Base de dados : MEDLINE
Pesquisa : D08.811.277.656 [Categoria DeCS]
Referências encontradas : 28511 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 2852 ir para página                         

  1 / 28511 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28463415
[Au] Autor:McCullough SD; On DM; Bowers EC
[Ad] Endereço:National Health and Environmental Effects Research Laboratory, U.S. Environmental Protection Agency, Research Triangle Park, North Carolina.
[Ti] Título:Using Chromatin Immunoprecipitation in Toxicology: A Step-by-Step Guide to Increasing Efficiency, Reducing Variability, and Expanding Applications.
[So] Source:Curr Protoc Toxicol;72:3.14.1-3.14.28, 2017 May 02.
[Is] ISSN:1934-9262
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histone modifications work in concert with DNA methylation to regulate cellular structure, function, and response to environmental stimuli. More than 130 unique histone modifications have been described to date, and chromatin immunoprecipitation (ChIP) allows for the exploration of their associations with the regulatory regions of target genes and other DNA/chromatin-associated proteins across the genome. Many variations of ChIP have been developed in the 30 years since its earliest version came into use, which makes it challenging for users to integrate the procedure into their research programs. Furthermore, the differences in ChIP protocols can confound efforts to increase reproducibility across studies. The streamlined ChIP procedure presented here can be readily applied to samples from a wide range of in vitro studies (cell lines and primary cells) and clinical samples (peripheral leukocytes) in toxicology. We also provide detailed guidance on the optimization of critical protocol parameters, such as chromatin fixation, fragmentation, and immunoprecipitation, to increase efficiency and improve reproducibility. Expanding toxicoepigenetic studies to more readily include histone modifications will facilitate a more comprehensive understanding of the role of the epigenome in environmental exposure effects and the integration of epigenetic data in mechanistic toxicology, adverse outcome pathways, and risk assessment. © 2017 by John Wiley & Sons, Inc.
[Mh] Termos MeSH primário: Imunoprecipitação da Cromatina/métodos
Toxicologia/métodos
[Mh] Termos MeSH secundário: Linhagem Celular
DNA/isolamento & purificação
Epigênese Genética
Redes Reguladoras de Genes
Marcação de Genes
Histonas/metabolismo
Seres Humanos
Leucócitos/química
Peptídeo Hidrolases/química
Reação em Cadeia da Polimerase
Cultura Primária de Células
Reprodutibilidade dos Testes
Sonicação
Toxicologia/normas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); 9007-49-2 (DNA); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1002/cptx.22


  2 / 28511 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29422098
[Au] Autor:Huyben D; Boqvist S; Passoth V; Renström L; Allard Bengtsson U; Andréoletti O; Kiessling A; Lundh T; Vågsholm I
[Ad] Endereço:Department of Animal Nutrition and Management, Swedish University of Agricultural Sciences, 75007, Uppsala, Sweden. david.huyben@slu.se.
[Ti] Título:Screening of intact yeasts and cell extracts to reduce Scrapie prions during biotransformation of food waste.
[So] Source:Acta Vet Scand;60(1):9, 2018 Feb 08.
[Is] ISSN:1751-0147
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Yeasts can be used to convert organic food wastes to protein-rich animal feed in order to recapture nutrients. However, the reuse of animal-derived waste poses a risk for the transmission of infectious prions that can cause neurodegeneration and fatality in humans and animals. The aim of this study was to investigate the ability of yeasts to reduce prion activity during the biotransformation of waste substrates-thereby becoming a biosafety hurdle in such a circular food system. During pre-screening, 30 yeast isolates were spiked with Classical Scrapie prions and incubated for 72 h in casein substrate, as a waste substitute. Based on reduced Scrapie seeding activity, waste biotransformation and protease activities, intact cells and cell extracts of 10 yeasts were further tested. Prion analysis showed that five yeast species reduced Scrapie seeding activity by approximately 1 log10 or 90%. Cryptococcus laurentii showed the most potential to reduce prion activity since both intact and extracted cells reduced Scrapie by 1 log10 and achieved the highest protease activity. These results show that select forms of yeast can act as a prion hurdle during the biotransformation of waste. However, the limited ability of yeasts to reduce prion activity warrants caution as a sole barrier to transmission as higher log reductions are needed before using waste-cultured yeast in circular food systems.
