Base de dados : MEDLINE
Pesquisa : D08.811.277.352.100.680.750.937.300 [Categoria DeCS]
Referências encontradas : 141 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 15 ir para página                         

  1 / 141 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28743497
[Au] Autor:Han CW; Jeong MS; Jang SB
[Ad] Endereço:Department of Molecular Biology, College of Natural Sciences, Pusan National University, Jangjeon-dong, Geumjeong-gu, Busan 46241, South Korea.
[Ti] Título:Molecular interaction between K-Ras and H-REV107 in the Ras signaling pathway.
[So] Source:Biochem Biophys Res Commun;491(2):257-264, 2017 09 16.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ras proteins are small GTPases that serve as master moderators of a large number of signaling pathways involved in various cellular processes. Activating mutations in Ras are found in about one-third of cancers. H-REV107, a K-Ras binding protein, plays an important role in determining K-Ras function. H-REV107 is a member of the HREV107 family of class II tumor suppressor genes and a growth inhibitory Ras target gene that suppresses cellular growth, differentiation, and apoptosis. Expression of H-REV107 was strongly reduced in about 50% of human carcinoma cell lines. However, the specific molecular mechanism by which H-REV107 inhibits Ras is still unknown. In the present study, we suggest that H-REV107 forms a strong complex with activating oncogenic mutation Q61H K-Ras from various biochemical binding assays and modeled structures. In addition, the interaction sites between K-Ras and H-REV107 were predicted based on homology modeling. Here, we found that some structure-based mutants of the K-Ras disrupted the complex formation with H-REV107. Finally, a novel molecular mechanism describing K-Ras and H-REV107 binding is suggested and insights into new K-Ras effector target drugs are provided.
[Mh] Termos MeSH primário: Simulação de Acoplamento Molecular
Fosfolipases A2 Independentes de Cálcio/química
Proteínas Proto-Oncogênicas p21(ras)/química
Transdução de Sinais/genética
Proteínas Supressoras de Tumor/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Seres Humanos
Cinética
Mutação
Fosfolipases A2 Independentes de Cálcio/genética
Fosfolipases A2 Independentes de Cálcio/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Estrutura Terciária de Proteína
Proteínas Proto-Oncogênicas p21(ras)/genética
Proteínas Proto-Oncogênicas p21(ras)/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Alinhamento de Sequência
Homologia Estrutural de Proteína
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (KRAS protein, human); 0 (Recombinant Fusion Proteins); 0 (Tumor Suppressor Proteins); EC 3.1.1.4 (PLA2G16 protein, human); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent); EC 3.6.5.2 (Proto-Oncogene Proteins p21(ras))
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171129
[Lr] Data última revisão:
171129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE


  2 / 141 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28618256
[Au] Autor:Kispert S; Schwartz T; McHowat J
[Ad] Endereço:Department of Pathology, Saint Louis University School of Medicine, St. Louis, Missouri.
[Ti] Título:Cigarette Smoke Regulates Calcium-Independent Phospholipase A Metabolic Pathways in Breast Cancer.
[So] Source:Am J Pathol;187(8):1855-1866, 2017 Aug.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phospholipase A (PLA )-dependent pathways are important in the regulation of cell proliferation, differentiation, motility, and immune responses, and can be dysregulated during tumor development and progression. We show herein, for the first time, that cigarette smoking leads to an increase in platelet-activating factor (PAF) content and PAF receptor expression in human breast cancer cells and tissue. PAF production could be abrogated in triple-negative breast cancer cells by inhibition of calcium-independent PLA (iPLA ). We also demonstrate that cigarette smoke induces the expression of cyclooxygenase-2 and microsomal prostaglandin E synthase-1 and reduces 15-hydroxyprostaglandin dehydrogenase, resulting in prostaglandin E release in human breast cancer. Increased cyclooxygenase-2 expression and prostaglandin E release could be abrogated in metastatic breast cancer cells by inhibition of iPLA . These studies indicate that iPLA -dependent metabolic pathways play an important role in tumor initiation or progression in smokers, representing novel therapeutic targets for breast cancer patients who smoke.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Fosfolipases A2 Independentes de Cálcio/metabolismo
Fator de Ativação de Plaquetas/metabolismo
Glicoproteínas da Membrana de Plaquetas/metabolismo
Receptores Acoplados a Proteínas-G/metabolismo
Fumaça
Fumar/metabolismo
Neoplasias de Mama Triplo Negativas/metabolismo
[Mh] Termos MeSH secundário: Mama/metabolismo
Mama/patologia
Neoplasias da Mama/patologia
Linhagem Celular Tumoral
Ciclo-Oxigenase 2/metabolismo
Feminino
Seres Humanos
Prostaglandina-E Sintases/metabolismo
Fumar/patologia
Neoplasias de Mama Triplo Negativas/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Platelet Activating Factor); 0 (Platelet Membrane Glycoproteins); 0 (Receptors, G-Protein-Coupled); 0 (Smoke); 0 (platelet activating factor receptor); EC 1.14.99.1 (Cyclooxygenase 2); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent); EC 5.3.99.3 (PTGES protein, human); EC 5.3.99.3 (Prostaglandin-E Synthases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE


  3 / 141 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28520213
[Au] Autor:BasuRay S; Smagris E; Cohen JC; Hobbs HH
[Ad] Endereço:Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX.
[Ti] Título:The PNPLA3 variant associated with fatty liver disease (I148M) accumulates on lipid droplets by evading ubiquitylation.
[So] Source:Hepatology;66(4):1111-1124, 2017 Oct.
[Is] ISSN:1527-3350
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A sequence variation (I148M) in patatin-like phospholipase domain-containing protein 3 (PNPLA3) is strongly associated with fatty liver disease, but the underlying mechanism remains obscure. In this study, we used knock-in (KI) mice (Pnpla3 ) to examine the mechanism responsible for accumulation of triglyceride (TG) and PNPLA3 in hepatic lipid droplets (LDs). No differences were found between Pnpla3 and Pnpla3 mice in hepatic TG synthesis, utilization, or secretion. These results are consistent with TG accumulation in the Pnpla3 mice being caused by impaired TG mobilization from LDs. Sucrose feeding, which is required to elicit fatty liver in KI mice, led to a much larger and more persistent increase in PNPLA3 protein in the KI mice than in wild-type (WT) mice. Inhibition of the proteasome (bortezomib), but not macroautophagy (3-methyladenine), markedly increased PNPLA3 levels in WT mice, coincident with the appearance of ubiquitylated forms of the protein. Bortezomib did not increase PNPLA3 levels in Pnpla3 mice, and only trace amounts of ubiquitylated PNPLA3 were seen in these animals. CONCLUSION: These results are consistent with the notion that the 148M variant disrupts ubiquitylation and proteasomal degradation of PNPLA3, resulting in accumulation of PNPLA3-148M and impaired mobilization of TG from LDs. (Hepatology 2017;66:1111-1124).
[Mh] Termos MeSH primário: Fígado Gorduroso/genética
Gotículas Lipídicas/metabolismo
Fosfolipases A2 Independentes de Cálcio/genética
[Mh] Termos MeSH secundário: Adenina/análogos & derivados
Animais
Restrição Calórica
Sacarose na Dieta
Fígado Gorduroso/metabolismo
Predisposição Genética para Doença
Metabolismo dos Lipídeos
Camundongos Transgênicos
Oxirredução
Fosfolipases A2 Independentes de Cálcio/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
Triglicerídeos/metabolismo
Triglicerídeos/secreção
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dietary Sucrose); 0 (Triglycerides); 5142-23-4 (3-methyladenine); EC 3.1.1.3 (PNPLA3 protein, mouse); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent); EC 3.4.25.1 (Proteasome Endopeptidase Complex); JAC85A2161 (Adenine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1002/hep.29273


