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Pesquisa : D08.811.277.656.262.500.126.550.910 [Categoria DeCS]
Referências encontradas : 225 [refinar]
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[PMID]:29182622
[Au] Autor:Vondálová Blanárová O; Safaríková B; Herudková J; Krkoska M; Tománková S; Kahounová Z; Andera L; Bouchal J; Kharaishvili G; Král M; Sova P; Kozubík A; Hyrslová Vaculová A
[Ad] Endereço:Department of Cytokinetics, Institute of Biophysics, Czech Academy of Sciences, v.v.i., Brno, Czech Republic.
[Ti] Título:Cisplatin or LA-12 enhance killing effects of TRAIL in prostate cancer cells through Bid-dependent stimulation of mitochondrial apoptotic pathway but not caspase-10.
[So] Source:PLoS One;12(11):e0188584, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Searching for new strategies for effective elimination of human prostate cancer cells, we investigated the cooperative cytotoxic action of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and two platinum-based complexes, cisplatin or LA-12, and related molecular mechanisms. We demonstrated a notable ability of cisplatin or LA-12 to enhance the sensitivity of several human prostate cancer cell lines to TRAIL-induced cell death via an engagement of mitochondrial apoptotic pathway. This was accompanied by augmented Bid cleavage, Bak activation, loss of mitochondrial membrane potential, activation of caspase-8, -10, -9, and -3, and XIAP cleavage. RNAi-mediated silencing of Bid or Bak in Bax-deficient DU 145 cells suppressed the drug combination-induced cytotoxicity, further underscoring the involvement of mitochondrial signaling. The caspase-10 was dispensable for enhancement of cisplatin/LA-12 and TRAIL combination-induced cell death and stimulation of Bid cleavage. Importantly, we newly demonstrated LA-12-mediated enhancement of TRAIL-induced cell death in cancer cells derived from human patient prostate tumor specimens. Our results provide convincing evidence that employing TRAIL combined with cisplatin/LA-12 could contribute to more effective killing of prostate cancer cells compared to the individual action of the drugs, and offer new mechanistic insights into their cooperative anticancer action.
[Mh] Termos MeSH primário: Amantadina/análogos & derivados
Apoptose/efeitos dos fármacos
Proteína Agonista de Morte Celular de Domínio Interatuante com BH3/metabolismo
Caspase 10/metabolismo
Cisplatino/farmacologia
Mitocôndrias/efeitos dos fármacos
Compostos Organoplatínicos/farmacologia
Neoplasias da Próstata/patologia
Ligante Indutor de Apoptose Relacionado a TNF/metabolismo
[Mh] Termos MeSH secundário: Amantadina/farmacologia
Seres Humanos
Masculino
Mitocôndrias/metabolismo
Neoplasias da Próstata/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BH3 Interacting Domain Death Agonist Protein); 0 (BID protein, human); 0 (Organoplatinum Compounds); 0 (TNF-Related Apoptosis-Inducing Ligand); 0 (bis(acetato)(1-adamantylamine)amminedichloroplatinum(IV)); BF4C9Z1J53 (Amantadine); EC 3.4.22.- (Caspase 10); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188584


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[PMID]:27799292
[Au] Autor:Choi SG; Kim H; Jeong EI; Lee HJ; Park S; Lee SY; Lee HJ; Lee SW; Chung CH; Jung YK
[Ad] Endereço:Department of Biological Science, Seoul National University, Seoul, South Korea.
[Ti] Título:SUMO-Modified FADD Recruits Cytosolic Drp1 and Caspase-10 to Mitochondria for Regulated Necrosis.
[So] Source:Mol Cell Biol;37(2), 2017 Jan 15.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fas-associated protein with death domain (FADD) plays a key role in extrinsic apoptosis. Here, we show that FADD is SUMOylated as an essential step during intrinsic necrosis. FADD was modified at multiple lysine residues (K120/125/149) by small ubiquitin-related modifier 2 (SUMO2) during necrosis caused by calcium ionophore A23187 and by ischemic damage. SUMOylated FADD bound to dynamin-related protein 1 (Drp1) in cells both in vitro and in ischemic tissue damage cores, thus promoting Drp1 recruitment by mitochondrial fission factor (Mff) to accomplish mitochondrial fragmentation. Mitochondrial-fragmentation-associated necrosis was blocked by FADD or Drp1 deficiency and SUMO-defective FADD expression. Interestingly, caspase-10, but not caspase-8, formed a ternary protein complex with SUMO-FADD/Drp1 on the mitochondria upon exposure to A23187 and potentiated Drp1 oligomerization for necrosis. Moreover, the caspase-10 L285F and A414V mutants, found in autoimmune lymphoproliferative syndrome and non-Hodgkin lymphoma, respectively, regulated this necrosis. Our study reveals an essential role of SUMOylated FADD in Drp1- and caspase-10-dependent necrosis, providing insights into the mechanism of regulated necrosis by calcium overload and ischemic injury.
[Mh] Termos MeSH primário: Caspase 10/metabolismo
Citosol/metabolismo
Dinaminas/metabolismo
Proteína de Domínio de Morte Associada a Fas/metabolismo
Mitocôndrias/metabolismo
Proteína SUMO-1/metabolismo
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Animais
Hipóxia Celular
Células HEK293
Células HeLa
Seres Humanos
Lisina/metabolismo
Camundongos Endogâmicos C57BL
Complexos Multiproteicos/metabolismo
Proteínas Mutantes/metabolismo
Necrose
Ligação Proteica
Multimerização Proteica
Transporte Proteico
RNA Interferente Pequeno/metabolismo
Sumoilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (FADD protein, human); 0 (Fadd protein, mouse); 0 (Fas-Associated Death Domain Protein); 0 (Multiprotein Complexes); 0 (Mutant Proteins); 0 (RNA, Small Interfering); 0 (SUMO-1 Protein); 0 (SUMO2 protein, human); 0 (Small Ubiquitin-Related Modifier Proteins); EC 3.4.22.- (Caspase 10); EC 3.6.5.5 (Dynamins); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161102
[St] Status:MEDLINE


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[PMID]:27827850
[Au] Autor:Shi WY; Cao C; Liu L
[Ad] Endereço:Department of Microbiology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100005, China. feiwudeyezi@126.com.
[Ti] Título:Interferon α Induces the Apoptosis of Cervical Cancer HeLa Cells by Activating both the Intrinsic Mitochondrial Pathway and Endoplasmic Reticulum Stress-Induced Pathway.
[So] Source:Int J Mol Sci;17(11), 2016 Nov 02.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The interferon α (IFN-α) has been often used as a sensitizing agent for the treatment of various malignancies such as hepatocellular carcinoma, malignant melanoma, and renal cell cancer by promoting the apoptosis of thesetumor cell types. However, the effect of IFN-α on cervical cancer remains unknown. In this study, HeLa cells were used as a testing model for the treatment of IFN-α on cervical cancer. The results indicate that IFN-α markedly inhibits the proliferation and induces the apoptosis of HeLa cells. The activation of caspase 3, the up-regulation of both Bim and cleaved poly (ADP-ribose) polymerase (PARP) 1, the down-regulation of Bcl-xL, as well as the release of cytochrome c from mitochondria were significantly induced upon IFN-α treatment, indicating that the intrinsic apoptotic pathway could be activated by IFN-α treatment. In addition, caspase 4-which is involved in the endoplasmic reticulum (ER) stress-induced apoptosis-was activated in response to IFN-α treatment. Knocking down caspase 4 by small interfering RNA (siRNA) markedly reduced the IFN-α-mediated cell apoptosis. However, no significant changes in the expressions of caspases 8 and 10 were observed upon IFN-α treatment, indicating that the apoptosis caused by IFN-α might be independent of the extrinsic apoptotic pathway. These findings suggest that IFN-α may possess anti-cervical cancer capacity by activating cell apoptosis via the intrinsic mitochondrial pathway and caspase-4-related ER stress-induced pathway.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Estresse do Retículo Endoplasmático/efeitos dos fármacos
Retículo Endoplasmático/efeitos dos fármacos
Regulação Neoplásica da Expressão Gênica
Interferon-alfa/farmacologia
Mitocôndrias/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Apoptose/genética
Caspase 10/genética
Caspase 10/metabolismo
Caspase 3/genética
Caspase 3/metabolismo
Caspase 8/genética
Caspase 8/metabolismo
Caspases Iniciadoras/genética
Caspases Iniciadoras/metabolismo
Proliferação Celular/efeitos dos fármacos
Citocromos c/secreção
Retículo Endoplasmático/genética
Estresse do Retículo Endoplasmático/genética
Células HeLa
Seres Humanos
Mitocôndrias/genética
Poli(ADP-Ribose) Polimerase-1/genética
Poli(ADP-Ribose) Polimerase-1/metabolismo
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Transdução de Sinais
Proteína bcl-X/genética
Proteína bcl-X/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BCL2L1 protein, human); 0 (Interferon-alpha); 0 (RNA, Small Interfering); 0 (bcl-X Protein); 9007-43-6 (Cytochromes c); EC 2.4.2.30 (PARP1 protein, human); EC 2.4.2.30 (Poly (ADP-Ribose) Polymerase-1); EC 3.4.22.- (CASP3 protein, human); EC 3.4.22.- (CASP4 protein, human); EC 3.4.22.- (CASP8 protein, human); EC 3.4.22.- (Caspase 10); EC 3.4.22.- (Caspase 3); EC 3.4.22.- (Caspase 8); EC 3.4.22.- (Caspases, Initiator); EC 3.4.22.63 (CASP10 protein, human)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170403
[Lr] Data última revisão:
170403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161110
[St] Status:MEDLINE


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[PMID]:27309814
[Au] Autor:Backus KM; Correia BE; Lum KM; Forli S; Horning BD; González-Páez GE; Chatterjee S; Lanning BR; Teijaro JR; Olson AJ; Wolan DW; Cravatt BF
[Ad] Endereço:Department of Chemical Physiology, The Scripps Research Institute. La Jolla, California 92307, USA.
[Ti] Título:Proteome-wide covalent ligand discovery in native biological systems.
[So] Source:Nature;534(7608):570-4, 2016 06 23.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Small molecules are powerful tools for investigating protein function and can serve as leads for new therapeutics. Most human proteins, however, lack small-molecule ligands, and entire protein classes are considered 'undruggable'. Fragment-based ligand discovery can identify small-molecule probes for proteins that have proven difficult to target using high-throughput screening of complex compound libraries. Although reversibly binding ligands are commonly pursued, covalent fragments provide an alternative route to small-molecule probes, including those that can access regions of proteins that are difficult to target through binding affinity alone. Here we report a quantitative analysis of cysteine-reactive small-molecule fragments screened against thousands of proteins in human proteomes and cells. Covalent ligands were identified for >700 cysteines found in both druggable proteins and proteins deficient in chemical probes, including transcription factors, adaptor/scaffolding proteins, and uncharacterized proteins. Among the atypical ligand-protein interactions discovered were compounds that react preferentially with pro- (inactive) caspases. We used these ligands to distinguish extrinsic apoptosis pathways in human cell lines versus primary human T cells, showing that the former is largely mediated by caspase-8 while the latter depends on both caspase-8 and -10. Fragment-based covalent ligand discovery provides a greatly expanded portrait of the ligandable proteome and furnishes compounds that can illuminate protein functions in native biological systems.
[Mh] Termos MeSH primário: Cisteína/metabolismo
Avaliação Pré-Clínica de Medicamentos/métodos
Proteoma/química
Proteoma/metabolismo
Bibliotecas de Moléculas Pequenas/metabolismo
Bibliotecas de Moléculas Pequenas/farmacologia
Linfócitos T/metabolismo
[Mh] Termos MeSH secundário: Apoptose
Caspase 10/química
Caspase 10/metabolismo
Caspase 8/química
Caspase 8/metabolismo
Células Cultivadas
Precursores Enzimáticos/química
Precursores Enzimáticos/metabolismo
Seres Humanos
Ligantes
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/metabolismo
Linfócitos T/química
Fatores de Transcrição/química
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Enzyme Precursors); 0 (Ligands); 0 (Peptide Fragments); 0 (Proteome); 0 (Small Molecule Libraries); 0 (Transcription Factors); EC 3.4.22.- (CASP8 protein, human); EC 3.4.22.- (Caspase 10); EC 3.4.22.- (Caspase 8); EC 3.4.22.63 (CASP10 protein, human); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170324
[Lr] Data última revisão:
170324
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160617
[St] Status:MEDLINE
[do] DOI:10.1038/nature18002


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[PMID]:26969678
[Au] Autor:Chatterjee P; Basu S; Zubek J; Kundu M; Nasipuri M; Plewczynski D
[Ad] Endereço:Department of Computer Science and Engineering, Netaji Subhash Engineering College, Garia, Kolkata, 700152, India.
[Ti] Título:PDP-CON: prediction of domain/linker residues in protein sequences using a consensus approach.
[So] Source:J Mol Model;22(4):72, 2016 Apr.
[Is] ISSN:0948-5023
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The prediction of domain/linker residues in protein sequences is a crucial task in the functional classification of proteins, homology-based protein structure prediction, and high-throughput structural genomics. In this work, a novel consensus-based machine-learning technique was applied for residue-level prediction of the domain/linker annotations in protein sequences using ordered/disordered regions along protein chains and a set of physicochemical properties. Six different classifiers-decision tree, Gaussian naïve Bayes, linear discriminant analysis, support vector machine, random forest, and multilayer perceptron-were exhaustively explored for the residue-level prediction of domain/linker regions. The protein sequences from the curated CATH database were used for training and cross-validation experiments. Test results obtained by applying the developed PDP-CON tool to the mutually exclusive, independent proteins of the CASP-8, CASP-9, and CASP-10 databases are reported. An n-star quality consensus approach was used to combine the results yielded by different classifiers. The average PDP-CON accuracy and F-measure values for the CASP targets were found to be 0.86 and 0.91, respectively. The dataset, source code, and all supplementary materials for this work are available at https://cmaterju.org/cmaterbioinfo/ for noncommercial use.
[Mh] Termos MeSH primário: Caspase 10/química
Caspase 8/química
Caspase 9/química
Biologia Computacional/métodos
Máquina de Vetores de Suporte
[Mh] Termos MeSH secundário: Teorema de Bayes
Bases de Dados de Proteínas
Árvores de Decisões
Análise Discriminante
Seres Humanos
Redes Neurais (Computação)
Domínios Proteicos
Análise de Sequência de Proteína
Homologia Estrutural de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.4.22.- (CASP8 protein, human); EC 3.4.22.- (CASP9 protein, human); EC 3.4.22.- (Caspase 10); EC 3.4.22.- (Caspase 8); EC 3.4.22.- (Caspase 9); EC 3.4.22.63 (CASP10 protein, human)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160313
[St] Status:MEDLINE
[do] DOI:10.1007/s00894-016-2933-0


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[PMID]:26760959
[Au] Autor:Faridi U; Dhawan SS; Pal S; Gupta S; Shukla AK; Darokar MP; Sharma A; Shasany AK
[Ad] Endereço:Biotechnology Division, CSIR-Central Institute of Medicinal and Aromatic Plants , Lucknow, U.P., India .
[Ti] Título:Repurposing L-Menthol for Systems Medicine and Cancer Therapeutics? L-Menthol Induces Apoptosis through Caspase 10 and by Suppressing HSP90.
[So] Source:OMICS;20(1):53-64, 2016 Jan.
[Is] ISSN:1557-8100
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The objective of the present study was to repurpose L-menthol, which is frequently used in oral health and topical formulations, for cancer therapeutics. In this article, we argue that monoterpenes such as L-menthol might offer veritable potentials in systems medicine, for example, as cheaper anti-cancer compounds. Other monoterpenes such as limonene, perillyl alcohol, and geraniol have been shown to induce apoptosis in various cancer cell lines, but their mechanisms of action are yet to be completely elucidated. Earlier, we showed that L-menthol modulates tubulin polymerization and apoptosis to inhibit cancer cell proliferation. In the present report, we used an apoptosis-related gene microarray in conjunction with proteomics analyses, as well as in silico interpretations, to study gene expression modulation in human adenocarcinoma Caco-2 cell line in response to L-menthol treatment. The microarray analysis identified caspase 10 as the important initiator caspase, instead of caspase 8. The proteomics analyses showed downregulation of HSP90 protein (also corroborated by its low transcript abundance), which in turn indicated inhibition of AKT-mediated survival pathway, release of pro-apoptotic factor BAD from BAD and BCLxL complex, besides regulation of other factors related to apoptosis. Based on the combined microarray, proteomics, and in silico data, a signaling pathway for L-menthol-induced apoptosis is being presented for the first time here. These data and literature analysis have significant implications for "repurposing" L-menthol beyond oral medicine, and in understanding the mode of action of plant-derived monoterpenes towards development of cheaper anticancer drugs in future.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Caspase 10/metabolismo
Proteínas de Choque Térmico HSP90/metabolismo
Mentol/farmacologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Seres Humanos
Análise de Sistemas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HSP90 Heat-Shock Proteins); 1490-04-6 (Menthol); EC 3.4.22.- (Caspase 10)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160114
[St] Status:MEDLINE
[do] DOI:10.1089/omi.2015.0118


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[PMID]:26637366
[Au] Autor:Rosebeck S; Alonge MM; Kandarpa M; Mayampurath A; Volchenboum SL; Jasielec J; Dytfeld D; Maxwell SP; Kraftson SJ; McCauley D; Shacham S; Kauffman M; Jakubowiak AJ
[Ad] Endereço:Department of Medicine, University of Chicago, Chicago, Illinois.
[Ti] Título:Synergistic Myeloma Cell Death via Novel Intracellular Activation of Caspase-10-Dependent Apoptosis by Carfilzomib and Selinexor.
[So] Source:Mol Cancer Ther;15(1):60-71, 2016 Jan.
[Is] ISSN:1538-8514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Exportin1 (XPO1; also known as chromosome maintenance region 1, or CRM1) controls nucleo-cytoplasmic transport of most tumor suppressors and is overexpressed in many cancers, including multiple myeloma, functionally impairing tumor suppressive function via target mislocalization. Selective inhibitor of nuclear export (SINE) compounds block XPO1-mediated nuclear escape by disrupting cargo protein binding, leading to retention of tumor suppressors, induction of cancer cell death, and sensitization to other drugs. Combined treatment with the clinical stage SINE compound selinexor and the irreversible proteasome inhibitor (PI) carfilzomib induced synergistic cell death of myeloma cell lines and primary plasma cells derived from relapsing/refractory myeloma patients and completely impaired the growth of myeloma cell line-derived tumors in mice. Investigating the details of SINE/PI-induced cell death revealed (i) reduced Bcl-2 expression and cleavage and inactivation of Akt, two prosurvival regulators of apoptosis and autophagy; (ii) intracellular membrane-associated aggregation of active caspases, which depended on caspase-10 protease activity; and (iii) novel association of caspase-10 and autophagy-associated proteins p62 and LC3 II, which may prime activation of the caspase cascade. Overall, our findings provide novel mechanistic rationale behind the potent cell death induced by combining selinexor with carfilzomib and support their use in the treatment of relapsed/refractory myeloma and potentially other cancers.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Caspase 10/metabolismo
Hidrazinas/farmacologia
Mieloma Múltiplo/metabolismo
Oligopeptídeos/farmacologia
Triazóis/farmacologia
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacologia
Autofagia/efeitos dos fármacos
Caspase 8/metabolismo
Linhagem Celular Tumoral
Modelos Animais de Doenças
Sinergismo Farmacológico
Ativação Enzimática/efeitos dos fármacos
Seres Humanos
Espaço Intracelular
Camundongos
Inibidores de Proteassoma/farmacologia
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Hydrazines); 0 (KPT-330); 0 (Oligopeptides); 0 (Proteasome Inhibitors); 0 (Triazoles); 72X6E3J5AR (carfilzomib); EC 3.4.22.- (Caspase 10); EC 3.4.22.- (Caspase 8)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151206
[St] Status:MEDLINE
[do] DOI:10.1158/1535-7163.MCT-15-0488


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[PMID]:26323380
[Au] Autor:Martínez-Feito A; Melero J; Mora-Díaz S; Rodríguez-Vigil C; Elduayen R; González-Granado LI; Pérez-Méndez D; Sánchez-Zapardiel E; Ruiz-García R; Menchén M; Díaz-Madroñero J; Paz-Artal E; Del Orbe-Barreto R; Riñón M; Allende LM
[Ad] Endereço:Servicio de Inmunología, Hospital Universitario 12 de Octubre, Madrid, Spain.
[Ti] Título:Autoimmune lymphoproliferative syndrome due to somatic FAS mutation (ALPS-sFAS) combined with a germline caspase-10 (CASP10) variation.
[So] Source:Immunobiology;221(1):40-7, 2016 Jan.
[Is] ISSN:1878-3279
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Autoimmune lymphoproliferative syndrome (ALPS) is a primary immunodeficiency caused by impaired Fas/FasL-mediated apoptosis of lymphocytes and is characterized by chronic nonmalignant or benign lymphoproliferation, autoimmune manifestations and expansion of double negative (DN) T-cells (TCRαß+CD4-CD8-). Most cases of ALPS are associated with germline (ALPS-FAS) or somatic (ALPS-sFAS) heterozygous FAS mutations or a combination of both. Here we report three unrelated patients with ALPS-sFAS. Only one of them showed impaired Fas function in PHA-activated T-cells. In this patient, the genetic analysis of the caspase-10 gene (CASP10) identified a heterozygous germline change in exon 9 (c.1337A>G) causing Y446C substitution in the caspase-10 protein. In addition, this patient had a dysregulated T- and B-cell phenotype; circulating lymphocytes showed expansion of T effector memory CD45RA+ (TEMRA) CD4 T-cells, effector memory CD8 T-cells, CD21(low) B-cells and reduced memory switched B-cells. Additionally, this patient showed altered expression in T-cells of several molecules that change during differentiation from naïve to effector cells (CD27, CD95, CD57 and perforin). Molecular alterations in genes of the Fas pathway are necessary for the development of ALPS and this syndrome could be influenced by the concurrent effect of other mutations hitting different genes involved in Fas or related pathways.
[Mh] Termos MeSH primário: Síndrome Linfoproliferativa Autoimune/genética
Linfócitos B/imunologia
Linfócitos T CD4-Positivos/imunologia
Linfócitos T CD8-Positivos/imunologia
Caspase 10/genética
Receptor fas/genética
[Mh] Termos MeSH secundário: Adolescente
Antígenos CD/genética
Antígenos CD/imunologia
Síndrome Linfoproliferativa Autoimune/imunologia
Síndrome Linfoproliferativa Autoimune/patologia
Linfócitos B/patologia
Linfócitos T CD4-Positivos/patologia
Linfócitos T CD8-Positivos/patologia
Caspase 10/imunologia
Éxons
Feminino
Expressão Gênica
Seres Humanos
Memória Imunológica
Doenças Linfáticas/genética
Doenças Linfáticas/imunologia
Doenças Linfáticas/patologia
Ativação Linfocitária/efeitos dos fármacos
Masculino
Meia-Idade
Mutação
Perforina/genética
Perforina/imunologia
Fito-Hemaglutininas/farmacologia
Cultura Primária de Células
Esplenomegalia/genética
Esplenomegalia/imunologia
Esplenomegalia/patologia
Receptor fas/imunologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD); 0 (FAS protein, human); 0 (Phytohemagglutinins); 0 (fas Receptor); 126465-35-8 (Perforin); EC 3.4.22.- (Caspase 10); EC 3.4.22.63 (CASP10 protein, human)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150902
[St] Status:MEDLINE


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[PMID]:26606169
[Au] Autor:LeJeune TM; Tsui HY; Parsons LB; Miller GE; Whitted C; Lynch KE; Ramsauer RE; Patel JU; Wyatt JE; Street DS; Adams CB; McPherson B; Tsui HM; Evans JA; Livesay C; Torrenegra RD; Palau VE
[Ad] Endereço:Bill Gatton College of Pharmacy, East Tennessee State University, Johnson City, TN, 37614, United States of America.
[Ti] Título:Mechanism of Action of Two Flavone Isomers Targeting Cancer Cells with Varying Cell Differentiation Status.
[So] Source:PLoS One;10(11):e0142928, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Apoptosis can be triggered in two different ways, through the intrinsic or the extrinsic pathway. The intrinsic pathway is mediated by the mitochondria via the release of cytochrome C while the extrinsic pathway is prompted by death receptor signals and bypasses the mitochondria. These two pathways are closely related to cell proliferation and survival signaling cascades, which thereby constitute possible targets for cancer therapy. In previous studies we introduced two plant derived isomeric flavonoids, flavone A and flavone B which induce apoptosis in highly tumorigenic cancer cells of the breast, colon, pancreas, and the prostate. Flavone A displayed potent cytotoxic activity against more differentiated carcinomas of the colon (CaCo-2) and the pancreas (Panc28), whereas flavone B cytotoxic action is observed on poorly differentiated carcinomas of the colon (HCT 116) and pancreas (MIA PaCa). Apoptosis is induced by flavone A in better differentiated colon cancer CaCo-2 and pancreatic cancer Panc 28 cells via the intrinsic pathway by the inhibition of the activated forms of extracellular signal-regulated kinase (ERK) and pS6, and subsequent loss of phosphorylation of Bcl-2 associated death promoter (BAD) protein, while apoptosis is triggered by flavone B in poorly differentiated colon cancer HCT 116 and MIA PaCa pancreatic cancer cells through the extrinsic pathway with the concomitant upregulation of the phosphorylated forms of ERK and c-JUN at serine 73. These changes in protein levels ultimately lead to activation of apoptosis, without the involvement of AKT.
[Mh] Termos MeSH primário: Diferenciação Celular/efeitos dos fármacos
Flavonas/farmacologia
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Caspase 10/metabolismo
Caspase 8/metabolismo
Caspase 9/metabolismo
Ciclo Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Flavonas/química
Flavonas/isolamento & purificação
Seres Humanos
Fosforilação
Extratos Vegetais/química
Extratos Vegetais/farmacologia
Proteínas Quinases S6 Ribossômicas/metabolismo
Transdução de Sinais/efeitos dos fármacos
Proteína de Morte Celular Associada a bcl/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Flavones); 0 (Plant Extracts); 0 (bcl-Associated Death Protein); EC 2.7.11.1 (Ribosomal Protein S6 Kinases); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 3.4.22.- (Caspase 10); EC 3.4.22.- (Caspase 8); EC 3.4.22.- (Caspase 9); S2V45N7G3B (flavone)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151126
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0142928


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[PMID]:26164758
[Au] Autor:Wang L; Liu C; Li C; Xue J; Zhao S; Zhan P; Lin Y; Zhang P; Jiang A; Chen W
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Medical School of Shandong University, Jinan 250012, Shandong, China; Jinan Infectious Disease Hospital, Jinan 250012, Shandong, China.
[Ti] Título:Effects of microRNA-221/222 on cell proliferation and apoptosis in prostate cancer cells.
[So] Source:Gene;572(2):252-8, 2015 Nov 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To investigate the role of miR-221/222 in cell proliferation and apoptosis in human prostate cancer cells, and examine the effects of miR-221/222 on caspase-10 expression. METHODS: Prostate cancer cells were transfected with miR-221/222 mimics or inhibitors. Cell proliferation was assessed by MTT assay. The expression levels of miR-221/222 were detected with quantitative real-time PCR. Apoptosis was induced with TNF-α/CHX treatment, and evaluated by Hoechst 33342 staining, propidium iodide (PI) flow cytometric analysis, caspase-3 activity measurement, and Western blot analysis. Luciferase activity assay, quantitative real-time PCR, and Western blot were performed to evaluate the effects of miR-221/222 on caspase-10 expression. RESULTS: Our results showed that miR-221/222 could promote the proliferation of prostate cancer cells, including LNCaP and PC3 cells. After transfection and apoptosis induction, Hoechst 33342 staining and PI flow cytometric assay showed that apoptosis was dramatically decreased in prostate cancer cells treated with miR-221/222 mimics. Moreover, caspase-3 activity was dramatically decreased, and the cleaved forms of caspase-3 were reduced, in the miR-221/222 mimic-treated group. On the contrary, miR-221/222 knockdown sensitized the prostate cancer cells to TNF-α/CHX-induced apoptosis. In addition, a negative correlation was observed between the expressions of miR-221/222 and caspase-10 in prostate cancer cells. miR-221/222 could repress the expression of caspase-10, which was confirmed by the luciferase reporter assay. CONCLUSION: miR-221/222 promote cell proliferation and repress apoptosis, through suppressing caspase-10, in prostate cancer cells. Our results provide promising evidence for the miRNA-based therapeutic strategy of prostate cancers.
[Mh] Termos MeSH primário: Caspase 10/genética
MicroRNAs/genética
Neoplasias da Próstata/genética
Neoplasias da Próstata/patologia
[Mh] Termos MeSH secundário: Apoptose
Linhagem Celular Tumoral
Proliferação Celular
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Masculino
Fator de Necrose Tumoral alfa/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (MIRN221 microRNA, human); 0 (MIRN222 microRNA, human); 0 (MicroRNAs); 0 (Tumor Necrosis Factor-alpha); EC 3.4.22.- (Caspase 10); EC 3.4.22.63 (CASP10 protein, human)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150713
[St] Status:MEDLINE



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