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[PMID]:28448977
[Au] Autor:Aydemir L; Bireller ES; Avci H; Boy Metin Z; Deger K; Unur M; Cakmakoglu B
[Ad] Endereço:Department of Otolaryngology, Faculty of Medicine, Istanbul University, Istanbul, Turkey.
[Ti] Título:Is Human Oxoguanine Glycosylase 1 Genetic Variant Successful Even on Oral Squamous Cell Carcinoma?
[So] Source:Pathobiology;84(4):223-228, 2017.
[Is] ISSN:1423-0291
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Oral squamous cell carcinoma (OSCC) is one of the most widespread cancer types that arise from different sites of oral cavity and has a 5-year survival rate. This study is aimed at investigating the human oxoguanine glycosylase 1 (hOGG1)-Ser326Cys and APE-Asp148Glu polymorphisms of DNA repair genes in OSCC. MATERIALS AND METHODS: We investigated the hOGG1-Ser326Cys and APE-Asp148Glu polymorphisms of DNA repair genes in the oral cavity. Genotyping was conducted using polymerase chain reaction-restriction fragment length polymorphism analysis based on 132 patients who were diagnosed as having OSCC and 160 healthy subjects. RESULTS: Individuals with the genotype hOGG1-Ser326Cys, Cys allele carriers, were found significantly more frequently in the patient group compared to the control group as increase in risk (p < 0.001). Furthermore, it was observed that there were significantly more individuals with the Ser allele in the control group (p < 0.001). Individuals with genotype APE-Asp148Glu were not statistically significant; however, they were still more in the control group and provided protection against the disease. CONCLUSION: Our findings showed that hOGG1-Ser326Cys Cys allele is statistically important and relevant with respect to the development of oral squamous cancer. In view of our results, further studies including expression levels are required in which hOGG1-Ser326Cys should be investigated as molecular biomarkers for the early prediction of squamous cell carcinoma.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/genética
DNA Glicosilases/genética
Variação Genética
Neoplasias Bucais/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Alelos
Carcinoma de Células Escamosas/enzimologia
Carcinoma de Células Escamosas/patologia
Feminino
Genótipo
Seres Humanos
Masculino
Neoplasias Bucais/enzimologia
Neoplasias Bucais/patologia
Polimorfismo de Fragmento de Restrição
Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (oxoguanine glycosylase 1, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1159/000466702


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[PMID]:28747435
[Au] Autor:Hendershot JM; O'Brien PJ
[Ad] Endereço:From the Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0600.
[Ti] Título:Search for DNA damage by human alkyladenine DNA glycosylase involves early intercalation by an aromatic residue.
[So] Source:J Biol Chem;292(39):16070-16080, 2017 09 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA repair enzymes recognize and remove damaged bases that are embedded in the duplex. To gain access, most enzymes use nucleotide flipping, whereby the target nucleotide is rotated 180° into the active site. In human alkyladenine DNA glycosylase (AAG), the enzyme that initiates base excision repair of alkylated bases, the flipped-out nucleotide is stabilized by intercalation of the side chain of tyrosine 162 that replaces the lesion nucleobase. Previous kinetic studies provided evidence for the formation of a transient complex that precedes the stable flipped-out complex, but it is not clear how this complex differs from nonspecific complexes. We used site-directed mutagenesis and transient-kinetic approaches to investigate the timing of Tyr intercalation for AAG. The tryptophan substitution (Y162W) appeared to be conservative, because the mutant protein retained a highly favorable equilibrium constant for flipping the 1, -ethenoadenine (ϵA) lesion, and the rate of -glycosidic bond cleavage was identical to that of the wild-type enzyme. We assigned the tryptophan fluorescence signal from Y162W by removing two native tryptophan residues (W270A/W284A). Stopped-flow experiments then demonstrated that the change in tryptophan fluorescence of the Y162W mutant is extremely rapid upon binding to either damaged or undamaged DNA, much faster than the lesion-recognition and nucleotide flipping steps that were independently determined by monitoring the ϵA fluorescence. These observations suggest that intercalation by this aromatic residue is one of the earliest steps in the search for DNA damage and that this interaction is important for the progression of AAG from nonspecific searching to specific-recognition complexes.