  4 / 141 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28079896
[Au] Autor:Chen TL; Yang HC; Hung CY; Ou MH; Pan YY; Cheng ML; Stern A; Lo SJ; Chiu DT
[Ad] Endereço:Graduate Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Taoyuan, Taiwan.
[Ti] Título:Impaired embryonic development in glucose-6-phosphate dehydrogenase-deficient Caenorhabditis elegans due to abnormal redox homeostasis induced activation of calcium-independent phospholipase and alteration of glycerophospholipid metabolism.
[So] Source:Cell Death Dis;8(1):e2545, 2017 Jan 12.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glucose-6-phosphate dehydrogenase (G6PD) deficiency is a commonly pervasive inherited disease in many parts of the world. The complete lack of G6PD activity in a mouse model causes embryonic lethality. The G6PD-deficient Caenorhabditis elegans model also shows embryonic death as indicated by a severe hatching defect. Although increased oxidative stress has been implicated in both cases as the underlying cause, the exact mechanism has not been clearly delineated. In this study with C. elegans, membrane-associated defects, including enhanced permeability, defective polarity and cytokinesis, were found in G6PD-deficient embryos. The membrane-associated abnormalities were accompanied by impaired eggshell structure as evidenced by a transmission electron microscopic study. Such loss of membrane structural integrity was associated with abnormal lipid composition as lipidomic analysis revealed that lysoglycerophospholipids were significantly increased in G6PD-deficient embryos. Abnormal glycerophospholipid metabolism leading to defective embryonic development could be attributed to the increased activity of calcium-independent phospholipase A (iPLA) in G6PD-deficient embryos. This notion is further supported by the fact that the suppression of multiple iPLAs by genetic manipulation partially rescued the embryonic defects in G6PD-deficient embryos. In addition, G6PD deficiency induced disruption of redox balance as manifested by diminished NADPH and elevated lipid peroxidation in embryos. Taken together, disrupted lipid metabolism due to abnormal redox homeostasis is a major factor contributing to abnormal embryonic development in G6PD-deficient C. elegans.
[Mh] Termos MeSH primário: Caenorhabditis elegans/genética
Desenvolvimento Embrionário/genética
Glucosefosfato Desidrogenase/genética
Fosfolipases A2 Independentes de Cálcio/genética
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/crescimento & desenvolvimento
Estruturas da Membrana Celular/ultraestrutura
Casca de Ovo/ultraestrutura
Deficiência de Glucosefosfato Desidrogenase/genética
Glicerofosfolipídeos/metabolismo
Homeostase
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycerophospholipids); EC 1.1.1.49 (Glucosephosphate Dehydrogenase); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2016.463


  5 / 141 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28077878
[Au] Autor:Staring J; von Castelmur E; Blomen VA; van den Hengel LG; Brockmann M; Baggen J; Thibaut HJ; Nieuwenhuis J; Janssen H; van Kuppeveld FJ; Perrakis A; Carette JE; Brummelkamp TR
[Ad] Endereço:Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
[Ti] Título:PLA2G16 represents a switch between entry and clearance of Picornaviridae.
[So] Source:Nature;541(7637):412-416, 2017 01 19.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Picornaviruses are a leading cause of human and veterinary infections that result in various diseases, including polio and the common cold. As archetypical non-enveloped viruses, their biology has been extensively studied. Although a range of different cell-surface receptors are bound by different picornaviruses, it is unclear whether common host factors are needed for them to reach the cytoplasm. Using genome-wide haploid genetic screens, here we identify the lipid-modifying enzyme PLA2G16 (refs 8, 9, 10, 11) as a picornavirus host factor that is required for a previously unknown event in the viral life cycle. We find that PLA2G16 functions early during infection, enabling virion-mediated genome delivery into the cytoplasm, but not in any virion-assigned step, such as cell binding, endosomal trafficking or pore formation. To resolve this paradox, we screened for suppressors of the ΔPLA2G16 phenotype and identified a mechanism previously implicated in the clearance of intracellular bacteria. The sensor of this mechanism, galectin-8 (encoded by LGALS8), detects permeated endosomes and marks them for autophagic degradation, whereas PLA2G16 facilitates viral genome translocation and prevents clearance. This study uncovers two competing processes triggered by virus entry: activation of a pore-activated clearance pathway and recruitment of a phospholipase to enable genome release.
[Mh] Termos MeSH primário: Citoplasma/virologia
Genoma Viral
Fatores Celulares Derivados do Hospedeiro/metabolismo
Fosfolipases A2 Independentes de Cálcio/metabolismo
Picornaviridae/genética
Picornaviridae/fisiologia
Proteínas Supressoras de Tumor/metabolismo
Internalização do Vírus
[Mh] Termos MeSH secundário: Animais
Autofagia
Transporte Biológico
Linhagem Celular
Citoplasma/genética
Endossomos/metabolismo
Feminino
Galectinas/genética
Galectinas/metabolismo
Fatores Celulares Derivados do Hospedeiro/deficiência
Fatores Celulares Derivados do Hospedeiro/genética
Seres Humanos
Masculino
Camundongos
Mutação
Fenótipo
Fosfolipases A2 Independentes de Cálcio/deficiência
Fosfolipases A2 Independentes de Cálcio/genética
Supressão Genética
Proteínas Supressoras de Tumor/deficiência
Proteínas Supressoras de Tumor/genética
Vírion/genética
Vírion/metabolismo
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Galectins); 0 (Host-Derived Cellular Factors); 0 (LGALS8 protein, human); 0 (Tumor Suppressor Proteins); EC 3.1.1.4 (PLA2G16 protein, human); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170414
[Lr] Data última revisão:
170414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE
[do] DOI:10.1038/nature21032


