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Pesquisa : D12.776.817 [Categoria DeCS]
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  1 / 25194 MEDLINE  
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[PMID]:29447197
[Au] Autor:Fujita T; Kozuka-Hata H; Hori Y; Takeuchi J; Kubo T; Oyama M
[Ad] Endereço:Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
[Ti] Título:Shotgun proteomics deciphered age/division of labor-related functional specification of three honeybee (Apis mellifera L.) exocrine glands.
[So] Source:PLoS One;13(2):e0191344, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The honeybee (Apis mellifera L.) uses various chemical signals produced by the worker exocrine glands to maintain the functioning of its colony. The roles of worker postcerebral glands (PcGs), thoracic glands (TGs), and mandibular glands (MGs) and the functional changes they undergo according to the division of labor from nursing to foraging are not as well studied. To comprehensively characterize the molecular roles of these glands in workers and their changes according to the division of labor of workers, we analyzed the proteomes of PcGs, TGs, and MGs from nurse bees and foragers using shotgun proteomics technology. We identified approximately 2000 proteins from each of the nurse bee or forager glands and highlighted the features of these glands at the molecular level by semiquantitative enrichment analyses of frequently detected, gland-selective, and labor-selective proteins. First, we found the high potential to produce lipids in PcGs and MGs, suggesting their relation to pheromone production. Second, we also found the proton pumps abundant in TGs and propose some transporters possibly related to the saliva production. Finally, our data unveiled candidate enzymes involved in labor-dependent acid production in MGs.
[Mh] Termos MeSH primário: Abelhas/genética
Glândulas Exócrinas/fisiologia
Proteômica/métodos
[Mh] Termos MeSH secundário: Fatores Etários
Sequência de Aminoácidos
Animais
Abelhas/metabolismo
Comportamento Animal/fisiologia
Glândulas Exócrinas/citologia
Glândulas Exócrinas/metabolismo
Proteínas de Insetos/metabolismo
Feromônios/metabolismo
Proteoma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Insect Proteins); 0 (Pheromones); 0 (Proteome)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191344


  2 / 25194 MEDLINE  
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[PMID]:29447168
[Au] Autor:Abraham PE; Garcia BJ; Gunter LE; Jawdy SS; Engle N; Yang X; Jacobson DA; Hettich RL; Tuskan GA; Tschaplinski TJ
[Ad] Endereço:Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, United States of America.
[Ti] Título:Quantitative proteome profile of water deficit stress responses in eastern cottonwood (Populus deltoides) leaves.
[So] Source:PLoS One;13(2):e0190019, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Drought stress is a recurring feature of world climate and the single most important factor influencing agricultural yield worldwide. Plants display highly variable, species-specific responses to drought and these responses are multifaceted, requiring physiological and morphological changes influenced by genetic and molecular mechanisms. Moreover, the reproducibility of water deficit studies is very cumbersome, which significantly impedes research on drought tolerance, because how a plant responds is highly influenced by the timing, duration, and intensity of the water deficit. Despite progress in the identification of drought-related mechanisms in many plants, the molecular basis of drought resistance remains to be fully understood in trees, particularly in poplar species because their wide geographic distribution results in varying tolerances to drought. Herein, we aimed to better understand this complex phenomenon in eastern cottonwood (Populus deltoides) by performing a detailed contrast of the proteome changes between two different water deficit experiments to identify functional intersections and divergences in proteome responses. We investigated plants subjected to cyclic water deficit and compared these responses to plants subjected to prolonged acute water deficit. In total, we identified 108,012 peptide sequences across both experiments that provided insight into the quantitative state of 22,737 Populus gene models and 8,199 functional protein groups in response to drought. Together, these datasets provide the most comprehensive insight into proteome drought responses in poplar to date and a direct proteome comparison between short period dehydration shock and cyclic, post-drought re-watering. Overall, this investigation provides novel insights into drought avoidance mechanisms that are distinct from progressive drought stress. Additionally, we identified proteins that have been associated as drought-relevant in previous studies. Importantly, we highlight the RD26 transcription factor as a gene regulated at both the transcript and protein level, regardless of species and drought condition, and, thus, represents a key, universal drought marker for Populus species.
[Mh] Termos MeSH primário: Proteínas de Plantas/metabolismo
Populus/metabolismo
Proteoma
Estresse Fisiológico
[Mh] Termos MeSH secundário: Cromatografia Líquida
Secas
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Proteome)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190019


  3 / 25194 MEDLINE  
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[PMID]:29366405
[Au] Autor:Walaszczyk A; Pietrowska M; Wojakowska A; Abramowicz A; Chmura A; Maslyk B; Rodziewicz P; Polanska J; Behrendt K; Nowicka E; Tarnawski R; Widlak P
[Ti] Título:Therapy-Related Changes in the Serum Proteome Patterns of Early Stage Breast Cancer Patients with Different Outcomes.
[So] Source:Protein Pept Lett;24(1):37-45, 2017.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Adjuvant chemo- and/or radiotherapy is applied in a majority of patients treated for early stage breast cancer, although only a small percentage of these individuals are at high risk of metastasis or recurrence. Hence, knowledge of the biomarkers associated with the risk of disease progression might facilitate the planning of an optimal therapy and protect many patients from the toxicity of unnecessary treatment. In this study, we characterized the serum proteome of patients diagnosed with early-stage breast cancer, exhibiting either no evidence of disease five years after the end of therapy or suffering from metastasis, relapse or a second cancer during the corresponding follow-up. Samples collected before treatment and one year after the end of therapy, when no clinical symptoms of a treatment failure was evidenced, were analyzed using two classical proteomics approaches: LC-MS/MS and 2D-PAGE. A total of 42 proteins with relative quantities that were significantly different between pre- and post-treatment samples were identified in either group of patients; however, the observed changes were more frequent in the treatment-failure group. Among the posttreatment samples, 30 proteins were upregulated, and 10 proteins were downregulated, while 11 proteins were upregulated, and eight proteins were downregulated in the control group. Moreover, several proteins exhibited different patterns of changes in both groups of patients. For example, haptoglobin expression increased in the treatment-failure group but decreased in the control group (this pattern of changes was confirmed using an immunoassay). Notably, proteins affected in posttreatment samples in either group of patients could be associated with different molecular and cellular functions, including angiogenesis, blood coagulation and wound healing in the treatment-failure group and cell adhesion and cell death in the control group.
[Mh] Termos MeSH primário: Proteínas Sanguíneas/análise
Neoplasias da Mama/sangue
Neoplasias da Mama/terapia
[Mh] Termos MeSH secundário: Idoso
Biomarcadores Tumorais/análise
Biomarcadores Tumorais/sangue
Eletroforese em Gel Bidimensional
Feminino
Haptoglobinas/análise
Seres Humanos
Meia-Idade
Proteoma/análise
Proteômica
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Blood Proteins); 0 (Haptoglobins); 0 (Proteome)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE
[do] DOI:10.2174/0929866523666161128154412


  4 / 25194 MEDLINE  
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[PMID]:29188662
[Au] Autor:Ren GH; Weng RH; Shi Y; Huang P; Deng KF; Liu NG; Chen YJ
[Ad] Endereço:Shanghai Key Laboratory of Forensic Medicine, Shanghai Forensic Service Platform, Institute of Forensic Science, Ministry of Justice, P.R.China, Shanghai 200063, China.
[Ti] Título:[Analysis of Differentially Expressed Proteins Distribution in the Rat Brains with DAI by MALDI-TOF-IMS].
[So] Source:Fa Yi Xue Za Zhi;32(4):241-244, 2016 Aug.
[Is] ISSN:1004-5619
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVES: To establish the imaging mass spectrometry for analysis of differentially expressed proteins distribution in the rat brains with diffuse axonal injury (DAI) based on matrix assisted laser desorption/ionization-time of flight imaging mass spectrometry (MALDI-TOF-IMS). METHODS: MALDI-TOF-IMS scanning were conducted on the brains of DAI group and control group in the range of 1 000 to 20 000 using AutoflexⅢ MALDI-TOF spectrometer. ClinProTool 2.2 software was used for statistical analysis on the data of two groups, and then the differentially expressed proteins were picked out to conduct imaging. The distribution of the proteins with different in the rat brains was observed. RESULTS: Five proteins with different , including 4 963, 5 634, 6 253, 6 714 and 7 532, differentially expressed in the rat brains with DAI. CONCLUSIONS: MALDI-TOF-IMS can be used for studying the differentially expressed proteins in rat brains with DAI and the analysis method is established for exploring the distribution of differentially expressed proteins in the rat brains with DAI using imaging mass spectrometry.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Lesão Axonal Difusa/metabolismo
Proteínas/metabolismo
Proteoma/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/patologia
Lesão Axonal Difusa/patologia
Proteômica
Ratos
Software
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins); 0 (Proteome)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.3969/j.issn.1004-5619.2016.04.001


  5 / 25194 MEDLINE  
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[PMID]:28453668
[Au] Autor:Kou Q; Wu S; Tolic N; Pasa-Tolic L; Liu Y; Liu X
[Ad] Endereço:Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN 46202, USA.
[Ti] Título:A mass graph-based approach for the identification of modified proteoforms using top-down tandem mass spectra.
[So] Source:Bioinformatics;33(9):1309-1316, 2017 05 01.
[Is] ISSN:1367-4811
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Motivation: Although proteomics has rapidly developed in the past decade, researchers are still in the early stage of exploring the world of complex proteoforms, which are protein products with various primary structure alterations resulting from gene mutations, alternative splicing, post-translational modifications, and other biological processes. Proteoform identification is essential to mapping proteoforms to their biological functions as well as discovering novel proteoforms and new protein functions. Top-down mass spectrometry is the method of choice for identifying complex proteoforms because it provides a 'bird's eye view' of intact proteoforms. The combinatorial explosion of various alterations on a protein may result in billions of possible proteoforms, making proteoform identification a challenging computational problem. Results: We propose a new data structure, called the mass graph, for efficient representation of proteoforms and design mass graph alignment algorithms. We developed TopMG, a mass graph-based software tool for proteoform identification by top-down mass spectrometry. Experiments on top-down mass spectrometry datasets showed that TopMG outperformed existing methods in identifying complex proteoforms. Availability and implementation: http://proteomics.informatics.iupui.edu/software/topmg/. Contact: xwliu@iupui.edu. Supplementary information: Supplementary data are available at Bioinformatics online.
[Mh] Termos MeSH primário: Proteoma/análise
Proteômica/métodos
Software
Espectrometria de Massas em Tandem/métodos
[Mh] Termos MeSH secundário: Algoritmos
Processamento Alternativo
Peso Molecular
Mutação
Processamento de Proteína Pós-Traducional
Proteoma/química
Proteoma/genética
Proteoma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Proteome)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1093/bioinformatics/btw806


  6 / 25194 MEDLINE  
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[PMID]:29348634
[Au] Autor:Wood RJ; Ormsby AR; Radwan M; Cox D; Sharma A; Vöpel T; Ebbinghaus S; Oliveberg M; Reid GE; Dickson A; Hatters DM
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.
[Ti] Título:A biosensor-based framework to measure latent proteostasis capacity.
[So] Source:Nat Commun;9(1):287, 2018 01 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The pool of quality control proteins (QC) that maintains protein-folding homeostasis (proteostasis) is dynamic but can become depleted in human disease. A challenge has been in quantitatively defining the depth of the QC pool. With a new biosensor, flow cytometry-based methods and mathematical modeling we measure the QC capacity to act as holdases and suppress biosensor aggregation. The biosensor system comprises a series of barnase kernels with differing folding stability that engage primarily with HSP70 and HSP90 family proteins. Conditions of proteostasis stimulation and stress alter QC holdase activity and aggregation rates. The method reveals the HSP70 chaperone cycle to be rate limited by HSP70 holdase activity under normal conditions, but this is overcome by increasing levels of the BAG1 nucleotide exchange factor to HSPA1A or activation of the heat shock gene cluster by HSF1 overexpression. This scheme opens new paths for biosensors of disease and proteostasis systems.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Citometria de Fluxo/métodos
Modelos Teóricos
Proteostase
[Mh] Termos MeSH secundário: Algoritmos
Western Blotting
Células HEK293
Proteínas de Choque Térmico HSP72/metabolismo
Proteínas de Choque Térmico HSP90/metabolismo
Fatores de Transcrição de Choque Térmico/metabolismo
Seres Humanos
Proteoma/metabolismo
Proteômica/métodos
Espectrometria de Massas em Tandem/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HSF1 protein, human); 0 (HSP72 Heat-Shock Proteins); 0 (HSP90 Heat-Shock Proteins); 0 (Heat Shock Transcription Factors); 0 (Proteome)
[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:180120
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02562-5


  7 / 25194 MEDLINE  
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[PMID]:28460433
[Au] Autor:Cheng DD; Zhang HZ; Yuan JQ; Li SJ; Yang QC; Fan CY
[Ad] Endereço:Department of Orthopedics, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai, 200233, China.
[Ti] Título:Minichromosome maintenance protein 2 and 3 promote osteosarcoma progression via DHX9 and predict poor patient prognosis.
[So] Source:Oncotarget;8(16):26380-26393, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A label free quantitative proteomic approach (SWATH™ experiment) was performed to identify tumor-associated nuclear proteins that are differentially expressed between osteosarcoma cells and osteoblast cells. By functional screening, minichromosome maintenance protein 2 (MCM2) and minichromosome maintenance protein 3 (MCM3) were found to be related to osteosarcoma cell growth. Here, we show that knockdown of MCM2 or MCM3 inhibits osteosarcoma growth in vitro and in vivo. In co-immunoprecipitation and co-localization experiments, MCM2 and MCM3 were found to interact with DExH-box helicase 9 (DHX9) in osteosarcoma cells. A rescue study showed that the decreased growth of osteosarcoma cells by MCM2 or MCM3 knockdown was reversed by DHX9 overexpression, indicating that MCM2 and MCM3 activity was DHX9-dependent. In addition, the depletion of DHX9 hindered osteosarcoma cell proliferation. Notably, MCM2 and MCM3 expression levels were positively correlated with the DHX9 expression level in tumor samples and were associated with a poor prognosis in patients with osteosarcoma. Taken together, these results suggest that the MCM2/MCM3-DHX9 axis has an important role in osteosarcoma progression.
[Mh] Termos MeSH primário: Neoplasias Ósseas/metabolismo
Neoplasias Ósseas/mortalidade
RNA Helicases DEAD-box/metabolismo
Componente 2 do Complexo de Manutenção de Minicromossomo/metabolismo
Componente 3 do Complexo de Manutenção de Minicromossomo/metabolismo
Proteínas de Neoplasias/metabolismo
Osteossarcoma/metabolismo
Osteossarcoma/mortalidade
[Mh] Termos MeSH secundário: Adolescente
Adulto
Animais
Neoplasias Ósseas/genética
Neoplasias Ósseas/patologia
Linhagem Celular Tumoral
Proliferação Celular/genética
Criança
Modelos Animais de Doenças
Progressão da Doença
Feminino
Expressão Gênica
Técnicas de Silenciamento de Genes
Xenoenxertos
Seres Humanos
Masculino
Camundongos
Componente 2 do Complexo de Manutenção de Minicromossomo/genética
Componente 3 do Complexo de Manutenção de Minicromossomo/genética
Metástase Neoplásica
Estadiamento de Neoplasias
Proteínas Nucleares/metabolismo
Osteossarcoma/genética
Osteossarcoma/patologia
Prognóstico
Modelos de Riscos Proporcionais
Ligação Proteica
Proteoma
Proteômica/métodos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MCM3 protein, human); 0 (Neoplasm Proteins); 0 (Nuclear Proteins); 0 (Proteome); EC 3.6.1.- (DHX9 protein, human); EC 3.6.4.12 (MCM2 protein, human); EC 3.6.4.12 (Minichromosome Maintenance Complex Component 2); EC 3.6.4.12 (Minichromosome Maintenance Complex Component 3); EC 3.6.4.13 (DEAD-box RNA Helicases)
[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.15474


  8 / 25194 MEDLINE  
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[PMID]:29212662
[Au] Autor:Chatterjee K; Majumder S; Wan Y; Shah V; Wu J; Huang HY; Hopper AK
[Ad] Endereço:The Ohio State University Comprehensive Cancer Research Center, The Ohio State University, Columbus, Ohio 43210, USA.
[Ti] Título:Sharing the load: Mex67-Mtr2 cofunctions with Los1 in primary tRNA nuclear export.
[So] Source:Genes Dev;31(21):2186-2198, 2017 11 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic transfer RNAs (tRNAs) are exported from the nucleus, their site of synthesis, to the cytoplasm, their site of function for protein synthesis. The evolutionarily conserved ß-importin family member Los1 (Exportin-t) has been the only exporter known to execute nuclear export of newly transcribed intron-containing pre-tRNAs. Interestingly, is unessential in all tested organisms. As tRNA nuclear export is essential, we previously interrogated the budding yeast proteome to identify candidates that function in tRNA nuclear export. Here, we provide molecular, genetic, cytological, and biochemical evidence that the Mex67-Mtr2 (TAP-p15) heterodimer, best characterized for its essential role in mRNA nuclear export, cofunctions with Los1 in tRNA nuclear export. Inactivation of Mex67 or Mtr2 leads to rapid accumulation of end-matured unspliced tRNAs in the nucleus. Remarkably, merely fivefold overexpression of Mex67-Mtr2 can substitute for Los1 in Δ cells. Moreover, in vivo coimmunoprecipitation assays with tagged Mex67 document that the Mex67 binds tRNAs. Our data also show that tRNA exporters surprisingly exhibit differential tRNA substrate preferences. The existence of multiple tRNA exporters, each with different tRNA preferences, may indicate that the proteome can be regulated by tRNA nuclear export. Thus, our data show that Mex67-Mtr2 functions in primary nuclear export for a subset of yeast tRNAs.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular/genética
Proteoma/genética
RNA de Transferência/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Inativação Gênica
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Proteínas de Transporte Nucleocitoplasmático/genética
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Ligação Proteica
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Los1 protein, S cerevisiae); 0 (MEX67 protein, S cerevisiae); 0 (Membrane Transport Proteins); 0 (Mtr2 protein, S cerevisiae); 0 (Nuclear Pore Complex Proteins); 0 (Nuclear Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (Proteome); 0 (RNA-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1101/gad.305904.117


  9 / 25194 MEDLINE  
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[PMID]:29317621
[Au] Autor:Lau E; Cao Q; Lam MPY; Wang J; Ng DCM; Bleakley BJ; Lee JM; Liem DA; Wang D; Hermjakob H; Ping P
[Ad] Endereço:NIH BD2K Center of Excellence in Biomedical Computing, Los Angeles, CA, 90095, USA.
[Ti] Título:Integrated omics dissection of proteome dynamics during cardiac remodeling.
[So] Source:Nat Commun;9(1):120, 2018 01 09.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Transcript abundance and protein abundance show modest correlation in many biological models, but how this impacts disease signature discovery in omics experiments is rarely explored. Here we report an integrated omics approach, incorporating measurements of transcript abundance, protein abundance, and protein turnover to map the landscape of proteome remodeling in a mouse model of pathological cardiac hypertrophy. Analyzing the hypertrophy signatures that are reproducibly discovered from each omics data type across six genetic strains of mice, we find that the integration of transcript abundance, protein abundance, and protein turnover data leads to 75% gain in discovered disease gene candidates. Moreover, the inclusion of protein turnover measurements allows discovery of post-transcriptional regulations across diverse pathways, and implicates distinct disease proteins not found in steady-state transcript and protein abundance data. Our results suggest that multi-omics investigations of proteome dynamics provide important insights into disease pathogenesis in vivo.
[Mh] Termos MeSH primário: Cardiomegalia/metabolismo
Miocárdio/metabolismo
Proteoma/metabolismo
Proteômica/métodos
[Mh] Termos MeSH secundário: Animais
Remodelamento Atrial/genética
Cardiomegalia/genética
Perfilação da Expressão Gênica/métodos
Redes Reguladoras de Genes
Masculino
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos DBA
Camundongos Endogâmicos
Miocárdio/patologia
Proteoma/genética
Transcriptoma
Remodelação Ventricular/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Proteome)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02467-3


  10 / 25194 MEDLINE  
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[PMID]:28468631
[Au] Autor:Lakhdar R; Drost EM; MacNee W; Bastos R; Rabinovich RA
[Ad] Endereço:ELEGI Colt Laboratory, Centre for Inflammation Research, The Queen's Medical Research Institute, University of Edinburgh, 47 Little France Crescent, Edinburgh, EH16 4TJ, Scotland, UK.
[Ti] Título:2D-DIGE proteomic analysis of vastus lateralis from COPD patients with low and normal fat free mass index and healthy controls.
[So] Source:Respir Res;18(1):81, 2017 May 03.
[Is] ISSN:1465-993X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Chronic obstructive pulmonary disease (COPD) is associated with several extra-pulmonary effects of which skeletal muscle wasting is one of the most common and contributes to reduced quality of life, increased morbidity and mortality. The molecular mechanisms leading to muscle wasting are not fully understood. Proteomic analysis of human skeletal muscle is a useful approach for gaining insight into the molecular basis for normal and pathophysiological conditions. METHODS: To identify proteins involved in the process of muscle wasting in COPD, we searched differentially expressed proteins in the vastus lateralis of COPD patients with low fat free mass index (FFMI), as a surrogate of muscle mass (COPD n = 10) (FEV 33 ± 4.3% predicted, FFMI 15 ± 0.2 Kg.m ), in comparison to patients with COPD and normal FFMI (COPD n = 8) and a group of age, smoking history, and sex matched healthy controls (C, n = 9) using two-dimensional fluorescence difference in gel electrophoresis (2D-DIGE) technology, combined with mass spectrometry (MS). The effect of silencing DOT1L protein expression on markers of cell arrest was analyzed in skeletal muscle satellite cells (HSkMSCs) in vitro and assessed by qPCR and Western blotting. RESULTS: A subset of 7 proteins was differentially expressed in COPD compared to both COPD and C. We found an increased expression of proteins associated with muscle homeostasis and protection against oxidative stress, and a decreased expression of structural muscle proteins and proteins involved in myofibrillogenesis, cell proliferation, cell cycle arrest and energy production. Among these was a decreased expression of the histone methyltransferase DOT1L. In addition, silencing of the DOT1L gene in human skeletal muscle satellite cells in vitro was significantly related to up regulation of p21 /CDKN1A, a marker of cell arrest and ageing. CONCLUSIONS: 2D-DIGE coupled with MS identified differences in the expression of several proteins in the wasted vastus lateralis that are relevant to the disease process. Down regulation of DOT1L in the vastus lateralis of COPD patients may mediate the muscle wasting process through up regulation of markers of cell arrest and senescence.
[Mh] Termos MeSH primário: Índice de Massa Corporal
Proteínas Musculares/metabolismo
Atrofia Muscular/metabolismo
Proteoma/metabolismo
Doença Pulmonar Obstrutiva Crônica/metabolismo
Músculo Quadríceps/metabolismo
Eletroforese em Gel Diferencial Bidimensional/métodos
[Mh] Termos MeSH secundário: Idoso
Biomarcadores/metabolismo
Feminino
Seres Humanos
Masculino
Atrofia Muscular/etiologia
Atrofia Muscular/patologia
Tamanho do Órgão
Doença Pulmonar Obstrutiva Crônica/complicações
Doença Pulmonar Obstrutiva Crônica/patologia
Reprodutibilidade dos Testes
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Muscle Proteins); 0 (Proteome)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1186/s12931-017-0525-x



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