Base de dados : MEDLINE
Pesquisa : D08.811.277.656.262.500.126.550.920 [Categoria DeCS]
Referências encontradas : 544 [refinar]
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[PMID]:29317203
[Au] Autor:Liu T; Duan W; Nizigiyimana P; Gao L; Liao Z; Xu B; Liu L; Lei M
[Ad] Endereço:Department of Endocrinology, Xiangya Hospital, Central South University, Changsha, Hunan, 410008, China; Department of Endocrinology, Haikou People's Hospital, Haikou, Hainan, 570208, China.
[Ti] Título:Alpha-mangostin attenuates diabetic nephropathy in association with suppression of acid sphingomyelianse and endoplasmic reticulum stress.
[So] Source:Biochem Biophys Res Commun;496(2):394-400, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIMS: Diabetic nephropathy is a common complication of diabetes, but there are currently few treatment options. The aim of this study was to gain insight into the effect of alpha-mangostin on diabetic nephropathy and possible related mechanisms. METHODS: Goto-Kakizaki rats were used as a diabetic model and received alpha-mangostin or desipramine treatment with normal saline as a control. Ten age-matched Sprague Dawley rats were used as normal controls and treated with normal saline. At week 12, blood glucose, albuminuria, apoptosis and renal pathologic changes were assessed. Protein levels for acid sphingomyelinase, glucose-regulated protein 78, phosphorylated PKR-like ER-resident kinase, activated transcription factor 4, CCAAT/enhancer-binding protein, homologous protein), and cleaved-caspase12 were measured. RESULTS: The level of acid sphingomyelinase was significantly increased, and ER stress was activated in diabetic rat kidneys when compared to the control animals. When acid sphingomyelinase was inhibited by alpha-mangostin, the expression of ER stress-related proteins was down-regulated in association with decreased levels of diabetic kidney injury. CONCLUSIONS: Alpha-mangostin, an acid sphingomyelinase inhibitor plays a protective role in diabetic neuropathy by relieving ER stress induced-renal cell apoptosis.
[Mh] Termos MeSH primário: Diabetes Mellitus Experimental/tratamento farmacológico
Nefropatias Diabéticas/tratamento farmacológico
Inibidores Enzimáticos/farmacologia
Substâncias Protetoras/farmacologia
Esfingomielina Fosfodiesterase/antagonistas & inibidores
Xantonas/farmacologia
[Mh] Termos MeSH secundário: Fator 4 Ativador da Transcrição/genética
Fator 4 Ativador da Transcrição/metabolismo
Albuminúria/genética
Albuminúria/metabolismo
Albuminúria/patologia
Albuminúria/prevenção & controle
Animais
Apoptose/efeitos dos fármacos
Glicemia/metabolismo
Caspase 12/genética
Caspase 12/metabolismo
Desipramina/farmacologia
Diabetes Mellitus Experimental/induzido quimicamente
Diabetes Mellitus Experimental/genética
Diabetes Mellitus Experimental/patologia
Nefropatias Diabéticas/induzido quimicamente
Nefropatias Diabéticas/genética
Nefropatias Diabéticas/patologia
Estresse do Retículo Endoplasmático/efeitos dos fármacos
Regulação da Expressão Gênica
Proteínas de Choque Térmico/genética
Proteínas de Choque Térmico/metabolismo
Rim/efeitos dos fármacos
Rim/metabolismo
Rim/patologia
Masculino
Ratos
Ratos Sprague-Dawley
Esfingomielina Fosfodiesterase/genética
Esfingomielina Fosfodiesterase/metabolismo
Estreptozocina
eIF-2 Quinase/genética
eIF-2 Quinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Atf4 protein, rat); 0 (Blood Glucose); 0 (Enzyme Inhibitors); 0 (Heat-Shock Proteins); 0 (Hspa5 protein, rat); 0 (Protective Agents); 0 (Xanthones); 145891-90-3 (Activating Transcription Factor 4); 5W494URQ81 (Streptozocin); EC 2.7.11.1 (PERK kinase); EC 2.7.11.1 (eIF-2 Kinase); EC 3.1.4.- (acid sphingomyelinase-1); EC 3.1.4.12 (Sphingomyelin Phosphodiesterase); EC 3.4.22.- (Casp12 protein, rat); EC 3.4.22.- (Caspase 12); TG537D343B (Desipramine); U6RIV93RU1 (mangostin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE


  2 / 544 MEDLINE  
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[PMID]:28873095
[Au] Autor:Liu Y; Zhao N; Li C; Chang Q; Liu X; Liao Y; Pan R
[Ad] Endereço:Institute of Medicinal Plant Development, Chinese Academy of Medical Science, Peking Union Medical College, Beijing, China.
