Base de dados : MEDLINE
Pesquisa : D12.644.360.024.314 [Categoria DeCS]
Referências encontradas : 378 [refinar]
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[PMID]:28666867
[Au] Autor:Kuki K; Yamaguchi N; Iwasawa S; Takakura Y; Aoyama K; Yuki R; Nakayama Y; Kuga T; Hashimoto Y; Tomonaga T; Yamaguchi N
[Ad] Endereço:Laboratory of Molecular Cell Biology, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba 260-8675, Japan.
[Ti] Título:Enhancement of TGF-ß-induced Smad3 activity by c-Abl-mediated tyrosine phosphorylation of its coactivator SKI-interacting protein (SKIP).
[So] Source:Biochem Biophys Res Commun;490(3):1045-1051, 2017 Aug 26.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:c-Abl is a non-receptor-type tyrosine kinase that plays an important role in cell proliferation, migration, apoptosis, and fibrosis. Furthermore, although c-Abl is involved in transforming growth factor-ß (TGF-ß) signaling, its molecular functions in TGF-ß signaling are not fully understood. Here, we found that c-Abl phosphorylates SKI-interacting protein (SKIP), a nuclear cofactor of the transcription factor Smad3. The c-Abl inhibitor imatinib suppressed TGF-ß-induced expression of Smad3 targets as well as SKIP/Smad3 interaction. TGF-ß-stimulation induced tyrosine phosphorylation of SKIP, and this phosphorylation was suppressed by imatinib. Tyr , Tyr , and Tyr residues in SKIP were shown to be involved in c-Abl-mediated phosphorylation. Phosphomimetic glutamic acid substitution at Tyr in SKIP enhanced, whereas its phospho-dead phenylalanine substitution attenuated TGF-ß-induced SKIP/Smad3 interaction. Moreover, the phosphomimetic mutant of SKIP augmented transcriptional activity of Smad3. Taken together, these results suggest that c-Abl phosphorylates SKIP mainly at Tyr and promotes SKIP/Smad3 interaction for the full activation of TGF-ß/Smad3 signaling.
[Mh] Termos MeSH primário: Coativadores de Receptor Nuclear/metabolismo
Proteínas Proto-Oncogênicas c-abl/metabolismo
Proteína Smad3/metabolismo
Fator de Crescimento Transformador beta/metabolismo
Tirosina/metabolismo
[Mh] Termos MeSH secundário: Células A549
Animais
Células COS
Cercopithecus aethiops
Células HeLa
Seres Humanos
Fosforilação
Mapas de Interação de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Receptor Coactivators); 0 (SNW1 protein, human); 0 (Smad3 Protein); 0 (Transforming Growth Factor beta); 42HK56048U (Tyrosine); EC 2.7.10.2 (Proto-Oncogene Proteins c-abl)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170702
[St] Status:MEDLINE


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[PMID]:28615454
[Au] Autor:Philpott CC; Ryu MS; Frey A; Patel S
[Ad] Endereço:From the Genetics and Metabolism Section, Liver Diseases Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, Carolinep@mail.nih.gov.
[Ti] Título:Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells.
[So] Source:J Biol Chem;292(31):12764-12771, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular systems coordinating the uptake and distribution of metal cofactors. Iron cofactors include heme, iron-sulfur clusters, and simple iron ions. Poly(rC)-binding proteins are multifunctional adaptors that serve as iron ion chaperones in the cytosolic/nuclear compartment, binding iron at import and delivering it to enzymes, for storage (ferritin) and export (ferroportin). Ferritin iron is mobilized by autophagy through the cargo receptor, nuclear co-activator 4. The monothiol glutaredoxin Glrx3 and BolA2 function as a [2Fe-2S] chaperone complex. These proteins form a core system of cytosolic iron cofactor chaperones in mammalian cells.