[Mh] Termos MeSH primário: Dano ao DNA
DNA Glicosilases/metabolismo
Reparo do DNA
DNA/metabolismo
Modelos Moleculares
Tirosina/química
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Sítios de Ligação
Biocatálise
Domínio Catalítico
DNA/química
DNA Glicosilases/química
DNA Glicosilases/genética
Seres Humanos
Cinética
Mutagênese Sítio-Dirigida
Mutação
Conformação de Ácido Nucleico
Motivos de Nucleotídeos
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptide Fragments); 0 (Recombinant Proteins); 42HK56048U (Tyrosine); 9007-49-2 (DNA); EC 3.2.2.- (3-methyladenine-DNA glycosylase); EC 3.2.2.- (DNA Glycosylases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171230
[Lr] Data última revisão:
171230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.782813


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[PMID]:29227732
[Au] Autor:Lin Z; Xu W; Li C; Wang Y; Yang L; Zou B; Gao S; Yao W; Song Z; Liu G
[Ad] Endereço:1 Clinical Research Center, Affiliated Hospital of Guangdong Medical University , Zhanjiang, China .
[Ti] Título:ß-8-Oxoguanine DNA Glycosylase Overexpression Reduces Oxidative Stress-Induced Mitochondrial Dysfunction and Apoptosis Through the JNK Signaling Pathway in Human Bronchial Epithelial Cells.
[So] Source:DNA Cell Biol;36(12):1071-1080, 2017 Dec.
[Is] ISSN:1557-7430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:8-Oxoguanine DNA glycosylase (OGG1) is responsible for repairing 8-oxo-7,8-dihydroguanine (8-oxoG). Our previous study demonstrated that α-OGG1 protects cells from oxidative damage-induced apoptosis and mitochondrial dysfunction in human lung cancer cells. However, the function of ß-OGG1 remains to be elucidated. In this study, we demonstrated that overexpressed ß-OGG1 has the same role as α-OGG1 in protecting human bronchial epithelial cells from apoptosis and mitochondrial dysfunction. Furthermore, flow cytometry, confocal microscopy, and western blotting showed that the overexpression of ß-OGG1 could block oxidant-induced apoptosis in human bronchial epithelial cells. Additionally, knocking down OGG1 enhanced oxidative damage-induced apoptosis and mitochondrial dysfunction, whereas the overexpression of ß-OGG1 had the opposite effects and led to the downregulation of Bax and PARP. The antiapoptotic function of ß-OGG1 involved the JNK signaling pathway. These findings suggest that ß-OGG1 and α-OGG1 have a similar function on preventing oxidative damage-mediated apoptosis and mitochondrial dysfunction; these effects might be important in the molecular events underlying oxidant-induced cytotoxicity.
[Mh] Termos MeSH primário: Brônquios/metabolismo
DNA Glicosilases/metabolismo
Sistema de Sinalização das MAP Quinases
[Mh] Termos MeSH secundário: Apoptose
Brônquios/citologia
Linhagem Celular
Sobrevivência Celular
Dano ao DNA
DNA Glicosilases/antagonistas & inibidores
DNA Glicosilases/genética
Reparo do DNA
Regulação para Baixo
Células Epiteliais/citologia
Células Epiteliais/metabolismo
Técnicas de Silenciamento de Genes
Seres Humanos
Isoenzimas/antagonistas & inibidores
Isoenzimas/genética
Isoenzimas/metabolismo
Mitocôndrias/metabolismo
Estresse Oxidativo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (oxoguanine glycosylase 1, human)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.1089/dna.2017.3769


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[PMID]:29215473
[Au] Autor:Kallenberg FGJ; Latchford A; Lips NC; Aalfs CM; Bastiaansen BAJ; Clark SK; Dekker E
[Ad] Endereço:Department of Gastroenterology and Hepatology, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands.
