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[PMID]:28455144
[Au] Autor:Zhang F; Lu YX; Chen Q; Zou HM; Zhang JM; Hu YH; Li XM; Zhang WJ; Zhang W; Lin C; Li XN
[Ad] Endereço:Department of Pathology, School of Basic Medical Sciences, Southern Medical University, Guangzhou 510515, China. Electronic address: zfan1985@yeah.net.
[Ti] Título:Identification of NCK1 as a novel downstream effector of STAT3 in colorectal cancer metastasis and angiogenesis.
[So] Source:Cell Signal;36:67-78, 2017 Aug.
[Is] ISSN:1873-3913
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Signal transducer and activator of transcription 3 (STAT3) is known to activate targets associated with invasion, proliferation, and angiogenesis in a wide variety of cancers. The adaptor protein NCK1 is involved in cytoskeletal movement and was identified as a STAT3-associated target in human tumors. However, the underlying molecular mechanism associated with colorectal cancer (CRC) metastasis is not yet completely understood. In this study, we report a novel STAT3 to NCK1 signaling pathway in colorectal cancer (CRC). We investigated the expression of NCK1 and its potential clinical and biological significance in CRC. NCK1 was noticeably up-regulated in human CRC tissues. NCK1 was also significantly associated with serosal invasion, lymph metastasis, and tumor-node-metastasis classification but was inversely correlated with differentiation. Gain-of-function and loss-of-function studies have shown that ectopic expression of NCK1 enhanced metastasis and angiogenesis in CRC cells. By gene expression analyses, we revealed a high co-overexpression of STAT3 and NCK1 in CRC tissues. Ectopic overexpression of STAT3 in CRC cells induced the expression of NCK1, whereas STAT3 knockdown decreased the expression of NCK1. Promoter activation and binding analyses demonstrated that STAT3 promoted the expression of NCK1 via direct action on the NCK1 promoter. The knock down of NCK1 partially reduced the CRC cell metastasis and angiogenesis promoted by STAT3. Additionally, by co-immunoprecipitation assays, we verified that NCK1 interacted with PAK1, which resulted in the activation of the PAK1/ERK pathway. STAT3 induced the transcription of NCK1 and triggered a PAK1/ERK cascade in CRC. These findings suggest a novel STAT3 to NCK1 to PAK1/ERK signaling mechanism that is potentially critical for CRC metastasis and angiogenesis.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Neoplasias Colorretais/irrigação sanguínea
Neoplasias Colorretais/patologia
Metástase Linfática/patologia
Neovascularização Patológica/metabolismo
Proteínas Oncogênicas/metabolismo
Fator de Transcrição STAT3/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Animais
Movimento Celular
Galinhas
Neoplasias Colorretais/genética
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Feminino
Quinase 2 de Adesão Focal/metabolismo
Regulação Neoplásica da Expressão Gênica
Técnicas de Silenciamento de Genes
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Masculino
Camundongos Nus
Meia-Idade
Proteínas Oncogênicas/genética
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Nck protein); 0 (Oncogene Proteins); 0 (STAT3 Transcription Factor); EC 2.7.10.2 (Focal Adhesion Kinase 2); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:28455143
[Au] Autor:Li H; Li B; Larose L
[Ad] Endereço:Department of Medicine, McGill University, Montreal, QC H4A 3J1, Canada; The Research Institute of McGill University Health Centre, Montreal, QC H4A 3J1, Canada.
[Ti] Título:IRE1α links Nck1 deficiency to attenuated PTP1B expression in HepG2 cells.
[So] Source:Cell Signal;36:79-90, 2017 Aug.
[Is] ISSN:1873-3913
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PTP1B, a prototype of the non-receptor subfamily of the protein tyrosine phosphatase superfamily, plays a key role in regulating intracellular signaling from various receptor and non-receptor protein tyrosine kinases. Previously, we reported that silencing Nck1 in human hepatocellular carcinoma HepG2 cells enhances basal and growth factor-induced activation of the PI3K-Akt pathway through attenuating PTP1B expression. However, the underlying mechanism by which Nck1 depletion represses PTP1B expression remains unclear. In this study, we found that silencing Nck1 attenuates PTP1B expression in HepG2 cells through down-regulation of IRE1α. Indeed, we show that silencing Nck1 in HepG2 cells leads to decreased IRE1α expression and signaling. Accordingly, IRE1α depletion using siRNA in HepG2 cells enhances PI3K-dependent basal and growth factor-induced Akt activation, reproducing the effects of silencing Nck1 on activation of this pathway. In addition, depletion of IRE1α also leads to reduced PTP1B expression, which was rescued by ectopic expression of IRE1α in Nck1-depleted cells. Mechanistically, we found that silencing either Nck1 or IRE1α in HepG2 cells decreases PTP1B mRNA levels and stability. However, despite miR-122 levels, a miRNA targeting PTP1B 3' UTR and inducing PTP1B mRNA degradation in HepG2 cells, are increased in both Nck1- and IRE1α-depleted HepG2 cells, a miR-122 antagomir did not rescue PTP1B expression in these cells. Overall, this study highlights an important role for Nck1 in fine-tuning IRE1α expression and signaling that regulate PTP1B expression and subsequent activation of the PI3K-Akt pathway in HepG2 cells.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/deficiência
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Endorribonucleases/metabolismo
Proteínas Oncogênicas/deficiência
Proteínas Oncogênicas/metabolismo
Proteína Tirosina Fosfatase não Receptora Tipo 1/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/química
Animais
Ativação Enzimática/efeitos dos fármacos
Fibroblastos/efeitos dos fármacos
Fibroblastos/metabolismo
Inativação Gênica/efeitos dos fármacos
Células HeLa
Células Hep G2
Seres Humanos
Camundongos
MicroRNAs/metabolismo
Proteínas Oncogênicas/química
Fosfatidilinositol 3-Quinases/metabolismo
Fosforilação/efeitos dos fármacos
Ligação Proteica/efeitos dos fármacos
Domínios Proteicos
Proteína Tirosina Fosfatase não Receptora Tipo 1/genética
Proteínas Proto-Oncogênicas c-akt/metabolismo
Estabilidade de RNA/efeitos dos fármacos
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Transdução de Sinais/efeitos dos fármacos
Tapsigargina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (MIRN122 microRNA, human); 0 (MicroRNAs); 0 (Nck protein); 0 (Oncogene Proteins); 0 (RNA, Messenger); 67526-95-8 (Thapsigargin); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (ERN1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.1.- (Endoribonucleases); EC 3.1.3.48 (PTPN1 protein, human); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 1)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:28460463
[Au] Autor:Almeida LO; Neto MPC; Sousa LO; Tannous MA; Curti C; Leopoldino AM
[Ad] Endereço:Department of Clinical Analyses, Toxicology and Food Sciences, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, Brazil.
[Ti] Título:SET oncoprotein accumulation regulates transcription through DNA demethylation and histone hypoacetylation.
[So] Source:Oncotarget;8(16):26802-26818, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epigenetic modifications are essential in the control of normal cellular processes and cancer development. DNA methylation and histone acetylation are major epigenetic modifications involved in gene transcription and abnormal events driving the oncogenic process. SET protein accumulates in many cancer types, including head and neck squamous cell carcinoma (HNSCC); SET is a member of the INHAT complex that inhibits gene transcription associating with histones and preventing their acetylation. We explored how SET protein accumulation impacts on the regulation of gene expression, focusing on DNA methylation and histone acetylation. DNA methylation profile of 24 tumour suppressors evidenced that SET accumulation decreased DNA methylation in association with loss of 5-methylcytidine, formation of 5-hydroxymethylcytosine and increased TET1 levels, indicating an active DNA demethylation mechanism. However, the expression of some suppressor genes was lowered in cells with high SET levels, suggesting that loss of methylation is not the main mechanism modulating gene expression. SET accumulation also downregulated the expression of 32 genes of a panel of 84 transcription factors, and SET directly interacted with chromatin at the promoter of the downregulated genes, decreasing histone acetylation. Gene expression analysis after cell treatment with 5-aza-2'-deoxycytidine (5-AZA) and Trichostatin A (TSA) revealed that histone acetylation reversed transcription repression promoted by SET. These results suggest a new function for SET in the regulation of chromatin dynamics. In addition, TSA diminished both SET protein levels and SET capability to bind to gene promoter, suggesting that administration of epigenetic modifier agents could be efficient to reverse SET phenotype in cancer.
[Mh] Termos MeSH primário: Metilação de DNA
Regulação Neoplásica da Expressão Gênica
Chaperonas de Histonas/metabolismo
Histonas/metabolismo
Proteínas Oncogênicas/metabolismo
Fatores de Transcrição/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Acetilação
Carcinoma Pulmonar de Células não Pequenas/genética
Carcinoma Pulmonar de Células não Pequenas/metabolismo
Linhagem Celular Tumoral
Epigênese Genética
Perfilação da Expressão Gênica
Chaperonas de Histonas/genética
Seres Humanos
Modelos Biológicos
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histone Chaperones); 0 (Histones); 0 (Oncogene Proteins); 0 (SET protein, human); 0 (Transcription Factors)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15818


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[PMID]:28460453
[Au] Autor:Yu T; Wu Y; Hu Q; Zhang J; Nie E; Wu W; Wang X; Wang Y; Liu N
[Ad] Endereço:Department of Neurosurgery, The First Affiliated Hospital of Nanjing Medical University, Nanjing 210029, China.
[Ti] Título:CBX7 is a glioma prognostic marker and induces G1/S arrest via the silencing of CCNE1.
[So] Source:Oncotarget;8(16):26637-26647, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chromobox homolog 7 (CBX7) cooperates with other polycomb group (PcG) proteins to maintain target genes in a silenced state. However, the precise role of CBX7 in tumor progression is still controversial. We found that the expression of CBX7 in four public databases was significantly lower in high grade glioma (HGG). The reduced expression of CBX7 correlated with poor outcome in HGG patients. Both KEGG and GO analyses indicated that genes that were negatively correlated to CBX7 were strongly associated with the cell cycle pathway. We observed that decreased CBX7 protein levels enhanced glioma cells proliferation, migration and invasion. Then, we verified that CBX7 overexpression arrested cells in the G0/G1 phase. Moreover, we demonstrated that the underlying mechanism involved in CBX7 induced repression of CCNE1 promoter requiring the recruitment of histone deacetylase 2 (HADC2). Finally, in vivo bioluminescence imaging and survival times of nude mice revealed that CBX7 behaved as a tumor suppressor in gliomas. In summary, our results validate the assumption that CBX7 is a tumor suppressor of gliomas. Moreover, CBX7 is a potential and novel prognostic biomarker in glioma patients. We also clarified that CBX7 silences CCNE1 via the combination of CCNE1 promoter and the recruitment of HDAC2.
[Mh] Termos MeSH primário: Ciclina E/genética
Pontos de Checagem da Fase G1 do Ciclo Celular/genética
Inativação Gênica
Glioma/genética
Glioma/mortalidade
Proteínas Oncogênicas/genética
Complexo Repressor Polycomb 1/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Modelos Animais de Doenças
Feminino
Regulação Neoplásica da Expressão Gênica
Glioma/patologia
Xenoenxertos
Histona Desacetilase 2/metabolismo
Seres Humanos
Masculino
Camundongos
Gradação de Tumores
Complexo Repressor Polycomb 1/metabolismo
Prognóstico
Regiões Promotoras Genéticas
Ligação Proteica
RNA Interferente Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CBX7 protein, human); 0 (CCNE1 protein, human); 0 (Cyclin E); 0 (Oncogene Proteins); 0 (RNA, Small Interfering); EC 2.3.2.27 (Polycomb Repressive Complex 1); EC 3.5.1.98 (Histone Deacetylase 2)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15789


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[PMID]:29293510
[Au] Autor:Hijikata Y; Okazaki T; Tanaka Y; Murahashi M; Yamada Y; Yamada K; Takahashi A; Inoue H; Kishimoto J; Nakanishi Y; Oda Y; Nakamura Y; Tani K
[Ad] Endereço:Department of Advanced Cell and Molecular Therapy, Kyushu University Hospital, Fukuoka, Japan.
[Ti] Título:A phase I clinical trial of RNF43 peptide-related immune cell therapy combined with low-dose cyclophosphamide in patients with advanced solid tumors.
[So] Source:PLoS One;13(1):e0187878, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The objective of this study was to investigate the safety and the tolerability of combined cellular immunotherapy with low-dose cyclophosphamide (CPA) in patients with advanced solid tumors. This study targeted a novel tumor-associated antigen, ring finger protein 43 (RNF43). Eligible patients were resistant to standard therapy, HLA-A*24:02- or A*02:01-positive and exhibiting high RNF43 expression in their tumor cells. They were administered 300 mg/m2 CPA followed by autologous lymphocytes, preliminarily cultured with autologous RNF43 peptide-pulsed dendritic cells (DCs), RNF43 peptide-pulsed DCs and systemic low dose interleukin-2. The primary endpoint was safety whereas the secondary endpoint was immunological and clinical response to treatment. Ten patients, in total, were enrolled in this trial. Primarily, no adverse events greater than Grade 3 were observed. Six out of 10 patients showed stable disease (SD) on day 49, while 4 other patients showed progressive disease. In addition, one patient with SD exhibited a partial response after the second trial. The frequency of regulatory T cells (Tregs) in patients with SD significantly decreased after CPA administration. The ratio of interferon-γ-producing, tumor-reactive CD8+ T cells increased with time in patients with SD. We successfully showed that the combination of immune cell therapy and CPA was safe, might induce tumor-specific immune responses and clinical efficacy, and was accompanied by a decreased ratio of Tregs in patients with RNF43-positive advanced solid tumors.
[Mh] Termos MeSH primário: Antineoplásicos Alquilantes/uso terapêutico
Ciclofosfamida/uso terapêutico
Proteínas de Ligação a DNA/química
Imunoterapia
Neoplasias/terapia
Proteínas Oncogênicas/química
Peptídeos/uso terapêutico
[Mh] Termos MeSH secundário: Adulto
Idoso
Terapia Combinada
Relação Dose-Resposta a Droga
Estudos de Viabilidade
Feminino
Seres Humanos
Imunofenotipagem
Masculino
Meia-Idade
Neoplasias/tratamento farmacológico
Neoplasias/imunologia
Peptídeos/efeitos adversos
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:CLINICAL TRIAL, PHASE I; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents, Alkylating); 0 (DNA-Binding Proteins); 0 (Oncogene Proteins); 0 (Peptides); 0 (RNF43 protein, human); 8N3DW7272P (Cyclophosphamide)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0187878


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[PMID]:29326043
[Au] Autor:Zhang Z; Shen M; Zhou G
[Ad] Endereço:Department of Gastrointestinal Surgery, Huai'an First People's Hospital, Affiliated to Nanjing Medical University, Huai'an City, Jiangsu Province, PR China.
[Ti] Título:Upregulation of CDCA5 promotes gastric cancer malignant progression via influencing cyclin E1.
[So] Source:Biochem Biophys Res Commun;496(2):482-489, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cell division cycle associated 5(CDCA5) was reported to be associated with progression of several human cancers, however, its clinical significance and biological role still remain unknown in gastric cancer(GC). By analyzing The Cancer Genome Atlas(TCGA), we found CDCA5 was significantly upregulated in GC tissues compared to adjacent normal tissues. Tissue microarray(TMA) indicated upregulation of CDCA5 was significantly correlated with more advanced clinicopathological features, and acts as an independent risk factor for worse overall survival(OS) in GC patients. Moreover, silence of CDCA5 suppresses proliferation of GC cells by inducing G1-phase arrest via downregulating Cyclin E1(CCNE1). Our results demonstrate upregulation of CDCA5 promotes GC malignant progression, which may offer a potential prognostic and therapeutic strategy.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Adenocarcinoma/genética
Proteínas de Ciclo Celular/genética
Ciclina E/genética
Regulação Neoplásica da Expressão Gênica
Proteínas Oncogênicas/genética
Neoplasias Gástricas/genética
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Adenocarcinoma/diagnóstico
Adenocarcinoma/metabolismo
Adenocarcinoma/mortalidade
Idoso
Animais
Proteínas de Ciclo Celular/metabolismo
Linhagem Celular Tumoral
Proliferação Celular
Ciclina E/metabolismo
Feminino
Pontos de Checagem da Fase G1 do Ciclo Celular/genética
Perfilação da Expressão Gênica
Seres Humanos
Masculino
Camundongos
Camundongos Nus
Meia-Idade
Transplante de Neoplasias
Proteínas Oncogênicas/metabolismo
Prognóstico
Transdução de Sinais
Neoplasias Gástricas/diagnóstico
Neoplasias Gástricas/metabolismo
Neoplasias Gástricas/mortalidade
Análise de Sobrevida
Análise Serial de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (CCNE1 protein, human); 0 (CDCA5 protein, human); 0 (Cell Cycle Proteins); 0 (Cyclin E); 0 (Oncogene Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE


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[PMID]:28471386
[Au] Autor:Anwar SL; Wulaningsih W; Lehmann U
[Ad] Endereço:Division of Surgical Oncology, Department of Surgery Faculty of Medicine, Universitas Gadjah Mada, Yogyakarta 55281, Indonesia. sl.anwar@ugm.ac.id.
[Ti] Título:Transposable Elements in Human Cancer: Causes and Consequences of Deregulation.
[So] Source:Int J Mol Sci;18(5), 2017 May 04.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Transposable elements (TEs) comprise nearly half of the human genome and play an essential role in the maintenance of genomic stability, chromosomal architecture, and transcriptional regulation. TEs are repetitive sequences consisting of RNA transposons, DNA transposons, and endogenous retroviruses that can invade the human genome with a substantial contribution in human evolution and genomic diversity. TEs are therefore firmly regulated from early embryonic development and during the entire course of human life by epigenetic mechanisms, in particular DNA methylation and histone modifications. The deregulation of TEs has been reported in some developmental diseases, as well as for different types of human cancers. To date, the role of TEs, the mechanisms underlying TE reactivation, and the interplay with DNA methylation in human cancers remain largely unexplained. We reviewed the loss of epigenetic regulation and subsequent genomic instability, chromosomal aberrations, transcriptional deregulation, oncogenic activation, and aberrations of non-coding RNAs as the potential mechanisms underlying TE deregulation in human cancers.
[Mh] Termos MeSH primário: Elementos de DNA Transponíveis
Regulação Neoplásica da Expressão Gênica
Neoplasias/genética
[Mh] Termos MeSH secundário: Instabilidade Genômica
Seres Humanos
Proteínas Oncogênicas/genética
Proteínas Oncogênicas/metabolismo
RNA não Traduzido/genética
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (Oncogene Proteins); 0 (RNA, Untranslated); 0 (Tumor Suppressor Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


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[PMID]:28471450
[Au] Autor:Zhong J; Wang H; Chen W; Sun Z; Chen J; Xu Y; Weng M; Shi Q; Ma D; Miao C
[Ad] Endereço:Department of Anesthesiology, Fudan University Shanghai Cancer Center, Shanghai, China.
[Ti] Título:Ubiquitylation of MFHAS1 by the ubiquitin ligase praja2 promotes M1 macrophage polarization by activating JNK and p38 pathways.
[So] Source:Cell Death Dis;8(5):e2763, 2017 May 04.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sepsis is a systemic inflammation caused by infection. The balance between M1-M2 macrophage polarization has an essential role in the pathogenesis of sepsis. However, the exact mechanism underlying macrophage polarization is unclear. We previously showed that levels of malignant fibrous histiocytoma amplified sequence 1 (MFHAS1) were significantly elevated in septic patients compared with those in nonseptic patients, and involved in the activation of Toll-like receptor (TLR) 2/c-Jun N-terminal kinase (JNK)/nuclear factor (NF)-κB pathway. In the present study, we explored whether MFHAS1 was involved in macrophage polarization and determined the effect of MFHAS1 on inflammation. We performed in vitro pulldown assays and in vivo co-immunoprecipitation assays and found that E3 ubiquitin ligase praja2 could directly bind to MFHAS1. In situ immunostaining analysis confirmed the colocalization of endogenous praja2 with MFHAS1. We first reported that praja2 promotes the accumulation of ubiquitylated MFHAS1 but does not degrade it. Moreover, our results indicate that MFHAS1 ubiquitylation by praja2 positively regulates TLR2-mediated JNK/p38 pathway and promotes M1 macrophage polarization, M2 to M1 macrophage transformation and inflammation.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Proteínas de Ligação a DNA/metabolismo
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Proteínas Oncogênicas/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Ciclo Celular/química
Proteínas de Ciclo Celular/genética
Polaridade Celular/efeitos dos fármacos
Proteínas de Ligação a DNA/química
Proteínas de Ligação a DNA/genética
Células HEK293
Seres Humanos
Imidazóis/farmacologia
Inflamação/metabolismo
Inflamação/patologia
Interleucina-6/genética
Interleucina-6/metabolismo
Lipopeptídeos/farmacologia
Macrófagos/citologia
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Camundongos
Óxido Nítrico Sintase Tipo II/genética
Óxido Nítrico Sintase Tipo II/metabolismo
Proteínas Oncogênicas/química
Proteínas Oncogênicas/genética
Piridinas/farmacologia
Células RAW 264.7
Transdução de Sinais/efeitos dos fármacos
Receptor 2 Toll-Like/metabolismo
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/metabolismo
Ubiquitina-Proteína Ligases/química
Ubiquitinação/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (DNA-Binding Proteins); 0 (Imidazoles); 0 (Interleukin-6); 0 (Lipopeptides); 0 (MFHAS1 protein, human); 0 (Oncogene Proteins); 0 (Pam(3)CSK(4) peptide); 0 (Pyridines); 0 (Toll-Like Receptor 2); 0 (Tumor Necrosis Factor-alpha); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 2.3.2.27 (PJA2 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); OU13V1EYWQ (SB 203580)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2017.102


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[PMID]:29272308
[Au] Autor:Poplawski P; Wisniewski JR; Rijntjes E; Richards K; Rybicka B; Köhrle J; Piekielko-Witkowska A
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Centre of Postgraduate Medical Education, Warsaw, Poland.
[Ti] Título:Restoration of type 1 iodothyronine deiodinase expression in renal cancer cells downregulates oncoproteins and affects key metabolic pathways as well as anti-oxidative system.
[So] Source:PLoS One;12(12):e0190179, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Type 1 iodothyronine deiodinase (DIO1) contributes to deiodination of 3,5,3',5'-tetraiodo-L-thyronine (thyroxine, T4) yielding of 3,5,3'-triiodothyronine (T3), a powerful regulator of cell differentiation, proliferation, and metabolism. Our previous work showed that loss of DIO1 enhances proliferation and migration of renal cancer cells. However, the global effects of DIO1 expression in various tissues affected by cancer remain unknown. Here, the effects of stable DIO1 re-expression were analyzed on the proteome of renal cancer cells, followed by quantitative real-time PCR validation in two renal cancer-derived cell lines. DIO1-induced changes in intracellular concentrations of thyroid hormones were quantified by L-MS/MS and correlations between expression of DIO1 and potential target genes were determined in tissue samples from renal cancer patients. Stable re-expression of DIO1, resulted in 26 downregulated proteins while 59 proteins were overexpressed in renal cancer cells. The 'downregulated' group consisted mainly of oncoproteins (e.g. STAT3, ANPEP, TGFBI, TGM2) that promote proliferation, migration and invasion. Furthermore, DIO1 re-expression enhanced concentrations of two subunits of thyroid hormone transporter (SLC7A5, SLC3A2), enzymes of key pathways of cellular energy metabolism (e.g. TKT, NAMPT, IDH2), sex steroid metabolism and anti-oxidative response (AKR1C2, AKR1B10). DIO1 expression resulted in elevated intracellular concentration of T4. Expression of DIO1-affected genes strongly correlated with DIO1 transcript levels in tissue samples from renal cancer patients as well as with their poor survival. This first study addressing effects of deiodinase re-expression on proteome of cancer cells demonstrates that induced DIO1 re-expression in renal cancer robustly downregulates oncoproteins, affects key metabolic pathways, and triggers proteins involved in anti-oxidative protection. This data supports the notion that suppressed DIO1 expression and changes in local availability of thyroid hormones might favor a shift from a differentiated to a more proliferation-prone state of cancer tissues and cell lines.
[Mh] Termos MeSH primário: Antioxidantes/metabolismo
Regulação para Baixo
Iodeto Peroxidase/metabolismo
Neoplasias Renais/enzimologia
Proteínas Oncogênicas/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Seres Humanos
Neoplasias Renais/metabolismo
Neoplasias Renais/patologia
Proteômica
Reação em Cadeia da Polimerase em Tempo Real
Tiroxina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Antioxidants); 0 (Oncogene Proteins); EC 1.11.1.- (iodothyronine deiodinase type I); EC 1.11.1.8 (Iodide Peroxidase); Q51BO43MG4 (Thyroxine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190179


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[PMID]:28455653
[Au] Autor:Mazzoni E; Pietrobon S; Bilancia M; Vinante F; Rigo A; Ferrarini I; D'Agostino A; Casali MV; Martini F; Tognon M
[Ad] Endereço:Section of Pathology, Oncology and Experimental Biology, Department of Morphology, Surgery and Experimental Medicine, School of Medicine, University of Ferrara, Ferrara, Italy.
[Ti] Título:High prevalence of antibodies reacting to mimotopes of Simian virus 40 large T antigen, the oncoprotein, in serum samples of patients affected by non-Hodgkin lymphoma.
[So] Source:Cancer Immunol Immunother;66(9):1189-1198, 2017 Sep.
[Is] ISSN:1432-0851
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A new immunological investigation was carried out to study the association between non-Hodgkin lymphoma and Simian virus 40 (SV40). To this end, a new indirect ELISA was employed with two mimotopes from SV40 large T antigen (Tag), the viral oncoprotein, to analyse for specific reactions to antibodies in sera from non-Hodgkin lymphoma patients and controls, represented by healthy subjects (HS) and breast carcinoma (BC) patients. This study allowed us to assay a new sera collection from non-Hodgkin lymphoma patients (NHL, n = 254). To verify the association between NHL and SV40 Tag, two totally independent cohorts were analysed: NHL1 n = 150 and NHL2 n = 104. The epidemiological survey included sera from HS1, n = 150; HS2, n = 104 and BC, n = 78. This new indirect ELISA revealed that antibodies against SV40 Tag mimotopes are detectable in NHL1 and NHL2 sera with a prevalence of 37 and 36%, respectively. The prevalence of SV40-antibodies detected in both NHL1 and NHL2 cohorts differs statistically from controls, at 19% for HS1 (p < 0.01), HS2 (p < 0.05) and BC patients (p < 0.05). This study, carried out with an immunological assay with specific Tag oncoprotein mimotopes of Simian virus 40, reports the presence of IgG antibodies against the large Tumour antigen in non-Hodgkin lymphomas for the first time. Our immunological data with two independent NHL cohorts show a statistically significant association between Simian virus 40 Tag and non-Hodgkin lymphoma. These results suggest that SV40-positive non-Hodgkin lymphomas could be treated differently from those tested SV40-negative.
[Mh] Termos MeSH primário: Anticorpos Antivirais/imunologia
Antígenos Virais de Tumores/imunologia
Linfoma não Hodgkin/imunologia
Proteínas Oncogênicas/metabolismo
Vírus 40 dos Símios/imunologia
[Mh] Termos MeSH secundário: Adulto
Animais
Feminino
Seres Humanos
Linfoma não Hodgkin/patologia
Camundongos
Camundongos Transgênicos
Meia-Idade
Prevalência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Antigens, Viral, Tumor); 0 (Oncogene Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1007/s00262-017-2008-9



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