[Mh] Termos MeSH primário: Citosol/metabolismo
Ferritinas/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Ferro/metabolismo
Modelos Biológicos
Modelos Moleculares
Chaperonas Moleculares/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoenzimas/química
Apoenzimas/metabolismo
Apoferritinas/química
Apoferritinas/metabolismo
Autofagia
Proteínas de Transporte/química
Proteínas de Transporte/metabolismo
Proteínas de Transporte de Cátions/química
Proteínas de Transporte de Cátions/metabolismo
Dimerização
Células Precursoras Eritroides/citologia
Células Precursoras Eritroides/metabolismo
Ferritinas/química
Ribonucleoproteínas Nucleares Heterogêneas/química
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
Seres Humanos
Proteínas com Ferro-Enxofre/química
Chaperonas Moleculares/química
Coativadores de Receptor Nuclear/química
Coativadores de Receptor Nuclear/metabolismo
Multimerização Proteica
Transporte Proteico
Proteínas/química
Proteínas/metabolismo
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Apoenzymes); 0 (BOLA2 protein, human); 0 (Carrier Proteins); 0 (Cation Transport Proteins); 0 (GLRX3 protein, human); 0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Iron-Sulfur Proteins); 0 (Molecular Chaperones); 0 (NCOA4 protein, human); 0 (Nuclear Receptor Coactivators); 0 (PCBP1 protein, human); 0 (PCBP2 protein, human); 0 (Proteins); 0 (RNA-Binding Proteins); 0 (metal transporting protein 1); 9007-73-2 (Ferritins); 9013-31-4 (Apoferritins); E1UOL152H7 (Iron)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.791962


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[PMID]:28435063
[Au] Autor:Yoon J; Lee KJ; Oh GS; Kim GH; Kim SW
[Ad] Endereço:Department of Pharmacology, Asan Medical Center, University of Ulsan College of Medicine, Seoul 05505, Republic of Korea; Bio-medical Institute of Technology, University of Ulsan College of Medicine, Seoul 05505, Republic of Korea.
[Ti] Título:Regulation of Nampt expression by transcriptional coactivator NCOA6 in pancreatic ß-cells.
[So] Source:Biochem Biophys Res Commun;487(3):600-606, 2017 Jun 03.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nuclear receptor coactivator 6 (NCOA6) is a transcriptional coactivator and crucial for insulin secretion and glucose metabolism in pancreatic ß-cells. However, the regulatory mechanism of ß-cell function by NCOA6 is largely unknown. In this study, we found that the transcript levels of nicotinamide phosphoribosyltransferase (Nampt) were decreased in islets of NCOA6 mice compared with NCOA6 mice. Moreover, NCOA6 overexpression increased the levels of Nampt transcripts in the mouse pancreatic ß-cell line NIT-1. Promoter analyses showed that transcriptional activity of the Nampt promoter was stimulated by cooperation of sterol regulatory element binding protein-1c (SREBP-1c) and NCOA6. Additional studies using mutant promoters demonstrated that SREBP-1c activates Nampt promoter through the sterol regulatory element (SRE), but not through the E-box. Using chromatin immunoprecipitation assay, NCOA6 was also shown to be directly recruited to the SRE region of the Nampt promoter. Furthermore, treatment with nicotinamide mononucleotide (NMN), a product of the Nampt reaction and a key NAD intermediate, ameliorates glucose-stimulated insulin secretion from NCOA6 islets. These results suggest that NCOA6 stimulates insulin secretion, at least partially, by modulating Nampt expression in pancreatic ß-cells.
[Mh] Termos MeSH primário: Citocinas/metabolismo
Células Secretoras de Insulina/metabolismo
Nicotinamida Fosforribosiltransferase/metabolismo
Coativadores de Receptor Nuclear/metabolismo
Ativação Transcricional/genética
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Citocinas/genética
Células Secretoras de Insulina/efeitos dos fármacos
Camundongos
Mononucleotídeo de Nicotinamida/farmacologia
Nicotinamida Fosforribosiltransferase/genética
Coativadores de Receptor Nuclear/genética
Regiões Promotoras Genéticas/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Ncoa6 protein, mouse); 0 (Nuclear Receptor Coactivators); 1094-61-7 (Nicotinamide Mononucleotide); EC 2.4.2.12 (Nicotinamide Phosphoribosyltransferase); EC 2.4.2.12 (nicotinamide phosphoribosyltransferase, mouse)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170704
[Lr] Data última revisão:
170704
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170425
[St] Status:MEDLINE


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[PMID]:28375153
[Au] Autor:Ryu MS; Zhang D; Protchenko O; Shakoury-Elizeh M; Philpott CC
[Ti] Título:PCBP1 and NCOA4 regulate erythroid iron storage and heme biosynthesis.