  6 / 141 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28034646
[Au] Autor:Smyrniotou A; Kokotou MG; Mouchlis VD; Barbayianni E; Kokotos G; Dennis EA; Constantinou-Kokotou V
[Ad] Endereço:Chemical Laboratories, Agricultural University of Athens, Iera Odos 75, Athens 11855, Greece.
[Ti] Título:2-Oxoamides based on dipeptides as selective calcium-independent phospholipase A inhibitors.
[So] Source:Bioorg Med Chem;25(3):926-940, 2017 Feb 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Calcium-independent phospholipase A (GVIA iPLA ) has recently attracted interest as a medicinal target. The number of known GVIA iPLA inhibitors is limited to a handful of synthetic compounds (bromoenol lactone and polyfluoroketones). To expand the chemical diversity, a variety of 2-oxoamides based on dipeptides and ether dipeptides were synthesized and studied for their in vitro inhibitory activity on human GVIA iPLA and their selectivity over the other major intracellular GIVA cPLA and the secreted GV sPLA . Structure-activity relationship studies revealed the first 2-oxoamide derivative (GK317), which presents potent inhibition of GVIA iPLA (X (50) value of 0.007) and at the same time significant selectivity over GIVA cPLA and GV sPLA .
[Mh] Termos MeSH primário: Dipeptídeos/farmacologia
Inibidores de Fosfolipase A2/farmacologia
Fosfolipases A2 Independentes de Cálcio/antagonistas & inibidores
Piridinas/farmacologia
[Mh] Termos MeSH secundário: Dipeptídeos/síntese química
Dipeptídeos/química
Relação Dose-Resposta a Droga
Seres Humanos
Estrutura Molecular
Inibidores de Fosfolipase A2/síntese química
Inibidores de Fosfolipase A2/química
Fosfolipases A2 Independentes de Cálcio/metabolismo
Piridinas/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dipeptides); 0 (Phospholipase A2 Inhibitors); 0 (Pyridines); 713-05-3 (oxoamide); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161231
[St] Status:MEDLINE


  7 / 141 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27655917
[Au] Autor:Lee SH; Sud N; Lee N; Subramaniyam S; Chung CY
[Ad] Endereço:From the Department of Pharmacology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-6600.
[Ti] Título:Regulation of Integrin α6 Recycling by Calcium-independent Phospholipase A2 (iPLA2) to Promote Microglia Chemotaxis on Laminin.
[So] Source:J Biol Chem;291(45):23645-23653, 2016 Nov 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microglia are the immune effector cells that are activated in response to pathological changes in the central nervous system. Microglial activation is accompanied by the alteration of integrin expression on the microglia surface. However, changes of integrin expression upon chemoattractant (ADP) stimulation still remain unknown. In this study, we investigated whether ADP induces the alteration of integrin species on the cell surface, leading to changes in chemotactic ability on different extracellular matrix proteins. Flow cytometry scans and on-cell Western assays showed that ADP stimulation induced a significant increase of α6 integrin-GFP, but not α5, on the surface of microglia cells. Microglia also showed a greater motility increase on laminin than fibronectin after ADP stimulation. Time lapse microscopy and integrin endocytosis assay revealed the essential role of calcium-independent phospholipase A activity for the recycling of α6 integrin-GFP from the endosomal recycling complex to the plasma membrane. Lack of calcium-independent phospholipase A activity caused a reduced rate of focal adhesion formation on laminin at the leading edge. Our results suggest that the alteration of integrin-mediated adhesion may regulate the extent of microglial infiltration into the site of damage by controlling their chemotactic ability.
[Mh] Termos MeSH primário: Difosfato de Adenosina/metabolismo
Quimiotaxia
Integrina alfa6/metabolismo
Laminina/metabolismo
Microglia/citologia
Fosfolipases A2 Independentes de Cálcio/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Movimento Celular
Seres Humanos
Integrina alfa6/genética
Camundongos
Microglia/metabolismo
Fosfolipases A2 Independentes de Cálcio/genética
Transporte Proteico
Interferência de RNA
RNA Interferente Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin alpha6); 0 (Laminin); 0 (RNA, Small Interfering); 61D2G4IYVH (Adenosine Diphosphate); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171104
[Lr] Data última revisão:
171104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160923
[St] Status:MEDLINE


  8 / 141 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27412928
[Au] Autor:Tan L; Zhao Y; Jiang B; Yang B; Zhang H
[Ad] Endereço:Department of Pathology, Molecular Medicine and Cancer Research Center, College of Basic Medical Sciences, Chongqing Medical University, Chongqing 400016, China.
[Ti] Título:[Knockdown of PRDX6 in microglia reduces neuron viability after OGD/R injury].
[So] Source:Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi;32(8):1014-20, 2016 Aug.
[Is] ISSN:1007-8738
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Objective To observe the effects of peroxiredoxin 6 (PRDX6) knockdown in the microglia on neuron viability after oxygen-glucose deprivation and reoxygenation (OGD/R). Methods Microglia was treated with lentivirus PRDX6-siRNA and Ca(2+)-independent phospholipase A2 (iPLA2) inhibitor, 1-hexadecyl-3-(trifluoroethgl)-sn-glycerol-2 phosphomethanol (MJ33). Twenty-four hours later, it was co-cultured with primary neuron to establish the microglia-neuron co-culture OGD/R model. According to the different treatment of microglia, the cells were divided into normal group, OGD/R group, negative control-siRNA treated OGD/R group, PRDX6-siRNA treated OGD/R group and PRDX6-siRNA combined with MJ33 treated OGD/R group. Western blot analysis and real-time quantitative PCR were respectively performed to detect PRDX6 protein and mRNA levels after knockdown of PRDX6 in microglia. The iPLA2 activity was measured by ELISA. MTS and lactate dehydrogenase (LDH) assay were used to measure neuron viability and cell damage. The oxidative stress level of neuron was determined by measuring superoxide dismutase (SOD) and malonaldehyde (MDA) content. Results In PRDX6-siRNA group, neuron viability was inhibited and oxidative stress damage was aggravated compared with OGD/R group. In PRDX6-siRNA combined with MJ33 group, cell viability was promoted and oxidative stress damage was alleviated compared with PRDX6-siRNA group. Conclusion PRDX6 in microglia protects neuron against OGD/R-induced injury, and iPLA2 activity has an effect on PRDX6.
[Mh] Termos MeSH primário: Microglia/metabolismo
Neurônios/metabolismo
Peroxirredoxina VI/genética
Interferência de RNA
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Western Blotting
Hipóxia Celular
Sobrevivência Celular/efeitos dos fármacos
Sobrevivência Celular/genética
Células Cultivadas
Técnicas de Cocultura
Glucose/metabolismo
Glucose/farmacologia
Glicerofosfatos/farmacologia
Malondialdeído/metabolismo
Microglia/citologia
Microscopia de Fluorescência
Neurônios/citologia
Oxigênio/metabolismo
Oxigênio/farmacologia
Peroxirredoxina VI/metabolismo
Fosfolipases A2 Independentes de Cálcio/antagonistas & inibidores
Fosfolipases A2 Independentes de Cálcio/metabolismo
Ratos Sprague-Dawley
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycerophosphates); 137464-44-9 (1-hexadecyl-3-trifluoroethylglycero-sn-2-phosphomethanol); 4Y8F71G49Q (Malondialdehyde); EC 1.11.1.15 (Peroxiredoxin VI); EC 1.11.1.15 (Prdx6 protein, rat); EC 1.15.1.1 (Superoxide Dismutase); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent); IY9XDZ35W2 (Glucose); S88TT14065 (Oxygen)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170113
[Lr] Data última revisão:
170113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160715
[St] Status:MEDLINE


  9 / 141 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27226532
[Au] Autor:Elimam H; Papillon J; Kaufman DR; Guillemette J; Aoudjit L; Gross RW; Takano T; Cybulsky AV
[Ad] Endereço:From the Department of Medicine, McGill University Health Centre Research Institute, McGill University, Montreal, Quebec H4A 3J1, Canada and.
[Ti] Título:Genetic Ablation of Calcium-independent Phospholipase A2γ Induces Glomerular Injury in Mice.
[So] Source:J Biol Chem;291(28):14468-82, 2016 Jul 08.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glomerular visceral epithelial cells (podocytes) play a critical role in the maintenance of glomerular permselectivity. Podocyte injury, manifesting as proteinuria, is the cause of many glomerular diseases. We reported previously that calcium-independent phospholipase A2γ (iPLA2γ) is cytoprotective against complement-mediated glomerular epithelial cell injury. Studies in iPLA2γ KO mice have demonstrated an important role for iPLA2γ in mitochondrial lipid turnover, membrane structure, and metabolism. The aim of the present study was to employ iPLA2γ KO mice to better understand the role of iPLA2γ in normal glomerular and podocyte function as well as in glomerular injury. We show that deletion of iPLA2γ did not cause detectable albuminuria; however, it resulted in mitochondrial structural abnormalities and enhanced autophagy in podocytes as well as loss of podocytes in aging KO mice. Moreover, after induction of anti-glomerular basement membrane nephritis in young mice, iPLA2γ KO mice exhibited significantly increased levels of albuminuria, podocyte injury, and loss of podocytes compared with wild type. Thus, iPLA2γ has a protective functional role in the normal glomerulus and in glomerulonephritis. Understanding the role of iPLA2γ in glomerular pathophysiology provides opportunities for the development of novel therapeutic approaches to glomerular injury and proteinuria.
[Mh] Termos MeSH primário: Glomerulonefrite/genética
Fosfolipases A2 do Grupo VI/genética
Glomérulos Renais/patologia
Podócitos/patologia
[Mh] Termos MeSH secundário: Envelhecimento
Animais
Autofagia
Células Cultivadas
Estresse do Retículo Endoplasmático
Glomerulonefrite/patologia
Glomérulos Renais/metabolismo
Proteínas de Membrana/análise
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Mitocôndrias/genética
Mitocôndrias/patologia
Fosfolipases A2 Independentes de Cálcio/genética
Podócitos/metabolismo
Proteinúria/genética
Proteinúria/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (nephrin); EC 3.1.1.4 (Group VI Phospholipases A2); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent); EC 3.1.1.4 (Pla2g6 protein, mouse)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160527
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.696781


  10 / 141 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26944165
[Au] Autor:Mignarri A; Rubegni A; Tessa A; Stefanucci S; Malandrini A; Cardaioli E; Meschini MC; Stromillo ML; Doccini S; Federico A; Santorelli FM; Dotti MT
[Ad] Endereço:Unit of Neurology and Neurometabolic Disorders, Department of Medicine, Surgery and Neurosciences, University of Siena, Italy.
[Ti] Título:Mitochondrial dysfunction in hereditary spastic paraparesis with mutations in DDHD1/SPG28.
[So] Source:J Neurol Sci;362:287-91, 2016 Mar 15.
[Is] ISSN:1878-5883
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mutations in DDHD1 cause the SPG28 subtype of hereditary spastic paraplegia (HSP). Recent studies suggested that mitochondrial dysfunction occurs in SPG28. Here we describe two siblings with SPG28, and report evidence of mitochondrial impairment in skeletal muscle and skin fibroblasts. Patient 1 (Pt1) was a 35-year-old man with spastic paraparesis and urinary incontinence, while his 25-year-old brother (Pt2) had gait spasticity and motor axonal neuropathy. In these patients we identified the novel homozygous c.1429C>T/p.R477* mutation in DDHD1, using a next-generation sequencing (NGS) approach. Histochemical analyses in muscle showed mitochondrial alterations, and multiple mitochondrial DNA (mtDNA) deletions were evident. In Pt1, respiratory chain enzyme activities were altered in skeletal muscle, mitochondrial ATP levels reduced, and analysis of skin fibroblasts revealed mitochondrial fragmentation. It seems possible that the novel nonsense mutation identified abolishes DDHD1 protein function thus altering oxidative metabolism. Qualitative alterations of mtDNA could have a pathogenetic significance. We suggest to perform DDHD1 analysis in patients with multiple mtDNA deletions.
[Mh] Termos MeSH primário: Doenças Mitocondriais/etiologia
Fosfolipases A2 Independentes de Cálcio/genética
Paraplegia Espástica Hereditária/complicações
Paraplegia Espástica Hereditária/genética
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Adulto
Análise Mutacional de DNA
Seres Humanos
Masculino
Músculo Esquelético/metabolismo
Músculo Esquelético/patologia
Fosfolipases A2 Independentes de Cálcio/metabolismo
Irmãos
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
8L70Q75FXE (Adenosine Triphosphate); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170130
[Lr] Data última revisão:
170130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160306
[St] Status:MEDLINE



página 1 de 15 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde