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[PMID]:29442034
[Au] Autor:Li J; Ma L; Fan Y; Zhang Y; Sun D; Wu B
[Ti] Título:Crosstalk between 6-OHDA-induced autophagy and apoptosis in PC12 cells is mediated by phosphorylation of Raf-1/ERK1/2.
[So] Source:Pharmazie;71(8):465-471, 2016 08 01.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Parkinson's disease (PD) is a degenerative brain disorder characterized by motor symptoms and loss of dopaminergic (DA) neurons in the substantia nigra. The mechanisms for DA cell death in PD have been extensively investigated using PC12 cells treated with a dopamine neurotoxin 6-hydroxydopamine (6-OHDA). 6-OHDA may induce both autophagy and apoptosis in PC12 cells. However, it remains unclear whether crosstalk occurs between autophagy and apoptosis in PC12 cells treated with 6-OHDA and whether Raf-1/ERK1/2 and their phosphorylation status play a role in autophagy. In this study, we used MDC staining assay and flow cytometry and found that 6-OHDA induced autophagy in PC12 cells. This induction was inhibited by the autophagy inhibitor 3-MA. Our electron microscopy observations also supported 6-OHDA induced autophagy in PC12 cells. Apoptosis of PC12 cells was increased with inhibition of autophagy by 3-MA. In addition, Inhibition of Raf-1 resulted in a decreased 6-OHDA-induced autophagy rate among PC12 cells. Phosphorylation levels of Raf-1 and ERK1/2 were increased in PC12 cells treated with 6-OHDA and inhibited by co-treatment with 6-OHDA and 3-MA. These data suggest that crosstalk between 6-OHDA-induced apoptosis and autophagy in PC12 cells may be regulated via the Raf-1/ERK1/2 signaling pathway. Our data suggest a mechanism for 6-OHDA toxicity in PC12 cells, contributing to our understanding of the pathogenesis of PD.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Autofagia/efeitos dos fármacos
Hidroxidopaminas/farmacologia
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Fosforilação/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-raf/metabolismo
Receptor Cross-Talk/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adenosina/análogos & derivados
Adenosina/farmacologia
Animais
Sobrevivência Celular/efeitos dos fármacos
Células PC12
Proteínas Proto-Oncogênicas c-raf/efeitos dos fármacos
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hydroxydopamines); 72055-62-0 (3-methyladenosine); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.1 (Raf1 protein, rat); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180215
[St] Status:MEDLINE
[do] DOI:10.1691/ph.2016.6586


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[PMID]:29307174
[Au] Autor:Han L; Yu J; Chen Y; Cheng D; Wang X; Wang C
[Ad] Endereço:Key Laboratory of Food Nutrition and Safety, Ministry of Education, College of food Engineering and Biotechnology, Tianjin University of Science and Technology , No. 29, 13th Avenue, Tianjin Economy Technological Development Area, Tianjin 300457, People Republic of China.
[Ti] Título:Immunomodulatory Activity of Docosahexenoic Acid on RAW264.7 Cells Activation through GPR120-Mediated Signaling Pathway.
[So] Source:J Agric Food Chem;66(4):926-934, 2018 Jan 31.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, we elucidated the immunomodulatory activity of docosahexaenoic acid (DHA) on protein expression in RAW264.7 cells and its molecular mechanism. The results showed that the proliferation index of RAW264.7 cells at 48 h was about 173.03 ± 7.82% after the treatment of 2.4 µM DHA. DHA could activate RAW264.7 cells by the G-protein coupled cell membrane receptor GPR120-C-Raf- mitogen-activated protein kinases (MAPKs)-nuclear factor κB (NF-κB) p65 pathway. In addition, 2.4 µM of DHA could significantly increase (P < 0.01) the mRNA and protein expression of inducible nitric oxide synthase (iNOS), which is consistent with the result of the NO release. ELISA results revealed that DHA could enhance the protein expression of cytokines IL-1ß, IL-6, IL-10, IL-12, TNF-α, IFN-γ, and TGF-ß. These results indicated that the immunomodulatory mechanism of RAW264.7 cells by DHA was associated with the release of NO and cytokines by stimulating the GPR120, C-Raf, and MAPKs to the NF-κB p65 pathway.
[Mh] Termos MeSH primário: Ácidos Docosa-Hexaenoicos/farmacologia
Fatores Imunológicos/farmacologia
Ativação de Macrófagos/efeitos dos fármacos
Receptores Acoplados a Proteínas-G/fisiologia
[Mh] Termos MeSH secundário: Animais
Citocinas/metabolismo
Camundongos
Proteínas Quinases Ativadas por Mitógeno/fisiologia
Óxido Nítrico/metabolismo
Proteínas Proto-Oncogênicas c-raf/fisiologia
Células RAW 264.7
Transdução de Sinais
Fator de Transcrição RelA/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Immunologic Factors); 0 (O3far1 protein, mouse); 0 (Receptors, G-Protein-Coupled); 0 (Rela protein, mouse); 0 (Transcription Factor RelA); 25167-62-8 (Docosahexaenoic Acids); 31C4KY9ESH (Nitric Oxide); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[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:180109
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05894


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[PMID]:28743511
[Au] Autor:Yang L; Tang L; Dai F; Meng G; Yin R; Xu X; Yao W
[Ad] Endereço:School of pharmacy, Nantong University, 19 QiXiu Road, Nantong 226001, China.
[Ti] Título:Raf-1/CK2 and RhoA/ROCK signaling promote TNF-α-mediated endothelial apoptosis via regulating vimentin cytoskeleton.
[So] Source:Toxicology;389:74-84, 2017 08 15.
[Is] ISSN:1879-3185
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Both RhoA/ROCK and Raf-1/CK2 pathway play essential roles in cell proliferation, apoptosis, differentiation, and multiple other common cellular functions. We previously reported that vimentin is responsible for TNF-α-induced cell apoptosis. Herein, we investigated the regulation of RhoA/ROCK and Raf-1/CK2 signaling on vimentin filaments and endothelial apoptosis mediated by TNF-α. Treatment with TNF-α significantly induced the activation of RhoA and ROCK, and the expression of ROCK1. RhoA deficiency could obviously inhibit ROCK activation and ROCK1 expression induced by TNF-α. Both RhoA deficiency and ROCK activity inhibition (Y-27632) greatly inhibited endothelial apoptosis and preserved cell viability in TNF-α-induced human umbilical vein endothelial cells (HUVECs). Also vimentin phosphorylation and the remodeling of vimentin or phospho-vimentin induced by TNF-α were obviously attenuated by RhoA suppression and ROCK inhibition. TNF-α-mediated vimentin cleavage was significantly inhibited by RhoA suppression and ROCK inhibition through decreasing the activation of caspase3 and 8. Furthermore, TNF-α treatment greatly enhanced the activation of Raf-1. Suppression of Raf-1 or CK2 by its inhibitor (GW5074 or TBB) blocked vimentin phosphorylation, remodeling and endothelial apoptosis, and preserved cell viability in TNF-α-induced HUVECs. However, Raf-1 inhibition showed no significant effect on TNF-α-induced ROCK expression and activation, suggesting that the regulation of Raf-1/CK2 signaling on vimentin was independent of ROCK. Taken together, these results indicate that both RhoA/ROCK and Raf-1/CK2 pathway are responsible for TNF-α-mediated endothelial cytotoxicity via regulating vimentin cytoskeleton.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Caseína Quinase II/metabolismo
Citoesqueleto/efeitos dos fármacos
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-raf/metabolismo
Fator de Necrose Tumoral alfa/toxicidade
Vimentina/metabolismo
Quinases Associadas a rho/metabolismo
Proteína rhoA de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Caseína Quinase II/antagonistas & inibidores
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
Citoesqueleto/enzimologia
Citoesqueleto/patologia
Células Endoteliais da Veia Umbilical Humana/enzimologia
Células Endoteliais da Veia Umbilical Humana/patologia
Seres Humanos
Fosforilação
Inibidores de Proteínas Quinases/farmacologia
Proteínas Proto-Oncogênicas c-raf/antagonistas & inibidores
Interferência de RNA
Transdução de Sinais/efeitos dos fármacos
Transfecção
Proteína cdc42 de Ligação ao GTP/genética
Proteína cdc42 de Ligação ao GTP/metabolismo
Quinases Associadas a rho/antagonistas & inibidores
Proteína rhoA de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Kinase Inhibitors); 0 (Tumor Necrosis Factor-alpha); 0 (Vimentin); 124671-05-2 (RHOA protein, human); EC 2.7.11.1 (Casein Kinase II); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.1 (ROCK1 protein, human); EC 2.7.11.1 (rho-Associated Kinases); EC 3.6.5.2 (cdc42 GTP-Binding Protein); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180122
[Lr] Data última revisão:
180122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE


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[PMID]:29056104
[Au] Autor:Cuthbert CE; Foster JE; Ramdath DD
[Ad] Endereço:1Department of Pre-Clinical Sciences, Faculty of Medical Sciences,The University of the West Indies,St. Augustine,Trinidad and Tobago, West Indies.
[Ti] Título:A maternal high-fat, high-sucrose diet alters insulin sensitivity and expression of insulin signalling and lipid metabolism genes and proteins in male rat offspring: effect of folic acid supplementation.
[So] Source:Br J Nutr;118(8):580-588, 2017 Oct.
[Is] ISSN:1475-2662
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A maternal high-fat, high-sucrose (HFS) diet alters offspring glucose and lipid homoeostasis through unknown mechanisms and may be modulated by folic acid. We investigated the effect of a maternal HFS diet on glucose homoeostasis, expression of genes and proteins associated with insulin signalling and lipid metabolism and the effect of prenatal folic acid supplementation (HFS/F) in male rat offspring. Pregnant Sprague-Dawley rats were randomly fed control (CON), HFS or HFS/F diets. Offspring were weaned on CON; at postnatal day 70, fasting plasma insulin and glucose and liver and skeletal muscle gene and protein expression were measured. Treatment effects were assessed by one-way ANOVA. Maternal HFS diet induced higher fasting glucose in offspring v. HFS/F (P=0·027) and down-regulation (P<0·05) of genes coding for v-Akt murine thymoma viral oncogene homolog 2, resistin and v-Raf-1 murine leukaemia viral oncogene homolog 1 (Raf1) in offspring skeletal muscle and acetyl-CoA carboxylase (Acaca), fatty acid synthase and phosphatidylinositol-4,5-biphosphate 3-kinase, catalytic subunit ß in offspring liver. Skeletal muscle neuropeptide Y and hepatic Kruppel-like factor 10 were up-regulated in HFS v. CON offspring (P<0·05). Compared with CON, Acaca and Raf1 protein expression levels were significantly lower in HFS offspring. Maternal HFS induced higher homoeostasis model of assessment index of insulin resistance v. CON (P=0·030) and HFS/F was associated with higher insulin (P=0·016) and lower glucose (P=0·025). Maternal HFS diet alters offspring insulin sensitivity and de novo hepatic lipogenesis via altered gene and protein expression, which appears to be potentiated by folate supplementation.