[Ti] Título:Longistyline C acts antidepressant in vivo and neuroprotection in vitro against glutamate-induced cytotoxicity by regulating NMDAR/NR2B-ERK pathway in PC12 cells.
[So] Source:PLoS One;12(9):e0183702, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Depressive disorder is a common psychiatric disease which ranks among the leading cause of disability worldwide. The antidepressants presently used had low cure rate and caused a variety of side-effects. The screening of antidepressant drugs is usually used classic behavioural tests and neuroprotective strategy. Longistyline C, a natural stilbene isolated from the leaves of Cajanuscajan (L.) Millsp, was firstly investigated the antidepressant effect using animal behavioural tests, and studied the neuroprotection and its possible signaling pathways on glutamate-induced injury in PC12 cells. The results of animal test demonstrated that longistyline C had the antidepressant activity, which the effect is similar to the positive control. In current study, we investigated the effect of longistyline C on glutamate-induced injury in PC12 cells and explored its possible signaling pathways. The results demonstrated that pretreatment with longistyline C at the concentrations of 2-8 µmol/L for 24 h had a significant reduction of the cytotoxicity induced by glutamate (15 mmol/L) in PC12 cells using MTT, lactate dehydrogenase (LDH) release assay and Annexin V-PI double staining. Subsequently, we found that pretreatment with longistyline C (8 µmol/L) could drastically down-regulate the over-expression of NMDAR/NR2B and Ca2+/calmodulin-dependent protein kinase II (CaMKII), up-regulate the expressions of p-ERK and p-CREB and alleviate ER stress. In conclusison, longistyline C is most possibly through regulating NMDAR/NR2B-ERK1/2 related pathway and restoring endoplasmic reticulum function to exert neuroprotective effect against glutamate-induced injury in PC12 cells.
[Mh] Termos MeSH primário: Antidepressivos/farmacologia
Glutamatos/efeitos adversos
Receptores de N-Metil-D-Aspartato/metabolismo
Estilbenos/farmacologia
[Mh] Termos MeSH secundário: Animais
Comportamento Animal
Cálcio/metabolismo
Caspase 12/metabolismo
Caspase 9/metabolismo
Sobrevivência Celular
Teste de Esforço
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Proteínas de Choque Térmico/metabolismo
L-Lactato Desidrogenase/metabolismo
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Masculino
Camundongos
Camundongos Endogâmicos ICR
Neuroproteção
Células PC12
Ratos
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais
Natação
Fator de Transcrição CHOP/metabolismo
Proteína 1 de Ligação a X-Box/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antidepressive Agents); 0 (Ddit3 protein, mouse); 0 (Glutamates); 0 (Heat-Shock Proteins); 0 (NR2B NMDA receptor); 0 (Reactive Oxygen Species); 0 (Receptors, N-Methyl-D-Aspartate); 0 (Stilbenes); 0 (X-Box Binding Protein 1); 0 (Xbp1 protein, mouse); 0 (longistyline C); 0 (molecular chaperone GRP78); 147336-12-7 (Transcription Factor CHOP); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 3.4.22.- (Caspase 12); EC 3.4.22.- (Caspase 9); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183702


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[PMID]:28622016
[Au] Autor:Xie ZY; Chen L; Wang F; Liu L; Zhang C; Wang K; Cai F; Sinkemanni A; Hong X; Wu XT
[Ad] Endereço:1 Department of Spine Surgery, Zhongda Hospital, School of Medicine, Southeast University , Nanjing, China .
[Ti] Título:Endoplasmic Reticulum Stress Is Involved in Nucleus Pulposus Degeneration and Attenuates Low pH-Induced Apoptosis of Rat Nucleus Pulposus Cells.
[So] Source:DNA Cell Biol;36(8):627-637, 2017 Aug.