[So] Source:J Clin Invest;127(5):1786-1797, 2017 May 01.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Developing erythrocytes take up exceptionally large amounts of iron, which must be transferred to mitochondria for incorporation into heme. This massive iron flux must be precisely controlled to permit the coordinated synthesis of heme and hemoglobin while avoiding the toxic effects of chemically reactive iron. In cultured animal cells, iron chaperones poly rC-binding protein 1 (PCBP1) and PCBP2 deliver iron to ferritin, the sole cytosolic iron storage protein, and nuclear receptor coactivator 4 (NCOA4) mediates the autophagic turnover of ferritin. The roles of PCBP, ferritin, and NCOA4 in erythroid development remain unclear. Here, we show that PCBP1, NCOA4, and ferritin are critical for murine red cell development. Using a cultured cell model of erythroid differentiation, depletion of PCBP1 or NCOA4 impaired iron trafficking through ferritin, which resulted in reduced heme synthesis, reduced hemoglobin formation, and perturbation of erythroid regulatory systems. Mice lacking Pcbp1 exhibited microcytic anemia and activation of compensatory erythropoiesis via the regulators erythropoietin and erythroferrone. Ex vivo differentiation of erythroid precursors from Pcbp1-deficient mice confirmed defects in ferritin iron flux and heme synthesis. These studies demonstrate the importance of ferritin for the vectorial transfer of imported iron to mitochondria in developing red cells and of PCBP1 and NCOA4 in mediating iron flux through ferritin.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Eritrócitos/metabolismo
Heme/biossíntese
Ferro/metabolismo
Coativadores de Receptor Nuclear/metabolismo
[Mh] Termos MeSH secundário: Anemia/genética
Anemia/metabolismo
Animais
Transporte Biológico Ativo/genética
Células CHO
Proteínas de Transporte/genética
Cricetinae
Cricetulus
Citocinas/genética
Citocinas/metabolismo
Eritropoetina/genética
Eritropoetina/metabolismo
Ferritinas/genética
Ferritinas/metabolismo
Heme/genética
Seres Humanos
Camundongos
Camundongos Transgênicos
Mitocôndrias/genética
Mitocôndrias/metabolismo
Proteínas Musculares/genética
Proteínas Musculares/metabolismo
Coativadores de Receptor Nuclear/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CTRP15 protein, mouse); 0 (Carrier Proteins); 0 (Cytokines); 0 (Muscle Proteins); 0 (NcoA4 protein, mouse); 0 (Nuclear Receptor Coactivators); 0 (Pcbp1 protein, mouse); 11096-26-7 (Erythropoietin); 42VZT0U6YR (Heme); 9007-73-2 (Ferritins); E1UOL152H7 (Iron)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE


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[PMID]:28341745
[Au] Autor:Murakami A; Matsuda M; Harada Y; Hirata M
[Ad] Endereço:From the Laboratory of Molecular and Cellular Biochemistry, Faculty of Dental Science, and.
[Ti] Título:Phospholipase C-related, but catalytically inactive protein (PRIP) up-regulates osteoclast differentiation via calcium-calcineurin-NFATc1 signaling.
[So] Source:J Biol Chem;292(19):7994-8006, 2017 May 12.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phospholipase C-related, but catalytically inactive protein (PRIP) was previously identified as a novel inositol 1,4,5-trisphosphate-binding protein with a domain organization similar to that of phospholipase C-δ but lacking phospholipase activity. We recently showed that PRIP gene knock-out (KO) in mice increases bone formation and concomitantly decreases bone resorption, resulting in increased bone mineral density and trabecular bone volume. However, the role of PRIP in osteoclastogenesis has not yet been fully elucidated. Here, we investigated the effects of PRIP on bone remodeling by investigating dynamic tooth movement in mice fitted with orthodontic devices. Morphological analysis indicated that the extent of tooth movement was smaller in the PRIP-KO mice than in wild-type mice. Histological analysis revealed fewer osteoclasts on the bone-resorption side in maxillary bones of PRIP-KO mice, and osteoclast formation assays and flow cytometry indicated lower osteoclast differentiation in bone marrow cells isolated from these mice. The expression of genes implicated in bone resorption was lower in differentiated PRIP-KO cells, and genes involved in osteoclast differentiation, such as the transcription factor NFATc1, exhibited lower expression in immature PRIP-KO cells initiated by M-CSF. Moreover, calcineurin expression and activity were also lower in the PRIP-KO cells. The PRIP-KO cells also displayed fewer M-CSF-induced changes in intracellular Ca and exhibited reduced nuclear localization of NFATc1. Up-regulation of intracellular Ca restored osteoclastogenesis of the PRIP-KO cells. These results indicate that PRIP deficiency impairs osteoclast differentiation, particularly at the early stages, and that PRIP stimulates osteoclast differentiation through calcium-calcineurin-NFATc1 signaling via regulating intracellular Ca .
