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Pesquisa : D08.811.277.040.013.500 [Categoria DeCS]
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[PMID]:29182013
[Au] Autor:Dickerson T; Jauregui CE; Teng Y
[Ad] Endereço:College of Science & Mathematics, Augusta University, Augusta, GA 30912, USA.
[Ti] Título:Friend or foe? Mitochondria as a pharmacological target in cancer treatment.
[So] Source:Future Med Chem;9(18):2197-2210, 2017 12.
[Is] ISSN:1756-8927
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mitochondria have acquired numerous functions over the course of evolution, such as those involved in controlling energy production, cellular metabolism, cell survival, apoptosis and autophagy within host cells. Tumor cells can develop defects in mitochondrial function, presenting a potential strategy for designing selective anticancer therapies. Therefore, cancer has been the main focus of recent research to uncover possible mitochondrial targets for therapeutic benefit. This comprehensive review covers not only the recent discoveries of the roles of mitochondria in cancer development, progression and therapeutic implications but also the findings regarding emerging mitochondrial therapeutic targets and mitochondria-targeted agents. Current challenges and future directions for developments and applications of mitochondrial-targeted therapeutics are also discussed.
[Mh] Termos MeSH primário: Mitocôndrias/metabolismo
Neoplasias/tratamento farmacológico
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Antineoplásicos/farmacologia
Antineoplásicos/uso terapêutico
DNA Mitocondrial/efeitos dos fármacos
DNA Mitocondrial/metabolismo
Metabolismo Energético/efeitos dos fármacos
Seres Humanos
Proteínas de Membrana/metabolismo
Mitocôndrias/genética
Proteínas Mitocondriais/metabolismo
Neoplasias/metabolismo
Neoplasias/patologia
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ATAD3A protein, human); 0 (Antineoplastic Agents); 0 (DNA, Mitochondrial); 0 (Membrane Proteins); 0 (Mitochondrial Proteins); 0 (Reactive Oxygen Species); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.4155/fmc-2017-0110


  2 / 1106 MEDLINE  
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[PMID]:29413990
[Au] Autor:Kelly J; Murphy JE
[Ad] Endereço:Mitochondrial Biology & Radiation Research Centre, Dept. of Life Sciences, Institute of Technology Sligo, Ash Lane, Sligo, Ireland. Electronic address: janiskelly@mail.itsligo.ie.
[Ti] Título:Mitochondrial gene expression changes in cultured human skin cells following simulated sunlight irradiation.
[So] Source:J Photochem Photobiol B;179:167-174, 2018 Feb.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Exposure of skin to simulated sunlight irradiation (SSI) has being extensively researched and shown to be the main cause for changes in the skin including changes in cellular function and generation of reactive oxygen species (ROS). This oxidative stress can subsequently exert downstream effects and the subcellular compartments most affected by this oxidative stress are mitochondria. The importance of functional mitochondrial morphology is apparent as morphological defects are related to many human diseases including diabetes mellitus, liver disease, neurodegenerative diseases, aging and cancer. OBJECTIVE: The main objective of this study was to evaluate solar radiation-induced changes in mitochondrial gene expression in human skin cells using a Q-Sun solar simulator to deliver a close match to the intensity of summer sunlight. METHODS: Spontaneously immortalised human skin epidermal keratinocytes (HaCaT) and Human Dermal Fibroblasts (HDFn) were divided into two groups. Group A were irradiated once and Group B twice 7days apart; following irradiation, mitochondrial gene expression was evaluated 1, 4 and 7days post primary exposure for group A and 1, 4, 7 and 14days post-secondary exposure for group B. RESULTS: Both the epidermal and dermal cells displayed significant reduced expression of the genes analysed for mitochondrial morphology and function; however, epidermal cells displayed this reduction post SSI earlier then dermal cells at multiple time points. CONCLUSION: The data presented here reinforces the fact that epidermal cells, while displaying a heightened sensitivity to sunlight, are less prone to changes in gene expression, while dermal cells, which appear to be more resilient are possibly more prone to genomic instability and mitochondrial damage.
[Mh] Termos MeSH primário: Expressão Gênica/efeitos da radiação
Mitocôndrias/genética
Luz Solar
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares/genética
ATPases Associadas a Diversas Atividades Celulares/metabolismo
Linhagem Celular
Derme/citologia
Epiderme/citologia
GTP Fosfo-Hidrolases/genética
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Queratinócitos/citologia
Queratinócitos/metabolismo
Queratinócitos/efeitos da radiação
Metaloendopeptidases/genética
Metaloendopeptidases/metabolismo
Mitocôndrias/efeitos da radiação
Proteínas de Transporte da Membrana Mitocondrial/genética
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Superóxido Dismutase/genética
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Membrane Transport Proteins); 0 (Mitochondrial Proteins); 0 (Reactive Oxygen Species); EC 1.15.1.1 (Superoxide Dismutase); EC 1.15.1.1 (superoxide dismutase 2); EC 3.4.24.- (Metalloendopeptidases); EC 3.4.24.- (YME1L1 protein, human); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (MFN2 protein, human); EC 3.6.1.- (OPA1 protein, human); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities); EC 3.6.5.- (Mfn1 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180208
[St] Status:MEDLINE


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[PMID]:29220678
[Au] Autor:Falkenberg KD; Braverman NE; Moser AB; Steinberg SJ; Klouwer FCC; Schlüter A; Ruiz M; Pujol A; Engvall M; Naess K; van Spronsen F; Körver-Keularts I; Rubio-Gozalbo ME; Ferdinandusse S; Wanders RJA; Waterham HR
[Ad] Endereço:Laboratory Genetic Metabolic Diseases, Academic Medical Center, University of Amsterdam, Amsterdam 1105 AZ, the Netherlands.
[Ti] Título:Allelic Expression Imbalance Promoting a Mutant PEX6 Allele Causes Zellweger Spectrum Disorder.
[So] Source:Am J Hum Genet;101(6):965-976, 2017 Dec 07.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Zellweger spectrum disorders (ZSDs) are autosomal-recessive disorders that are caused by defects in peroxisome biogenesis due to bi-allelic mutations in any of 13 different PEX genes. Here, we identified seven unrelated individuals affected with an apparent dominant ZSD in whom a heterozygous mutant PEX6 allele (c.2578C>T [p.Arg860Trp]) was overrepresented due to allelic expression imbalance (AEI). We demonstrated that AEI of PEX6 is a common phenomenon and is correlated with heterozygosity for a frequent variant in the 3' untranslated region (UTR) of the mutant allele, which disrupts the most distal of two polyadenylation sites. Asymptomatic parents, who were heterozygous for PEX c.2578C>T, did not show AEI and were homozygous for the 3' UTR variant. Overexpression models confirmed that the overrepresentation of the pathogenic PEX6 c.2578T variant compared to wild-type PEX6 c.2578C results in a peroxisome biogenesis defect and thus constitutes the cause of disease in the affected individuals. AEI promoting the overrepresentation of a mutant allele might also play a role in other autosomal-recessive disorders, in which only one heterozygous pathogenic variant is identified.
[Mh] Termos MeSH primário: Regiões 3´ não Traduzidas/genética
ATPases Associadas a Diversas Atividades Celulares/genética
Desequilíbrio Alélico/genética
Síndrome de Zellweger/genética
[Mh] Termos MeSH secundário: Alelos
Células Cultivadas
Feminino
Regulação da Expressão Gênica/genética
Predisposição Genética para Doença
Seres Humanos
Masculino
Peroxissomos/genética
Peroxissomos/patologia
Sequenciamento Completo do Exoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities); EC 3.6.4.- (PEX6 protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


  4 / 1106 MEDLINE  
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[PMID]:29321502
[Au] Autor:Gardner BM; Castanzo DT; Chowdhury S; Stjepanovic G; Stefely MS; Hurley JH; Lander GC; Martin A
[Ad] Endereço:Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, 94720, USA.
