RFC2 Antibody

Total Page：16

File Type：pdf, Size：1020Kb

Product Datasheet RFC2 Antibody Catalog No: #43122 Orders: [email protected] Description Support: [email protected] Product Name RFC2 Antibody Host Species Rabbit Clonality Polyclonal Purification Antigen affinity purification. Applications WB Species Reactivity Hu Specificity The antibody detects endogenous levels of total RFC2 protein. Immunogen Type peptide Immunogen Description Synthetic peptide of human RFC2 Target Name RFC2 Other Names RFC40 Accession No. Swiss-Prot#: P35250Gene ID: 5982 Calculated MW 39kd Concentration 3.5mg/ml Formulation Rabbit IgG in pH7.4 PBS, 0.05% NaN3, 40% Glycerol. Storage Store at -20°C Application Details Western blotting: 1:200-1:1000 Immunohistochemistry: 1:30-1:150 Images Gel: 10%SDS-PAGE Lysate: 40 µg Lane: Human liver cancer tissue Primary antibody: 1/500 dilution Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution Exposure time: 20 seconds Background This gene encodes a member of the activator 1 small subunits family. The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins, proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). Replication factor C, also called activator 1, is a protein complex consisting of five distinct subunits. This gene encodes the 40 kD subunit, which has been shown to be responsible for binding ATP and may help promote cell survival. Disruption of this gene is associated with Williams syndrome. Alternatively spliced transcript variants Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 1 encoding distinct isoforms have been described. A pseudogene of this gene has been defined on chromosome 2. Note: This product is for in vitro research use only and is not intended for use in humans or animals. Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 2.

Copy Link

Recommended publications

Structure of the Human Clamp Loader Reveals an Autoinhibited Conformation of a Substrate-Bound AAA+ Switch
Structure of the human clamp loader reveals an autoinhibited conformation of a substrate-bound AAA+ switch Christl Gaubitza,1, Xingchen Liua,b,1, Joseph Magrinoa,b, Nicholas P. Stonea, Jacob Landecka,b, Mark Hedglinc, and Brian A. Kelcha,2 aDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester MA 01605; bGraduate School of Biomedical Sciences, University of Massachusetts Medical School, Worcester MA 01605; and cDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802 Edited by Michael E. O’Donnell, HHMI and Rockefeller University, New York, NY, and approved July 27, 2020 (received for review April 20, 2020) DNA replication requires the sliding clamp, a ring-shaped protein areflexia syndrome (15), Hutchinson–Gilford progeria syn- complex that encircles DNA, where it acts as an essential cofactor drome (16), and in the replication of some viruses (17–19). It for DNA polymerases and other proteins. The sliding clamp needs is unknown whether loading by RFC contributes to PARD to be opened and installed onto DNA by a clamp loader ATPase of disease. the AAA+ family. The human clamp loader replication factor C Clamp loaders are members of the AAA+ family of ATPases (RFC) and sliding clamp proliferating cell nuclear antigen (PCNA) (ATPases associated with various cellular activities), a large are both essential and play critical roles in several diseases. De- protein family that uses the chemical energy of adenosine 5′- spite decades of study, no structure of human RFC has been re- triphosphate (ATP) to generate mechanical force (20). Most solved. Here, we report the structure of human RFC bound to AAA+ proteins form hexameric motors that use an undulating PCNA by cryogenic electron microscopy to an overall resolution ∼ spiral staircase mechanism to processively translocate a substrate of 3.4 Å.