[Ti] Título:Duodenal Adenomas in Patients With Multiple Colorectal Adenomas Without Germline APC or MUTYH Mutations.
[So] Source:Dis Colon Rectum;61(1):58-66, 2018 Jan.
[Is] ISSN:1530-0358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Patients with genetic adenomatous polyposis syndromes have an increased risk for duodenal cancer, and clear surveillance recommendations exist for this group. However, limited data are available on the duodenal phenotype of patients with multiple colorectal adenomas (10-99) without a germline APC or MUTYH mutation. OBJECTIVE: We aimed to assess the frequency, extent, and progression of duodenal adenomas in patients with multiple colorectal adenomas without a germline APC or MUTYH mutation. DESIGN: This was an historical cohort study. SETTINGS: This study was undertaken at 2 polyposis registries: the Academic Medical Center in the Netherlands, and St. Mark's Hospital in the United Kingdom. PATIENTS: We collected data on all patients with 10 to 99 colorectal adenomas and absent APC and MUTYH mutations, who underwent ≥1 esophagogastroduodenoscopy. MAIN OUTCOME MEASURES: The frequency, extent, and progression of duodenal adenomas were measured. Demographic and endoscopic data were collected, described, and compared between patients with and without duodenal adenomas. RESULTS: Eighty-three patients were identified, of which 8 (9.6%) had duodenal adenomas, detected at a median of 58 years (range, 45-75 y). Duodenal adenomas were detected in 6 of 8 patients at first esophagogastroduodenoscopy. At diagnosis, all 8 patients had Spigelman stage I or II disease. Two of 5 patients with duodenal adenomas who underwent follow-up esophagogastroduodenoscopies increased to stage III disease. The other 3 remained stable. No one developed duodenal cancer. No differences in demographic and endoscopic data were found between patients with and without duodenal adenomas. LIMITATIONS: This study was limited by its retrospective design, selection bias, and small sample size. CONCLUSIONS: Duodenal adenomas are found in a minority of patients with multiple colorectal adenomas without a germline APC or MUTYH mutation, at an average age of 58 years, and, at diagnosis, disease severity is mild. These results are a first step in unraveling the duodenal phenotype of these patients, which is needed to provide appropriate upper GI screening and surveillance recommendations. See Video Abstract at http://links.lww.com/DCR/A357.
[Mh] Termos MeSH primário: Polipose Adenomatosa do Colo/genética
DNA Glicosilases/genética
Neoplasias Duodenais/genética
Genes APC/fisiologia
[Mh] Termos MeSH secundário: Adenoma/epidemiologia
Adenoma/genética
Polipose Adenomatosa do Colo/epidemiologia
Idoso
Neoplasias Duodenais/epidemiologia
Feminino
Mutação em Linhagem Germinativa
Seres Humanos
Masculino
Meia-Idade
Países Baixos/epidemiologia
Sistema de Registros
Estudos Retrospectivos
Reino Unido/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; MULTICENTER STUDY
[Nm] Nome de substância:
EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (mutY adenine glycosylase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171215
[Lr] Data última revisão:
171215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1097/DCR.0000000000000868


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[PMID]:28891849
[Au] Autor:Kallenberg FGJ; Bastiaansen BAJ; Nio CY; Soeters MR; Boermeester MA; Aalfs CM; Bossuyt PMM; Dekker E
[Ad] Endereço:1 Department of Gastroenterology and Hepatology, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands 2 Department of Radiology, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands 3 Department of Endocrinology, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands 4 Department of Surgery, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands 5 Department of Clinical Genetics, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands 6 Department of Clinical Epidemiology, Biostatistics, and Bioinformatics, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands.
[Ti] Título:Adrenal Lesions in Patients With (Attenuated) Familial Adenomatous Polyposis and MUTYH-Associated Polyposis.
[So] Source:Dis Colon Rectum;60(10):1057-1064, 2017 Oct.