[Ti] Título:The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading.
[So] Source:Nat Commun;9(1):135, 2018 01 10.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pex1 and Pex6 form a heterohexameric motor essential for peroxisome biogenesis and function, and mutations in these AAA-ATPases cause most peroxisome-biogenesis disorders in humans. The tail-anchored protein Pex15 recruits Pex1/Pex6 to the peroxisomal membrane, where it performs an unknown function required for matrix-protein import. Here we determine that Pex1/Pex6 from S. cerevisiae is a protein translocase that unfolds Pex15 in a pore-loop-dependent and ATP-hydrolysis-dependent manner. Our structural studies of Pex15 in isolation and in complex with Pex1/Pex6 illustrate that Pex15 binds the N-terminal domains of Pex6, before its C-terminal disordered region engages with the pore loops of the motor, which then processively threads Pex15 through the central pore. Furthermore, Pex15 directly binds the cargo receptor Pex5, linking Pex1/Pex6 to other components of the peroxisomal import machinery. Our results thus support a role of Pex1/Pex6 in mechanical unfolding of peroxins or their extraction from the peroxisomal membrane during matrix-protein import.
[Mh] Termos MeSH primário: ATPases Associadas a Diversas Atividades Celulares/metabolismo
Proteínas de Membrana/metabolismo
Peroxissomos/enzimologia
Fosfoproteínas/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/antagonistas & inibidores
Conformação Proteica
Saccharomyces cerevisiae
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (PEX15 protein, S cerevisiae); 0 (Phosphoproteins); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities); EC 3.6.4.- (PEX1 protein, S cerevisiae); EC 3.6.4.- (PEX6 protein, S cerevisiae)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02474-4


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[PMID]:29242539
[Au] Autor:Jin G; Xu C; Zhang X; Long J; Rezaeian AH; Liu C; Furth ME; Kridel S; Pasche B; Bian XW; Lin HK
[Ad] Endereço:Institute of Pathology and Southwest Cancer Center, Southwest Hospital, Third Military Medical University, Chongqing, China.
[Ti] Título:Atad3a suppresses Pink1-dependent mitophagy to maintain homeostasis of hematopoietic progenitor cells.
[So] Source:Nat Immunol;19(1):29-40, 2018 Jan.
[Is] ISSN:1529-2916
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although deletion of certain autophagy-related genes has been associated with defects in hematopoiesis, it remains unclear whether hyperactivated mitophagy affects the maintenance and differentiation of hematopoietic stem cells (HSCs) and committed progenitor cells. Here we report that targeted deletion of the gene encoding the AAA+-ATPase Atad3a hyperactivated mitophagy in mouse hematopoietic cells. Affected mice showed reduced survival, severely decreased bone-marrow cellularity, erythroid anemia and B cell lymphopenia. Those phenotypes were associated with skewed differentiation of stem and progenitor cells and an enlarged HSC pool. Mechanistically, Atad3a interacted with the mitochondrial channel components Tom40 and Tim23 and served as a bridging factor to facilitate appropriate transportation and processing of the mitophagy protein Pink1. Loss of Atad3a caused accumulation of Pink1 and activated mitophagy. Notably, deletion of Pink1 in Atad3a-deficient mice significantly 'rescued' the mitophagy defect, which resulted in restoration of the progenitor and HSC pools. Our data indicate that Atad3a suppresses Pink1-dependent mitophagy and thereby serves a key role in hematopoietic homeostasis.
[Mh] Termos MeSH primário: ATPases Associadas a Diversas Atividades Celulares/metabolismo
Células-Tronco Hematopoéticas/metabolismo
Homeostase
Degradação Mitocondrial
Proteínas Mitocondriais/metabolismo
Proteínas Quinases/metabolismo
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares/genética
Animais
Apoptose/genética
Diferenciação Celular/genética
Proliferação Celular/genética
Células HEK293
Seres Humanos
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
Camundongos Knockout
Mitocôndrias/genética
Mitocôndrias/metabolismo
Proteínas Mitocondriais/genética
Proteínas Quinases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Atad3a protein, mouse); 0 (Membrane Proteins); 0 (Membrane Transport Proteins); 0 (Mitochondrial Proteins); 0 (Timm23 protein, mouse); 0 (mitochondrial outer membrane protein 35-kDa, mouse); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (PTEN-induced putative kinase); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1038/s41590-017-0002-1


  6 / 1106 MEDLINE  
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[PMID]:29053956
[Au] Autor:Tan P; He L; Cui J; Qian C; Cao X; Lin M; Zhu Q; Li Y; Xing C; Yu X; Wang HY; Wang RF
[Ad] Endereço:Institute of Biosciences and Technology, College of Medicine, Texas A&M University, Houston, TX 77030, USA; Center for Inflammation and Epigenetics, Houston Methodist Research Institute, Houston, TX 77030, USA.
[Ti] Título:Assembly of the WHIP-TRIM14-PPP6C Mitochondrial Complex Promotes RIG-I-Mediated Antiviral Signaling.
[So] Source:Mol Cell;68(2):293-307.e5, 2017 Oct 19.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial antiviral signaling platform protein (MAVS) acts as a central hub for RIG-I receptor proximal signal propagation. However, key components in the assembly of the MAVS mitochondrial platform that promote RIG-I mitochondrial localization and optimal activation are still largely undefined. Employing pooled RNAi and yeast two-hybrid screenings, we report that the mitochondrial adaptor protein tripartite motif (TRIM)14 provides a docking platform for the assembly of the mitochondrial signaling complex required for maximal activation of RIG-I-mediated signaling, consisting of WHIP and protein phosphatase PPP6C. Following viral infection, the ubiquitin-binding domain in WHIP bridges RIG-I with MAVS by binding to polyUb chains of RIG-I at lysine 164. The ATPase domain in WHIP contributes to stabilization of the RIG-I-dsRNA interaction. Moreover, phosphatase PPP6C is responsible for RIG-I dephosphorylation. Together, our findings define the WHIP-TRIM14-PPP6C mitochondrial signalosome required for RIG-I-mediated innate antiviral immunity.
[Mh] Termos MeSH primário: Proteínas de Transporte/imunologia
Proteína DEAD-box 58/imunologia
Proteínas de Ligação a DNA/imunologia
Imunidade Inata
Mitocôndrias/imunologia
Proteínas Mitocondriais/imunologia
Complexos Multiproteicos/imunologia
Fosfoproteínas Fosfatases/imunologia
Transdução de Sinais/imunologia
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares
Animais
Proteínas de Transporte/genética
Linhagem Celular Tumoral
Cercopithecus aethiops
Proteína DEAD-box 58/genética
Proteínas de Ligação a DNA/genética
Seres Humanos
Mitocôndrias/genética
Proteínas Mitocondriais/genética
Complexos Multiproteicos/genética
Fosfoproteínas Fosfatases/genética
Transdução de Sinais/genética
Células Vero
Viroses/genética
Viroses/imunologia
Vírus/genética
Vírus/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (DNA-Binding Proteins); 0 (Mitochondrial Proteins); 0 (Multiprotein Complexes); 0 (TRIM14 protein, human); EC 3.1.3.16 (Phosphoprotein Phosphatases); EC 3.1.3.16 (protein phosphatase 6); EC 3.6.1.- (DDX58 protein, human); EC 3.6.1.3 (WRNIP1 protein, human); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities); EC 3.6.4.13 (DEAD Box Protein 58)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE


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[PMID]:28934429
[Au] Autor:Cabantous S; Doumbo O; Poudiougou B; Louis L; Barry A; Oumar AA; Traore A; Marquet S; Dessein A
[Ad] Endereço:INSERM UMR906, GIMP, Labex ParaFrap.
[Ti] Título:Gene Expression Analysis Reveals Genes Common to Cerebral Malaria and Neurodegenerative Disorders.
[So] Source:J Infect Dis;216(6):771-775, 2017 Sep 15.
[Is] ISSN:1537-6613
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cerebral malaria, a reversible encephalopathy affecting young children, is a medical emergency requiring urgent clinical assessment and treatment. We performed a whole-transcriptomic analysis of blood samples from Malian children with cerebral or uncomplicated malaria. We focused on transcripts from pathways for which dysfunction has been associated with neurodegenerative disorders. We found that SNCA, SIAH2, UBB, HSPA1A, TUBB2A, and PINK1 were upregulated (fold-increases, ≥2.6), whereas UBD and PSMC5 were downregulated (fold-decreases, ≤4.39) in children with cerebral malaria, compared with those with uncomplicated malaria. These findings provide the first evidence for pathogenic mechanisms common to human cerebral malaria and neurodegenerative disorders.
[Mh] Termos MeSH primário: Malária Cerebral/genética
Malária Falciparum/genética
Doenças Neurodegenerativas/genética
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares
Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Criança
Pré-Escolar
Regulação para Baixo
Feminino
Perfilação da Expressão Gênica
Proteínas de Choque Térmico HSP70/genética
Proteínas de Choque Térmico HSP70/metabolismo
Seres Humanos
Proteínas com Domínio LIM/genética
Proteínas com Domínio LIM/metabolismo
Leucócitos Mononucleares/parasitologia
Malária Cerebral/diagnóstico
Malária Falciparum/diagnóstico
Masculino
Doenças Neurodegenerativas/diagnóstico
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Plasmodium falciparum
Estudos Prospectivos
Complexo de Endopeptidases do Proteassoma
Proteínas Quinases/genética
Proteínas Quinases/metabolismo
Reprodutibilidade dos Testes
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Tubulina (Proteína)/genética
Tubulina (Proteína)/metabolismo
Ubiquitina/genética
Ubiquitina/metabolismo
Ubiquitina-Proteína Ligases/genética
Ubiquitina-Proteína Ligases/metabolismo
Ubiquitinas/genética
Ubiquitinas/metabolismo
Regulação para Cima
alfa-Sinucleína/genética
alfa-Sinucleína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (HSP70 Heat-Shock Proteins); 0 (HSPA1A protein, human); 0 (LIM Domain Proteins); 0 (Nuclear Proteins); 0 (PSMC5 protein, human); 0 (SNCA protein, human); 0 (TUBB2B protein, human); 0 (Transcription Factors); 0 (Tubulin); 0 (UBB protein, human); 0 (UBD protein, human); 0 (Ubiquitin); 0 (Ubiquitins); 0 (alpha-Synuclein); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (seven in absentia proteins); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (PTEN-induced putative kinase); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
[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:170922
[St] Status:MEDLINE
[do] DOI:10.1093/infdis/jix359


  8 / 1106 MEDLINE  
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[PMID]:28844861
[Au] Autor:Rinaldi VD; Bolcun-Filas E; Kogo H; Kurahashi H; Schimenti JC
[Ad] Endereço:Cornell University, Departments of Biomedical Sciences and Molecular Biology and Genetics, Ithaca, NY 14850, USA.
[Ti] Título:The DNA Damage Checkpoint Eliminates Mouse Oocytes with Chromosome Synapsis Failure.
[So] Source:Mol Cell;67(6):1026-1036.e2, 2017 Sep 21.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pairing and synapsis of homologous chromosomes during meiosis is crucial for producing genetically normal gametes and is dependent upon repair of SPO11-induced double-strand breaks (DSBs) by homologous recombination. To prevent transmission of genetic defects, diverse organisms have evolved mechanisms to eliminate meiocytes containing unrepaired DSBs or unsynapsed chromosomes. Here we show that the CHK2 (CHEK2)-dependent DNA damage checkpoint culls not only recombination-defective mouse oocytes but also SPO11-deficient oocytes that are severely defective in homolog synapsis. The checkpoint is triggered in oocytes that accumulate a threshold level of spontaneous DSBs (∼10) in late prophase I, the repair of which is inhibited by the presence of HORMAD1/2 on unsynapsed chromosome axes. Furthermore, Hormad2 deletion rescued the fertility of oocytes containing a synapsis-proficient, DSB repair-defective mutation in a gene (Trip13) required for removal of HORMADs from synapsed chromosomes, suggesting that many meiotic DSBs are normally repaired by intersister recombination in mice.
[Mh] Termos MeSH primário: Quinase do Ponto de Checagem 2/metabolismo
Pareamento Cromossômico
Dano ao DNA
Meiose
Oócitos/enzimologia
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares
Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Animais
Proteínas de Ciclo Celular/genética
Proteínas de Ciclo Celular/metabolismo
Morte Celular
Quinase do Ponto de Checagem 2/genética
Endodesoxirribonucleases/deficiência
Endodesoxirribonucleases/genética
Feminino
Fertilidade
Genótipo
Infertilidade Feminina/enzimologia
Infertilidade Feminina/genética
Infertilidade Feminina/patologia
Camundongos Endogâmicos C3H
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Oócitos/patologia
Estágio Paquíteno
Fenótipo
Reparo de DNA por Recombinação
Fatores de Tempo
Técnicas de Cultura de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (HORMAD2 protein, mouse); 0 (Nohma protein, mouse); EC 2.7.1.11 (Checkpoint Kinase 2); EC 2.7.11.1 (Chek2 protein, mouse); EC 3.1.- (Endodeoxyribonucleases); EC 3.1.- (meiotic recombination protein SPO11); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities); EC 3.6.4.- (Trip13 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE


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[PMID]:28833338
[Au] Autor:Raymond AA; Javary J; Breig O; Neaud V; Rosenbaum J
[Ad] Endereço:University of Bordeaux, INSERM, U1053, Bordeaux Research In Translational Oncology, BaRITOn, Bordeaux, France.
[Ti] Título:Reptin regulates insulin-stimulated Akt phosphorylation in hepatocellular carcinoma via the regulation of SHP-1/PTPN6.
[So] Source:Cell Biochem Funct;35(6):289-295, 2017 Aug.
[Is] ISSN:1099-0844
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Hepatocellular carcinoma (HCC) is the main primary cancer of the liver. Many studies have shown that insulin resistance is a risk factor for HCC. We previously discovered the overexpression and oncogenic role of the Reptin/RUVBL2 ATPase in HCC. Here, we found that Reptin silencing enhanced insulin sensitivity in 2 HCC cell lines, as shown by a large potentiation of insulin-induced AKT phosphorylation on Ser473 and Thr308, and of downstream signalling. Reptin silencing did not affect the tyrosine phosphorylation of the insulin receptor nor of IRS1, but it enhanced the tyrosine phosphorylation of the p85 subunit of PI3K. The expression of the SHP-1/PTPN6 phosphatase, which dephosphorylates p85, was reduced after Reptin depletion. Forced expression of SHP-1 restored a normal AKT phosphorylation after insulin treatment in cells where Reptin was silenced, demonstrating that the downregulation of SHP1 is mechanistically linked to increased Akt phosphorylation. In conclusion, we have uncovered a new function for Reptin in regulating insulin signalling in HCC cells via the regulation of SHP-1 expression. We suggest that the regulation of insulin sensitivity by Reptin contributes to its oncogenic action in the liver.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
DNA Helicases/metabolismo
Proteína Tirosina Fosfatase não Receptora Tipo 6/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares
Carcinoma Hepatocelular/metabolismo
Carcinoma Hepatocelular/patologia
Proteínas de Transporte/antagonistas & inibidores
Proteínas de Transporte/genética
Linhagem Celular Tumoral
DNA Helicases/antagonistas & inibidores
DNA Helicases/genética
Doxiciclina/farmacologia
Seres Humanos
Insulina/farmacologia
Neoplasias Hepáticas/metabolismo
Neoplasias Hepáticas/patologia
Fosforilação/efeitos dos fármacos
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Insulin); 0 (RNA, Small Interfering); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.1.3.48 (PTPN6 protein, human); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 6); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (RUVBL2 protein, human); N12000U13O (Doxycycline)
[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:170824
[St] Status:MEDLINE
[do] DOI:10.1002/cbf.3274


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[PMID]:28821611
[Au] Autor:Wang X; Chemmama IE; Yu C; Huszagh A; Xu Y; Viner R; Block SA; Cimermancic P; Rychnovsky SD; Ye Y; Sali A; Huang L
[Ad] Endereço:From the Department of Physiology and Biophysics, University of California, Irvine, California 92697.
[Ti] Título:The proteasome-interacting Ecm29 protein disassembles the 26S proteasome in response to oxidative stress.
[So] Source:J Biol Chem;292(39):16310-16320, 2017 Sep 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oxidative stress has been implicated in multiple human neurological and other disorders. Proteasomes are multi-subunit proteases critical for the removal of oxidatively damaged proteins. To understand stress-associated human pathologies, it is important to uncover the molecular events underlying the regulation of proteasomes upon oxidative stress. To this end, we investigated H O stress-induced molecular changes of the human 26S proteasome and determined that stress-induced 26S proteasome disassembly is conserved from yeast to human. Moreover, we developed and employed a new proteomic approach, XAP ( cross-linking-assisted affinity purification), coupled with stable isotope labeling with amino acids in cell culture (SILAC)-based quantitative MS, to capture and quantify several weakly bound proteasome-interacting proteins and examine their roles in stress-mediated proteasomal remodeling. Our results indicate that the adapter protein Ecm29 is the main proteasome-interacting protein responsible for stress-triggered remodeling of the 26S proteasome in human cells. Importantly, using a disuccinimidyl sulfoxide-based cross-linking MS platform, we mapped the interactions of Ecm29 within itself and with proteasome subunits and determined the architecture of the Ecm29-proteasome complex with integrative structure modeling. These results enabled us to propose a structural model in which Ecm29 intrudes on the interaction between the 20S core particle and the 19S regulatory particle in the 26S proteasome, disrupting the proteasome structure in response to oxidative stress.
[Mh] Termos MeSH primário: Modelos Moleculares
Estresse Oxidativo
Complexo de Endopeptidases do Proteassoma/metabolismo
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares
Proteínas Adaptadoras de Transdução de Sinal/química
Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Marcadores de Afinidade
Reagentes para Ligações Cruzadas/farmacologia
Células HEK293
Seres Humanos
Marcação por Isótopo
Proteínas com Domínio LIM/química
Proteínas com Domínio LIM/genética
Proteínas com Domínio LIM/metabolismo
Complexo de Endopeptidases do Proteassoma/química
Complexo de Endopeptidases do Proteassoma/genética
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Mapeamento de Interação de Proteínas
Multimerização Proteica
Proteólise
Interferência de RNA
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Espectrometria de Massas em Tandem
Fatores de Transcrição/química
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Ubiquitinas/química
Ubiquitinas/genética
Ubiquitinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Affinity Labels); 0 (Cross-Linking Reagents); 0 (KIAA0368 protein, human); 0 (LIM Domain Proteins); 0 (PSMC5 protein, human); 0 (Recombinant Fusion Proteins); 0 (Transcription Factors); 0 (Ubiquitins); 0 (Ubl4A protein, human); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.4.99.- (ATP dependent 26S protease); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.803619



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