[Mh] Termos MeSH primário: Dieta Hiperlipídica
Resistência à Insulina
Insulina/sangue
Metabolismo dos Lipídeos
Fenômenos Fisiológicos da Nutrição Materna
[Mh] Termos MeSH secundário: Acetil-CoA Carboxilase/genética
Acetil-CoA Carboxilase/metabolismo
Animais
Animais Recém-Nascidos
Glicemia/metabolismo
Regulação para Baixo
Ácido Graxo Sintases/genética
Ácido Graxo Sintases/metabolismo
Feminino
Ácido Fólico/administração & dosagem
Fígado/metabolismo
Masculino
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Gravidez
Efeitos Tardios da Exposição Pré-Natal
Proteínas Proto-Oncogênicas c-akt/genética
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteínas Proto-Oncogênicas c-raf/genética
Proteínas Proto-Oncogênicas c-raf/metabolismo
Ratos
Ratos Sprague-Dawley
Resistina/genética
Resistina/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Insulin); 0 (Resistin); 0 (Retn protein, rat); 935E97BOY8 (Folic Acid); EC 2.3.1.85 (Fatty Acid Synthases); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.- (phosphatidylinositol 4,5-biphosphate kinase); EC 2.7.11.1 (Akt2 protein, rat); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.1 (Raf1 protein, rat); EC 6.4.1.2 (Acetyl-CoA Carboxylase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171024
[St] Status:MEDLINE
[do] DOI:10.1017/S0007114517002501


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[PMID]:28993193
[Au] Autor:Yang L; Wen Y; Lv G; Lin Y; Tang J; Lu J; Zhang M; Liu W; Sun X
[Ad] Endereço:Shenzhen Tumor Immuno-gene Therapy Clinical Application Engineering Lab, Biobank of Shenzhen Second People's Hospital, The First Affiliated Hospital of Shenzhen University, Shenzhen 518035, PR China; Institute of Immunology of Zhongshan School of Medicine, Sun Yat-Sen University, Guangzhou 510060, G
[Ti] Título:α-Lipoic acid inhibits human lung cancer cell proliferation through Grb2-mediated EGFR downregulation.
[So] Source:Biochem Biophys Res Commun;494(1-2):325-331, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Alpha lipoic acid (α -LA) is a naturally occurring antioxidant and metabolic enzyme co-factor. Recently, α -LA has been reported to inhibit the growth of various cancer cells, but the precise signaling pathways that mediate the effects of α -LA on non-small cell lung cancer (NSCLC) development remain unclear. METHODS: The CCK-8 assay was used to assess cell proliferation in NSCLC cell lines after α -LA treatment. The expression of growth factor receptor-bound protein 2 (Grb2), cyclin-dependent kinase (CDK)-2, CDK4, CDK6, Cyclin D3, Cyclin E1, Ras, c-Raf, epidermal growth factor receptor (EGFR), ERK1/2 and activated EGFR and ERK1/2 was evaluated by western blotting. Grb2 levels were restored in α-LA-treated cells by transfection of a plasmid carrying Grb2 and were reduced in NSCLC cells via specific siRNA-mediated knockdown. RESULTS: α -LA dramatically decreased NSCLC cell proliferation by downregulating Grb2; in contrast, Grb2 overexpression significantly prevented α-LA-induced decrease in cell growth in vitro. Western blot analysis indicated that α-LA decreased the levels of phospho-EGFR, CDK2/4/6, Cyclins D3 and E1, which are associated with the inhibition of G1/S-phase transition. Additional experiments indicated that Grb2 inhibition partially abolished EGF-induced phospho-EGFR and phospho-ERK1/2 activity. In addition, α-LA exerted greater inhibitory effects than gefitinib on NSCLC cells by preventing EGF-induced EGFR activation. CONCLUSION: For the first time, these findings provide the first evidence that α-LA inhibits cell proliferation through Grb2 by suppressing EGFR phosphorylation and that MAPK/ERK is involved in this pathway.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Pontos de Checagem da Fase G1 do Ciclo Celular/efeitos dos fármacos
Proteína Adaptadora GRB2/antagonistas & inibidores
Regulação Neoplásica da Expressão Gênica
Ácido Tióctico/farmacologia
[Mh] Termos MeSH secundário: Células A549
Proliferação Celular/efeitos dos fármacos
Ciclina D3/genética
Ciclina D3/metabolismo
Ciclina E/genética
Ciclina E/metabolismo
Quinase 2 Dependente de Ciclina/genética
Quinase 2 Dependente de Ciclina/metabolismo
Quinase 4 Dependente de Ciclina/genética
Quinase 4 Dependente de Ciclina/metabolismo
Quinase 6 Dependente de Ciclina/genética
Quinase 6 Dependente de Ciclina/metabolismo
Proteína Adaptadora GRB2/genética
Proteína Adaptadora GRB2/metabolismo
Seres Humanos
Proteína Quinase 1 Ativada por Mitógeno/genética
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/genética
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
Proteínas Oncogênicas/genética
Proteínas Oncogênicas/metabolismo
Fosforilação/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-raf/genética