[Mh] Termos MeSH primário: Biotransformação
Príons/metabolismo
Scrapie/prevenção & controle
Gerenciamento de Resíduos/métodos
Leveduras/metabolismo
[Mh] Termos MeSH secundário: Animais
Extratos Celulares/análise
Alimentos
Parasitologia de Alimentos/normas
Parasitologia de Alimentos/tendências
Peptídeo Hidrolases/metabolismo
Gerenciamento de Resíduos/normas
Leveduras/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Extracts); 0 (Prions); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180210
[St] Status:MEDLINE
[do] DOI:10.1186/s13028-018-0363-y


  3 / 28511 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28465355
[Au] Autor:Lan L; Guo M; Ai Y; Chen F; Zhang Y; Xia L; Huang D; Niu L; Zheng Y; Suzuki CK; Zhang Y; Liu Y; Lu B
[Ad] Endereço:Department of Biochemistry, Institute of Biophysics, Attardi Institute of Mitochondrial Biomedicine and Zhejiang Provincial Key Laboratory of Medical Genetics, School of Life Sciences, Wenzhou Medical University, Wenzhou, Zhejiang 325035, China.
[Ti] Título:Tetramethylpyrazine blocks TFAM degradation and up-regulates mitochondrial DNA copy number by interacting with TFAM.
[So] Source:Biosci Rep;37(3), 2017 Jun 30.
[Is] ISSN:1573-4935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The natural small molecule compound: 2,3,5,6-tetramethylpyrazine (TMP), is a major component of the Chinese medicine , which has wide clinical applications in dilating blood vessels, inhibiting platelet aggregation and treating thrombosis. Recent work suggests that TMP is also an antitumour agent. Despite its chemotherapeutic potential, the mechanism(s) underlying TMP action are unknown. Herein, we demonstrate that TMP binds to mitochondrial transcription factor A (TFAM) and blocks its degradation by the mitochondrial Lon protease. TFAM is a key regulator of mtDNA replication, transcription and transmission. Our previous work showed that when TFAM is not bound to DNA, it is rapidly degraded by the ATP-dependent Lon protease, which is essential for mitochondrial proteostasis. In cultured cells, TMP specifically blocks Lon-mediated degradation of TFAM, leading to TFAM accumulation and subsequent up-regulation of mtDNA content in cells with substantially low levels of mtDNA. protease assays show that TMP does not directly inhibit mitochondrial Lon, rather interacts with TFAM and blocks degradation. Pull-down assays show that biotinylated TMP interacts with TFAM. These findings suggest a novel mechanism whereby TMP stabilizes TFAM and confers resistance to Lon-mediated degradation, thereby promoting mtDNA up-regulation in cells with low mtDNA content.
[Mh] Termos MeSH primário: DNA Mitocondrial/efeitos dos fármacos
Proteínas de Ligação a DNA/genética
Dosagem de Genes/efeitos dos fármacos
Mitocôndrias/efeitos dos fármacos
Proteínas Mitocondriais/genética
Pirazinas/farmacologia
Fatores de Transcrição/genética
Regulação para Cima/efeitos dos fármacos
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Replicação do DNA/efeitos dos fármacos
Células HCT116
Células HeLa
Seres Humanos
Peptídeo Hidrolases/genética
Transcrição Genética/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (DNA-Binding Proteins); 0 (Mitochondrial Proteins); 0 (Pyrazines); 0 (TFAM protein, human); 0 (Transcription Factors); EC 3.4.- (Peptide Hydrolases); V80F4IA5XG (tetramethylpyrazine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  4 / 28511 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29334221
[Au] Autor:Liu L; Gong W; Sun X; Chen G; Wang L
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University , 27 Shandanan Road, Jinan 250100, China.
[Ti] Título:Extracellular Enzyme Composition and Functional Characteristics of Aspergillus niger An-76 Induced by Food Processing Byproducts and Based on Integrated Functional Omics.