[Show full text]
Identification and Characterization of a Novel Non-Homologous End Joining Factor MRI
Washington University in St. Louis Washington University Open Scholarship Arts & Sciences Electronic Theses and Dissertations Arts & Sciences Spring 5-15-2020 Identification and Characterization of a Novel Non-homologous End Joining Factor MRI Putzer Joseph Hung Washington University in St. Louis Follow this and additional works at: https://openscholarship.wustl.edu/art_sci_etds Part of the Allergy and Immunology Commons, Immunology and Infectious Disease Commons, and the Medical Immunology Commons Recommended Citation Hung, Putzer Joseph, "Identification and Characterization of a Novel Non-homologous End Joining Factor MRI" (2020). Arts & Sciences Electronic Theses and Dissertations. 2201. https://openscholarship.wustl.edu/art_sci_etds/2201 This Dissertation is brought to you for free and open access by the Arts & Sciences at Washington University Open Scholarship. It has been accepted for inclusion in Arts & Sciences Electronic Theses and Dissertations by an authorized administrator of Washington University Open Scholarship. For more information, please contact [email protected]. WASHINGTON UNIVERSITY IN ST. LOUIS Division of Biology and Biomedical Sciences Immunology Dissertation Examination Committee: Barry Sleckman, Chair Gaya Amarasinghe Brian Edelson Takeshi Egawa Nima Mosammaparast Kenneth Murphy Sheila Stewart Identification and Characterization of a Novel Non-homologous End Joining Factor MRI by Putzer Joseph Hung A dissertation presented to The Graduate School of Washington University in partial fulfillment of the requirements
[Show full text]
Datasheet Blank Template
SAN TA C RUZ BI OTEC HNOL OG Y, INC . RFC4 (E-12): sc-28300 BACKGROUND RECOMMENDED SUPPORT REAGENTS Replication factor C (RFC) is an essential DNA polymerase accessory protein To ensure optimal results, the following support reagents are recommended: that is required for numerous aspects of DNA metabolism including DNA 1) Western Blotting: use m-IgG κ BP-HRP: sc-516102 or m-IgG κ BP-HRP replication, DNA repair and telomere metabolism. RFC is a heteropentameric (Cruz Marker): sc-516102-CM (dilution range: 1:1000-1:10000), Cruz Marker™ complex that recognizes a primer on a template DNA, binds to a primer termi - Molecular Weight Standards: sc-2035, TBS Blotto A Blocking Reagent: nus, and loads proliferating cell nuclear antigen (PCNA) onto DNA at primer- sc-2333 and Western Blotting Luminol Reagent: sc-2048. 2) Immunoprecip- template junctions in an ATP-dependent reaction. All five of the RFC subunits itation: use Protein A/G PLUS-Agarose: sc-2003 (0.5 ml agarose/2.0 ml). share a set of related sequences (RFC boxes) that include nucleotide-binding 3) Immunofluorescence: use m-IgG κ BP-FITC: sc-516140 or m-IgG κ BP-PE: consensus sequences. Four of the five RFC genes (RFC1, RFC2, RFC3 and RFC4) sc-516141 (dilution range: 1:50-1:200) with UltraCruz ® Mounting Medium: have consensus ATP-binding motifs. The small RFC proteins, RFC2, RFC3, RFC4 sc-24941 or UltraCruz ® Hard-set Mounting Medium: sc-359850. and RFC5, interact with Rad24, whereas the RFC1 subunit does not. Speci- fically, RFC4 plays a role in checkpoint regulation.
[Show full text]
Control of Genome Integrity by RFC Complexes; Conductors of PCNA Loading Onto and Unloading from Chromatin During DNA Replication
Review Control of Genome Integrity by RFC Complexes; Conductors of PCNA Loading onto and Unloading from Chromatin during DNA Replication Yasushi Shiomi *and Hideo Nishitani * Graduate School of Life Science, University of Hyogo, Kamigori, Ako‐gun, Hyogo 678‐1297, Japan Correspondence: [email protected]‐hyogo.ac.jp (Y.S.); [email protected]‐hyogo.ac.jp (H.N.) Academic Editor: Eishi Noguchi Received: 28 November 2016; Accepted: 21 January 2017; Published: 26 January 2017 Abstract: During cell division, genome integrity is maintained by faithful DNA replication during S phase, followed by accurate segregation in mitosis. Many DNA metabolic events linked with DNA replication are also regulated throughout the cell cycle. In eukaryotes, the DNA sliding clamp, proliferating cell nuclear antigen (PCNA), acts on chromatin as a processivity factor for DNA polymerases. Since its discovery, many other PCNA binding partners have been identified that function during DNA replication, repair, recombination, chromatin remodeling, cohesion, and proteolysis in cell‐cycle progression. PCNA not only recruits the proteins involved in such events, but it also actively controls their function as chromatin assembles. Therefore, control of PCNA‐loading onto chromatin is fundamental for various replication‐coupled reactions. PCNA is loaded onto chromatin by PCNA‐loading replication factor C (RFC) complexes. Both RFC1‐RFC and Ctf18‐RFC fundamentally function as PCNA loaders. On the other hand, after DNA synthesis, PCNA must be removed from chromatin by Elg1‐RFC. Functional defects in RFC complexes lead to chromosomal abnormalities. In this review, we summarize the structural and functional relationships among RFC complexes, and describe how the regulation of PCNA loading/unloading by RFC complexes contributes to maintaining genome integrity.
[Show full text]
Cshperspect-REP-A015727 Table3 1..10
Table 3. Nomenclature for proteins and protein complexes in different organisms Mammals Budding yeast Fission yeast Flies Plants Archaea Bacteria Prereplication complex assembly H. sapiens S. cerevisiae S. pombe D. melanogaster A. thaliana S. solfataricus E. coli Hs Sc Sp Dm At Sso Eco ORC ORC ORC ORC ORC [Orc1/Cdc6]-1, 2, 3 DnaA Orc1/p97 Orc1/p104 Orc1/Orp1/p81 Orc1/p103 Orc1a, Orc1b Orc2/p82 Orc2/p71 Orc2/Orp2/p61 Orc2/p69 Orc2 Orc3/p66 Orc3/p72 Orc3/Orp3/p80 Orc3/Lat/p82 Orc3 Orc4/p50 Orc4/p61 Orc4/Orp4/p109 Orc4/p52 Orc4 Orc5L/p50 Orc5/p55 Orc5/Orp5/p52 Orc5/p52 Orc5 Orc6/p28 Orc6/p50 Orc6/Orp6/p31 Orc6/p29 Orc6 Cdc6 Cdc6 Cdc18 Cdc6 Cdc6a, Cdc6b [Orc1/Cdc6]-1, 2, 3 DnaC Cdt1/Rlf-B Tah11/Sid2/Cdt1 Cdt1 Dup/Cdt1 Cdt1a, Cdt1b Whip g MCM helicase MCM helicase MCM helicase MCM helicase MCM helicase Mcm DnaB Mcm2 Mcm2 Mcm2/Nda1/Cdc19 Mcm2 Mcm2 Mcm3 Mcm3 Mcm3 Mcm3 Mcm3 Mcm4 Mcm4/Cdc54 Mcm4/Cdc21 Mcm4/Dpa Mcm4 Mcm5 Mcm5/Cdc46/Bob1 Mcm5/Nda4 Mcm5 Mcm5 Mcm6 Mcm6 Mcm6/Mis5 Mcm6 Mcm6 Mcm7 Mcm7/Cdc47 Mcm7 Mcm7 Mcm7/Prolifera Gmnn/Geminin Geminin Mcm9 Mcm9 Hbo1 Chm/Hat1 Ham1 Ham2 DiaA Ihfa Ihfb Fis SeqA Replication fork assembly Hs Sc Sp Dm At Sso Eco Mcm8 Rec/Mcm8 Mcm8 Mcm10 Mcm10/Dna43 Mcm10/Cdc23 Mcm10 Mcm10 DDK complex DDK complex DDK complex DDK complex Cdc7 Cdc7 Hsk1 l(1)G0148 Hsk1-like 1 Dbf4/Ask Dbf4 Dfp1/Him1/Rad35 Chif/chiffon Drf1 Continued 2 Replication fork assembly (Continued ) Hs Sc Sp Dm At Sso Eco CDK complex CDK complex CDK complex CDK complex CDK complex Cdk1 Cdc28/Cdk1 Cdc2/Cdk1 Cdc2 CdkA Cdk2 Cdc2c CcnA1, A2 CycA CycA1, A2,
[Show full text]
Characterization of the Roles of DNA Polymerases, Clamp, and Clamp Loaders During S-Phase Progression and Cell Cycle Regulation in the Silkworm, Bombyx Mori
Journal of Insect Biotechnology and Sericology 85, 21-29 (2016) Characterization of the roles of DNA polymerases, clamp, and clamp loaders during S-phase progression and cell cycle regulation in the silkworm, Bombyx mori Masato Hino, Daisuke Morokuma, Hiroaki Mon, Jae Man Lee and Takahiro Kusakabe＊ Laboratory of Insect Genome Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences, Hakozaki 6-10-1, Higashi-ku, Fukuoka 812-8581, Japan (Received February 17, 2016; Accepted April 4, 2016) DNA replication is one of key event in cell-cycle progression, yet due to their importance and lethality, the chronological phenotypes of DNA synthesis machineries after the depletion of corresponding genes have proved difficult to study. In the present study, mRNAs for three DNA polymerases, a clamp, and three clamp loaders were gradually depleted from cultured silkworm cells by soaking RNAi. Interestingly, the depletion of these DNA synthesis factors had different effects on the cell growth rate and arrest of cell-cycle progression during time- lapse observation. The depletion of DNA polymerases immediately arrested the cell-cycle progression at the S phase, while that of PCNA, a DNA clamp, required more time to slow cell growth and finally induced apoptosis. Surprisingly, silkworm cells continued to undergo several rounds of cell division when the components of clamp loaders were knocked down. Key words: Cell cycle, Clamp loaders, DNA polymerases, replication factors, Silkworm In eukaryotes, three DNA polymerases are mainly in- INTRODUCTION volved in replication (Burgers, 1998). Pol α forms a com- Semiconservative DNA replication is an essential bio- plex with primase, and is needed to initiate DNA replication logical phenomenon that enables each daughter cell to at the start of replication and Okazaki fragment synthesis have the same sets of chromosomes.
[Show full text]
RFC2 Mouse Monoclonal Antibody [Clone ID: OTI4E1] Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TA504956 RFC2 Mouse Monoclonal Antibody [Clone ID: OTI4E1] Product data: Product Type: Primary Antibodies Clone Name: OTI4E1 Applications: FC, WB Recommended Dilution: WB 1:200~2000, FLOW 1:100 Reactivity: Human, Mouse, Rat Host: Mouse Isotype: IgG1 Clonality: Monoclonal Immunogen: Human recombinant protei fragment corresponding to amino acids 1-234 of human RFC2(NP_002905) produced in E.coli. Formulation: PBS (PH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide. Concentration: 1 mg/ml Purification: Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G) Conjugation: Unconjugated Storage: Store at -20°C as received. Stability: Stable for 12 months from date of receipt. Predicted Protein Size: 35.1 kDa Gene Name: replication factor C subunit 2 Database Link: NP_002905 Entrez Gene 19718 MouseEntrez Gene 116468 RatEntrez Gene 5982 Human P35250 This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 3 RFC2 Mouse Monoclonal Antibody [Clone ID: OTI4E1] – TA504956 Background: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins, proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). RFC, also called activator 1, is a protein complex consisting of five distinct subunits of 145, 40, 38, 37, and 36.5 kD.
