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[PMID]:28741530
[Au] Autor:Voon HPJ; Collas P; Wong LH
[Ad] Endereço:Department of Biochemistry and Molecular Biology, The Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia.
[Ti] Título:Compromised Telomeric Heterochromatin Promotes ALTernative Lengthening of Telomeres.
[So] Source:Trends Cancer;2(3):114-116, 2016 Mar.
[Is] ISSN:2405-8025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alternative lengthening of telomeres (ALT) is an enigmatic process that allows certain cancers to maintain telomeres in the absence of telomerase. ALT cancers are frequently defective for ATRX/DAXX, a chaperone complex that deposits histone variant H3.3 at telomeres. We propose that mutations in alpha thalassemia-mental retardation syndrome X-linked (ATRX)/death-domain associated protein (DAXX) prime ALT activation by disrupting telomeric heterochromatin.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Heterocromatina/metabolismo
Neoplasias/genética
Proteínas Nucleares/genética
Homeostase do Telômero
Proteína Nuclear Ligada ao X/genética
[Mh] Termos MeSH secundário: Seres Humanos
Mutação
Telômero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (DAXX protein, human); 0 (Heterochromatin); 0 (Nuclear Proteins); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


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[PMID]:28452859
[Au] Autor:Duan XF; Zhao Q
[Ad] Endereço:Departments of Esophageal Cancer.
[Ti] Título:TERT-mediated and ATRX-mediated Telomere Maintenance and Neuroblastoma.
[So] Source:J Pediatr Hematol Oncol;40(1):1-6, 2018 Jan.
[Is] ISSN:1536-3678
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neuroblastomas (NB) are one of the most common extracranial solid tumors in children, and they frequently display high heterogeneity in the disease course. With ongoing research, more information regarding the genetic etiology and molecular mechanisms underlying these contrasting phenotypes is being uncovered. The proto-oncogene MYCN is amplified in approximately 20% of NB cases and is considered a indicator of poor prognosis and an indicator of high-risk NB. The poor prognosis of high risk NB is incompletely explained by MYCN amplification. Recently, massive parallel sequencing studies reported several relatively common gene alterations, such as ATRX mutation and TERT rearrangement that are involved in telomere maintenance through telomerase activity and alternative lengthening of telomeres. Thus, these are important for understanding the etiology and molecular pathogenesis of NB, and hence, for identifying diagnostic and treatment markers. Development of telomerase inhibitors and identification of alternative lengthening of telomeres related targets will contribute to the individualized treatment for high-risk NB. In this mini-review, we will discuss the research progress of TERT-mediated and ATRX-mediated telomere maintenance and NB, especially high-risk tumors.
[Mh] Termos MeSH primário: Neuroblastoma/genética
Telomerase/fisiologia
Telômero/metabolismo
Proteína Nuclear Ligada ao X/fisiologia
[Mh] Termos MeSH secundário: Seres Humanos
Neuroblastoma/etiologia
Neuroblastoma/patologia
Neuroblastoma/ultraestrutura
Prognóstico
Telômero/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 2.7.7.49 (TERT protein, human); EC 2.7.7.49 (Telomerase); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1097/MPH.0000000000000840


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[PMID]:28719461
[Au] Autor:Casar-Borota O; Botling J; Granberg D; Stigare J; Wikström J; Boldt HB; Kristensen BW; Pontén F; Trouillas J
[Ad] Endereço:Departments of *Immunology, Genetics and Pathology §Medical Sciences ∥Surgical Sciences, Uppsala University †Department of Clinical Pathology, Uppsala University Hospital, Uppsala, Sweden ‡Department of Pathology, Oslo University Hospital, Oslo, Norway ¶Department of Pathology, Odense University Hospital #Department of Clinical Research, University of Southern Denmark, Odense, Denmark **Faculty of Medicine Lyon-Est ††Centre de Pathologie et de Biologie Est, Groupement Hospitalier Est, Hospices Civils de Lyon, University of Lyon, Lyon, France.
[Ti] Título:Serotonin, ATRX, and DAXX Expression in Pituitary Adenomas: Markers in the Differential Diagnosis of Neuroendocrine Tumors of the Sellar Region.
[So] Source:Am J Surg Pathol;41(9):1238-1246, 2017 Sep.
[Is] ISSN:1532-0979
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Differential diagnosis based on morphology and immunohistochemistry between a clinically nonfunctioning pituitary neuroendocrine tumor (NET)/pituitary adenoma and a primary or secondary NET of nonpituitary origin in the sellar region may be difficult. Serotonin, a frequently expressed marker in the NETs, has not been systematically evaluated in pituitary NETs. Although mutations in ATRX or DAXX have been reported in a significant proportion of pancreatic NETs, the mutational status of ATRX and DAXX and their possible pathogenetic role in pituitary NETs are unknown. Facing a difficult diagnostic case of an invasive serotonin and adrenocorticotroph hormone immunoreactive NET in the sellar region, we explored the immunohistochemical expression of serotonin, ATRX, and DAXX in a large series of pituitary endocrine tumors of different types from 246 patients and in 2 corticotroph carcinomas. None of the pituitary tumors expressed serotonin, suggesting that serotonin immunoreactive sellar tumors represent primary or secondary NETs of nonpituitary origin. Normal expression of ATRX and DAXX in pituitary tumors suggests that ATRX and DAXX do not play a role in the pathogenesis of pituitary endocrine tumors that remain localized to the sellar and perisellar region. A lack of ATRX or DAXX in a sellar NET suggests a nonpituitary NET, probably of pancreatic origin. One of the 2 examined corticotroph carcinomas, however, demonstrated negative ATRX immunolabeling due to an ATRX gene mutation. Further studies on a larger cohort of pituitary carcinomas are needed to clarify whether ATRX mutations may contribute to the metastatic potential in a subset of pituitary NETs.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/biossíntese
Adenoma/metabolismo
Biomarcadores Tumorais/biossíntese
DNA Helicases/biossíntese
Tumores Neuroendócrinos/diagnóstico
Proteínas Nucleares/biossíntese
Neoplasias Hipofisárias/metabolismo
Sela Túrcica
Serotonina/biossíntese
Neoplasias Cranianas/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/análise
Adenoma/diagnóstico
Adulto
Idoso
Biomarcadores Tumorais/análise
DNA Helicases/análise
Diagnóstico Diferencial
Feminino
Seres Humanos
Imuno-Histoquímica
Masculino
Proteínas Nucleares/análise
Neoplasias Hipofisárias/diagnóstico
Serotonina/análise
Neoplasias Cranianas/diagnóstico
Proteína Nuclear Ligada ao X
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Biomarkers, Tumor); 0 (DAXX protein, human); 0 (Nuclear Proteins); 333DO1RDJY (Serotonin); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1097/PAS.0000000000000908


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[PMID]:28666128
[Au] Autor:Chu HP; Cifuentes-Rojas C; Kesner B; Aeby E; Lee HG; Wei C; Oh HJ; Boukhali M; Haas W; Lee JT
[Ad] Endereço:Howard Hughes Medical Institute, Boston, MA 02114, USA; Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA; Department of Genetics, Harvard Medical School, Boston, MA 02114, USA.
[Ti] Título:TERRA RNA Antagonizes ATRX and Protects Telomeres.
[So] Source:Cell;170(1):86-101.e16, 2017 Jun 29.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Through an integration of genomic and proteomic approaches to advance understanding of long noncoding RNAs, we investigate the function of the telomeric transcript, TERRA. By identifying thousands of TERRA target sites in the mouse genome, we demonstrate that TERRA can bind both in cis to telomeres and in trans to genic targets. We then define a large network of interacting proteins, including epigenetic factors, telomeric proteins, and the RNA helicase, ATRX. TERRA and ATRX share hundreds of target genes and are functionally antagonistic at these loci: whereas TERRA activates, ATRX represses gene expression. At telomeres, TERRA competes with telomeric DNA for ATRX binding, suppresses ATRX localization, and ensures telomeric stability. Depleting TERRA increases telomerase activity and induces telomeric pathologies, including formation of telomere-induced DNA damage foci and loss or duplication of telomeric sequences. We conclude that TERRA functions as an epigenomic modulator in trans and as an essential regulator of telomeres in cis.
[Mh] Termos MeSH primário: DNA Helicases/metabolismo
Proteínas Nucleares/metabolismo
Proteoma/metabolismo
RNA Longo não Codificante/metabolismo
Telômero/metabolismo
[Mh] Termos MeSH secundário: Animais
Ensaio de Desvio de Mobilidade Eletroforética
Camundongos
Motivos de Nucleotídeos
Células-Tronco/metabolismo
Telomerase/metabolismo
Proteína Nuclear Ligada ao X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (Proteome); 0 (RNA, Long Noncoding); EC 2.7.7.49 (Telomerase); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (Atrx protein, mouse); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170701
[St] Status:MEDLINE


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[PMID]:28395727
[Au] Autor:Tang S; Liu Z; Li R; Chen Y; Zhao L; Shen H; Wan Y
[Ad] Endereço:Hunan Provincial Key Laboratory for Special Pathogens Prevention and Control, Institute of Pathogenic Biology, University of South China, Hengyang 421001, China.
[Ti] Título:[Preparation and identification of the polyclonal antibody against ATRX-C ].
[So] Source:Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi;33(4):536-539, 2017 Apr.
[Is] ISSN:1007-8738
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Objective To prepare the polyclonal antibody against human alpha thalassemia/mental retardation syndrome X-linked (ATRX) C-terminal and study the distribution and expression of ATRX protein in human cervical cancer tissues. Methods The antiserum was obtained from the BALB/c mice immunized with His-ATRX-C protein and then purified by the saturated ammonium sulfate precipitation and affinity chromatography. The titer of anti-ATRX polyclonal antibody was determined by ELISA. Its specificity was identified by SDS-PAGE analysis and Western blotting. The expression and location of ATRX in human cervical tissues were analyzed by immunohistochemistry. Results The titer of the polyclonal antibody against His-ATRX-C protein was about 1:12 800. The antibody could recognize His-ATRX-C protein specifically. With the polyclonal antibody, the target protein was found mainly in the nucleus of para-carcinoma tissues, and it was also expressed in the nucleus of cervical cancer tissue cells, but the expression in the latter was obviously lower. Conclusion The polyclonal antibody against His-ATRX-C protein has been produced successfully and used to detect ATRX protein in human cervical cancer tissues.
[Mh] Termos MeSH primário: Anticorpos/imunologia
DNA Helicases/análise
Retardo Mental Ligado ao Cromossomo X/diagnóstico
Proteínas Nucleares/análise
Talassemia alfa/diagnóstico
[Mh] Termos MeSH secundário: Animais
DNA Helicases/genética
DNA Helicases/imunologia
Feminino
Seres Humanos
Imunização
Imuno-Histoquímica
Retardo Mental Ligado ao Cromossomo X/imunologia
Camundongos
Camundongos Endogâmicos BALB C
Proteínas Nucleares/genética
Proteínas Nucleares/imunologia
Proteína Nuclear Ligada ao X
Talassemia alfa/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Nuclear Proteins); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE


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[PMID]:28371511
[Au] Autor:VandenBussche CJ; Allison DB; Graham MK; Charu V; Lennon AM; Wolfgang CL; Hruban RH; Heaphy CM
[Ad] Endereço:Department of Pathology, The Sol Goldman Pancreatic Cancer Research Center, The Johns Hopkins University School of Medicine, Baltimore, Maryland.
[Ti] Título:Alternative lengthening of telomeres and ATRX/DAXX loss can be reliably detected in FNAs of pancreatic neuroendocrine tumors.
[So] Source:Cancer;125(7):544-551, 2017 Jul.
[Is] ISSN:1097-0142
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pancreatic neuroendocrine tumors (PanNETs) frequently use the alternative lengthening of telomeres (ALT) pathway for telomere maintenance. ALT is strongly correlated with α thalassemia-mental retardation, X linked (ATRX), and death domain-associated protein 6 (DAXX) alterations and a poor prognosis in patients with primary PanNET. Because fine-needle aspiration (FNA) is a noninvasive way to sample tumors, the authors evaluated whether they could accurately detect ALT and loss of ATRX/DAXX in a primary PanNET cohort of FNAs. METHODS: All preoperative FNA cytology cases (2005-2016) with adequate remnant FNA cell block material were assessed for ALT by telomere-specific fluorescence in situ hybridization and for ATRX and DAXX protein expression by immunohistochemistry. For 21 patients who underwent tumor resection, the resected specimen also was assessed to determine the concordance between the FNA and surgical specimens. RESULTS: In the primary PanNET cohort of 65 FNAs, ALT was detected in 15 specimens (23%). Although all ATRX-negative and DAXX-negative tumors were ALT-positive, 3 of 14 (21%) ALT-positive tumors did not exhibit nuclear loss of either ATRX or DAXX. The ALT-positive tumors were associated with larger radiographic size (4.9 vs 2.4 cm, on average; P < .05) and higher grade (P < .05). Overall, there was 100% concordance in ALT status and ATRX/DAXX immunohistochemistry results between the FNA and surgical specimens. CONCLUSIONS: Both ALT and loss of ATRX/DAXX can be accurately performed on FNA specimens with adequate material. Because ALT is a fundamental mechanism of pathogenesis, the ability to determine ALT in small biospecimens has implications for the design of clinical trials. Cancer Cytopathol 2017;125:544-51. © 2017 American Cancer Society.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
DNA Helicases/genética
Tumores Neuroendócrinos/genética
Proteínas Nucleares/genética
Neoplasias Pancreáticas/genética
Homeostase do Telômero/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Biópsia por Agulha Fina
Estudos de Coortes
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Hibridização in Situ Fluorescente
Masculino
Meia-Idade
Tumores Neuroendócrinos/mortalidade
Tumores Neuroendócrinos/patologia
Neoplasias Pancreáticas/mortalidade
Neoplasias Pancreáticas/patologia
Modelos de Riscos Proporcionais
Estudos Retrospectivos
Taxa de Sobrevida
Proteína Nuclear Ligada ao X
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (DAXX protein, human); 0 (Nuclear Proteins); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1002/cncy.21857


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[PMID]:28371217
[Au] Autor:Ji J; Quindipan C; Parham D; Shen L; Ruble D; Bootwalla M; Maglinte DT; Gai X; Saitta SC; Biegel JA; Mascarenhas L
[Ad] Endereço:Department of Pathology and Laboratory Medicine, Center for Personalized Medicine, Children's Hospital Los Angeles, Los Angeles, California.
[Ti] Título:Inherited germline ATRX mutation in two brothers with ATR-X syndrome and osteosarcoma.
[So] Source:Am J Med Genet A;173(5):1390-1395, 2017 May.
[Is] ISSN:1552-4833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We report a family in which two brothers had an undiagnosed genetic disorder comprised of dysmorphic features, microcephaly, severe intellectual disability (non-verbal), mild anemia, and cryptorchidism. Both developed osteosarcoma. Trio exome sequencing (using blood samples from the younger brother and both parents) was performed and a nonsense NM_000489.4:c.7156C>T (p.Arg2386*) mutation in the ATRX gene was identified in the proband (hemizygous) and in the mother's peripheral blood DNA (heterozygous). The mother is healthy, does not exhibit any clinical manifestations of ATR-X syndrome and there was no family history of cancer. The same hemizygous pathogenic variant was confirmed in the affected older brother's skin tissue by subsequent Sanger sequencing. Chromosomal microarray studies of both brothers' osteosarcomas revealed complex copy number alterations consistent with the clinical diagnosis of osteosarcoma. Recently, somatic mutations in the ATRX gene have been observed as recurrent alterations in both osteosarcoma and brain tumors. However, it is unclear if there is any association between osteosarcoma and germline ATRX mutations, specifically in patients with constitutional ATR-X syndrome. This is the first report of osteosarcoma diagnosed in two males with ATR-X syndrome, suggesting a potential increased risk for cancer in patients with this disorder.
[Mh] Termos MeSH primário: DNA Helicases/genética
Deficiência Intelectual/genética
Retardo Mental Ligado ao Cromossomo X/genética
Proteínas Nucleares/genética
Osteossarcoma/genética
Talassemia alfa/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Sequência de Bases
Exoma/genética
Feminino
Mutação em Linhagem Germinativa
Heterozigoto
Seres Humanos
Deficiência Intelectual/complicações
Deficiência Intelectual/fisiopatologia
Masculino
Retardo Mental Ligado ao Cromossomo X/complicações
Retardo Mental Ligado ao Cromossomo X/fisiopatologia
Osteossarcoma/complicações
Osteossarcoma/fisiopatologia
Linhagem
Irmãos
Proteína Nuclear Ligada ao X
Talassemia alfa/complicações
Talassemia alfa/fisiopatologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.38184


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[PMID]:28368372
[Au] Autor:Chatzinikolaou G; Apostolou Z; Aid-Pavlidis T; Ioannidou A; Karakasilioti I; Papadopoulos GL; Aivaliotis M; Tsekrekou M; Strouboulis J; Kosteas T; Garinis GA
[Ad] Endereço:Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, Nikolaou Plastira 100, 70013 Heraklion, Crete, Greece.
[Ti] Título:ERCC1-XPF cooperates with CTCF and cohesin to facilitate the developmental silencing of imprinted genes.
[So] Source:Nat Cell Biol;19(5):421-432, 2017 May.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Inborn defects in DNA repair are associated with complex developmental disorders whose causal mechanisms are poorly understood. Using an in vivo biotinylation tagging approach in mice, we show that the nucleotide excision repair (NER) structure-specific endonuclease ERCC1-XPF complex interacts with the insulator binding protein CTCF, the cohesin subunits SMC1A and SMC3 and with MBD2; the factors co-localize with ATRX at the promoters and control regions (ICRs) of imprinted genes during postnatal hepatic development. Loss of Ercc1 or exposure to MMC triggers the localization of CTCF to heterochromatin, the dissociation of the CTCF-cohesin complex and ATRX from promoters and ICRs, altered histone marks and the aberrant developmental expression of imprinted genes without altering DNA methylation. We propose that ERCC1-XPF cooperates with CTCF and cohesin to facilitate the developmental silencing of imprinted genes and that persistent DNA damage triggers chromatin changes that affect gene expression programs associated with NER disorders.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Reparo do DNA
Proteínas de Ligação a DNA/metabolismo
Endonucleases/metabolismo
Inativação Gênica
Impressão Genômica
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Animais Recém-Nascidos
Fator de Ligação a CCCTC
Proteínas de Ciclo Celular/genética
Células Cultivadas
Proteoglicanas de Sulfatos de Condroitina/genética
Proteoglicanas de Sulfatos de Condroitina/metabolismo
Proteínas Cromossômicas não Histona/genética
Técnicas de Cocultura
Dano ao DNA
DNA Helicases/genética
DNA Helicases/metabolismo
Proteínas de Ligação a DNA/genética
Endonucleases/genética
Fibroblastos/enzimologia
Regulação da Expressão Gênica no Desenvolvimento
Genótipo
Histonas/metabolismo
Fígado/enzimologia
Camundongos da Linhagem 129
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Fenótipo
Regiões Promotoras Genéticas
Proteínas Repressoras/genética
Proteína Nuclear Ligada ao X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCCTC-Binding Factor); 0 (Cell Cycle Proteins); 0 (Chondroitin Sulfate Proteoglycans); 0 (Chromosomal Proteins, Non-Histone); 0 (Cspg6 protein, mouse); 0 (Ctcf protein, mouse); 0 (DNA-Binding Proteins); 0 (Histones); 0 (Mbd2 protein, mouse); 0 (Nuclear Proteins); 0 (Repressor Proteins); 0 (cohesins); 0 (structural maintenance of chromosome protein 1); 0 (xeroderma pigmentosum group F protein); EC 3.1.- (Endonucleases); EC 3.1.- (Ercc1 protein, mouse); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (Atrx protein, mouse); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3499


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[PMID]:28271343
[Au] Autor:Karsy M; Guan J; Cohen AL; Jensen RL; Colman H
[Ad] Endereço:Department of Neurosurgery, Clinical Neurosciences Center, University of Utah, Salt Lake City, UT, USA.
[Ti] Título:New Molecular Considerations for Glioma: IDH, ATRX, BRAF, TERT, H3 K27M.
[So] Source:Curr Neurol Neurosci Rep;17(2):19, 2017 Feb.
[Is] ISSN:1534-6293
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE OF REVIEW: This review will discuss the role of several key players in glioma classification and biology, namely isocitrate dehydrogenase 1 and 2 (IDH1/2), alpha thalassemia/mental retardation syndrome X-linked (ATRX), B-Raf (BRAF), telomerase reverse transcriptase (TERT), and H3K27M. RECENT FINDINGS: IDH1/2 mutation delineates oligoden-droglioma, astrocytoma, and secondary glioblastoma (GBM) from primary GBM and lower-grade gliomas with biology similar to GBM. Additional mutations including TERT, 1p/19q, and ATRX further guide glioma classification and diagnosis, as well as pointing directions toward individualized treatments for these distinct molecular subtypes. ATRX and TERT mutations suggest the importance of telomere maintenance in gliomagenesis. BRAF alterations are key in certain low-grade gliomas and pediatric gliomas but rarely in high-grade gliomas in adults. Histone mutations (e.g., H3K27M) and their effect on chromatin modulation are novel mechanisms of cancer generation and uniquely seen in midline gliomas in children and young adults. Over the past decade, a remarkable accumulation of knowledge from the genomic study of gliomas has led to reclassification of tumors, new understanding of oncogenic mechanisms, and novel treatment strategies.
[Mh] Termos MeSH primário: DNA Helicases/genética
Glioma/classificação
Glioma/genética
Histonas/genética
Isocitrato Desidrogenase/genética
Proteínas Nucleares/genética
Proteínas Proto-Oncogênicas B-raf/genética
Telomerase/genética
[Mh] Termos MeSH secundário: Neoplasias Encefálicas/genética
Genômica
Glioma/diagnóstico
Seres Humanos
Mutação
Proteína Nuclear Ligada ao X
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Histones); 0 (Nuclear Proteins); EC 1.1.1.41 (Isocitrate Dehydrogenase); EC 2.7.11.1 (BRAF protein, human); EC 2.7.11.1 (Proto-Oncogene Proteins B-raf); EC 2.7.7.49 (TERT protein, human); EC 2.7.7.49 (Telomerase); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1007/s11910-017-0722-5


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[PMID]:28251430
[Au] Autor:Ogishima T; Tamura K; Kobayashi D; Inaji M; Hayashi S; Tamura R; Nariai T; Ishii K; Maehara T
[Ad] Endereço:Department of Neurosurgery, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo, 113-8519, Japan.
[Ti] Título:ATRX status correlates with 11 C-methionine uptake in WHO grade II and III gliomas with IDH1 mutations.
[So] Source:Brain Tumor Pathol;34(1):20-27, 2017 Jan.
[Is] ISSN:1861-387X
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Recent studies on gliomas have shown frequent alterations in the alpha-thalassemia/mental retardation syndrome X-linked gene (ATRX). This study was designed to determine whether ATRX status correlates with uptake of C-methionine in WHO grades II and III gliomas. Sixty-two patients underwent C-methionine positron emission tomography scans prior to histological diagnosis. The tumor-to-normal ratio (T/N) of C-methionine uptake was calculated by dividing the maximum standardized uptake value (SUV) for the tumor by the mean SUV of the normal brain. After surgery, tumor samples were subjected to immunohistochemistry for ATRX and IDH1-R132H followed by IDH1/2 sequencing. Twenty-seven of the sixty-two patients were found to have the IDH mutation. Nine of the twenty-seven gliomas harboring IDH mutations exhibited loss of nuclear ATRX expression, which is accompanied with an astrocytic tumor lineage and a poor prognosis. The mean T/N ratio in tumors with loss of nuclear ATRX expression was 2.20 ± 0.53, i.e., significantly lower than that of tumors with ATRX retention (3.28 ± 1.32, p = 0.0171, U test). Our study showed ATRX status to correlate with the T/N ratio and the outcomes of WHO grade II and III glioma patients with the IDH1 mutation. Our data provide new information on the biology and imaging characteristics of gliomas.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/genética
DNA Helicases/genética
Glioma/genética
Isocitrato Desidrogenase/genética
Mutação/genética
Proteínas Nucleares/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Astrocitoma/patologia
Neoplasias Encefálicas/patologia
Feminino
Glioma/diagnóstico
Glioma/patologia
Seres Humanos
Imuno-Histoquímica/métodos
Masculino
Metionina/metabolismo
Meia-Idade
Gradação de Tumores/métodos
Proteína Nuclear Ligada ao X
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); AE28F7PNPL (Methionine); EC 1.1.1.41 (Isocitrate Dehydrogenase); EC 1.1.1.42. (IDH1 protein, human); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170303
[St] Status:MEDLINE
[do] DOI:10.1007/s10014-017-0280-1



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