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Pesquisa : D08.811.277.352.100.680.750.937.625 [Categoria DeCS]
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[PMID]:28341536
[Au] Autor:Yuan J; Zhu C; Hong Y; Sun Z; Fang X; Wu B; Li S
[Ad] Endereço:Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, PR China.
[Ti] Título:The role of cPLA2 in Methylglyoxal-induced cell apoptosis of HUVECs.
[So] Source:Toxicol Appl Pharmacol;323:44-52, 2017 May 15.
[Is] ISSN:1096-0333
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Methylglyoxal (MGO), a highly reactive dicarbonyl compound, is mainly formed as a byproduct of glycolysis. Elevated MGO level is known to induce apoptosis of vascular endothelial cells, which is implicated with progression of atherosclerosis and diabetic complications. However, the underlying mechanisms have not been exhaustively investigated yet. Here, we further characterized the mechanisms how MGO induced apoptosis in human umbilical vein endothelial cells (HUVECs). Our data revealed that cytosolic phospholipase A2 (cPLA2) played an important role in MGO-induced cell apoptosis. It was found that MGO could increase both the activity and expression of cPLA2. Inhibition of cPLA2 by Pyrrophenone (PYR) or siRNA significantly attenuated the MGO-induced apoptosis. Additionally, MGO time-dependently decreased the phosphorylation of nuclear factor κB (NF-κB). Pretreatment of the cells with NF-κB inhibitor, BAY11-7082, further increased MGO-induced apoptosis of HUVECs, indicating that NF-κB played a survival role in this MGO-induced apoptosis. Furthermore, in the presence of si-cPLA2 or PYR, MGO no longer decreased NF-κB phosphorylation. Beyond that, the antioxidant N-acetyl cysteine (NAC) could reverse the changes of both cPLA2 and NF-κB caused by MGO. p38, the upstream of cPLA2, was also significantly phosphorylated by MGO. However, p38 inhibitor failed to reverse the apoptosis induced by MGO. This study gives an important insight into the downstream signaling mechanisms of MGO, cPLA2-NF-κB, in endothelial apoptosis.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Fosfolipases A2 Citosólicas/metabolismo
Aldeído Pirúvico/toxicidade
[Mh] Termos MeSH secundário: Antioxidantes/farmacologia
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
Relação Dose-Resposta a Droga
Células Endoteliais da Veia Umbilical Humana/enzimologia
Células Endoteliais da Veia Umbilical Humana/patologia
Seres Humanos
NF-kappa B/antagonistas & inibidores
NF-kappa B/metabolismo
Estresse Oxidativo/efeitos dos fármacos
Inibidores de Fosfodiesterase/farmacologia
Fosfolipases A2 Citosólicas/antagonistas & inibidores
Fosfolipases A2 Citosólicas/genética
Fosforilação
Inibidores de Proteínas Quinases/farmacologia
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Interferência de RNA
Transdução de Sinais/efeitos dos fármacos
Fatores de Tempo
Transfecção
Proteínas Quinases p38 Ativadas por Mitógeno/antagonistas & inibidores
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (BCL2 protein, human); 0 (NF-kappa B); 0 (Phosphodiesterase Inhibitors); 0 (Protein Kinase Inhibitors); 0 (Proto-Oncogene Proteins c-bcl-2); 722KLD7415 (Pyruvaldehyde); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.1.1.4 (Phospholipases A2, Cytosolic)
[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:170326
[St] Status:MEDLINE


  2 / 213 MEDLINE  
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[PMID]:28004066
[Au] Autor:Huang Z; Ge YF; Jing J; Wu L; Zhou ZY; Zhu QF; Sun TZ
[Ad] Endereço:The Province Key Laboratory of the Biodiversity Study and Ecology Conservation in Southwest Anhui, Life Science College of Anqing Normal University, Anqing 246011, China. huangzhu@xmu.edu.cn.
[Ti] Título:[Effect of secretin on the expression of cPLA and mPGEs-1 in mouse endometrial stromal cell during early pregnancy].
[So] Source:Sheng Li Xue Bao;68(6):725-732, 2016 Dec 25.