[Show full text]
Oxidized Phospholipids Regulate Amino Acid Metabolism Through MTHFD2 to Facilitate Nucleotide Release in Endothelial Cells
ARTICLE DOI: 10.1038/s41467-018-04602-0 OPEN Oxidized phospholipids regulate amino acid metabolism through MTHFD2 to facilitate nucleotide release in endothelial cells Juliane Hitzel1,2, Eunjee Lee3,4, Yi Zhang 3,5,Soﬁa Iris Bibli2,6, Xiaogang Li7, Sven Zukunft 2,6, Beatrice Pﬂüger1,2, Jiong Hu2,6, Christoph Schürmann1,2, Andrea Estefania Vasconez1,2, James A. Oo1,2, Adelheid Kratzer8,9, Sandeep Kumar 10, Flávia Rezende1,2, Ivana Josipovic1,2, Dominique Thomas11, Hector Giral8,9, Yannick Schreiber12, Gerd Geisslinger11,12, Christian Fork1,2, Xia Yang13, Fragiska Sigala14, Casey E. Romanoski15, Jens Kroll7, Hanjoong Jo 10, Ulf Landmesser8,9,16, Aldons J. Lusis17, 1234567890():,; Dmitry Namgaladze18, Ingrid Fleming2,6, Matthias S. Leisegang1,2, Jun Zhu 3,4 & Ralf P. Brandes1,2 Oxidized phospholipids (oxPAPC) induce endothelial dysfunction and atherosclerosis. Here we show that oxPAPC induce a gene network regulating serine-glycine metabolism with the mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase (MTHFD2) as a cau- sal regulator using integrative network modeling and Bayesian network analysis in human aortic endothelial cells. The cluster is activated in human plaque material and by atherogenic lipo- proteins isolated from plasma of patients with coronary artery disease (CAD). Single nucleotide polymorphisms (SNPs) within the MTHFD2-controlled cluster associate with CAD. The MTHFD2-controlled cluster redirects metabolism to glycine synthesis to replenish purine nucleotides. Since endothelial cells secrete purines in response to oxPAPC, the MTHFD2- controlled response maintains endothelial ATP. Accordingly, MTHFD2-dependent glycine synthesis is a prerequisite for angiogenesis. Thus, we propose that endothelial cells undergo MTHFD2-mediated reprogramming toward serine-glycine and mitochondrial one-carbon metabolism to compensate for the loss of ATP in response to oxPAPC during atherosclerosis.
[Show full text]
CHTF18 Polyclonal Antibody Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP55350
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 CHTF18 Polyclonal Antibody Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP55350 Specification CHTF18 Polyclonal Antibody - Product Information Application WB, IHC-P, IHC-F, IF, ICC Primary Accession Q8WVB6 Reactivity Rat Host Rabbit Clonality Polyclonal Calculated MW 107383 CHTF18 Polyclonal Antibody - Additional Information Gene ID 63922 Other Names Chromosome transmission fidelity protein 18 homolog, hCTF18, CHL12, CHTF18, C16orf41, CTF18 Format 0.01M TBS(pH7.4) with 1% BSA, 0.09% (W/V) sodium azide and 50% Glyce Storage Store at -20 ℃ for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 ℃. CHTF18 Polyclonal Antibody - Protein Information Name CHTF18 Synonyms C16orf41, CTF18 Function Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. Page 1/2 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 The CTF18-RFC complex binds to single-stranded and primed DNAs and has weak ATPase activity that is stimulated by the presence of primed DNA, replication protein A (RPA) and by proliferating cell nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP- dependent loading of PCNA onto primed and gapped DNA. Interacts with and stimulates DNA polymerase POLH.
[Show full text]
Williams Syndrome
Williams syndrome Description Williams syndrome is a developmental disorder that affects many parts of the body. This condition is characterized by mild to moderate intellectual disability or learning problems, unique personality characteristics, distinctive facial features, and heart and blood vessel (cardiovascular) problems. People with Williams syndrome typically have difficulty with visual-spatial tasks such as drawing and assembling puzzles, but they tend to do well on tasks that involve spoken language, music, and learning by repetition (rote memorization). Affected individuals have outgoing, engaging personalities and tend to take an extreme interest in other people. Attention deficit disorder (ADD), problems with anxiety, and phobias are common among people with this disorder. Young children with Williams syndrome have distinctive facial features including a broad forehead, a short nose with a broad tip, full cheeks, and a wide mouth with full lips. Many affected people have dental problems such as teeth that are small, widely spaced, crooked, or missing. In older children and adults, the face appears longer and more gaunt. A form of cardiovascular disease called supravalvular aortic stenosis (SVAS) occurs frequently in people with Williams syndrome. Supravalvular aortic stenosis is a narrowing of the large blood vessel that carries blood from the heart to the rest of the body (the aorta). If this condition is not treated, the aortic narrowing can lead to shortness of breath, chest pain, and heart failure. Other problems with the heart and blood vessels, including high blood pressure (hypertension), have also been reported in people with Williams syndrome. Additional signs and symptoms of Williams syndrome include abnormalities of connective tissue (tissue that supports the body's joints and organs) such as joint problems and soft, loose skin.
[Show full text]
Autocrine IFN Signaling Inducing Profibrotic Fibroblast Responses By
Downloaded from http://www.jimmunol.org/ by guest on September 23, 2021 Inducing is online at: average * The Journal of Immunology , 11 of which you can access for free at: 2013; 191:2956-2966; Prepublished online 16 from submission to initial decision 4 weeks from acceptance to publication August 2013; doi: 10.4049/jimmunol.1300376 http://www.jimmunol.org/content/191/6/2956 A Synthetic TLR3 Ligand Mitigates Profibrotic Fibroblast Responses by Autocrine IFN Signaling Feng Fang, Kohtaro Ooka, Xiaoyong Sun, Ruchi Shah, Swati Bhattacharyya, Jun Wei and John Varga J Immunol cites 49 articles Submit online. Every submission reviewed by practicing scientists ? is published twice each month by Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts http://jimmunol.org/subscription Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html http://www.jimmunol.org/content/suppl/2013/08/20/jimmunol.130037 6.DC1 This article http://www.jimmunol.org/content/191/6/2956.full#ref-list-1 Information about subscribing to The JI No Triage! Fast Publication! Rapid Reviews! 30 days* Why • • • Material References Permissions Email Alerts Subscription Supplementary The Journal of Immunology The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2013 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. This information is current as of September 23, 2021. The Journal of Immunology A Synthetic TLR3 Ligand Mitigates Proﬁbrotic Fibroblast Responses by Inducing Autocrine IFN Signaling Feng Fang,* Kohtaro Ooka,* Xiaoyong Sun,† Ruchi Shah,* Swati Bhattacharyya,* Jun Wei,* and John Varga* Activation of TLR3 by exogenous microbial ligands or endogenous injury-associated ligands leads to production of type I IFN.
[Show full text]
Gain of Chromosome Band 7Q11 in Papillary Thyroid Carcinomas of Young Patients Is Associated with Exposure to Low-Dose Irradiation
Gain of chromosome band 7q11 in papillary thyroid carcinomas of young patients is associated with exposure to low-dose irradiation Julia Heßa, Gerry Thomasb, Herbert Braselmanna, Verena Bauera, Tatjana Bogdanovac, Johannes Wienbergd, Horst Zitzelsbergera, and Kristian Ungerb,1 aResearch Unit of Radiation Cytogenetics, Helmholtz Zentrum München, German Research Center for Environmental Health GmbH, 85764 Neuherberg, Germany; bHuman Cancer Studies Group, Department of Surgery and Cancer, Hammersmith Hospital, London W12 0HS, United Kingdom; cInstitute of Endocrinology and Metabolism, Academy of Medical Sciences of the Ukraine, 254114 Kiev, Ukraine; and dDepartment Biologie II, Anthropologie und Humangenetik, Ludwig-Maximilians-University, 82152 Martinsried, Germany Edited* by Janet D. Rowley, University of Chicago, Chicago, IL, and approved April 26, 2011 (received for review November 21, 2010) The main consequence of the Chernobyl accident has been an in the development of radiation-associated PTC that appropriate increase in papillary thyroid carcinomas (PTCs) in those exposed to tumor, sex, and age-matched cohorts with exposed cases and radioactive fallout as young children. Our aim was to identify nonexposed individuals for comparison are used. This approach genomic alterations that are associated with exposure to radiation. minimizes variability in the study that results particularly with We used array comparative genomic hybridization to analyze a respect to age at diagnosis. Studies of early Chernobyl-related main (n = 52) and a validation cohort (n = 28) of PTC from patients tumors by several groups found that a very high proportion aged <25 y at operation and matched for age at diagnosis and showed RET rearrangements, predominantly RET/PTC3 (3–6). residency. Both cohorts consisted of patients exposed and not ex- It was speculated that this rearrangement might be a marker posed to radioiodine fallout.
[Show full text]