[Is] ISSN:1557-7430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The microenvironment of degenerative intervertebral disk (IVD) is characteristic of a high concentration of lactic acid and low pH levels, whereas the underlying mechanism has not been clearly defined. Endoplasmic reticulum (ER) is the hub of interactions between environmental signals and cellular biological functions, the malfunction of which is closely involved in the pathogenesis of multiple disorders, including IVD degeneration (IVDD). This research mainly aims at exploring what role ER stress plays in the natural process of IVDD and pH-induced apoptosis of rat nucleus pulposus (NP) cells (NPCs). The IVD of Sprague-Dawley rats at different ages was stained by Hematoxylin-Eosin staining to visualize the histocytological changes during the nature process of IVDD. Immunohistochemical staining was performed to evaluate the expression of ER stress markers within normal and degenerated NP. The ER stress markers were also quantified by quantitative real-time-polymerase chain reaction (PCR) and Western blotting analysis, respectively. NPCs were exposed to the culturing media with acidity of pH 7.4, 7.0, 6.5, or 6.0 for 24-72 h, with or without the supplement of 4-phenylbutyrayte (4-PBA, the blocker of ER stress pathways). Changes in cell viability were evaluated by CCK-8 assay and neutral red assay, whereas apoptosis was stained by Annexin-V/PI staining and quantified by flow cytometry analysis. The acidity-induced changes in the expression of ER stress markers were studied by immunofluorescent staining, qRT-PCR, and Western blotting analysis. In vivo, the expression of GRP78 and XBP1 was downregulated whereas CHOP and Caspase12 were upregulated in natural degeneration. In vitro, low pH induced apoptosis of rat NPCs; prolonged exposure of acid reduced cell viability and caused upregulation of ER stress markers. 4-PBA was used to alleviate ER stress, and it promoted acid-induced apoptosis of NPCs. ER stress is involved in NP natural degeneration and attenuates low-pH-induced apoptosis of NPCs.
[Mh] Termos MeSH primário: Apoptose/fisiologia
Estresse do Retículo Endoplasmático/fisiologia
Degeneração do Disco Intervertebral/patologia
Núcleo Pulposo/patologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Biomarcadores/metabolismo
Butilaminas/efeitos adversos
Butilaminas/metabolismo
Caspase 12/metabolismo
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
Proteínas de Choque Térmico/metabolismo
Concentração de Íons de Hidrogênio
Degeneração do Disco Intervertebral/metabolismo
Masculino
Núcleo Pulposo/metabolismo
Ratos
Ratos Sprague-Dawley
Fator de Transcrição CHOP/metabolismo
Proteína 1 de Ligação a X-Box/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-phenylbutylamine); 0 (Actins); 0 (Biomarkers); 0 (Butylamines); 0 (Ddit3 protein, rat); 0 (Heat-Shock Proteins); 0 (Hspa5 protein, rat); 0 (X-Box Binding Protein 1); 0 (Xbp1 protein, rat); 147336-12-7 (Transcription Factor CHOP); EC 3.4.22.- (Casp12 protein, rat); EC 3.4.22.- (Caspase 12)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170617
[St] Status:MEDLINE
[do] DOI:10.1089/dna.2017.3736


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[PMID]:28591178
[Au] Autor:Zhang C; Tang Y; Li Y; Xie L; Zhuang W; Liu J; Gong J
[Ad] Endereço:Department of Cardiology, Jinling Hospital, Nanjing University School of Medicine, Nanjing, Jiangsu, China.
[Ti] Título:Unfolded protein response plays a critical role in heart damage after myocardial ischemia/reperfusion in rats.
[So] Source:PLoS One;12(6):e0179042, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The unfolded protein response (UPR) plays a critical role in cell death mediated by ischemia/reperfusion (I/R) injury. However, little is known about the exact mechanism of UPR signaling pathways after myocardial I/R injury in rats. An attempt was therefore made to assess whether the myocardial I/R induced UPR, and which branch of UPR (ATF6, IRE1 and PERK) signal pathway was activated. Sprague-Dawley rats were pretreated with UPR stimulator dithiothreitol (DTT) and UPR inhibitor 4-phenylbutyrate (4PBA) and then subjected to myocardial I/R surgery. Compared with sham-operated group, the expression of GRP78, ATF6, CHOP and sXBP1 in the I/R injured group is significantly increased at transcript and protein levels, which indicated that all the three signal pathways of UPR were activated in the myocardial I/R injury. Compared with the I/R injured group, treatment with 4PBA effectively decreased myocardium infarct size, reduced myocardial apoptosis, down-regulated caspase-12 expression, diminished serum creatine kinase and lactate dehydrogenase levels. In contrast, these effects were reversed in DTT treated group. In summary, these results demonstrated that myocardial I/R injury activates UPR and inhibiting cell UPR possesses a cardioprotective effect through the suppression of ER stress-induced apoptosis. Therefore, inhibition of UPR might be used as a therapeutic target during myocardial I/R injury.