[Is] ISSN:0371-0874
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Secretin, a gastrointestinal peptide, has been found to be expressed in mouse endometrial stromal cells (mESCs) during early pregnancy. In order to further investigate the function of secretin during embryo implantation, the expression levels of secretin, secretin receptor, cytosolic phospholipase A (cPLA ) and membrane prostaglandin E synthase 1 (mPGEs-1) were detected in the mice uterus from day 4 to 8 of pregnancy by real-time PCR, ELISA and in situ hybridization. mESCs isolated and cultured from day 4 of pregnancy were transfected with secretin expression vectors or treated with H89, a PKA inhibitor. Then the expression levels of cPLA , mPGEs-1 and cAMP responsive element-binding protein (CREB) were detected by real-time PCR and Western blot. The concentration of prostaglandin E2 (PGE ) in the supernatant was determined by ELISA. The result showed that secretin, cPLA and mPGEs-1 mRNA expression increased gradually in implantation sites from day 5 to day 7 of pregnancy with the same tendency. The secretin levels in serum were significantly higher on days 6, 7 and 8 of pregnancy than that on day 5 of pregnancy. The concentration of secretin was significantly higher in implantation sites on days 6, 7 than that in non-implantation site on day 5. Transfection of secretin expression vector promoted cPLA , p-cPLA and mPGEs-1 expressions in mESCs, but not PGE level in the supernatant. H89 could effectively inhibit the expression of CREB, p-CREB, p-cPLA and cPLA induced by secretin. The results showed that the increased secretin expression in mESCs during embryo implantation may promote p-cPLA , cPLA and mPGEs-1 expression, and the promotion may be through PKA signaling pathway.
[Mh] Termos MeSH primário: Células Estromais
[Mh] Termos MeSH secundário: Animais
Western Blotting
Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico
Dinoprostona
Feminino
Camundongos
Fosfolipases A2 Citosólicas
Gravidez
Prostaglandina-E Sintases
Reação em Cadeia da Polimerase em Tempo Real
Secretina
Útero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclic AMP Response Element-Binding Protein); 1393-25-5 (Secretin); EC 3.1.1.4 (Phospholipases A2, Cytosolic); EC 5.3.99.3 (Prostaglandin-E Synthases); K7Q1JQR04M (Dinoprostone)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE


  3 / 213 MEDLINE  
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[PMID]:27838690
[Au] Autor:Kim HK; Song CH; Bae YS; Im SY; Lee HK
[Ad] Endereço:Department of Immunology, Chonbuk National University Medical School, Jeonju, Republic of Korea.
[Ti] Título:Glutamine Prevents Late-Phase Anaphylaxis via MAPK Phosphatase 1-Dependent Cytosolic Phospholipase A2 Deactivation.
[So] Source:Int Arch Allergy Immunol;171(1):61-70, 2016.
[Is] ISSN:1423-0097
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Cytosolic phospholipase A2 (cPLA2) plays a key role in the development of late-phase anaphylaxis. L-Glutamine (Gln), a nonessential amino acid, has anti-inflammatory activity via inhibiting cPLA2. METHODS: We used a penicillin-induced murine model of anaphylaxis, and late-phase anaphylaxis was quantified by measuring the increase in the hematocrit (Ht) value. Various inhibitors, small interfering RNA, and knockout mice were used in inhibition experiments. Phosphorylation and protein expression of cPLA2, ERK, and MAPK phosphatase 1 (MKP-1) were detected by Western blotting. RESULTS: Leukotriene (LT) B4 was found to be another potent inducer of late-phase anaphylaxis besides the known mediator platelet-activating-factor (PAF). Gln efficiently prevented late-phase anaphylaxis when it was administered up to 3 h after challenge injection via inhibiting cPLA2. Inhibition studies indicated that p38 MAPK was the major upstream regulator of cPLA2. Gln dephosphorylated p38 and cPLA2 via up-regulating the negative regulator of p38 MAPK, i.e., MKP-1 protein. MKP-1 blockade abrogated all the effects of Gln. CONCLUSION: Of the cPLA2 metabolites, PAF and LTB4 play a key role in the development of late-phase anaphylaxis, and Gln prevents the reaction via MKP-1-dependent deactivation of cPLA2.