[Mh] Termos MeSH primário: Calcineurina/metabolismo
Cálcio/metabolismo
Fatores de Transcrição NFATC/metabolismo
Coativadores de Receptor Nuclear/metabolismo
Osteoclastos/citologia
Fosfolipases Tipo C/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Animais
Reabsorção Óssea
Catálise
Diferenciação Celular
Técnicas de Cocultura
Feminino
Citometria de Fluxo
Peptídeos e Proteínas de Sinalização Intracelular/genética
Masculino
Maxila/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Ortodontia
Osteoclastos/metabolismo
Transdução de Sinais
Microtomografia por Raio-X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Intracellular Signaling Peptides and Proteins); 0 (NFATC Transcription Factors); 0 (Ncoa6 protein, mouse); 0 (Nfatc1 protein, mouse); 0 (Nuclear Receptor Coactivators); 0 (PRIP-1 protein, mouse); 0 (Plcl2 protein, mouse); EC 3.1.3.16 (Calcineurin); EC 3.1.4.- (Type C Phospholipases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170326
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.784777


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[PMID]:28231739
[Au] Autor:Kim MH; Kim EJ; Choi YY; Hong J; Yang WM
[Ad] Endereço:* Department of Convergence Korean Medical Science, College of Korean Medicine, Republic of Korea.
[Ti] Título:Lycium chinense Improves Post-Menopausal Obesity via Regulation of PPAR-γ and Estrogen Receptor-α/ß Expressions.
[So] Source:Am J Chin Med;45(2):269-282, 2017.
[Is] ISSN:0192-415X
[Cp] País de publicação:Singapore
[La] Idioma:eng
[Ab] Resumo:The fruit of Lycium chinense Miller (Solanaceae) is used as a functional food and a medicinal herb for treating many specific health concerns. Weight gain induced by estrogen deficiency is a problem for post-menopausal women around the globe. The present study investigates the effects of aqueous extract of L. chinense (LC) on post-menopausal obesity. Female C57BL/6 mice were ovariectomized and fed on high-fat diet (HFD) for 12 weeks to induce post-menopausal obesity. LC extract (1[Formula: see text]mg/kg and 10[Formula: see text]mg/kg) was orally administrated for 6 weeks with continuous HFD feeding. Ovarian adipose tissues and uterus were weighed. Serum triglyceride, cholesterol, LDL-cholesterol and fasting glucose levels were analyzed. The expressions of adipocyte-specific factors and estrogen receptors (ERs) were investigated. Additionally, lipid accumulation was confirmed in differentiated 3T3-L1 adipocytes. Increased body weight due to post-menopausal obesity was ameliorated about 14.7% and 17.76% by treatment of 1[Formula: see text]mg/kg and 10[Formula: see text]mg/kg LC, respectively. LC treatment reduced both of serum lipid and fasting blood glucose levels. Adipocyte hypertrophy and fatty liver were ameliorated in LC-treated groups. In LC-treated adipocyte cells, lipid accumulation was significantly inhibited. The expression of perilipin in adipose tissues was decreased by LC. In addition, expression of PPAR-[Formula: see text] protein was down-regulated in adipose tissues and differentiated adipocytes, while GLUT4 expression was increased in adipose tissues by LC treatment. Moreover, LC treatment up-regulated the expressions of ER-[Formula: see text]/[Formula: see text] accompanied with increased uterine weight. These results showed the ameliorative effects of LC on overweight after menopause. Post-menopausal obesity may be improved by LC treatment.
[Mh] Termos MeSH primário: Receptor alfa de Estrogênio/metabolismo
Receptor beta de Estrogênio/metabolismo
Regulação da Expressão Gênica/efeitos dos fármacos
Lycium
Obesidade/tratamento farmacológico
Obesidade/genética
Extratos Vegetais/farmacologia
Pós-Menopausa
[Mh] Termos MeSH secundário: Células 3T3-L1
Administração Oral
Animais
Receptor alfa de Estrogênio/genética
Receptor beta de Estrogênio/genética
Feminino
Expressão Gênica/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Coativadores de Receptor Nuclear
Extratos Vegetais/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Estrogen Receptor alpha); 0 (Estrogen Receptor beta); 0 (Ncoa6 protein, mouse); 0 (Nuclear Receptor Coactivators); 0 (Plant Extracts)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE
[do] DOI:10.1142/S0192415X17500173


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[PMID]:28137631
[Au] Autor:Liu X; Liu F; Gao S; Reske J; Li A; Wu CL; Yang C; Chen F; Luo R; Xiao H
[Ad] Endereço:Department of Physiology, Michigan State University, East Lansing, MI, 48824, USA; Cancer Center, Southern Medical University, Guangzhou, Guangdong, 510315, China; Traditional Chinese Medicine-Integrated Hospital, Southern Medical University, Guangzhou, Guangdong, 510315, China.
[Ti] Título:A single non-synonymous NCOA5 variation in type 2 diabetic patients with hepatocellular carcinoma impairs the function of NCOA5 in cell cycle regulation.
[So] Source:Cancer Lett;391:152-161, 2017 04 10.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Type 2 Diabetes (T2D) is a risk factor for hepatocellular carcinoma (HCC). We have previously described that haploinsufficiency of nuclear receptor coactivator 5 (NCOA5) is a genetic defect linking glucose intolerance to HCC. Here we report identification and characterization of a single nucleotide variation (T445A) in NCOA5, causing an amino acid Thr to Ala substitution, in adjacent non-tumorous liver tissues derived from patients with concurrent HCC and T2D. By using Tet-On inducible expression cells, we show that ectopic expression of NCOA5wt suppressed proliferation of HCC cells via induction of G2/M arrest, while ectopic expression of NCOA5T445A had a significantly lesser effect compared to ectopic expression of NCOA5wt. Furthermore, ectopic expression of NCOA5wt increased the occurrence of DNA damage and cell senescence, whereas expression of NCOA5T445A partly lost this activity. Xenograft tumor model analysis demonstrated that ectopic NCOA5wt expression reduced HCC tumor growth and the T445A variation impairs its tumor growth inhibitory function. Collectively, our data show that the T445A variation impairs the ability of NCOA5 to inhibit growth of HCC, suggesting that this variation may have potential to increase susceptibility to HCC comorbid with T2D.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/genética
Diabetes Mellitus Tipo 2/complicações
Neoplasias Hepáticas/genética
Coativadores de Receptor Nuclear/genética
[Mh] Termos MeSH secundário: Animais
Carcinoma Hepatocelular/patologia
Pontos de Checagem do Ciclo Celular
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Neoplasias Hepáticas/patologia
Camundongos
Camundongos Nus
Coativadores de Receptor Nuclear/metabolismo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NCOA5 protein, human); 0 (Nuclear Receptor Coactivators)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171029
[Lr] Data última revisão:
171029
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE


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[PMID]:28122051
[Au] Autor:Holvoet P; Vanhaverbeke M; Geeraert B; De Keyzer D; Hulsmans M; Janssens S
[Ad] Endereço:Department of Cardiovascular Sciences, Atherosclerosis and Metabolism Unit, KU Leuven, Belgium.
[Ti] Título:Low Cytochrome Oxidase 1 Links Mitochondrial Dysfunction to Atherosclerosis in Mice and Pigs.
[So] Source:PLoS One;12(1):e0170307, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Cytochrome oxidase IV complex regulates energy production in mitochondria. Therefore, we determined the relation of COX genes with atherosclerosis in mice and pigs. METHODS AND RESULTS: First, we compared atherosclerosis in the aortic arch of age-matched (24 weeks) C57BL/6J control (n = 10), LDL-receptor deficient (n = 8), leptin-deficient ob/ob (n = 10), and double knock-out (lacking LDL-receptor and leptin) mice (n = 12). Low aortic mitochondria-encoded cytochrome oxidase 1 in obese diabetic double knock-out mice was associated with a larger plaque area and higher propensity of M1 macrophages and oxidized LDL. Caloric restriction increased mitochondria-encoded cytochrome oxidase 1 and reduced plaque area and oxidized LDL. This was associated with a reduction of titer of anti-oxidized LDL antibodies, a proxy of systemic oxidative stress. Low of mitochondria-encoded cytochrome oxidase 1 was related to low expression of peroxisome proliferative activated receptors α, δ, and γ and of peroxisome proliferative activated receptor, gamma, co-activator 1 alpha reflecting mitochondrial dysfunction. Caloric restriction increased them. To investigate if there was a diabetic/obesity requirement for mitochondria-encoded cytochrome oxidase 1 to be down-regulated, we then studied atherosclerosis in LAD of hypercholesterolemic pigs (n = 37). Pigs at the end of the study were divided in three groups based on increasing LAD plaque complexity according to Stary (Stary I: n = 12; Stary II: n = 13; Stary III: n = 12). Low mitochondria-encoded cytochrome oxidase 1 in isolated plaque macrophages was associated with more complex coronary plaques and oxidized LDL. Nucleus-encoded cytochrome oxidase 4I1 and cytochrome oxidase 10 did not correlate with plaque complexity and oxidative stress. In mice and pigs, MT-COI was inversely related to insulin resistance. CONCLUSIONS: Low MT-COI is related to mitochondrial dysfunction, oxidative stress and atherosclerosis and plaque complexity.
[Mh] Termos MeSH primário: Aterosclerose/etiologia
Deficiência de Citocromo-c Oxidase/complicações
Deficiência de Citocromo-c Oxidase/fisiopatologia
Complexo IV da Cadeia de Transporte de Elétrons/fisiologia
Mitocôndrias/metabolismo
Porco Miniatura/metabolismo
[Mh] Termos MeSH secundário: Animais
Aorta Torácica/metabolismo
Aorta Torácica/patologia
Aterosclerose/enzimologia
Aterosclerose/genética
Restrição Calórica
Vasos Coronários/metabolismo
Vasos Coronários/patologia
Deficiência de Citocromo-c Oxidase/patologia
Diabetes Mellitus Experimental/genética
Diabetes Mellitus Experimental/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/genética
Metabolismo Energético
Hipercolesterolemia/enzimologia
Hipercolesterolemia/patologia
Resistência à Insulina
Leptina/deficiência
Leptina/genética
Lipoproteínas LDL/metabolismo
Macrófagos/patologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Camundongos Obesos
Coativadores de Receptor Nuclear/biossíntese
Coativadores de Receptor Nuclear/genética
Estresse Oxidativo
Receptores Ativados por Proliferador de Peroxissomo/biossíntese
Receptores Ativados por Proliferador de Peroxissomo/genética
Placa Aterosclerótica/patologia
Receptores de LDL/deficiência
Receptores de LDL/genética
Receptores para Leptina/deficiência
Receptores para Leptina/genética
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Leptin); 0 (Lipoproteins, LDL); 0 (Ncoa6 protein, mouse); 0 (Nuclear Receptor Coactivators); 0 (Peroxisome Proliferator-Activated Receptors); 0 (Receptors, LDL); 0 (Receptors, Leptin); 0 (leptin receptor, mouse); 0 (oxidized low density lipoprotein); EC 1.9.3.1 (Cox4i1 protein, mouse); EC 1.9.3.1 (Electron Transport Complex IV)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170126
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0170307


  9 / 378 MEDLINE  
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Texto completo
[PMID]:28057584
[Au] Autor:Schnyder S; Kupr B; Handschin C
[Ad] Endereço:Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland.
[Ti] Título:Coregulator-mediated control of skeletal muscle plasticity - A mini-review.
[So] Source:Biochimie;136:49-54, 2017 May.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Skeletal muscle plasticity is a complex process entailing massive transcriptional programs. These changes are mediated by the action of nuclear receptors and other transcription factors. In addition, coregulator proteins have emerged as important players in this process by linking transcription factors to the RNA polymerase II complex and inducing changes in the chromatic structure. An accumulating body of work highlights the pleiotropic functions of coregulator proteins in the control of tissue-specific and whole body metabolism. In skeletal muscle, several coregulators have been identified as potent modulators of metabolic and myofibrillar plasticity. In this mini-review, we will discuss the control, function and physiological significance of these coregulators in skeletal muscle biology.
