HD090289 to M.A.B-E. A seed grant from the Cornell Center for 23 Reproductive Genomics to M.A.B-E, using funds obtained as part of the NICHD National Centers for Translational Research in Reproduction 24 and Infertility (NCTRI), award number P50HD076210 to P.E.C.