[Mh] Termos MeSH primário: Anafilaxia/imunologia
Anafilaxia/metabolismo
Fosfatase 1 de Especificidade Dupla/metabolismo
Glutamina/farmacologia
Fosfolipases A2 Citosólicas/metabolismo
[Mh] Termos MeSH secundário: Anafilaxia/genética
Anafilaxia/prevenção & controle
Animais
Modelos Animais de Doenças
Ativação Enzimática/efeitos dos fármacos
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Feminino
Leucotrieno B4/sangue
Camundongos
Camundongos Knockout
Fosfolipases A2 Citosólicas/genética
Fosforilação/efeitos dos fármacos
Fator de Ativação de Plaquetas/metabolismo
RNA Interferente Pequeno/genética
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Platelet Activating Factor); 0 (RNA, Small Interfering); 0RH81L854J (Glutamine); 1HGW4DR56D (Leukotriene B4); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.1.1.4 (Phospholipases A2, Cytosolic); EC 3.1.3.48 (Dual Specificity Phosphatase 1)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161114
[St] Status:MEDLINE


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[PMID]:27783042
[Au] Autor:Seo J; Maeng J; Kim HJ
[Ad] Endereço:College of Pharmacy, Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul 120-750, Korea. hui7505@hanmail.net.
[Ti] Título:Translationally Controlled Tumor Protein Stimulates Dopamine Release from PC12 Cells via Ca -Independent Phospholipase A2 Pathways.
[So] Source:Int J Mol Sci;17(10), 2016 Oct 24.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The translationally controlled tumor protein (TCTP), initially identified as a tumor- and growth-related protein, is also known as a histamine-releasing factor (HRF). TCTP is widely distributed in the neuronal systems, but its function is largely uncharacterized. Here, we report a novel function of TCTP in the neurotransmitter release from a neurosecretory, pheochromocytoma (PC12) cells. Treatment with recombinant TCTP (rTCTP) enhanced both basal and depolarization (50 mM KCl)-evoked [³H]dopamine release in concentration- and time-dependent manners. Interestingly, even though rTCTP induced the increase in intracellular calcium levels ([Ca ] ), the rTCTP-driven effect on dopamine release was mediated by a Ca -independent pathway, as evidenced by the fact that Ca -modulating agents such as Ca chelators and a voltage-gated L-type Ca -channel blocker did not produce any changes in rTCTP-evoked dopamine release. In a study to investigate the involvement of phospholipase A2 (PLA2) in rTCTP-induced dopamine release, the inhibitor for Ca -independent PLA2 (iPLA2) produced a significant inhibitory effect on rTCTP-induced dopamine release, whereas this release was not significantly inhibited by Ca -dependent cytosolic PLA2 (cPLA2) and secretory PLA2 (sPLA2) inhibitors. We found that rTCTP-induced dopamine release from neuronal PC12 cells was modulated by a Ca -independent mechanism that involved PLA2 in the process, suggesting the regulatory role of TCTP in the neuronal functions.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Dopamina/metabolismo
Fosfolipases A2 do Grupo II/metabolismo
Neurônios/metabolismo
Fosfolipases A2 Citosólicas/metabolismo
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Células PC12
Ratos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (tumor protein, translationally-controlled 1); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (Phospholipases A2, Cytosolic); SY7Q814VUP (Calcium); VTD58H1Z2X (Dopamine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170328
[Lr] Data última revisão:
170328
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161027
[St] Status:MEDLINE


  5 / 213 MEDLINE  
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[PMID]:27702653
[Au] Autor:Zhu C; Cao C; Wang X; Yuan J; Jin L; Li S
[Ad] Endereço:Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular Intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, PR China.
[Ti] Título:UCN enhances TGF-beta-mediated mitoinhibition of VSMCs via counteracting TGF-beta-induced cPLA2 expression and activation.
[So] Source:Int J Biochem Cell Biol;80:98-108, 2016 Nov.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Urocortins (UCNs) and transforming growth factor-beta (TGF-beta) have been demonstrated to participate in various cardiovascular diseases, many of which involve vascular smooth muscle cells (VSMCs) proliferation. Cytosolic phospholipase A2 (cPLA2)-mediated arachidonic acid (AA) release is an important cause of VSMCs proliferation. The work was to investigate the regulation of VSMCs proliferation by UCN/TGF-beta and whether cPLA2 was a link between their signaling pathways. VSMCs proliferation was measured by colorimetric assay and immunofluorescence microscopy. Using cell flow cytometry, the changes in the cell cycle phases were investigated. Lentiviral Vector Particle was performed to overexpress cPLA2 gene. Both UCN and TGF-beta inhibited VSMCs proliferation and an additive effect was observed when the cells were treated with UCN plus TGF-beta. TGF-beta increased the percentage of cells in G1-phase while UCN increased the cell percentage in G2-phase with a concomitant decrease in S-phase. Furthermore, cPLA2 expression was increased by TGF-beta but decreased by UCN and UCN attenuated TGF-beta-induced cPLA2 expression. In primary VSMCs, TGF-beta induced cPLA2 phosphorylation, and this effect was also attenuated by UCN. Similar to UCN, the cPLA2 inhibitor, pyrrophenone (PYR), also played a role in enhancing TGF-beta-mediated mitoinhibition. Inversely, overexpression of cPLA2 eliminated the effect of UCN on the mitoinhibition. The pretreatment with UCN counteracted TGF-beta-mediated cPLA2 expression and activation, thereby contributing to TGF-beta-mediated mitoinhibition of VSMCs.
[Mh] Termos MeSH primário: Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Mitose/efeitos dos fármacos
Músculo Liso Vascular/citologia
Fosfolipases A2 Citosólicas/genética
Fosfolipases A2 Citosólicas/metabolismo
Fator de Crescimento Transformador beta1/farmacologia
Urocortinas/farmacologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Proliferação Celular/efeitos dos fármacos
Sinergismo Farmacológico
Ativação Enzimática/efeitos dos fármacos
Seres Humanos
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Transforming Growth Factor beta1); 0 (Urocortins); EC 3.1.1.4 (Phospholipases A2, Cytosolic)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE


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[PMID]:27527133
[Au] Autor:Park KI; Kim DG; Yoo JM; Ma JY
[Ad] Endereço:Korean Medicine (KM)-Application Center, Korea Institute of Oriental Medicine (KIOM), 70 Cheomdan-ro, Dong-gu, Daegu 41062, Korea. kipark@kiom.re.kr.
[Ti] Título:The Herbal Medicine KIOM-MA128 Inhibits the Antigen/IgE-Mediated Allergic Response in Vitro and in Vivo.
[So] Source:Molecules;21(8), 2016 Aug 04.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:KIOM-MA128, a novel herbal medicine, has been reported to exert some beneficial effects on various biological events, such as atopic dermatitis, inflammation and cancer. The aim of this study is to investigate how KIOM-MA128 regulates the allergic response. We measured the activity of ß-hexosaminidase and the levels of allergic mediators in the conditioned media of antigen/IgE (Ag/IgE)-activated RBL-2H3 mast cells. We examined the levels of proteins associated with both the FcεRI and arachidonate cascades. Finally, we established the passive cutaneous anaphylaxis (PCA) model in mice to confirm the anti-allergic effects of KIOM-MA128 in vivo. KIOM-MA128 dose-dependently inhibited degranulation and the production of the allergic mediators described above, with no significant cytotoxicity. In the arachidonate cascade, KIOM-MA128 significantly reduced both cytosolic phospholipase A2 (cPLA2) phosphorylation and cyclooxygenase-2 (COX-2) expression. Moreover, in the FcεRI cascade, KIOM-MA128 not only inhibited activation of LYN, FYN and SYK, known as the rate-limiting proteins of the FcεRI cascade, but also suppressed the phosphorylation of ERK, p38 and JNK, which is related to cytokine expression. Finally, 50 to 100 mg/kg KIOM-MA128 significantly attenuated the Ag/IgE-induced PCA reaction in mice. These findings provide novel information and improve our understanding of the anti-allergic effects of KIOM-MA128 on allergic diseases.
[Mh] Termos MeSH primário: Anafilaxia/tratamento farmacológico
Antialérgicos/administração & dosagem
Mastócitos/citologia
Extratos Vegetais/administração & dosagem
Plantas Medicinais/química
[Mh] Termos MeSH secundário: Anafilaxia/imunologia
Anafilaxia/metabolismo
Animais
Antialérgicos/química
Antialérgicos/farmacologia
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Ciclo-Oxigenase 2/metabolismo
Modelos Animais de Doenças
Regulação da Expressão Gênica/efeitos dos fármacos
Imunoglobulina E/metabolismo
Técnicas In Vitro
Masculino
Mastócitos/efeitos dos fármacos
Mastócitos/imunologia
Camundongos
Fosfolipases A2 Citosólicas/metabolismo
Fosforilação/efeitos dos fármacos
Extratos Vegetais/química
Extratos Vegetais/farmacologia
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Allergic Agents); 0 (Plant Extracts); 37341-29-0 (Immunoglobulin E); EC 1.14.99.1 (Cyclooxygenase 2); EC 3.1.1.4 (Phospholipases A2, Cytosolic)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160817
[St] Status:MEDLINE


  7 / 213 MEDLINE  
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[PMID]:27481248
[Au] Autor:Bhattacharjee A; Majumder S; Das S; Ghosh S; Biswas S; Majumdar S
[Ad] Endereço:Division of Molecular Medicine, Bose Institute, Kolkata, India.
[Ti] Título:Leishmania donovani-Induced Prostaglandin E2 Generation Is Critically Dependent on Host Toll-Like Receptor 2-Cytosolic Phospholipase A2 Signaling.
[So] Source:Infect Immun;84(10):2963-73, 2016 Oct.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Visceral leishmaniasis (VL) is the second-largest parasitic killer disease after malaria. During VL, the protozoan Leishmania donovani induces prostaglandin E2 (PGE2) generation within host macrophages to aid parasite survival. PGE2 significantly influences leishmanial pathogenesis, as L. donovani proliferation is known to be attenuated in PGE2-inhibited macrophages. Here, we report for the first time that signaling via macrophage Toll-like receptor 2 (TLR2) plays an instrumental role in inducing PGE2 release from L. donovani-infected macrophages. This signaling cascade, mediated via the TLR2-phosphatidylinositol 3-kinase (PI3K)-phospholipase C (PLC) signaling pathway, was found to be indispensable for activation of two major enzymes required for PGE2 generation: cytosolic phospholipase A2 (cPLA2) and cyclooxygenase 2 (Cox2). Inhibition of cPLA2, but not secreted phospholipase A2 (sPLA2) or calcium-independent phospholipase A2 (iPLA2), arrested L. donovani infection. During infection, cPLA2 activity increased >7-fold in a calcium-dependent and extracellular signal-regulated kinase (ERK)-dependent manner, indicating that elevation of intracellular calcium and ERK-mediated phosphorylation was necessary for L. donovani-induced cPLA2 activation. For transcriptional upregulation of cyclooxygenase 2, activation of the calcium-calcineurin-nuclear factor of activated T cells (NFAT) signaling was required in addition to the TLR2-PI3K-PLC pathway. Detailed studies by site-directed mutagenesis of potential NFAT binding sites and chromatin immunoprecipitation (ChIP) analysis revealed that the binding of macrophage NFATc2, at the -73/-77 site on the cox2 promoter, induced L. donovani-driven cox2 transcriptional activation. Collectively, these findings highlight the contribution of TLR2 downstream signaling toward activation of cPLA2 and Cox2 and illustrate how the TLR2-PI3K-PLC pathway acts in a concerted manner with calcium-calcineurin-NFATc2 signaling to modulate PGE2 release from L. donovani-infected macrophages.
[Mh] Termos MeSH primário: Dinoprostona/fisiologia
Fosfolipases A2 Citosólicas/fisiologia
Receptor 2 Toll-Like/fisiologia
[Mh] Termos MeSH secundário: Análise de Variância
Animais
Western Blotting
Ciclo-Oxigenase 2/metabolismo
Dinoprostona/metabolismo
Modelos Animais de Doenças
Ensaio de Imunoadsorção Enzimática
Leishmania donovani
Leishmaniose Visceral
Macrófagos/metabolismo
Camundongos
Camundongos Endogâmicos BALB C
Fosfolipases A2 Citosólicas/metabolismo
Transdução de Sinais/fisiologia
Receptor 2 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Toll-Like Receptor 2); EC 1.14.99.1 (Cyclooxygenase 2); EC 3.1.1.4 (Phospholipases A2, Cytosolic); K7Q1JQR04M (Dinoprostone)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170525
[Lr] Data última revisão:
170525
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160803
[St] Status:MEDLINE
[do] DOI:10.1128/IAI.00528-16


  8 / 213 MEDLINE  
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[PMID]:27203112
[Au] Autor:Enyedi B; Jelcic M; Niethammer P
[Ad] Endereço:Cell Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
[Ti] Título:The Cell Nucleus Serves as a Mechanotransducer of Tissue Damage-Induced Inflammation.
[So] Source:Cell;165(5):1160-1170, 2016 May 19.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tissue damage activates cytosolic phospholipase A2 (cPLA2), releasing arachidonic acid (AA), which is oxidized to proinflammatory eicosanoids by 5-lipoxygenase (5-LOX) on the nuclear envelope. How tissue damage is sensed to activate cPLA2 is unknown. We investigated this by live imaging in wounded zebrafish larvae, where damage of the fin tissue causes osmotic cell swelling at the wound margin and the generation of a chemotactic eicosanoid signal. Osmotic swelling of cells and their nuclei activates cPla2 by translocating it from the nucleoplasm to the nuclear envelope. Elevated cytosolic Ca(2+) was necessary but not sufficient for cPla2 translocation, and nuclear swelling was required in parallel. cPla2 translocation upon nuclear swelling was reconstituted in isolated nuclei and appears to be a simple physical process mediated by tension in the nuclear envelope. Our data suggest that the nucleus plays a mechanosensory role in inflammation by transducing cell swelling and lysis into proinflammatory eicosanoid signaling.
[Mh] Termos MeSH primário: Ácido Araquidônico/metabolismo
Núcleo Celular/metabolismo
Inflamação/metabolismo
Mecanotransdução Celular
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Araquidonato 5-Lipoxigenase/metabolismo
Cálcio/metabolismo
Ativação Enzimática
Técnicas de Silenciamento de Genes
Técnicas de Inativação de Genes
Células HeLa
Seres Humanos
Leucócitos/metabolismo
Lâmina Nuclear/metabolismo
Fosfolipases A2 Citosólicas/metabolismo
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Actins); 27YG812J1I (Arachidonic Acid); EC 1.13.11.34 (Arachidonate 5-Lipoxygenase); EC 3.1.1.4 (Phospholipases A2, Cytosolic); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160521
[St] Status:MEDLINE


  9 / 213 MEDLINE  
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[PMID]:26980157
[Au] Autor:Jamwal SV; Mehrotra P; Singh A; Siddiqui Z; Basu A; Rao KV
[Ad] Endereço:Immunology Group International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi, 110067, India.
[Ti] Título:Mycobacterial escape from macrophage phagosomes to the cytoplasm represents an alternate adaptation mechanism.
[So] Source:Sci Rep;6:23089, 2016 Mar 16.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Survival of Mycobacterium tuberculosis (Mtb) within the host macrophage is mediated through pathogen-dependent inhibition of phagosome-lysosome fusion, which enables bacteria to persist within the immature phagosomal compartment. By employing ultrastructural examination of different field isolates supported by biochemical analysis, we found that some of the Mtb strains were in fact poorly adapted for subsistence within endocytic vesicles of infected macrophages. Instead, through a mechanism involving activation of host cytosolic phospholipase A2, these bacteria rapidly escaped from phagosomes, and established residence in the cytoplasm of the host cell. Interestingly, by facilitating an enhanced suppression of host cellular autophagy, this translocation served as an alternate virulence acquisition mechanism. Thus, our studies reveal plasticity in the adaptation strategies employed by Mtb, for survival in the host macrophage.
[Mh] Termos MeSH primário: Adaptação Fisiológica/imunologia
Citoplasma/imunologia
Macrófagos/imunologia
Mycobacterium tuberculosis/imunologia
Fagossomos/imunologia
[Mh] Termos MeSH secundário: Autofagia/imunologia
Linhagem Celular Tumoral
Células Cultivadas
Citoplasma/microbiologia
Citoplasma/ultraestrutura
Interações Hospedeiro-Patógeno/imunologia
Seres Humanos
Evasão da Resposta Imune/imunologia
Macrófagos/microbiologia
Macrófagos/ultraestrutura
Microscopia Confocal
Microscopia Eletrônica de Transmissão
Mycobacterium tuberculosis/patogenicidade
Mycobacterium tuberculosis/fisiologia
Fagocitose/imunologia
Fagossomos/microbiologia
Fagossomos/ultraestrutura
Fosfolipases A2 Citosólicas/imunologia
Fosfolipases A2 Citosólicas/metabolismo
Vesículas Transportadoras/imunologia
Vesículas Transportadoras/microbiologia
Vesículas Transportadoras/ultraestrutura
Virulência/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.1.1.4 (Phospholipases A2, Cytosolic)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160317
[St] Status:MEDLINE
[do] DOI:10.1038/srep23089


  10 / 213 MEDLINE  
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[PMID]:26951085
[Au] Autor:Kim E; Tunset HM; Cebulla J; Vettukattil R; Helgesen H; Feuerherm AJ; Engebråten O; Mælandsmo GM; Johansen B; Moestue SA
[Ad] Endereço:Department of Circulation and Medical Imaging, Faculty of Medicine, Norwegian University of Science and Technology, P.O. Box 8905, 7491, Trondheim, Norway. eugene.kim@ntnu.no.
[Ti] Título:Anti-vascular effects of the cytosolic phospholipase A2 inhibitor AVX235 in a patient-derived basal-like breast cancer model.
[So] Source:BMC Cancer;16:191, 2016 Mar 07.
[Is] ISSN:1471-2407
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Group IVA cytosolic phospholipase A2 (cPLA2α) plays an important role in tumorigenesis and angiogenesis. It is overexpressed in basal-like breast cancer (BLBC), which is aggressive and usually triple-negative, making it unresponsive to current targeted therapies. Here, we evaluated the anti-angiogenic effects of a specific cPLA2α inhibitor, AVX235, in a patient-derived triple-negative BLBC model. METHODS: Mice bearing orthotopic xenografts received i.p. injections of AVX235 or DMSO vehicle daily for 1 week and then every other day for up to 19 days. Six treated and six control mice were terminated after 2 days of treatment, and the tumors excised for high resolution magic angle spinning magnetic resonance spectroscopy (HR MAS MRS) and prostaglandin E2 (PGE2) enzyme immunoassay (EIA) analysis. A 1-week imaging study was performed on a separate cohort of mice. Longitudinal dynamic contrast enhanced (DCE)-MRI was performed before, after 4 days, and after 1 week of treatment. The mice were then perfused with a radiopaque vascular casting agent, and the tumors excised for micro-CT angiography. Subsequently, tumors were sectioned and stained with lectin and for Ki67 or α-smooth muscle actin to quantify endothelial cell proliferation and vessel maturity, respectively. Partial least squares discriminant analysis was performed on the multivariate HR MAS MRS data, and non-parametric univariate analyses using Mann-Whitney U tests (α = 0.05) were performed on all other data. RESULTS: Glycerophosphocholine and PGE2 levels, measured by HR MAS MRS and EIA, respectively, were lower in treated tumors after 2 days of treatment. These molecular changes are expected downstream effects of cPLA2α inhibition and were followed by significant tumor growth inhibition after 8 days of treatment. DCE-MRI revealed that AVX235 treatment caused a decrease in tumor perfusion. Concordantly, micro-CT angiography showed that vessel volume fraction, density, and caliber were reduced in treated tumors. Moreover, histology showed decreased endothelial cell proliferation and fewer immature vessels in treated tumors. CONCLUSIONS: These results demonstrate that cPLA2α inhibition with AVX235 resulted in decreased vascularization and perfusion and subsequent inhibition of tumor growth. Thus, cPLA2α inhibition may be a potential new therapeutic option for triple-negative basal-like breast cancer.
[Mh] Termos MeSH primário: Inibidores da Angiogênese/farmacologia
Antineoplásicos/farmacologia
Neoplasias da Mama/diagnóstico
Neoplasias da Mama/metabolismo
Neoplasia de Células Basais/patologia
Neovascularização Patológica
Inibidores de Fosfolipase A2/farmacologia
[Mh] Termos MeSH secundário: Animais
Neoplasias da Mama/tratamento farmacológico
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Dinoprostona/metabolismo
Modelos Animais de Doenças
Células Endoteliais/efeitos dos fármacos
Células Endoteliais/metabolismo
Feminino
Seres Humanos
Imagem por Ressonância Magnética
Camundongos
Neoplasia de Células Basais/tratamento farmacológico
Neoplasia de Células Basais/metabolismo
Neovascularização Patológica/tratamento farmacológico
Neovascularização Patológica/metabolismo
Fosfolipases A2 Citosólicas/metabolismo
Neoplasias de Mama Triplo Negativas/diagnóstico
Neoplasias de Mama Triplo Negativas/tratamento farmacológico
Neoplasias de Mama Triplo Negativas/metabolismo
Carga Tumoral/efeitos dos fármacos
Microtomografia por Raio-X
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Angiogenesis Inhibitors); 0 (Antineoplastic Agents); 0 (Phospholipase A2 Inhibitors); EC 3.1.1.4 (Phospholipases A2, Cytosolic); K7Q1JQR04M (Dinoprostone)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160309
[St] Status:MEDLINE
[do] DOI:10.1186/s12885-016-2225-1



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