[Is] ISSN:1530-0358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The reported proportion of patients with familial adenomatous polyposis who have adrenal lesions varies between 7% and 13% compared with 4% in the general population; the prevalence of adrenal lesions in patients with attenuated familial adenomatous polyposis and MUTYH-associated polyposis is unknown. Data on the clinical relevance and clinical course are limited. OBJECTIVE: We aimed to report on the frequency, characteristics, and progression of adrenal lesions in polyposis patients. DESIGN: This was a historical cohort study. SETTINGS: The study was performed at the Academic Medical Center, Amsterdam. PATIENTS: All of the patients with familial adenomatous polyposis, attenuated familial adenomatous polyposis, and MUTYH-associated polyposis were included. Medical charts and imaging reports were analyzed for data on adrenal lesions. A radiologist reassessed all of the images. Patients had not routinely been screened for adrenal lesions. MAIN OUTCOME MEASURES: The frequency, characteristics, and progression of adrenal lesions in patients with polyposis who underwent abdominal imaging were assessed. Findings were compared with a reference. RESULTS: A total of 39 adrenal lesions were identified in 23 (26%) of 90 patients with familial adenomatous polyposis, 2 (18%) of 11 with attenuated familial adenomatous polyposis, and 5 (24%) of 21 with MUTYH-associated polyposis. Mean age at time of detection was 50.7 years (range, 17.1-83.3 y). Median lesion size at baseline was 1.4 cm (range, 1.0-5.0 cm) versus 1.7 cm (range, 1.0-5.7 cm) after a median of 3.5 years (range, 1.0-11.4 y). Two patients were diagnosed with a hyperfunctioning lesion, and 4 underwent adrenalectomy: 3 lesions appeared benign, and 1 was oncocytic of uncertain malignant potential. The OR for detecting at least 1 lesion in a patient with polyposis versus reference was 6.2 (95% CI, 3.2-12.3), with no significant differences in ORs among the 3 syndromes. LIMITATIONS: The study was limited by its retrospective design. CONCLUSIONS: Adrenal lesions are frequent in patients with polyposis who undergo abdominal imaging. They appear to follow a benign and slowly progressive course and are mostly nonhyperfunctioning. See Abstract Video at http://links.lww.com/DCR/A323.
[Mh] Termos MeSH primário: Neoplasias das Glândulas Suprarrenais
Glândulas Suprarrenais/diagnóstico por imagem
DNA Glicosilases/genética
[Mh] Termos MeSH secundário: Polipose Adenomatosa do Colo/epidemiologia
Polipose Adenomatosa do Colo/genética
Polipose Adenomatosa do Colo/patologia
Polipose Adenomatosa do Colo/cirurgia
Neoplasias das Glândulas Suprarrenais/epidemiologia
Neoplasias das Glândulas Suprarrenais/patologia
Neoplasias das Glândulas Suprarrenais/fisiopatologia
Neoplasias das Glândulas Suprarrenais/cirurgia
Adrenalectomia/estatística & dados numéricos
Adulto
Colectomia/métodos
Colectomia/estatística & dados numéricos
Feminino
Seres Humanos
Imagem por Ressonância Magnética/estatística & dados numéricos
Masculino
Meia-Idade
Países Baixos/epidemiologia
Tomografia Computadorizada com Tomografia por Emissão de Pósitrons/estatística & dados numéricos
Estudos Retrospectivos
Estatística como Assunto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (mutY adenine glycosylase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE
[do] DOI:10.1097/DCR.0000000000000809


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[PMID]:28886188
[Au] Autor:Margulies CM; Chaim IA; Mazumder A; Criscione J; Samson LD
[Ad] Endereço:Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America.
[Ti] Título:Alkylation induced cerebellar degeneration dependent on Aag and Parp1 does not occur via previously established cell death mechanisms.