Proteínas Proto-Oncogênicas c-raf/metabolismo
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Receptor do Fator de Crescimento Epidérmico/genética
Receptor do Fator de Crescimento Epidérmico/metabolismo
Transdução de Sinais
Proteínas ras/genética
Proteínas ras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (CCND3 protein, human); 0 (CCNE1 protein, human); 0 (Cyclin D3); 0 (Cyclin E); 0 (GRB2 Adaptor Protein); 0 (GRB2 protein, human); 0 (Oncogene Proteins); 0 (RNA, Small Interfering); 73Y7P0K73Y (Thioctic Acid); EC 2.7.10.1 (EGFR protein, human); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.22 (CDK2 protein, human); EC 2.7.11.22 (CDK4 protein, human); EC 2.7.11.22 (CDK6 protein, human); EC 2.7.11.22 (Cyclin-Dependent Kinase 2); EC 2.7.11.22 (Cyclin-Dependent Kinase 4); EC 2.7.11.22 (Cyclin-Dependent Kinase 6); EC 2.7.11.24 (MAPK1 protein, human); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 3.6.5.2 (ras Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE


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[PMID]:28888848
[Au] Autor:Shibata S; Furuta K; Oh-Hashi K; Ueda H; Kiuchi K; Hirata Y
[Ad] Endereço:Department of Chemistry and Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido, Gifu 501-1193, Japan.
[Ti] Título:Prevention of oxytosis-induced c-Raf down-regulation by (arylthio)cyclopentenone prostaglandins is neuroprotective.
[So] Source:Toxicology;390:83-87, 2017 Sep 01.
[Is] ISSN:1879-3185
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Prolonged exposure to high concentrations of glutamate leads to cell type specific glutathione depletion and resulting oxidative stress, known as oxytosis. As a result of glutathione depletion, accumulation of reactive oxygen species and Ca influx are increased; however, the specific target of oxytosis has yet to be identified. In the present study, we focused on the effect of glutamate-induced oxidative stress on the extracellular-regulated protein kinase (ERK) pathway using the murine hippocampal HT22 cell line. Although the contribution of the ERK pathway to glutamate-induced oxytosis in HT22 cells is controversial, Western blot analysis revealed that glutamate caused down-regulation of mitogen-activated protein kinase kinase kinase (c-Raf) and a resulting decrease in the phosphorylation of c-Raf, as well as of mitogen-activated protein kinase kinase1/2 (MEK1/2) and ERK1/2, downstream components of the c-Raf/MEK/ERK pathway. Furthermore, neuroprotective (arylthio)cyclopentenone prostaglandins prevented glutamate-induced c-Raf down-regulation and consequently maintained the basal activity of c-Raf and its downstream signaling components. A pull-down assay using biotin-labeled cyclopentenone prostaglandins revealed that they preferentially bound to c-Raf relative to other signaling molecules of the ERK pathway, including Ras, MEK1/2, and ERK. These results suggest that neuroprotective (arylthio)cyclopentenone prostaglandins directly bind to c-Raf protein and protect cells from down-regulation of the c-Raf protein itself, resulting in neuroprotection against oxidative stress.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Ciclopentanos/farmacologia
Ácido Glutâmico/toxicidade
Glutationa/metabolismo
Hipocampo/efeitos dos fármacos
Neurônios/efeitos dos fármacos
Fármacos Neuroprotetores/farmacologia
Síndromes Neurotóxicas/prevenção & controle
Estresse Oxidativo/efeitos dos fármacos
Prostaglandinas/farmacologia
Proteínas Proto-Oncogênicas c-raf/metabolismo
[Mh] Termos MeSH secundário: Animais
Antioxidantes/metabolismo
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Ciclopentanos/metabolismo
Citoproteção
Relação Dose-Resposta a Droga
Regulação para Baixo
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Hipocampo/enzimologia
Hipocampo/patologia
MAP Quinase Quinase Quinases/metabolismo
Camundongos
Neurônios/enzimologia
Neurônios/patologia
Fármacos Neuroprotetores/metabolismo
Síndromes Neurotóxicas/etiologia
Síndromes Neurotóxicas/metabolismo
Síndromes Neurotóxicas/patologia
Fosforilação
Prostaglandinas/metabolismo
Ligação Proteica
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Cyclopentanes); 0 (Neuroprotective Agents); 0 (Prostaglandins); 3KX376GY7L (Glutamic Acid); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 2.7.11.25 (MAP Kinase Kinase Kinases); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170911
[St] Status:MEDLINE


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[PMID]:28807789
[Au] Autor:Dai X; Song R; Xiong Y
[Ad] Endereço:Key Laboratory of Trace Elements and Endemic Diseases, National Health and Family Planning Commission of the people's Rupublic of China, Xi'an Jiaotong University Health Science Center, No. 76 Yanta West Road, Xi'an, Shaanxi 710061, China.