[Mh] Termos MeSH primário: Infarto do Miocárdio/genética
Traumatismo por Reperfusão Miocárdica/genética
Resposta a Proteínas não Dobradas/genética
[Mh] Termos MeSH secundário: Fator 6 Ativador da Transcrição/genética
Animais
Apoptose/genética
Caspase 12/sangue
Creatina Quinase/sangue
Estresse do Retículo Endoplasmático/genética
Proteínas de Choque Térmico/genética
Seres Humanos
L-Lactato Desidrogenase/sangue
Infarto do Miocárdio/fisiopatologia
Traumatismo por Reperfusão Miocárdica/fisiopatologia
Ratos
Transdução de Sinais
Fator de Transcrição CHOP/genética
Proteína 1 de Ligação a X-Box/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Activating Transcription Factor 6); 0 (Atf6 protein, rat); 0 (Ddit3 protein, rat); 0 (Heat-Shock Proteins); 0 (Hspa5 protein, rat); 0 (X-Box Binding Protein 1); 0 (Xbp1 protein, rat); 147336-12-7 (Transcription Factor CHOP); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 2.7.3.2 (Creatine Kinase); EC 3.4.22.- (Caspase 12)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179042


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[PMID]:28296042
[Au] Autor:Zou L; Su L; Sun Y; Han A; Chang X; Zhu A; Liu F; Li J; Sun Y
[Ad] Endereço:Department of Toxicology, School of Public Health, Lanzhou University, Lanzhou, 730000, China.
[Ti] Título:Nickel sulfate induced apoptosis via activating ROS-dependent mitochondria and endoplasmic reticulum stress pathways in rat Leydig cells.
[So] Source:Environ Toxicol;32(7):1918-1926, 2017 Jul.
[Is] ISSN:1522-7278
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nickel can induce apoptosis of testicular Leydig cells in mice, whereas the mechanisms remain unclear. In this study, we investigated the role of nickel-induced reactive oxygen species (ROS) generation in mitochondria and endoplasmic reticulum stress (ERS) mediated apoptosis pathways in rat Leydig cells. Fluorescent DCF and Annexin-V FITC/PI staining were performed to measure the production of ROS and apoptosis in Leydig cells. RT-qPCR and Western blot were conducted to analyze the key genes and proteins involved in mitochondria and ERS apoptotic pathways. The results showed that nickel sulfate induced ROS generation, consequently resulted in nucleolus deformation and apoptosis in testicular Leydig cells, which were then attenuated by ROS inhibitors of N-acetylcysteine (NAC) and 2,2,6,6-tetramethyl-1-piperidinyloxy (TEMPO). Nickel sulfate-triggered Leydig cells apoptosis via mitochondria and ERS pathways was characterized by the upregulated mRNA and proteins expression of Bak, cytochrome c, caspase 9, caspase 3, GRP78, GADD153, and caspase 12, which were inhibited by NAC and TEMPO respectively. The findings indicated that nickel-induced ROS generation was involved in apoptosis via mitochondria and ERS pathways in rat Leydig cells.
[Mh] Termos MeSH primário: Estresse do Retículo Endoplasmático/efeitos dos fármacos
Células Intersticiais do Testículo/efeitos dos fármacos
Mitocôndrias/metabolismo
Níquel/toxicidade
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Acetilcisteína/farmacologia
Animais
Apoptose/efeitos dos fármacos
Caspase 12/metabolismo
Caspase 3/metabolismo
Caspase 9/metabolismo
Óxidos N-Cíclicos/farmacologia
Citocromos c/metabolismo
Proteínas de Choque Térmico/metabolismo
Células Intersticiais do Testículo/metabolismo
Masculino
Ratos Wistar
Espécies Reativas de Oxigênio/antagonistas & inibidores
Transdução de Sinais
Fator de Transcrição CHOP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclic N-Oxides); 0 (Ddit3 protein, rat); 0 (Heat-Shock Proteins); 0 (Reactive Oxygen Species); 0 (molecular chaperone GRP78); 147336-12-7 (Transcription Factor CHOP); 4FLT4T3WUN (nickel sulfate); 7OV03QG267 (Nickel); 9007-43-6 (Cytochromes c); EC 3.4.22.- (Caspase 12); EC 3.4.22.- (Caspase 3); EC 3.4.22.- (Caspase 9); VQN7359ICQ (TEMPO); WYQ7N0BPYC (Acetylcysteine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1002/tox.22414


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[PMID]:28117681
[Au] Autor:Paridaens A; Raevens S; Devisscher L; Bogaerts E; Verhelst X; Hoorens A; Van Vlierberghe H; van Grunsven LA; Geerts A; Colle I
[Ad] Endereço:Department of Hepatology and Gastroenterology, Ghent University, 9000 Ghent, Belgium. Annelies.paridaens@ugent.be.
[Ti] Título:Modulation of the Unfolded Protein Response by Tauroursodeoxycholic Acid Counteracts Apoptotic Cell Death and Fibrosis in a Mouse Model for Secondary Biliary Liver Fibrosis.
[So] Source:Int J Mol Sci;18(1), 2017 Jan 20.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The role of endoplasmic reticulum stress and the unfolded protein response (UPR) in cholestatic liver disease and fibrosis is not fully unraveled. Tauroursodeoxycholic acid (TUDCA), a hydrophilic bile acid, has been shown to reduce endoplasmic reticulum (ER) stress and counteract apoptosis in different pathologies. We aimed to investigate the therapeutic potential of TUDCA in experimental secondary biliary liver fibrosis in mice, induced by common bile duct ligation. The kinetics of the hepatic UPR and apoptosis during the development of biliary fibrosis was studied by measuring markers at six different timepoints post-surgery by qPCR and Western blot. Next, we investigated the therapeutic potential of TUDCA, 10 mg/kg/day in drinking water, on liver damage (AST/ALT levels) and fibrosis (Sirius red-staining), in both a preventive and therapeutic setting. Common bile duct ligation resulted in the increased protein expression of CCAAT/enhancer-binding protein homologous protein (CHOP) at all timepoints, along with upregulation of pro-apoptotic caspase 3 and 12, tumor necrosis factor receptor superfamily, member 1A (TNFRsf1a) and Fas-Associated protein with Death Domain (FADD) expression. Treatment with TUDCA led to a significant reduction of liver fibrosis, accompanied by a slight reduction of liver damage, decreased hepatic protein expression of CHOP and reduced gene and protein expression of pro-apoptotic markers. These data indicate that TUDCA exerts a beneficial effect on liver fibrosis in a model of cholestatic liver disease, and suggest that this effect might, at least in part, be attributed to decreased hepatic UPR signaling and apoptotic cell death.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Sistema Biliar/efeitos dos fármacos
Fígado/efeitos dos fármacos
Ácido Tauroquenodesoxicólico/farmacologia
Resposta a Proteínas não Dobradas/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Apoptose/genética
Sistema Biliar/metabolismo
Sistema Biliar/patologia
Doenças Biliares/etiologia
Doenças Biliares/genética
Doenças Biliares/prevenção & controle
Western Blotting
Caspase 12/genética
Caspase 12/metabolismo
Caspase 3/genética
Caspase 3/metabolismo
Colagogos e Coleréticos/farmacologia
Colestase/complicações
Modelos Animais de Doenças
Fibrose
Expressão Gênica/efeitos dos fármacos
Fígado/metabolismo
Fígado/patologia
Cirrose Hepática/etiologia
Cirrose Hepática/genética
Cirrose Hepática/prevenção & controle
Masculino
Camundongos
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Fator de Transcrição CHOP/metabolismo
Fator de Necrose Tumoral alfa/genética
Resposta a Proteínas não Dobradas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholagogues and Choleretics); 0 (Ddit3 protein, mouse); 0 (Tumor Necrosis Factor-alpha); 147336-12-7 (Transcription Factor CHOP); 516-35-8 (Taurochenodeoxycholic Acid); 60EUX8MN5X (tauroursodeoxycholic acid); EC 3.4.22.- (Caspase 12); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170125
[St] Status:MEDLINE


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[PMID]:28082356
[Au] Autor:Diamanti MA; Gupta J; Bennecke M; De Oliveira T; Ramakrishnan M; Braczynski AK; Richter B; Beli P; Hu Y; Saleh M; Mittelbronn M; Dikic I; Greten FR
[Ad] Endereço:Institute for Tumor Biology and Experimental Therapy, Georg-Speyer-Haus, 60596 Frankfurt am Main, Germany.
[Ti] Título:IKKα controls ATG16L1 degradation to prevent ER stress during inflammation.
[So] Source:J Exp Med;214(2):423-437, 2017 Feb.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inhibition of the IκB kinase complex (IKK) has been implicated in the therapy of several chronic inflammatory diseases including inflammatory bowel diseases. In this study, using mice with an inactivatable IKKα kinase (Ikkα ), we show that loss of IKKα function markedly impairs epithelial regeneration in a model of acute colitis. Mechanistically, this is caused by compromised secretion of cytoprotective IL-18 from IKKα-mutant intestinal epithelial cells because of elevated caspase 12 activation during an enhanced unfolded protein response (UPR). Induction of the UPR is linked to decreased ATG16L1 stabilization in Ikkα mice. We demonstrate that both TNF-R and nucleotide-binding oligomerization domain stimulation promote ATG16L1 stabilization via IKKα-dependent phosphorylation of ATG16L1 at Ser278. Thus, we propose IKKα as a central mediator sensing both cytokine and microbial stimulation to suppress endoplasmic reticulum stress, thereby assuring antiinflammatory function during acute intestinal inflammation.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Quinase I-kappa B/fisiologia
Inflamação/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/química
Caspase 12/fisiologia
Colite/prevenção & controle
Estresse do Retículo Endoplasmático
Endorribonucleases/fisiologia
Interleucina-18/secreção
Camundongos
NF-kappa B/fisiologia
Proteína Adaptadora de Sinalização NOD2/fisiologia
Estabilidade Proteica
Proteínas Serina-Treonina Quinases/fisiologia
Resposta a Proteínas não Dobradas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Atg16l1 protein, mouse); 0 (Card15 protein, mouse); 0 (Carrier Proteins); 0 (Interleukin-18); 0 (NF-kappa B); 0 (Nod2 Signaling Adaptor Protein); EC 2.7.11.1 (Ern1 protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.10 (I-kappa B Kinase); EC 3.1.- (Endoribonucleases); EC 3.4.22.- (Caspase 12)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170114
[St] Status:MEDLINE
[do] DOI:10.1084/jem.20161867


  8 / 544 MEDLINE  
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[PMID]:28070110
[Au] Autor:Tungkum W; Jumnongprakhon P; Tocharus C; Govitrapong P; Tocharus J
[Ad] Endereço:Department of Biochemistry, Faculty of Medical Science Naresuan University, Thailand.
[Ti] Título:Melatonin suppresses methamphetamine-triggered endoplasmic reticulum stress in C6 cells glioma cell lines.
[So] Source:J Toxicol Sci;42(1):63-71, 2017.
[Is] ISSN:1880-3989
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Methamphetamine (METH) is a neurotoxic drug that causes brain damage by inducing neuronal and glial cell death together with glial cell hyperactivity-mediated progressive neurodegeneration. Previous studies have shown that METH induced glial cell hyperactivity and death via oxidative stress, the inflammatory response, and endoplasmic reticulum stress (ER stress) mechanisms, and melatonin could reverse these effects. However, the exact mechanism of the protective role of melatonin in METH-mediated ER stress has not been understood. This study investigated the protective effect of melatonin against METH toxicity-mediated ER stress in glial cells. Our study demonstrated that METH increased glial cell toxicity related to METH-induced ER stress by stimulating the unfolded protein response (UPR) to activate the expression of ER stress transducers, including phosphorylated double-stranded RNA-activated protein kinase (PKR)-like ER kinase (p-PERK), activating transcription factor (ATF6), and phosphorylated inositol-requiring enzyme 1 (p-IRE1). Moreover, the expression of binding immunoglobulin protein (Bip), CCAAT/enhancer-binding protein homologous protein (CHOP), caspase-12, phosphorylated eukaryotic translation initiation factor 2 alpha (p-eIF2α) and spliced X-box-binding protein-1 (XBP-1) mRNA were also increased. Melatonin reduced ER stress induced by METH toxicity by reducing the expression of ER stress response genes and proteins in a concentration-dependent manner. In addition, melatonin promoted the expression of Bip chaperone in a concentration-dependent manner. Taken together, our findings suggest that melatonin can protect against ER stress-induced glial cell death induced by METH.
[Mh] Termos MeSH primário: Estresse do Retículo Endoplasmático/efeitos dos fármacos
Melatonina/farmacologia
Metanfetamina/toxicidade
[Mh] Termos MeSH secundário: Fator 6 Ativador da Transcrição/metabolismo
Animais
Caspase 12/metabolismo
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Glioma/metabolismo
Proteínas de Choque Térmico/genética
Proteínas de Membrana/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Ratos
Fator de Transcrição CHOP/genética
Fator de Transcrição CHOP/metabolismo
Proteína 1 de Ligação a X-Box/genética
eIF-2 Quinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Activating Transcription Factor 6); 0 (Atf6 protein, rat); 0 (Ddit3 protein, rat); 0 (Heat-Shock Proteins); 0 (Hspa5 protein, rat); 0 (Membrane Proteins); 0 (X-Box Binding Protein 1); 0 (Xbp1 protein, rat); 147336-12-7 (Transcription Factor CHOP); 44RAL3456C (Methamphetamine); EC 2.7.1.- (Ern2 protein, rat); EC 2.7.11.1 (PERK kinase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (eIF-2 Kinase); EC 3.4.22.- (Caspase 12); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170111
[St] Status:MEDLINE
[do] DOI:10.2131/jts.42.63


  9 / 544 MEDLINE  
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[PMID]:27959410
[Au] Autor:Zou X; Qu Z; Fang Y; Shi X; Ji Y
[Ad] Endereço:Engineering Research Center of Natural Antineoplastic Drugs, Ministry of Education, Harbin, Heilongjiang 150076, P.R. China.
[Ti] Título:Endoplasmic reticulum stress mediates sulforaphane-induced apoptosis of HepG2 human hepatocellular carcinoma cells.
[So] Source:Mol Med Rep;15(1):331-338, 2017 Jan.
[Is] ISSN:1791-3004
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Sulforaphane (SFN) is a naturally occurring chemopreventive agent, which effectively inhibits proliferation of HepG2 human hepatocellular carcinoma cells via mitochondria­mediated apoptosis. Endoplasmic reticulum stress is considered the most important cause of cell apoptosis; therefore, the present study aimed to determine whether the endoplasmic reticulum pathway was involved in SFN-induced apoptosis of HepG2 cells. An MTT assay was used to detect the inhibitory effects of SFN on HepG2 cells. Fluorescence microscopy was used to observe the morphological changes in apoptotic cells, and western blot analysis was conducted to detect the expression of binding immunoglobulin protein (Bip)/glucose-regulated protein 78 (GRP78), X­box binding protein­1 (XBP­1) and BH3 interacting domain death agonist (Bid). Furthermore, flow cytometry was used to determine the apoptotic rate of HepG2 cells, and the protein expression of C/EBP homologous protein (CHOP)/growth arrest­ and DNA damage­inducible gene 153 (GADD153) and caspase-12 in HepG2 cells. The results indicated that SFN significantly inhibited the proliferation of HepG2 cells; the half maximal inhibitory concentration values were 32.03±0.96, 20.90±1.96 and 13.87±0.44 µmol/l, following treatment with SFN for 24, 48 and 72 h, respectively. Following 48 h of SFN treatment (10, 20 and 40 µmol/l), the apoptotic rates of HepG2 cells were 31.8, 61.3 and 77.1%, respectively. Furthermore, after 48 h of exposure to SFN, the cells presented typical morphological alterations of apoptosis, as detected under fluorescence microscopy. Treatment with SFN for 48 h also significantly upregulated the protein expression levels of Bip/GRP78, XBP­1, caspase­12, CHOP/GADD153 and Bid in HepG2 cells. In conclusion, endoplasmic reticulum stress may be considered the most important mechanism underlying SFN-induced apoptosis in HepG2 cells.
[Mh] Termos MeSH primário: Anticarcinógenos/farmacologia
Apoptose/efeitos dos fármacos
Carcinoma Hepatocelular/tratamento farmacológico
Estresse do Retículo Endoplasmático/efeitos dos fármacos
Isotiocianatos/farmacologia
Neoplasias Hepáticas/tratamento farmacológico
[Mh] Termos MeSH secundário: Proteína Agonista de Morte Celular de Domínio Interatuante com BH3/metabolismo
Carcinoma Hepatocelular/metabolismo
Carcinoma Hepatocelular/patologia
Caspase 12/metabolismo
Proteínas de Choque Térmico/metabolismo
Células Hep G2
Seres Humanos
Neoplasias Hepáticas/metabolismo
Neoplasias Hepáticas/patologia
Fator de Transcrição CHOP/metabolismo
Proteína 1 de Ligação a X-Box/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticarcinogenic Agents); 0 (BH3 Interacting Domain Death Agonist Protein); 0 (BID protein, human); 0 (DDIT3 protein, human); 0 (Heat-Shock Proteins); 0 (Isothiocyanates); 0 (X-Box Binding Protein 1); 0 (molecular chaperone GRP78); 147336-12-7 (Transcription Factor CHOP); EC 3.4.22.- (Caspase 12); GA49J4310U (sulforafan)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170330
[Lr] Data última revisão:
170330
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161214
[St] Status:MEDLINE
[do] DOI:10.3892/mmr.2016.6016


  10 / 544 MEDLINE  
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[PMID]:27655243
[Au] Autor:Sun Y; Ke L; Zheng X; Li T; Ouyang W; Zhang Z
[Ad] Endereço:College of Chemistry and Life Science, Zhejiang Normal University, Jinhua, 321004, People's Republic of China.
[Ti] Título:Effects of Different Levels of Calcium Intake on Brain Cell Apoptosis in Fluorosis Rat Offspring and Its Molecular Mechanism.
[So] Source:Biol Trace Elem Res;176(2):355-366, 2017 Apr.
[Is] ISSN:1559-0720
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The purpose of the investigation is to reveal the influence of dietary calcium on fluorosis-induced brain cell apoptosis in rat offspring, as well as the underlying molecular mechanism. Sprague-Dawley (SD) female rats were randomly divided into five groups: control group, fluoride group, low calcium, low calcium fluoride group, and high calcium fluoride group. SD male rats were used for breeding only. After 3 months, male and female rats were mated in a 1:1 ratio. Subsequently, 18-day-old gestation rats and 14- and 28-day-old rats were used as experimental subjects. We determined the blood/urine fluoride, the blood/urine calcium, the apoptosis in the hippocampus, and the expression levels of apoptosis-related genes, namely Bcl-2, caspase 12, and JNK. Blood or blood/urine fluoride levels and apoptotic cells were found significantly increased in fluorosis rat offspring as compared to controls. Furthermore, the Bcl-2 messenger RNA (mRNA) expression levels significantly decreased, and caspase 12 mRNA levels significantly increased in each age group as compared to controls. Compared with the fluoride group, the blood/urine fluoride content and apoptotic cells evidently decreased in the high calcium fluoride group, Bcl-2 mRNA expression significantly increased and caspase 12 mRNA expression significantly decreased in each age group. All results showed no gender difference. Based on these results, the molecular mechanisms of fluorosis-induced brain cell apoptosis in rat offspring may include the decrease in Bcl-2 mRNA expression level and increase in caspase 12 mRNA expression signaling pathways. High calcium intake could reverse these gene expression trends. By contrast, low calcium intake intensified the toxic effects of fluoride on brain cells.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Encéfalo/efeitos dos fármacos
Encéfalo/patologia
Cálcio/administração & dosagem
Cálcio/farmacologia
Intoxicação por Flúor/patologia
[Mh] Termos MeSH secundário: Administração Oral
Animais
Encéfalo/embriologia
Caspase 12/genética
Caspase 12/metabolismo
Feminino
Masculino
Proteínas Proto-Oncogênicas c-bcl-2/antagonistas & inibidores
Proteínas Proto-Oncogênicas c-bcl-2/genética
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proto-Oncogene Proteins c-bcl-2); 0 (RNA, Messenger); EC 3.4.22.- (Caspase 12); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160923
[St] Status:MEDLINE
[do] DOI:10.1007/s12011-016-0850-9



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