[So] Source:J Agric Food Chem;66(5):1285-1295, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Byproducts of food processing can be utilized for the production of high-value-added enzyme cocktails. In this study, we utilized integrated functional omics technology to analyze composition and functional characteristics of extracellular enzymes produced by Aspergillus niger grown on food processing byproducts. The results showed that oligosaccharides constituted by arabinose, xylose, and glucose in wheat bran were able to efficiently induce the production of extracellular enzymes of A. niger. Compared with other substrates, wheat bran was more effective at inducing the secretion of ß-glucosidases from GH1 and GH3 families, as well as >50% of proteases from A1-family aspartic proteases. Compared with proteins induced by single wheat bran or soybean dregs, the protein yield induced by their mixture was doubled, and the time required to reach peak enzyme activity was shortened by 25%. This study provided a technical platform for the complex formulation of various substrates and functional analysis of extracellular enzymes.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Aspergillus niger/crescimento & desenvolvimento
Indução Enzimática/efeitos dos fármacos
Manipulação de Alimentos
Oligossacarídeos/farmacologia
Resíduos
[Mh] Termos MeSH secundário: Arabinose/farmacologia
Ácido Aspártico Proteases/biossíntese
Celulases/biossíntese
Fibras na Dieta/análise
Grãos Comestíveis/química
Fermentação
Glucose/farmacologia
Glicosídeo Hidrolases/biossíntese
Peptídeo Hidrolases/biossíntese
Xilose/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dietary Fiber); 0 (Oligosaccharides); 0 (Waste Products); A1TA934AKO (Xylose); B40ROO395Z (Arabinose); EC 3.2.1.- (Cellulases); EC 3.2.1.- (Glycoside Hydrolases); EC 3.4.- (Aspartic Acid Proteases); EC 3.4.- (Peptide Hydrolases); IY9XDZ35W2 (Glucose)
[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:180116
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05164


  5 / 28511 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29192497
[Au] Autor:Liang Q; Chalamaiah M; Ren X; Ma H; Wu J
[Ad] Endereço:School of Food and Biological Engineering, Jiangsu University , 301 Xuefu Road, Zhenjiang, Jiangsu 212013, China.
[Ti] Título:Identification of New Anti-inflammatory Peptides from Zein Hydrolysate after Simulated Gastrointestinal Digestion and Transport in Caco-2 Cells.
[So] Source:J Agric Food Chem;66(5):1114-1120, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chronic inflammation is an underlying contributor to various chronic diseases. The objectives of this study were to investigate the anti-inflammatory activity of zein hydrolysate after simulated gastrointestinal digestion and Caco-2 cell absorption and to identify novel anti-inflammatory peptides after transport across Caco-2 cells. Three zein hydrolysates were prepared and further digested using gastrointestinal proteases; their transports were studied in Caco-2 cells. Anti-inflammatory activity was studied in endothelial EA.hy926 cells. Three zein hydrolysates and their digests significantly decreased the expression of tumor necrosis factor-α (TNF-α) induced pro-inflammatory vascular cell adhesion molecule-1 (VCAM-1) by 37.3-66.0%. Eleven novel peptides with 5-9 amino acid residues were sequenced; three peptides showed strong anti-inflammatory activity by inhibiting the VCAM-1 by 54-38.9% and intercellular cell adhesion molecule-1 (ICAM-1) by 36.5-28.6% at 0.2 mM. A new approach to identify novel anti-inflammatory peptides that could survive gastrointestinal digestion and absorption was developed.
[Mh] Termos MeSH primário: Anti-Inflamatórios/análise
Digestão
Trato Gastrointestinal/metabolismo
Peptídeos/análise
Zeína/química
[Mh] Termos MeSH secundário: Anti-Inflamatórios/farmacologia
Transporte Biológico
Células CACO-2
Linhagem Celular
Trato Gastrointestinal/enzimologia
Seres Humanos
Hidrólise
Molécula 1 de Adesão Intercelular/efeitos dos fármacos
Peptídeo Hidrolases/metabolismo
Peptídeos/metabolismo
Peptídeos/farmacologia
Fator de Necrose Tumoral alfa/antagonistas & inibidores
Molécula 1 de Adesão de Célula Vascular/antagonistas & inibidores
Zeína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Peptides); 0 (Tumor Necrosis Factor-alpha); 0 (Vascular Cell Adhesion Molecule-1); 126547-89-5 (Intercellular Adhesion Molecule-1); 9010-66-6 (Zein); EC 3.4.- (Peptide Hydrolases)
[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:171202
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04562


  6 / 28511 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27771726
[Au] Autor:Obi AT; Andraska E; Kanthi Y; Luke CE; Elfline M; Madathilparambil S; Siahaan TJ; Jaffer FA; Wakefield TW; Raghavendran K; Henke PK
[Ad] Endereço:Conrad Jobst Vascular Research Laboratory, University of Michigan Medical School, Ann Arbor, Mich., USA.
[Ti] Título:Gram-Negative Pneumonia Alters Large-Vein Cell-Adhesion Molecule Profile and Potentiates Experimental Stasis Venous Thrombosis.
[So] Source:J Vasc Res;53(3-4):186-195, 2016.
[Is] ISSN:1423-0135
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Pneumonia is a significant risk factor for the development of venous thrombosis (VT). Cell-adhesion molecules (CAMs) are linked to the pathogenesis of both pneumonia and VT. We hypothesized that remote infection would confer a prothrombogenic milieu via systemic elevation of CAMs. METHODS: Lung injury was induced in wild-type (C57BL/6) mice by lung contusion or intratracheal inoculation with Klebsiella pneumoniae or saline controls. K. pneumoniae-treated mice and controls additionally underwent inferior vena cava (IVC) ligation to generate VT. RESULTS: Lung-contusion mice demonstrated no increase in E-selectin or P-selectin whereas mice infected with K. pneumoniae demonstrated increased circulating P-selectin, ICAM-1, VCAM-1 and thrombin-antithrombin (TAT) complexes. Mice with pneumonia formed VT 3 times larger than controls, demonstrated significantly more upregulation of vein-wall and systemic CAMs, and formed erythrocyte-rich thrombi. CONCLUSION: Elevated CAM expression was identified in mice with pneumonia, but not lung contusion, indicating that the type of inflammatory stimulus and the presence of infection drive the vein-wall response. Elevation of CAMs was associated with amplified VT and may represent an alternate mechanism by which to target the prevention of VT.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular/sangue
Infecções por Klebsiella/complicações
Klebsiella pneumoniae/patogenicidade
Pneumonia Bacteriana/complicações
Veia Cava Inferior/metabolismo
Trombose Venosa/etiologia
[Mh] Termos MeSH secundário: Lesão Pulmonar Aguda/sangue
Lesão Pulmonar Aguda/complicações
Animais
Antitrombina III
Moléculas de Adesão Celular/antagonistas & inibidores
Modelos Animais de Doenças
Fibrinolíticos/farmacologia
Molécula 1 de Adesão Intercelular/sangue
Infecções por Klebsiella/sangue
Infecções por Klebsiella/tratamento farmacológico
Infecções por Klebsiella/microbiologia
Ligadura
Masculino
Camundongos Endogâmicos C57BL
Selectina-P/sangue
Peptídeo Hidrolases/sangue
Pneumonia Bacteriana/sangue
Pneumonia Bacteriana/tratamento farmacológico
Pneumonia Bacteriana/microbiologia
Regulação para Cima
Molécula 1 de Adesão de Célula Vascular/sangue
Veia Cava Inferior/cirurgia
Trombose Venosa/sangue
Trombose Venosa/microbiologia
Trombose Venosa/prevenção & controle
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Fibrinolytic Agents); 0 (Icam1 protein, mouse); 0 (P-Selectin); 0 (Vascular Cell Adhesion Molecule-1); 0 (antithrombin III-protease complex); 126547-89-5 (Intercellular Adhesion Molecule-1); 9000-94-6 (Antithrombin III); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  7 / 28511 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29273505
[Au] Autor:Wadhawan M; Tiwari S; Sharma S; Rathaur S
[Ad] Endereço:Department of Biochemistry, Institute of Science, Banaras Hindu University, Varanasi, India.
[Ti] Título:Identification and characterization of a novel prolyl oligopeptidase in filarial parasite Setaria cervi.
[So] Source:Biochem Biophys Res Commun;495(3):2235-2241, 2018 01 15.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A 75 kDa serine protease having prolyl oligopeptidase activity has been purified from Setaria cervi, a bovine filarial parasite. The MALDI-MS/MS analysis of the purified protein revealed 6 peptides showing nearest match S9A (prolyl oligopeptidase) family protein from Plesiocystis pacifica. The ScPOP was found to be unique compared to mammalian POP with respect to its kinetic properties. To elucidate its role, filarial parasites were exposed to specific inhibitor of POP, Z-Pro-prolinal (ZPP) for 8 h. The inhibition of POP induced calcium signaling via phospholipase c stimulation which further triggered mitochondrial mediated apoptosis in filarial parasites.
[Mh] Termos MeSH primário: Apoptose/fisiologia
Sinalização do Cálcio/fisiologia
Mitocôndrias/enzimologia
Peptídeo Hidrolases/química
Peptídeo Hidrolases/metabolismo
Setaria (Nematoide)/enzimologia
Setaria (Nematoide)/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação
Ativação Enzimática
Ligação Proteica
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.4.- (Peptide Hydrolases); EC 3.4.- (oligopeptidase)
[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:171224
[St] Status:MEDLINE


  8 / 28511 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28456986
[Au] Autor:Rawlings ND
[Ad] Endereço:European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, Hinxton, Cambridge, CB10 1SD, UK. ndr@ebi.ac.uk.
[Ti] Título:Using the MEROPS Database for Investigation of Lysosomal Peptidases, Their Inhibitors, and Substrates.
[So] Source:Methods Mol Biol;1594:213-226, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This chapter describes how to retrieve data on lysosomal peptidases from the MEROPS database for proteolytic enzymes, their substrates and inhibitors ( http://merops.sanger.ac.uk ). Features described in this chapter include the summary page, pages for structure, interactions with inhibitors, substrates, literature and involvement in physiological pathways, and how to download data from the MEROPS FTP site. The lysosomal peptidase legumain is used as an example.
[Mh] Termos MeSH primário: Bases de Dados de Proteínas
Peptídeo Hidrolases/análise
Proteínas/análise
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Inibidores de Proteases
Proteínas/antagonistas & inibidores
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protease Inhibitors); 0 (Proteins); 0 (lysosomal proteins); EC 3.4.- (Peptide Hydrolases)
[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:170501
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6934-0_14


  9 / 28511 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27770804
[Au] Autor:Natarajan K; Gottipati KR; Berhane K; Samten B; Pendurthi U; Boggaram V
[Ad] Endereço:Department of Cellular and Molecular Biology, University of Texas Health Science Center at Tyler, 11937 US Highway 271, Tyler, TX, 75708-3154, USA.
[Ti] Título:Proteases and oxidant stress control organic dust induction of inflammatory gene expression in lung epithelial cells.
[So] Source:Respir Res;17(1):137, 2016 10 22.
[Is] ISSN:1465-993X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Persistant inflammatory responses to infectious agents and other components in organic dust underlie lung injury and development of respiratory diseases. Organic dust components responsible for eliciting inflammation and the mechanisms by which they cause lung inflammation are not fully understood. We studied the mechanisms by which protease activities in poultry dust extracts and intracellular oxidant stress induce inflammatory gene expression in A549 and Beas2B lung epithelial cells. METHODS: The effects of dust extracts on inflammatory gene expression were analyzed by quantitative polymerase chain reaction (qPCR), enzyme linked immunosorbent (ELISA) and western blot assays. Oxidant stress was probed by dihydroethidium (DHE) labeling, and immunostaining for 4-hydroxynonenal (4-HNE). Effects on interleukin-8 (IL-8) promoter regulation were determined by transient transfection assay. RESULTS: Dust extracts contained trypsin and elastase activities, and activated protease activated receptor (PAR)-1 and -2. Serine protease inhibitors and PAR-1 or PAR-2 knockdown suppressed inflammatory gene induction. Dust extract induction of IL-8 gene expression was associated with increased DHE-fluorescence and 4-HNE staining, and antioxidants suppressed inflammatory gene induction. Protease inhibitors and antioxidants suppressed protein kinase C and NF-κB activation and induction of IL-8 promoter activity in cells exposed to dust extract. CONCLUSIONS: Our studies demonstrate that proteases and intracellular oxidants control organic dust induction of inflammatory gene expression in lung epithelial cells. Targeting proteases and oxidant stress may serve as novel approaches for the treatment of organic dust induced lung diseases. This is the first report on the involvement of oxidant stress in the induction of inflammatory gene expression by organic dust.
