Base de dados : MEDLINE
Pesquisa : D12.776.512 [Categoria DeCS]
Referências encontradas : 2204 [refinar]
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[PMID]:28451636
[Au] Autor:Erb M; Lee B; Yeon Seo S; Lee JW; Lee S; Lee SK
[Ad] Endereço:Papé Family Pediatric Research Institute, Department of Pediatrics, Oregon Health and Science University, Portland, OR 97239.
[Ti] Título:The Isl1-Lhx3 Complex Promotes Motor Neuron Specification by Activating Transcriptional Pathways that Enhance Its Own Expression and Formation.
[So] Source:eNeuro;4(2), 2017 Mar-Apr.
[Is] ISSN:2373-2822
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Motor neuron (MN) progenitor cells rapidly induce high expression of the transcription factors Islet-1 (Isl1), LIM-homeobox 3 (Lhx3), and the transcriptional regulator LMO4, as they differentiate. While these factors are critical for MN specification, the mechanisms regulating their precise temporal and spatial expression patterns are not well characterized. Isl1 and Lhx3 form the Isl1-Lhx3 complex, which induces the transcription of genes critical for MN specification and maturation. Here, we report that , , and are direct target genes of the Isl1-Lhx3 complex. Our results show that specific genomic loci associated with these genes recruit the Isl1-Lhx3 complex to activate the transcription of , , and in embryonic MNs of chick and mouse. These findings support a model in which the Isl1-Lhx3 complex amplifies its own expression through a potent autoregulatory feedback loop and simultaneously enhances the transcription of . LMO4 blocks the formation of the V2 interneuron-specifying Lhx3 complex. In developing MNs, this action inhibits the expression of V2 interneuron genes and increases the pool of unbound Lhx3 available to incorporate into the Isl1-Lhx3 complex. Identifying the pathways that regulate the expression of these key factors provides important insights into the genetic strategies utilized to promote MN differentiation and maturation.
[Mh] Termos MeSH primário: Proteínas com Homeodomínio LIM/metabolismo
Neurônios Motores/metabolismo
Fatores de Transcrição/metabolismo
Ativação Transcricional
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Animais
Proteínas Aviárias/metabolismo
Embrião de Galinha
Proteínas de Ligação a DNA/metabolismo
Proteínas com Domínio LIM/metabolismo
Camundongos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Avian Proteins); 0 (DNA-Binding Proteins); 0 (LIM Domain Proteins); 0 (LIM-Homeodomain Proteins); 0 (Lhx3 protein); 0 (Lmo4 protein, mouse); 0 (Transcription Factors); 0 (insulin gene enhancer binding protein Isl-1)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE


  2 / 2204 MEDLINE  
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[PMID]:29278703
[Au] Autor:Miyashita K; Kitajima K; Goyama S; Kitamura T; Hara T
[Ad] Endereço:Stem Cell Project, Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya-ku, Tokyo 156-8506, Japan; Division of Cellular Therapy, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
[Ti] Título:Overexpression of Lhx2 suppresses proliferation of human T cell acute lymphoblastic leukemia-derived cells, partly by reducing LMO2 protein levels.