[Mh] Termos MeSH primário: Músculo Esquelético/fisiologia
Coativadores de Receptor Nuclear/fisiologia
[Mh] Termos MeSH secundário: Animais
Histona Acetiltransferases/metabolismo
Histona Desacetilases/metabolismo
Seres Humanos
Correpressor 1 de Receptor Nuclear/fisiologia
Proteína-Arginina N-Metiltransferases/metabolismo
Proteína do Retinoblastoma/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Nuclear Receptor Co-Repressor 1); 0 (Nuclear Receptor Coactivators); 0 (Retinoblastoma Protein); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases); EC 2.3.1.48 (Histone Acetyltransferases); EC 3.5.1.98 (Histone Deacetylases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170107
[St] Status:MEDLINE


  10 / 378 MEDLINE  
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Fotocópia
[PMID]:27885055
[Au] Autor:Galmés-Pascual BM; Nadal-Casellas A; Bauza-Thorbrügge M; Sbert-Roig M; García-Palmer FJ; Proenza AM; Gianotti M; Lladó I
[Ad] Endereço:Departament de Biologia Fonamental i Ciències de la SalutGrup Metabolisme Energètic i Nutrició, Institut Universitari d'Investigació en Ciències de la Salut (IUNICS), Universitat de les Illes Balears, Palma de Mallorca, Illes Balears, Spain.
[Ti] Título:17ß-estradiol improves hepatic mitochondrial biogenesis and function through PGC1B.
[So] Source:J Endocrinol;232(2):297-308, 2017 Feb.
[Is] ISSN:1479-6805
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sexual dimorphism in mitochondrial biogenesis and function has been described in many rat tissues, with females showing larger and more functional mitochondria. The family of the peroxisome proliferator-activated receptor gamma coactivator 1 (PGC1) plays a central role in the regulatory network governing mitochondrial biogenesis and function, but little is known about the different contribution of hepatic PGC1A and PGC1B in these processes. The aim of this study was to elucidate the role of 17ß-estradiol (E2) in mitochondrial biogenesis and function in liver and assess the contribution of both hepatic PGC1A and PGC1B as mediators of these effects. In ovariectomized (OVX) rats (half of which were treated with E2) estrogen deficiency led to impaired mitochondrial biogenesis and function, increased oxidative stress, and defective lipid metabolism, but was counteracted by E2 treatment. In HepG2 hepatocytes, the role of E2 in enhancing mitochondrial biogenesis and function was confirmed. These effects were unaffected by the knockdown of PGC1A, but were impaired when PGC1B expression was knocked down by specific siRNA. Our results reveal a widespread protective role of E2 in hepatocytes, which is explained by enhanced mitochondrial content and oxidative capacity, lower hepatic lipid accumulation, and a reduction of oxidative stress. We also suggest a novel hepatic protective role of PGC1B as a modulator of E2 effects on mitochondrial biogenesis and function supporting activation of PGC1B as a therapeutic target for hepatic mitochondrial disorders.
[Mh] Termos MeSH primário: Estradiol/farmacologia
Metabolismo dos Lipídeos/efeitos dos fármacos
Fígado/efeitos dos fármacos
Mitocôndrias/metabolismo
Coativadores de Receptor Nuclear/metabolismo
Estresse Oxidativo/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Feminino
Metabolismo dos Lipídeos/fisiologia
Fígado/metabolismo
Camundongos Transgênicos
Coativadores de Receptor Nuclear/genética
Biogênese de Organelas
Ovariectomia
Oxirredução
Estresse Oxidativo/fisiologia
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/genética
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/metabolismo
RNA Interferente Pequeno
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Receptor Coactivators); 0 (Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha); 0 (Ppargc1a protein, rat); 0 (Ppargc1b protein, rat); 0 (RNA, Small Interfering); 4TI98Z838E (Estradiol)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170614
[Lr] Data última revisão:
170614
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161126
[St] Status:MEDLINE



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