[Ti] Título:The expression of ERK and JNK in patients with an endemic osteochondropathy, Kashin-Beck disease.
[So] Source:Exp Cell Res;359(2):337-341, 2017 Oct 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Kashin-Beck disease (KBD) is a chronic, endemic osteochondropathy. Its etiopathogenesis is still obscure until now. Epidemiological observation has shown that low selenium play a crucial role in the pathogenesis of KBD. Extracellular signal-regulated kinases (ERKs) and C-Jun N-terminal kinase (JNK), members of the mitogen-activated protein kinase (MAPK) superfamily, play an important role in cell proliferation and differentiation. Nuclear factor-ĸB (NF-ĸB), an important signaling mediator for inflammatory and immune responses, is involved in the regulation of osteoclastogenesis. In the present study, we investigated the expression of ERK and JNK signal molecular, as well as nuclear factor-ĸB in the pathogenesis of Kashin-Beck disease, evaluated the effect of selenium on ERK signal pathway. The expression levels of ERK and JNK signal pathway, as well as nuclear factor-ĸB were investigated for 218 patients and 209 controls by immunoblot analysis in whole blood. Evaluated the effect of selenium on ERK signal pathway by Na SeO treatment. The protein levels of pRaf-1, pMek1/2 and pErk1/2 decreased significantly in KBD patients, p-JNK and NF-ĸB increased in KBD patients. Furthermore, Na SeO treatment improved the reduction of proteins in ERK signal pathway. These findings indicated that ERK and JNK signaling pathways, as well as the expression level of NF-κB signaling molecular are important contributor to the pathogenesis of KBD. Selenium stimulates the phosphorylation of the ERK signaling pathway.
[Mh] Termos MeSH primário: Cartilagem Articular/metabolismo
Doença de Kashin-Bek/genética
MAP Quinase Quinase 4/genética
Proteína Quinase 1 Ativada por Mitógeno/genética
Proteína Quinase 3 Ativada por Mitógeno/genética
NF-kappa B/genética
Selênio/deficiência
[Mh] Termos MeSH secundário: Cartilagem Articular/patologia
Estudos de Casos e Controles
Linhagem Celular
Condrócitos/citologia
Condrócitos/efeitos dos fármacos
Condrócitos/metabolismo
Feminino
Regulação da Expressão Gênica
Seres Humanos
Doença de Kashin-Bek/metabolismo
Doença de Kashin-Bek/patologia
MAP Quinase Quinase 1/genética
MAP Quinase Quinase 1/metabolismo
MAP Quinase Quinase 2/genética
MAP Quinase Quinase 2/metabolismo
MAP Quinase Quinase 4/metabolismo
Masculino
Meia-Idade
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
NF-kappa B/metabolismo
Fosforilação/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-raf/genética
Proteínas Proto-Oncogênicas c-raf/metabolismo
Transdução de Sinais
Selenito de Sódio/farmacologia
terc-Butil Hidroperóxido/antagonistas & inibidores
terc-Butil Hidroperóxido/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NF-kappa B); 955VYL842B (tert-Butylhydroperoxide); EC 2.7.1.- (MAP2K2 protein, human); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.24 (MAPK1 protein, human); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 2.7.12.2 (MAP Kinase Kinase 1); EC 2.7.12.2 (MAP Kinase Kinase 2); EC 2.7.12.2 (MAP Kinase Kinase 4); EC 2.7.12.2 (MAP2K1 protein, human); H6241UJ22B (Selenium); HIW548RQ3W (Sodium Selenite)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE


  8 / 3517 MEDLINE  
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[PMID]:28630043
[Au] Autor:Johnson CW; Reid D; Parker JA; Salter S; Knihtila R; Kuzmic P; Mattos C
[Ad] Endereço:From the Department of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115 and.
[Ti] Título:The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects.
[So] Source:J Biol Chem;292(31):12981-12993, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:H-Ras, K-Ras, and N-Ras are small GTPases that are important in the control of cell proliferation, differentiation, and survival, and their mutants occur frequently in human cancers. The G-domain, which catalyzes GTP hydrolysis and mediates downstream signaling, is 95% conserved between the Ras isoforms. Because of their very high sequence identity, biochemical studies done on H-Ras have been considered representative of all three Ras proteins. We show here that this is not a valid assumption. Using enzyme kinetic assays under identical conditions, we observed clear differences between the three isoforms in intrinsic catalysis of GTP by Ras in the absence and presence of the Ras-binding domain (RBD) of the c-Raf kinase protein (Raf-RBD). Given their identical active sites, isoform G-domain differences must be allosteric in origin, due to remote isoform-specific residues that affect conformational states. We present the crystal structure of N-Ras bound to a GTP analogue and interpret the kinetic data in terms of structural features specific for H-, K-, and N-Ras.
[Mh] Termos MeSH primário: GTP Fosfo-Hidrolases/metabolismo
Guanosina Trifosfato/metabolismo
Proteínas de Membrana/metabolismo
Modelos Moleculares
Proteínas Proto-Oncogênicas c-raf/metabolismo
Proteínas Proto-Oncogênicas p21(ras)/metabolismo
[Mh] Termos MeSH secundário: Regulação Alostérica
Sítio Alostérico
Substituição de Aminoácidos
Biocatálise
Domínio Catalítico
Cristalografia por Raios X
Fosfatos de Dinucleosídeos/química
Fosfatos de Dinucleosídeos/metabolismo
Estabilidade Enzimática
GTP Fosfo-Hidrolases/química
GTP Fosfo-Hidrolases/genética
Guanosina Trifosfato/análogos & derivados
Guanosina Trifosfato/química
Seres Humanos
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
Ligantes
Proteínas de Membrana/química
Proteínas de Membrana/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Mutação Puntual
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Proto-Oncogênicas c-raf/química
Proteínas Proto-Oncogênicas c-raf/genética
Proteínas Proto-Oncogênicas p21(ras)/química
Proteínas Proto-Oncogênicas p21(ras)/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dinucleoside Phosphates); 0 (Isoenzymes); 0 (KRAS protein, human); 0 (Ligands); 0 (Membrane Proteins); 0 (Peptide Fragments); 0 (Recombinant Proteins); 78101-73-2 (diguanosine pentaphosphate); 86-01-1 (Guanosine Triphosphate); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (NRAS protein, human); EC 3.6.5.2 (HRAS protein, human); EC 3.6.5.2 (Proto-Oncogene Proteins p21(ras))
[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:170621
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.778886


  9 / 3517 MEDLINE  
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[PMID]:28601637
[Au] Autor:Yamana S; Tokiyama A; Fujita H; Terao Y; Horibe S; Sasaki N; Satomi-Kobayashi S; Hirata KI; Rikitake Y
[Ad] Endereço:Division of Cardiovascular Medicine, Department of Internal Medicine, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
[Ti] Título:Necl-4 enhances the PLCγ-c-Raf-MEK-ERK pathway without affecting internalization of VEGFR2.
[So] Source:Biochem Biophys Res Commun;490(2):169-175, 2017 Aug 19.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have reported that knockdown of Necl-4 decreases vascular endothelial growth factor (VEGF)-induced phosphorylation of extracellular signal-regulated kinase (ERK) without affecting phosphorylation of VEGF receptor 2 (VEGFR2) in sparsely cultured human umbilical vein endothelial cells (HUVECs). However, the underlying molecular mechanism is unknown. Compared with control HUVECs, VEGF-induced phosphorylation of phospholipase Cγ (PLCγ), c-Raf, mitogen-activated protein kinase/ERK kinase (MEK) and ERK were all inhibited in Necl-4-knockdown HUVECs. However, VEGF-induced internalization of VEGFR2 was not different between control and Necl-4-knockdown HUVECs. We have reported that protein-tyrosine phosphatase, non-receptor type 13 (PTPN13) and Rho-associated kinase (ROCK) are involved in the Necl-4-knockdown-induced inhibition of the VEGF-induced activation of Rac1. However, the effects of Necl-4-knockdown on VEGF-induced phosphorylation of VEGFR2 and ERK were not affected either by knockdown of PTPN13 or by ROCK inhibitors. These results suggest that Necl-4 enhances VEGF-induced activation of PLCγ-c-Raf-MEK-ERK pathway without affecting the phosphorylation and internalization of VEGFR2.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular/metabolismo
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Imunoglobulinas/metabolismo
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Fosfolipase C gama/metabolismo
Proteínas Proto-Oncogênicas c-raf/metabolismo
Receptor 2 de Fatores de Crescimento do Endotélio Vascular/metabolismo
[Mh] Termos MeSH secundário: Células Cultivadas
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CADM4 protein, human); 0 (Cell Adhesion Molecules); 0 (Immunoglobulins); EC 2.7.10.1 (KDR protein, human); EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-2); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 2.7.11.24 (Mitogen-Activated Protein Kinases); EC 3.1.4.3 (Phospholipase C gamma)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170612
[St] Status:MEDLINE


  10 / 3517 MEDLINE  
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[PMID]:28548040
[Au] Autor:Zhou F; Wang S; Wang J
[Ti] Título:PAQR3 Inhibits the Proliferation and Tumorigenesis in Esophageal Cancer Cells.
[So] Source:Oncol Res;25(5):663-671, 2017 May 24.
[Is] ISSN:1555-3906
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Progestin and adipoQ receptor family member III (PAQR3), a member of the PAQR family, is frequently downregulated in different types of human cancer. However, its expression and functions in esophageal cancer are still unknown. This study aimed to explore the expression of PAQR3 in esophageal cancer cell lines and to investigate the role of PAQR3 in the development of esophageal cancer. Our data showed that PAQR3 is expressed in low amounts in human esophageal cancer cell lines. Overexpression of PAQR3 significantly suppressed the proliferation, migration, and invasion of esophageal cancer cells. In addition, overexpression of PAQR3 downregulated the protein expression levels of RAF1, p-MEK1, and p-ERK1/2 in esophageal cancer cells. Furthermore, overexpression of PAQR3 attenuated the tumor growth in a tumor xenograft model. In conclusion, we demonstrated that overexpression of PAQR3 suppresses cell proliferation, migration, and invasion in esophageal cancer in vitro and in vivo. Therefore, PAQR3 may act as a therapeutic target for human esophageal cancer.
[Mh] Termos MeSH primário: Transformação Celular Neoplásica/genética
Neoplasias Esofágicas/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
Proteínas de Membrana/genética
Proteínas Proto-Oncogênicas c-raf/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Modelos Animais de Doenças
Neoplasias Esofágicas/metabolismo
Neoplasias Esofágicas/patologia
Feminino
Expressão Gênica
Xenoenxertos
Seres Humanos
Sistema de Sinalização das MAP Quinases
Camundongos
Carga Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Membrane Proteins); 0 (RKTG protein, human); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.3727/096504016X14761384026719



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