[So] Source:Biochem Biophys Res Commun;495(3):2310-2316, 2018 01 15.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:T cell acute lymphoblastic leukemia (T-ALL) is a malignant cancer with poor prognosis. The transcriptional co-factor LIM domain only 2 (LMO2) and its target gene HHEX are essential for self-renewal of T cell precursors and T-ALL etiology. LMO2 directly associates with LDB1 in a large DNA-containing nuclear complex and controls the transcription of T-ALL-related genes. Recently, we reported that overexpression of the LIM-homeodomain transcription factor, Lhx2, results in liberation of the Lmo2 protein from the Lmo2-Ldb1 complex, followed by ubiquitin proteasome mediated degradation. Here, we found that proliferation of five human T-ALL-derived cell lines, including CCRF-CEM, was significantly suppressed by retroviral overexpression of Lhx2. The majority of Lhx2-transduced CCRF-CEM cells arrested in G phase and subsequently underwent apoptosis. Expression of LMO2 protein as well as HHEX, ERG, HES1 and MYC genes was repressed in CCRF-CEM cells by transduction with Lhx2. Lhx2-mediated growth inhibition was partially rescued by simultaneous overexpression of Lmo2; however, both the C-terminal LIM domain and the homeodomain of Lhx2 were required for its growth-suppressive activity. These data indicate that Lhx2 is capable of blocking proliferation of T-ALL-derived cells by both LMO2-dependent and -independent means. We propose Lhx2 as a new molecular tool for anti-T-ALL drug development.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Proliferação Celular
Proteínas com Domínio LIM/metabolismo
Proteínas com Homeodomínio LIM/metabolismo
Leucemia-Linfoma Linfoblástico de Células T Precursoras/metabolismo
Leucemia-Linfoma Linfoblástico de Células T Precursoras/patologia
Proteínas Proto-Oncogênicas/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Regulação para Baixo
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (LHX2 protein, human); 0 (LIM Domain Proteins); 0 (LIM-Homeodomain Proteins); 0 (LMO2 protein, human); 0 (Proto-Oncogene Proteins); 0 (Transcription Factors)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


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[PMID]:29179181
[Au] Autor:He G; Zou L; Zhou L; Gao P; Qian X; Cui J
[Ad] Endereço:Department of Pathology, Xinxiang Medical University, Xinxiang, China.
[Ti] Título:Cysteine-Rich Intestinal Protein 1 Silencing Inhibits Migration and Invasion in Human Colorectal Cancer.
[So] Source:Cell Physiol Biochem;44(3):897-906, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Cysteine-rich intestinal protein 1 (CRIP1), a member of the LIM/double zinc finger protein family, is abnormally expressed in several tumour types. However, few data are available on the role of CRIP1 in cancer. In the present study, we aimed to investigate the expression profile and functions of CRIP1 in colorectal cancer. METHODS: To examine the protein expression level of CRIP1, immunohistochemistry (IHC) was performed on 56 pairs of colon cancer tissue samples. Western blotting was performed to investigate CRIP1 protein expression in four colon cancer cell lines. The endogenous expression of CRIP1 was suppressed using short interfering RNAs (siRNAs). Cell proliferation assays were used to determine whether CRIP1 silencing affected cell proliferation. Flow cytometry analysis was used to detect cell apoptosis. The effects of silencing CRIP1 on cell migration and invasion was detected using the transwell and wound-healing assays. RESULTS: IHC analysis showed that protein level of CRIP1 was significantly higher in tumour tissue samples than in paired non-tumour tissue samples and that the CRIP1 level was higher in metastatic tissue samples than in non-metastatic tissue samples. In addition, protein levels of CRIP1 were higher in highly metastatic colon cancer cell lines than in colon cancer cell lines with low metastasis. Further, CRIP1 silencing had no effect on cell proliferation or apoptosis in SW620 and HT29 cells. CRIP1 silencing suppressed cell migration and invasion obviously in SW620 and HT29 cells. CONCLUSION: The present study provides new evidence that abnormal expression of CRIP1 might be related to the degree of metastasis in colorectal cancer and that CRIP1 silencing could effectively inhibit migration and invasion during colorectal cancer development. These findings might aid the development of a biomarker for colon cancer prognosis and metastasis, and thus help to treat this common type of cancer.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Neoplasias Colorretais/patologia
Proteínas com Domínio LIM/metabolismo
Interferência de RNA
[Mh] Termos MeSH secundário: Idoso
Proteínas de Transporte/antagonistas & inibidores
Proteínas de Transporte/genética
Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Neoplasias Colorretais/metabolismo
Feminino
Células HT29
Seres Humanos
Imuno-Histoquímica
Proteínas com Domínio LIM/antagonistas & inibidores
Proteínas com Domínio LIM/genética
Masculino
Meia-Idade
RNA Interferente Pequeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CRIP1 protein, human); 0 (Carrier Proteins); 0 (LIM Domain Proteins); 0 (RNA, Small Interfering)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1159/000485357


  4 / 2204 MEDLINE  
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[PMID]:29191657
[Au] Autor:Shiozawa K; Shuting J; Yoshioka Y; Ochiya T; Kondo T
[Ad] Endereço:Division of Rare Cancer Research, National Cancer Center Research Institute, Tokyo, Japan, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan. Electronic address: kshiozaw@ncc.go.jp.
[Ti] Título:Extracellular vesicle-encapsulated microRNA-761 enhances pazopanib resistance in synovial sarcoma.
[So] Source:Biochem Biophys Res Commun;495(1):1322-1327, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The development of drug resistance in tumor cells leads to relapse and distant metastasis. Secreted microRNAs (miRNAs) enclosed in extracellular vesicles (EVs) can act as intercellular messengers. The objective of our study was to elucidate the role of secreted miRNAs to better understand the regulatory network underlying pazopanib-resistance in synovial sarcoma cells. We performed a comprehensive analysis of secreted miRNA abundance in pazopanib treated/untreated synovial sarcoma cells from four different cell lines (SYO-1, HS-SYII, 1273/99, and YaFuSS) using microarray technology, and discovered miR-761 in EVs as a potential biomarker of pazopanib-resistance in synovial sarcoma. Furthermore, we showed that miR-761 putatively targeted three proteins, thyroid hormone receptor interactor 6 (TRIP6), lamin A/C (LMNA), and NAD-dependent protein deacetylase sirtuin-3 (SIRT3). Knockdown of any of these proteins was shown in previous studies to confer increased resistance to chemotherapeutic agents. Our findings provide new insight into the potential role of miR-761, an EV-secreted miRNA from synovial sarcoma cells, making it a potential candidate for use in sarcoma therapy in the future.
[Mh] Termos MeSH primário: Resistência a Medicamentos Antineoplásicos
Vesículas Extracelulares/metabolismo
MicroRNAs/metabolismo
Pirimidinas/administração & dosagem
Sarcoma Sinovial/tratamento farmacológico
Sarcoma Sinovial/metabolismo
Sulfonamidas/administração & dosagem
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Antineoplásicos/administração & dosagem
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Seres Humanos
Proteínas com Domínio LIM/metabolismo
Lamina Tipo A/metabolismo
Sarcoma Sinovial/patologia
Sirtuína 3/metabolismo
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Antineoplastic Agents); 0 (LIM Domain Proteins); 0 (LMNA protein, human); 0 (Lamin Type A); 0 (MicroRNAs); 0 (Pyrimidines); 0 (Sulfonamides); 0 (TRIP6 protein, human); 0 (Transcription Factors); 0 (microRNA761 microRNA, human); 7RN5DR86CK (pazopanib); EC 3.5.1.- (SIRT3 protein, human); EC 3.5.1.- (Sirtuin 3)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE


  5 / 2204 MEDLINE  
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[PMID]:28973433
[Au] Autor:Stanulovic VS; Cauchy P; Assi SA; Hoogenkamp M
[Ad] Endereço:Institute of Cancer and Genomic Sciences, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, UK.
[Ti] Título:LMO2 is required for TAL1 DNA binding activity and initiation of definitive haematopoiesis at the haemangioblast stage.
[So] Source:Nucleic Acids Res;45(17):9874-9888, 2017 Sep 29.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:LMO2 is a bridging factor within a DNA binding complex and is required for definitive haematopoiesis to occur. The developmental stage of the block in haematopoietic specification is not known. We show that Lmo2-/- mouse embryonic stem cells differentiated to Flk-1+ haemangioblasts, but less efficiently to haemogenic endothelium, which only produced primitive haematopoietic progenitors. Genome-wide approaches indicated that LMO2 is required at the haemangioblast stage to position the TAL1/LMO2/LDB1 complex to regulatory elements that are important for the establishment of the haematopoietic developmental program. In the absence of LMO2, the target site recognition of TAL1 is impaired. The lack of LMO2 resulted in altered gene expression levels already at the haemangioblast stage, with transcription factor genes accounting for ∼15% of affected genes. Comparison of Lmo2-/- with Tal1-/- Flk-1+ cells further showed that TAL1 was required to initiate or sustain Lmo2 expression.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Proteínas de Ligação a DNA/genética
DNA/genética
Genoma
Hemangioblastos/metabolismo
Proteínas com Domínio LIM/genética
Células-Tronco Embrionárias Murinas/metabolismo
Proteínas Proto-Oncogênicas/genética
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/deficiência
Animais
Sequência de Bases
Fatores de Transcrição Hélice-Alça-Hélice Básicos/deficiência
Diferenciação Celular
Linhagem Celular
DNA/metabolismo
Proteínas de Ligação a DNA/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Hemangioblastos/citologia
Hematopoese/genética
Proteínas com Domínio LIM/deficiência
Proteínas com Domínio LIM/metabolismo
Camundongos
Células-Tronco Embrionárias Murinas/citologia
Ligação Proteica
Proteínas Proto-Oncogênicas/deficiência
Elementos Reguladores de Transcrição
Transdução de Sinais
Proteína 1 de Leucemia Linfocítica Aguda de Células T
Transcrição Genética
Receptor 2 de Fatores de Crescimento do Endotélio Vascular/deficiência
Receptor 2 de Fatores de Crescimento do Endotélio Vascular/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Basic Helix-Loop-Helix Transcription Factors); 0 (DNA-Binding Proteins); 0 (LIM Domain Proteins); 0 (Ldb1 protein, mouse); 0 (Lmo2 protein, mouse); 0 (Proto-Oncogene Proteins); 0 (T-Cell Acute Lymphocytic Leukemia Protein 1); 0 (Tal1 protein, mouse); 9007-49-2 (DNA); EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx573


  6 / 2204 MEDLINE  
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[PMID]:28934429
[Au] Autor:Cabantous S; Doumbo O; Poudiougou B; Louis L; Barry A; Oumar AA; Traore A; Marquet S; Dessein A
[Ad] Endereço:INSERM UMR906, GIMP, Labex ParaFrap.
[Ti] Título:Gene Expression Analysis Reveals Genes Common to Cerebral Malaria and Neurodegenerative Disorders.
[So] Source:J Infect Dis;216(6):771-775, 2017 Sep 15.
[Is] ISSN:1537-6613
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cerebral malaria, a reversible encephalopathy affecting young children, is a medical emergency requiring urgent clinical assessment and treatment. We performed a whole-transcriptomic analysis of blood samples from Malian children with cerebral or uncomplicated malaria. We focused on transcripts from pathways for which dysfunction has been associated with neurodegenerative disorders. We found that SNCA, SIAH2, UBB, HSPA1A, TUBB2A, and PINK1 were upregulated (fold-increases, ≥2.6), whereas UBD and PSMC5 were downregulated (fold-decreases, ≤4.39) in children with cerebral malaria, compared with those with uncomplicated malaria. These findings provide the first evidence for pathogenic mechanisms common to human cerebral malaria and neurodegenerative disorders.
[Mh] Termos MeSH primário: Malária Cerebral/genética
Malária Falciparum/genética
Doenças Neurodegenerativas/genética
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares
Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Criança
Pré-Escolar
Regulação para Baixo
Feminino
Perfilação da Expressão Gênica
Proteínas de Choque Térmico HSP70/genética
Proteínas de Choque Térmico HSP70/metabolismo
Seres Humanos
Proteínas com Domínio LIM/genética
Proteínas com Domínio LIM/metabolismo
Leucócitos Mononucleares/parasitologia
Malária Cerebral/diagnóstico
Malária Falciparum/diagnóstico
Masculino
Doenças Neurodegenerativas/diagnóstico
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Plasmodium falciparum
Estudos Prospectivos
Complexo de Endopeptidases do Proteassoma
Proteínas Quinases/genética
Proteínas Quinases/metabolismo
Reprodutibilidade dos Testes
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Tubulina (Proteína)/genética
Tubulina (Proteína)/metabolismo
Ubiquitina/genética
Ubiquitina/metabolismo
Ubiquitina-Proteína Ligases/genética
Ubiquitina-Proteína Ligases/metabolismo
Ubiquitinas/genética
Ubiquitinas/metabolismo
Regulação para Cima
alfa-Sinucleína/genética
alfa-Sinucleína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (HSP70 Heat-Shock Proteins); 0 (HSPA1A protein, human); 0 (LIM Domain Proteins); 0 (Nuclear Proteins); 0 (PSMC5 protein, human); 0 (SNCA protein, human); 0 (TUBB2B protein, human); 0 (Transcription Factors); 0 (Tubulin); 0 (UBB protein, human); 0 (UBD protein, human); 0 (Ubiquitin); 0 (Ubiquitins); 0 (alpha-Synuclein); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (seven in absentia proteins); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (PTEN-induced putative kinase); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/infdis/jix359


  7 / 2204 MEDLINE  
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[PMID]:28867147
[Au] Autor:Zhu S; Zhang X; Weichert-Leahey N; Dong Z; Zhang C; Lopez G; Tao T; He S; Wood AC; Oldridge D; Ung CY; van Ree JH; Khan A; Salazar BM; Lummertz da Rocha E; Zimmerman MW; Guo F; Cao H; Hou X; Weroha SJ; Perez-Atayde AR; Neuberg DS; Meves A; McNiven MA; van Deursen JM; Li H; Maris JM; Look AT
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Mayo Clinic Cancer Center, Rochester, MN 55902, USA. Electronic address: zhu.shizhen@mayo.edu.
[Ti] Título:LMO1 Synergizes with MYCN to Promote Neuroblastoma Initiation and Metastasis.
[So] Source:Cancer Cell;32(3):310-323.e5, 2017 Sep 11.
[Is] ISSN:1878-3686
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A genome-wide association study identified LMO1, which encodes an LIM-domain-only transcriptional cofactor, as a neuroblastoma susceptibility gene that functions as an oncogene in high-risk neuroblastoma. Here we show that dßh promoter-mediated expression of LMO1 in zebrafish synergizes with MYCN to increase the proliferation of hyperplastic sympathoadrenal precursor cells, leading to a reduced latency and increased penetrance of neuroblastomagenesis. The transgenic expression of LMO1 also promoted hematogenous dissemination and distant metastasis, which was linked to neuroblastoma cell invasion and migration, and elevated expression levels of genes affecting tumor cell-extracellular matrix interaction, including loxl3, itga2b, itga3, and itga5. Our results provide in vivo validation of LMO1 as an important oncogene that promotes neuroblastoma initiation, progression, and widespread metastatic dissemination.
[Mh] Termos MeSH primário: Carcinogênese/patologia
Proteínas de Ligação a DNA/metabolismo
Proteínas com Domínio LIM/metabolismo
Proteína Proto-Oncogênica N-Myc/metabolismo
Neuroblastoma/metabolismo
Neuroblastoma/patologia
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Carcinogênese/metabolismo
Linhagem Celular Tumoral
Movimento Celular/genética
Matriz Extracelular/metabolismo
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Hiperplasia
Modelos Biológicos
Invasividade Neoplásica
Metástase Neoplásica
Neuroblastoma/genética
Transdução de Sinais/genética
Transgenes
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (LIM Domain Proteins); 0 (LMO1 protein, human); 0 (MYCN protein, human); 0 (N-Myc Proto-Oncogene Protein); 0 (Transcription Factors)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE


  8 / 2204 MEDLINE  
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[PMID]:28837644
[Au] Autor:Yang T; Kersigo J; Wu S; Fritzsch B; Bassuk AG
[Ad] Endereço:Department of Biology, University of Iowa, Iowa City, Iowa, United States of America.
[Ti] Título:Prickle1 regulates neurite outgrowth of apical spiral ganglion neurons but not hair cell polarity in the murine cochlea.
[So] Source:PLoS One;12(8):e0183773, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the mammalian organ of Corti (OC), the stereocilia on the apical surface of hair cells (HCs) are uniformly organized in a neural to abneural axis (or medial-laterally). This organization is regulated by planar cell polarity (PCP) signaling. Mutations of PCP genes, such as Vangl2, Dvl1/2, Celsr1, and Fzd3/6, affect the formation of HC orientation to varying degrees. Prickle1 is a PCP signaling gene that belongs to the prickle / espinas / testin family. Prickle1 protein is shown to be asymmetrically localized in the HCs of the OC, and this asymmetric localization is associated with loss of PCP in Smurf mutants, implying that Prickle1 is involved in HC PCP development in the OC. A follow-up study found no PCP polarity defects after loss of Prickle1 (Prickle1-/-) in the cochlea. We show here strong Prickle1 mRNA expression in the spiral ganglion by in situ hybridization and ß-Gal staining, and weak expression in the OC by ß-Gal staining. Consistent with this limited expression in the OC, cochlear HC PCP is unaffected in either Prickle1C251X/C251X mice or Prickle1f/f; Pax2-cre conditional null mice. Meanwhile, type II afferents of apical spiral ganglion neurons (SGN) innervating outer hair cells (OHC) have unusual neurite growth. In addition, afferents from the apex show unusual collaterals in the cochlear nuclei that overlap with basal turn afferents. Our findings argue against the role of Prickle1 in regulating hair cell polarity in the cochlea. Instead, Prickle1 regulates the polarity-related growth of distal and central processes of apical SGNs.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/fisiologia
Polaridade Celular/fisiologia
Cóclea/citologia
Células Ciliadas Auditivas/citologia
Proteínas com Domínio LIM/fisiologia
Neuritos
Neurônios/citologia
Gânglio Espiral da Cóclea/citologia
[Mh] Termos MeSH secundário: Animais
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Microscopia Eletrônica de Varredura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (LIM Domain Proteins); 0 (Prickle1 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170825
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183773


  9 / 2204 MEDLINE  
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[PMID]:28821611
[Au] Autor:Wang X; Chemmama IE; Yu C; Huszagh A; Xu Y; Viner R; Block SA; Cimermancic P; Rychnovsky SD; Ye Y; Sali A; Huang L
[Ad] Endereço:From the Department of Physiology and Biophysics, University of California, Irvine, California 92697.
[Ti] Título:The proteasome-interacting Ecm29 protein disassembles the 26S proteasome in response to oxidative stress.
[So] Source:J Biol Chem;292(39):16310-16320, 2017 Sep 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oxidative stress has been implicated in multiple human neurological and other disorders. Proteasomes are multi-subunit proteases critical for the removal of oxidatively damaged proteins. To understand stress-associated human pathologies, it is important to uncover the molecular events underlying the regulation of proteasomes upon oxidative stress. To this end, we investigated H O stress-induced molecular changes of the human 26S proteasome and determined that stress-induced 26S proteasome disassembly is conserved from yeast to human. Moreover, we developed and employed a new proteomic approach, XAP ( cross-linking-assisted affinity purification), coupled with stable isotope labeling with amino acids in cell culture (SILAC)-based quantitative MS, to capture and quantify several weakly bound proteasome-interacting proteins and examine their roles in stress-mediated proteasomal remodeling. Our results indicate that the adapter protein Ecm29 is the main proteasome-interacting protein responsible for stress-triggered remodeling of the 26S proteasome in human cells. Importantly, using a disuccinimidyl sulfoxide-based cross-linking MS platform, we mapped the interactions of Ecm29 within itself and with proteasome subunits and determined the architecture of the Ecm29-proteasome complex with integrative structure modeling. These results enabled us to propose a structural model in which Ecm29 intrudes on the interaction between the 20S core particle and the 19S regulatory particle in the 26S proteasome, disrupting the proteasome structure in response to oxidative stress.
[Mh] Termos MeSH primário: Modelos Moleculares
Estresse Oxidativo
Complexo de Endopeptidases do Proteassoma/metabolismo
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares
Proteínas Adaptadoras de Transdução de Sinal/química
Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Marcadores de Afinidade
Reagentes para Ligações Cruzadas/farmacologia
Células HEK293
Seres Humanos
Marcação por Isótopo
Proteínas com Domínio LIM/química
Proteínas com Domínio LIM/genética
Proteínas com Domínio LIM/metabolismo
Complexo de Endopeptidases do Proteassoma/química
Complexo de Endopeptidases do Proteassoma/genética
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Mapeamento de Interação de Proteínas
Multimerização Proteica
Proteólise
Interferência de RNA
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Espectrometria de Massas em Tandem
Fatores de Transcrição/química
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Ubiquitinas/química
Ubiquitinas/genética
Ubiquitinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Affinity Labels); 0 (Cross-Linking Reagents); 0 (KIAA0368 protein, human); 0 (LIM Domain Proteins); 0 (PSMC5 protein, human); 0 (Recombinant Fusion Proteins); 0 (Transcription Factors); 0 (Ubiquitins); 0 (Ubl4A protein, human); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.4.99.- (ATP dependent 26S protease); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.803619


  10 / 2204 MEDLINE  
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[PMID]:28813482
[Au] Autor:Kihara T; Sugimoto Y; Shinohara S; Takaoka S; Miyake J
[Ad] Endereço:Department of Life and Environment Engineering, Faculty of Environmental Engineering, The University of Kitakyushu, Hibikino, Wakamatsu, Kitakyushu, Fukuoka, Japan.
[Ti] Título:Cysteine-rich protein 2 accelerates actin filament cluster formation.
[So] Source:PLoS One;12(8):e0183085, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Filamentous actin (F-actin) forms many types of structures and dynamically regulates cell morphology and movement, and plays a mechanosensory role for extracellular stimuli. In this study, we determined that the smooth muscle-related transcription factor, cysteine-rich protein 2 (CRP2), regulates the supramolecular networks of F-actin. The structures of CRP2 and F-actin in solution were analyzed by small-angle X-ray solution scattering (SAXS). The general shape of CRP2 was partially unfolded and relatively ellipsoidal in structure, and the apparent cross sectional radius of gyration (Rc) was about 15.8 Å. The predicted shape, derived by ab initio modeling, consisted of roughly four tandem clusters: LIM domains were likely at both ends with the middle clusters being an unfolded linker region. From the SAXS analysis, the Rc of F-actin was about 26.7 Å, and it was independent of CRP2 addition. On the other hand, in the low angle region of the CRP2-bound F-actin scattering, the intensities showed upward curvature with the addition of CRP2, which indicates increasing branching of F-actin following CRP2 binding. From biochemical analysis, the actin filaments were augmented and clustered by the addition of CRP2. This F-actin clustering activity of CRP2 was cooperative with α-actinin. Thus, binding of CRP2 to F-actin accelerates actin polymerization and F-actin cluster formation.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Proteínas de Transporte/metabolismo
Proteínas com Domínio LIM/metabolismo
Multimerização Proteica
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/química
Animais
Proteínas de Transporte/química
Proteínas com Domínio LIM/química
Camundongos
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Crip2 protein, mouse); 0 (LIM Domain Proteins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183085



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