[So] Source:PLoS One;12(9):e0184619, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alkylating agents are ubiquitous in our internal and external environments, causing DNA damage that contributes to mutations and cell death that can result in aging, tissue degeneration and cancer. Repair of methylated DNA bases occurs primarily through the base excision repair (BER) pathway, a multi-enzyme pathway initiated by the alkyladenine DNA glycosylase (Aag, also known as Mpg). Previous work demonstrated that mice treated with the alkylating agent methyl methanesulfonate (MMS) undergo cerebellar degeneration in an Aag-dependent manner, whereby increased BER initiation by Aag causes increased tissue damage that is dependent on activation of poly (ADP-ribose) polymerase 1 (Parp1). Here, we dissect the molecular mechanism of cerebellar granule neuron (CGN) sensitivity to MMS using primary ex vivo neuronal cultures. We first established a high-throughput fluorescent imaging method to assess primary neuron sensitivity to treatment with DNA damaging agents. Next, we verified that the alkylation sensitivity of CGNs is an intrinsic phenotype that accurately recapitulates the in vivo dependency of alkylation-induced CGN cell death on Aag and Parp1 activity. Finally, we show that MMS-induced CGN toxicity is independent of all the cellular events that have previously been associated with Parp-mediated toxicity, including mitochondrial depolarization, AIF translocation, calcium fluxes, and NAD+ consumption. We therefore believe that further investigation is needed to adequately describe all varieties of Parp-mediated cell death.
[Mh] Termos MeSH primário: Cerebelo/citologia
DNA Glicosilases/metabolismo
Neurônios/citologia
Neurônios/metabolismo
Poli(ADP-Ribose) Polimerase-1/metabolismo
[Mh] Termos MeSH secundário: Alquilantes/farmacologia
Alquilação/efeitos dos fármacos
Animais
Morte Celular/efeitos dos fármacos
Células Cultivadas
DNA Glicosilases/genética
Reparo do DNA/efeitos dos fármacos
Reparo do DNA/genética
Hibridização in Situ Fluorescente
Metanossulfonato de Metila/farmacologia
Camundongos
Poli(ADP-Ribose) Polimerase-1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alkylating Agents); AT5C31J09G (Methyl Methanesulfonate); EC 2.4.2.30 (Parp1 protein, mouse); EC 2.4.2.30 (Poly (ADP-Ribose) Polymerase-1); EC 3.2.2.- (3-methyladenine-DNA glycosylase); EC 3.2.2.- (DNA Glycosylases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184619


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[PMID]:28843610
[Au] Autor:Seifermann M; Ulges A; Bopp T; Melcea S; Schäfer A; Oka S; Nakabeppu Y; Klungland A; Niehrs C; Epe B
[Ad] Endereço:Institute of Pharmacy and Biochemistry, University of Mainz, Staudingerweg 5, D-55099 Mainz, Germany.
[Ti] Título:Role of the DNA repair glycosylase OGG1 in the activation of murine splenocytes.
[So] Source:DNA Repair (Amst);58:13-20, 2017 Oct.
[Is] ISSN:1568-7856
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:OGG1 (8-oxoguanine-DNA glycosylase) is the major DNA repair glycosylase removing the premutagenic DNA base modification 8-oxo-7,8-dihydroguanine (8-oxoG) from the genome of mammalian cells. In addition, there is accumulating evidence that OGG1 and its substrate 8-oxoG might function in the regulation of certain genes, which could account for an attenuated immune response observed in Ogg1 mice in several settings. Indications for at least two different mechanisms have been obtained. Thus, OGG1 could either act as an ancillary transcription factor cooperating with the lysine-specific demethylase LSD1 or as an activator of small GTPases. Here, we analysed the activation by lipopolysaccaride (LPS) of primary splenocytes obtained from two different Ogg1 mouse strains. We found that the induction of TNF-α expression was reduced in splenocytes (in particular macrophages) of both Ogg1 strains. Notably, an inhibitor of LSD1, OG-L002, reduced the induction of TNF-α mRNA in splenocytes from wild-type mice to the level observed in splenocytes from Ogg1 mice and had no influence in the latter cells. In contrast, inhibitors of the MAP kinases p38 and JNK as well as the antioxidant N-acetylcysteine attenuated the LPS-stimulated TNF-α expression both in the absence and presence of OGG1. The free base 8-oxo-7,8-dihydroguanine had no influence on the TNF-α expression in the splenocytes. The data demonstrate that OGG1 plays a role in an LSD1-dependent pathway of LPS-induced macrophage activation in mice.
[Mh] Termos MeSH primário: DNA Glicosilases/imunologia
Baço/imunologia
Fator de Necrose Tumoral alfa/genética
[Mh] Termos MeSH secundário: Animais
DNA/metabolismo
Dano ao DNA
DNA Glicosilases/metabolismo
DNA Glicosilases/fisiologia
Reparo do DNA
Regulação da Expressão Gênica
Guanina/análogos & derivados
Guanina/metabolismo
Macrófagos/imunologia
Macrófagos/metabolismo
Camundongos
Baço/citologia
Baço/metabolismo
Fatores de Transcrição/imunologia
Fatores de Transcrição/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Transcription Factors); 0 (Tumor Necrosis Factor-alpha); 5614-64-2 (8-hydroxyguanine); 5Z93L87A1R (Guanine); 9007-49-2 (DNA); EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (Ogg1 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170828
[St] Status:MEDLINE


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[PMID]:28787572
[Au] Autor:Rodriguez G; Esadze A; Weiser BP; Schonhoft JD; Cole PA; Stivers JT
[Ad] Endereço:Department of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine , 725 North Wolfe Street, Baltimore, Maryland 21205-2185, United States.
[Ti] Título:Disordered N-Terminal Domain of Human Uracil DNA Glycosylase (hUNG2) Enhances DNA Translocation.
[So] Source:ACS Chem Biol;12(9):2260-2263, 2017 Sep 15.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nuclear human uracil-DNA glycosylase (hUNG2) initiates base excision repair (BER) of genomic uracils generated through misincorporation of dUMP or through deamination of cytosines. Like many human DNA glycosylases, hUNG2 contains an unstructured N-terminal domain that encodes a nuclear localization signal, protein binding motifs, and sites for post-translational modifications. Although the N-terminal domain has minimal effects on DNA binding and uracil excision kinetics, we report that this domain enhances the ability of hUNG2 to translocate on DNA chains as compared to the catalytic domain alone. The enhancement is most pronounced when physiological ion concentrations and macromolecular crowding agents are used. These data suggest that crowded conditions in the human cell nucleus promote the interaction of the N-terminus with duplex DNA during translocation. The increased contact time with the DNA chain likely contributes to the ability of hUNG2 to locate densely spaced uracils that arise during somatic hypermutation and during fluoropyrimidine chemotherapy.
[Mh] Termos MeSH primário: DNA Glicosilases/metabolismo
DNA/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Transporte Biológico
DNA Glicosilases/química
Seres Humanos
Sinais de Localização Nuclear/química
Sinais de Localização Nuclear/metabolismo
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Localization Signals); 9007-49-2 (DNA); EC 3.2.2.- (CCNO protein, human); EC 3.2.2.- (DNA Glycosylases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00521


  9 / 3416 MEDLINE  
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[PMID]:28727777
[Au] Autor:Vartanian V; Tumova J; Dobrzyn P; Dobrzyn A; Nakabeppu Y; Lloyd RS; Sampath H
[Ad] Endereço:From the Oregon Institute of Occupational Health Sciences, Oregon Health & Science University, Portland, Oregon, United States of America.
[Ti] Título:8-oxoguanine DNA glycosylase (OGG1) deficiency elicits coordinated changes in lipid and mitochondrial metabolism in muscle.
[So] Source:PLoS One;12(7):e0181687, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oxidative stress resulting from endogenous and exogenous sources causes damage to cellular components, including genomic and mitochondrial DNA. Oxidative DNA damage is primarily repaired via the base excision repair pathway that is initiated by DNA glycosylases. 8-oxoguanine DNA glycosylase (OGG1) recognizes and cleaves oxidized and ring-fragmented purines, including 8-oxoguanine, the most commonly formed oxidative DNA lesion. Mice lacking the OGG1 gene product are prone to multiple features of the metabolic syndrome, including high-fat diet-induced obesity, hepatic steatosis, and insulin resistance. Here, we report that OGG1-deficient mice also display skeletal muscle pathologies, including increased muscle lipid deposition and alterations in genes regulating lipid uptake and mitochondrial fission in skeletal muscle. In addition, expression of genes of the TCA cycle and of carbohydrate and lipid metabolism are also significantly altered in muscle of OGG1-deficient mice. These tissue changes are accompanied by marked reductions in markers of muscle function in OGG1-deficient animals, including decreased grip strength and treadmill endurance. Collectively, these data indicate a role for skeletal muscle OGG1 in the maintenance of optimal tissue function.
[Mh] Termos MeSH primário: DNA Glicosilases/deficiência
Metabolismo dos Lipídeos/fisiologia
Mitocôndrias/metabolismo
Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: Adiposidade
Animais
Dano ao DNA/fisiologia
DNA Glicosilases/genética
DNA Mitocondrial/metabolismo
Ácidos Graxos/metabolismo
Perfilação da Expressão Gênica
Masculino
Camundongos Endogâmicos C57BL
Mitocôndrias/genética
Dinâmica Mitocondrial/fisiologia
Modelos Animais
Força Muscular/fisiologia
Músculo Esquelético/patologia
Resistência Física/fisiologia
Ácido Pirúvico/metabolismo
Corrida/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (Fatty Acids); 8558G7RUTR (Pyruvic Acid); EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (Ogg1 protein, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181687


  10 / 3416 MEDLINE  
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[PMID]:28723094
[Au] Autor:Manlove AH; McKibbin PL; Doyle EL; Majumdar C; Hamm ML; David SS
[Ad] Endereço:Department of Chemistry, University of California at Davis , One Shields Avenue, Davis, California 95616, United States.
[Ti] Título:Structure-Activity Relationships Reveal Key Features of 8-Oxoguanine: A Mismatch Detection by the MutY Glycosylase.
[So] Source:ACS Chem Biol;12(9):2335-2344, 2017 Sep 15.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Base excision repair glycosylases locate and remove damaged bases in DNA with remarkable specificity. The MutY glycosylases, unusual for their excision of undamaged adenines mispaired to the oxidized base 8-oxoguanine (OG), must recognize both bases of the mispair in order to prevent promutagenic activity. Moreover, MutY must effectively find OG:A mismatches within the context of highly abundant and structurally similar T:A base pairs. Very little is known about the factors that initiate MutY's interaction with the substrate when it first encounters an intrahelical OG:A mispair, or about the order of recognition checkpoints. Here, we used structure-activity relationships (SAR) to investigate the features that influence the in vitro measured parameters of mismatch affinity and adenine base excision efficiency by E. coli MutY. We also evaluated the impacts of the same substrate alterations on MutY-mediated repair in a cellular context. Our results show that MutY relies strongly on the presence of the OG base and recognizes multiple structural features at different stages of recognition and catalysis to ensure that only inappropriately mispaired adenines are excised. Notably, some OG modifications resulted in more dramatic reductions in cellular repair than in the in vitro kinetic parameters, indicating their importance for initial recognition events needed to locate the mismatch within DNA. Indeed, the initial encounter of MutY with its target base pair may rely on specific interactions with the 2-amino group of OG in the major groove, a feature that distinguishes OG:A from T:A base pairs. These results furthermore suggest that inefficient substrate location in human MutY homologue variants may prove predictive for the early onset colorectal cancer phenotype known as MUTYH-Associated Polyposis, or MAP.
[Mh] Termos MeSH primário: Adenina/metabolismo
Pareamento Incorreto de Bases
DNA Glicosilases/metabolismo
Reparo do DNA
Escherichia coli/enzimologia
Guanina/análogos & derivados
[Mh] Termos MeSH secundário: Adenina/análise
Escherichia coli/química
Escherichia coli/genética
Escherichia coli/metabolismo
Guanina/análise
Guanina/metabolismo
Modelos Moleculares
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
5614-64-2 (8-hydroxyguanine); 5Z93L87A1R (Guanine); EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (mutY adenine glycosylase); JAC85A2161 (Adenine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00389



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