[Mh] Termos MeSH primário: Poeira
Células Epiteliais/efeitos dos fármacos
Mediadores da Inflamação/metabolismo
Pulmão/efeitos dos fármacos
Compostos Orgânicos/toxicidade
Estresse Oxidativo/efeitos dos fármacos
Peptídeo Hidrolases/metabolismo
Pneumonia/induzido quimicamente
[Mh] Termos MeSH secundário: Células A549
Animais
Anti-Inflamatórios/farmacologia
Antioxidantes/farmacologia
Células Epiteliais/enzimologia
Regulação da Expressão Gênica
Abrigo para Animais
Seres Humanos
Exposição por Inalação/efeitos adversos
Interleucina-8/genética
Interleucina-8/metabolismo
Pulmão/enzimologia
Metaloproteinases da Matriz/genética
Metaloproteinases da Matriz/metabolismo
Pneumonia/enzimologia
Pneumonia/genética
Pneumonia/prevenção & controle
Aves Domésticas
Receptor PAR-1/genética
Receptor PAR-1/metabolismo
Receptor PAR-2/genética
Receptor PAR-2/metabolismo
Inibidores de Serino Proteinase/farmacologia
Transdução de Sinais/efeitos dos fármacos
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Antioxidants); 0 (Dust); 0 (IL8 protein, human); 0 (Inflammation Mediators); 0 (Interleukin-8); 0 (Organic Chemicals); 0 (Receptor, PAR-1); 0 (Receptor, PAR-2); 0 (Serine Proteinase Inhibitors); EC 3.4.- (Peptide Hydrolases); EC 3.4.24.- (Matrix Metalloproteinases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  10 / 28511 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29235321
[Au] Autor:Nidialkova NA; Varbanets LD; Chernyshenko VO
[Ti] Título:Isolation and purification of Bacillus thuringiensis var. israelensis IÐœV Ð’-7465 peptidase with specificity toward elastin and collagen.
[So] Source:Ukr Biochem J;88(3):18-28, 2016 May-Jun.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Peptidase of Bacillus thuringiensis var. israelensis IÐœV Ð’-7465 was isolated from culture supernatant using consecutive fractionations by an ammonium sulphate (60% saturation), ion-exchange chromatography and gel-filtration on the TSK-gels Toyoperl HW-55 and DEAE 650(M). Specific elastase (442 U∙mg of protein-1) and collagenase (212.7 U∙mg of protein-1) activities of the purified enzyme preparation were 8.0- and 6.1-fold, respectively higher than ones of the culture supernatant. Peptidase yields were 33.5% for elastase activity and 30.1% for collagenase activity. It was established that the enzyme is serine metal-dependent alkaline peptidase with Mr about 37 kDa. Maximal hydrolysis of elastin and collagen occurs at the optimum pH 8.0 and t° ­ 40 and 50 °Ð¡, respectively. The purified preparation has high stability at pH in the range of 7.0 to 10.0 and 40-50 °Ð¡.
[Mh] Termos MeSH primário: Bacillus thuringiensis/química
Proteínas de Bactérias/isolamento & purificação
Colágeno/química
Elastina/química
Peptídeo Hidrolases/isolamento & purificação
[Mh] Termos MeSH secundário: Sulfato de Amônio/química
Bacillus thuringiensis/enzimologia
Proteínas de Bactérias/química
Cromatografia em Gel
Cromatografia por Troca Iônica
Ensaios Enzimáticos
Estabilidade Enzimática
Concentração de Íons de Hidrogênio
Hidrólise
Peso Molecular
Peptídeo Hidrolases/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 9007-34-5 (Collagen); 9007-58-3 (Elastin); EC 3.4.- (Peptide Hydrolases); SU46BAM238 (Ammonium Sulfate)
[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:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.03.018



página 1 de 2852 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde