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Pesquisa : D12.644.848.906 [Categoria DeCS]
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[PMID]:28735872
[Au] Autor:Cardoso THS; Lu S; Gonzalez BRG; Torquato RJS; Tanaka AS
[Ad] Endereço:Department of Biochemistry, Escola Paulista de Medicina, Universidade de Federal de São Paulo (UNIFESP), Rua 3 de Maio 100, 04044-020 São Paulo, SP, Brazil.
[Ti] Título:Characterization of a novel cystatin type 2 from Rhipicephalus microplus midgut.
[So] Source:Biochimie;140:117-121, 2017 Sep.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The Rhipicephalus (Boophilus) microplus is an exclusive bovine ectoparasite responsible for the transmission of pathogens that decrease meat, leather and milk productions. Cattle vaccination is an alternative to control tick infestations, but the discovery of potential antigens is still a challenge for researchers. Recently, our group performed a midgut transcriptome of engorged R. microplus tick, and out of 800 ESTs sequences one cystatin-coding sequence was identified and named Rmcystatin-4. In order to understand the physiological role of Rmcystatin-4, the aim of this work was the expression, purification and functional characterization of a novel type 2 cystatin from the tick R. microplus. Rmcystatin-4 gene expression was identified mostly in tick midgut suggesting its possible role in blood digestion control. Our data showed that rRmcystatin-4 was successfully expressed in active form using Pichia pastoris system and the purified inhibitor presented high selectivity to BmCl-1 (Ki = 0.046 nM). Moreover, rRmcystatin-4 was able to impaired BmCl-1 activity towards bovine hemoglobin.
[Mh] Termos MeSH primário: Proteínas de Artrópodes
Intestinos/metabolismo
Rhipicephalus
Cistatinas Salivares
[Mh] Termos MeSH secundário: Animais
Proteínas de Artrópodes/biossíntese
Proteínas de Artrópodes/química
Proteínas de Artrópodes/genética
Proteínas de Artrópodes/isolamento & purificação
Bovinos
Expressão Gênica
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Rhipicephalus/química
Rhipicephalus/genética
Rhipicephalus/metabolismo
Cistatinas Salivares/biossíntese
Cistatinas Salivares/química
Cistatinas Salivares/genética
Cistatinas Salivares/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Recombinant Proteins); 0 (Salivary Cystatins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE


  2 / 118 MEDLINE  
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[PMID]:28667066
[Au] Autor:Go YM; Jones DP
[Ad] Endereço:Division of Pulmonary Medicine, Department of Medicine, Emory University, Atlanta, GA 30322, U.S.A.
[Ti] Título:Redox theory of aging: implications for health and disease.
[So] Source:Clin Sci (Lond);131(14):1669-1688, 2017 Jul 15.
[Is] ISSN:1470-8736
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Genetics ultimately defines an individual, yet the phenotype of an adult is extensively determined by the sequence of lifelong exposures, termed the exposome. The redox theory of aging recognizes that animals evolved within an oxygen-rich environment, which created a critical redox interface between an organism and its environment. Advances in redox biology show that redox elements are present throughout metabolic and structural systems and operate as functional networks to support the genome in adaptation to environmental resources and challenges during lifespan. These principles emphasize that physical and functional phenotypes of an adult are determined by gene-environment interactions from early life onward. The principles highlight the critical nature of cumulative exposure memories in defining changes in resilience progressively during life. Both plasma glutathione and cysteine systems become oxidized with aging, and the recent finding that cystine to glutathione ratio in human plasma predicts death in coronary artery disease (CAD) patients suggests this could provide a way to measure resilience of redox networks in aging and disease. The emerging concepts of cumulative gene-environment interactions warrant focused efforts to elucidate central mechanisms by which exposure memory governs health and etiology, onset and progression of disease.
[Mh] Termos MeSH primário: Envelhecimento/fisiologia
Oxirredução
[Mh] Termos MeSH secundário: Biomarcadores/sangue
Doença da Artéria Coronariana/sangue
Interação Gene-Ambiente
Glutationa/sangue
Seres Humanos
Metais/metabolismo
Modelos Biológicos
Estresse Oxidativo/fisiologia
Medicina Regenerativa/métodos
Cistatinas Salivares/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biomarkers); 0 (CST4 protein, human); 0 (Metals); 0 (Salivary Cystatins); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170702
[St] Status:MEDLINE
[do] DOI:10.1042/CS20160897


  3 / 118 MEDLINE  
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[PMID]:28339625
[Au] Autor:Martini D; Gallo A; Vella S; Sernissi F; Cecchettini A; Luciano N; Polizzi E; Conaldi PG; Mosca M; Baldini C
[Ad] Endereço:Department of Clinical and Experimental Medicine, University of Pisa.
[Ti] Título:Cystatin S-a candidate biomarker for severity of submandibular gland involvement in Sjögren's syndrome.
[So] Source:Rheumatology (Oxford);56(6):1031-1038, 2017 Jun 01.
[Is] ISSN:1462-0332
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Objectives.: Salivary cystatin S is a defence protein mainly produced by submandibular glands and involved in innate oral immunity. This study aimed to verify whether cystatin S was diversely expressed in different disease subsets of primary Sjogren's syndrome (pSS) patients, defined on the basis of salivary flow [unstimulated salivary flow rate (USFR)], minor salivary gland (MSG) focus score and submandibular gland ultrasonography abnormalities. We also evaluated miR-126 and miR-335-5p expression in MSG biopsies to verify whether an aberrant regulation of cystatin S at the glandular level may influence its salivary expression. Methods.: Forty pSS patients and 20 sex- and age-matched healthy volunteers were included. Salivary cystatin S levels were assessed by western blot analysis using a stain-free technology. The expression of miR-126, miR-335-5p and cystatin S was assessed by quantitative PCR in 15 MSG biopsies differing for USFR and MSG focus score. Results.: We found that salivary cystatin S was significantly decreased in pSS patients vs healthy volunteers ( P = 0.000), especially in those with hyposalivation. A positive correlation was observed between cystatin S and USFR ( r = 0.75, P = 0.01). Salivary cystatin S was also significantly reduced in patients with a submandibular gland ultrasonography score ⩾2. The expression levels of miR-126 and miR-335-5P increased in inverse proportion with USFR. The mRNA of cystatin S did not change significantly, suggesting post-transcriptional regulation. Conclusion.: Cystatin S emerged as a promising biomarker for pSS, strongly correlated with glandular dysfunction. An upregulation of miR-126 and miR-335-5P might be implicated in its expression.
[Mh] Termos MeSH primário: Cistatinas Salivares/metabolismo
Síndrome de Sjogren/complicações
Doenças da Glândula Submandibular/etiologia
[Mh] Termos MeSH secundário: Biomarcadores/metabolismo
Estudos de Casos e Controles
Feminino
Seres Humanos
MicroRNAs/metabolismo
MicroRNAs/fisiologia
Meia-Idade
Saliva/secreção
Síndrome de Sjogren/metabolismo
Glândula Submandibular/metabolismo
Doenças da Glândula Submandibular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (MIRN126 microRNA, human); 0 (MIRN335 microRNA, human); 0 (MicroRNAs); 0 (Salivary Cystatins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE
[do] DOI:10.1093/rheumatology/kew501


  4 / 118 MEDLINE  
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[PMID]:28300829
[Au] Autor:Oh BM; Lee SJ; Cho HJ; Park YS; Kim JT; Yoon SR; Lee SC; Lim JS; Kim BY; Choe YK; Lee HG
[Ad] Endereço:Immunotherapy Convergence Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea.
[Ti] Título:Cystatin SN inhibits auranofin-induced cell death by autophagic induction and ROS regulation via glutathione reductase activity in colorectal cancer.
[So] Source:Cell Death Dis;8(3):e2682, 2017 Mar 16.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cystatin SN (CST1) is a specific inhibitor belonging to the cystatin superfamily that controls the proteolytic activities of cysteine proteases such as cathepsins. Our previous study showed that high CST1 expression enhances tumor metastasis and invasiveness in colorectal cancer. Recently, auranofin (AF), a gold(I)-containing thioredoxin reductase 1 (TrxR1) inhibitor, has been used clinically to treat rheumatoid arthritis. AF is a proteasome-associated deubiquitinase inhibitor and can act as an anti-tumor agent. In this study, we investigated whether CST1 expression induces autophagy and tumor cell survival. We also investigated the therapeutic effects of AF as an anti-tumor agent in colorectal cancer (CRC) cells. We found that CRC cells expressing high levels of CST1 undergo increased autophagy and exhibit chemotherapeutic resistance to AF-induced cell death, while those expressing low levels of CST1 are sensitive to AF. We also observed that knockdown of CST1 in high-CST1 CRC cells using CST1-specific small interfering RNAs attenuated autophagic activation and restored AF-induced cell mortality. Conversely, the overexpression of CST1 increased autophagy and viability in cells expressing low levels of CST1. Interestingly, high expression of CST1 attenuates AF-induced cell death by inhibiting intracellular reactive oxygen species (ROS) generation, as demonstrated by the fact that the blockage of ROS production reversed AF-induced cell death in CRC cells. In addition, upregulation of CST1 expression increased cellular glutathione reductase (GR) activity, reducing the cellular redox state and inducing autophagy in AF-treated CRC cells. These results suggest that high CST1 expression may be involved in autophagic induction and protects from AF-induced cell death by inhibition of ROS generation through the regulation of GR activity.
[Mh] Termos MeSH primário: Auranofina/farmacologia
Autofagia/efeitos dos fármacos
Morte Celular/efeitos dos fármacos
Neoplasias Colorretais/metabolismo
Glutationa Redutase/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Cistatinas Salivares/farmacologia
[Mh] Termos MeSH secundário: Catepsinas/farmacologia
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Células HCT116
Células HT29
Seres Humanos
Oxirredução/efeitos dos fármacos
Complexo de Endopeptidases do Proteassoma/metabolismo
Inibidores de Proteassoma/farmacologia
Cistatinas Salivares/metabolismo
Tiorredoxina Redutase 1/metabolismo
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CST1 protein, human); 0 (Proteasome Inhibitors); 0 (Reactive Oxygen Species); 0 (Salivary Cystatins); 3H04W2810V (Auranofin); EC 1.8.1.7 (Glutathione Reductase); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 3.4.- (Cathepsins); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2017.100


  5 / 118 MEDLINE  
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[PMID]:28055279
[Au] Autor:Marvin RK; Saepoo MB; Ye S; White DB; Liu R; Hensley K; Rega P; Kazan V; Giovannucci DR; Isailovic D
[Ad] Endereço:a Department of Chemistry and Biochemistry , University of Toledo , Toledo , OH , USA.
[Ti] Título:Salivary protein changes in response to acute stress in medical residents performing advanced clinical simulations: a pilot proteomics study.
[So] Source:Biomarkers;22(3-4):372-382, 2017 May - Jun.
[Is] ISSN:1366-5804
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:CONTEXT: Quantitative changes of salivary proteins due to acute stress were detected. OBJECTIVE: To explore protein markers of stress in saliva of eight medical residents who performed emergency medicine simulations. MATERIALS AND METHODS: Saliva was collected before the simulations, after the simulations, and following morning upon waking. Proteins were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), identified by mass spectrometry (MS), and relatively quantified by densitometry. RESULTS: Salivary alpha-amylase and S-type cystatins significantly increased, while the ∼26 kDa and low-molecular weight (MW) (<10 kDa) SDS-PAGE bands exhibited changes after stress. DISCUSSION AND CONCLUSION: Alpha-amylase and cystatins are potential salivary markers of acute stress, but further validation should be performed using larger sample populations.
[Mh] Termos MeSH primário: Proteômica/métodos
Proteínas e Peptídeos Salivares/metabolismo
Estresse Psicológico/metabolismo
[Mh] Termos MeSH secundário: Adulto
Eletroforese em Gel de Poliacrilamida
Serviços Médicos de Emergência/métodos
Feminino
Seres Humanos
Internato e Residência
Masculino
Espectrometria de Massas
Projetos Piloto
Cistatinas Salivares/análise
Proteínas e Peptídeos Salivares/análise
Adulto Jovem
alfa-Amilases/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Salivary Cystatins); 0 (Salivary Proteins and Peptides); EC 3.2.1.1 (alpha-Amylases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170106
[St] Status:MEDLINE
[do] DOI:10.1080/1354750X.2017.1279215


  6 / 118 MEDLINE  
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[PMID]:27764212
[Au] Autor:Nandy SK; Seal A
[Ad] Endereço:Department of Biochemistry & Biophysics, University of Kalyani, Kalyani, West Bengal, India.
[Ti] Título:Structural Dynamics Investigation of Human Family 1 & 2 Cystatin-Cathepsin L1 Interaction: A Comparison of Binding Modes.
[So] Source:PLoS One;11(10):e0164970, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cystatin superfamily is a large group of evolutionarily related proteins involved in numerous physiological activities through their inhibitory activity towards cysteine proteases. Despite sharing the same cystatin fold, and inhibiting cysteine proteases through the same tripartite edge involving highly conserved N-terminal region, L1 and L2 loop; cystatins differ widely in their inhibitory affinity towards C1 family of cysteine proteases and molecular details of these interactions are still elusive. In this study, inhibitory interactions of human family 1 & 2 cystatins with cathepsin L1 are predicted and their stability and viability are verified through protein docking & comparative molecular dynamics. An overall stabilization effect is observed in all cystatins on complex formation. Complexes are mostly dominated by van der Waals interaction but the relative participation of the conserved regions varied extensively. While van der Waals contacts prevail in L1 and L2 loop, N-terminal segment chiefly acts as electrostatic interaction site. In fact the comparative dynamics study points towards the instrumental role of L1 loop in directing the total interaction profile of the complex either towards electrostatic or van der Waals contacts. The key amino acid residues surfaced via interaction energy, hydrogen bonding and solvent accessible surface area analysis for each cystatin-cathepsin L1 complex influence the mode of binding and thus control the diverse inhibitory affinity of cystatins towards cysteine proteases.
[Mh] Termos MeSH primário: Catepsina L/metabolismo
Cistatinas Salivares/química
Cistatinas Salivares/metabolismo
[Mh] Termos MeSH secundário: Sequência Conservada
Seres Humanos
Ligações de Hidrogênio
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
Ligação Proteica
Conformação Proteica
Estabilidade Proteica
Termodinâmica
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CST1 protein, human); 0 (CST2 protein, human); 0 (Salivary Cystatins); EC 3.4.22.15 (Cathepsin L)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161021
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0164970


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[PMID]:25809904
[Au] Autor:Prodan A; Brand HS; Ligtenberg AJ; Imangaliyev S; Tsivtsivadze E; van der Weijden F; Crielaard W; Keijser BJ; Veerman EC
[Ad] Endereço:Top Institute Food and Nutrition, Wageningen, The Netherlands; Department of Oral Biochemistry, Academic Center for Dentistry Amsterdam (ACTA), University of Amsterdam and Free University Amsterdam, Amsterdam, The Netherlands.
[Ti] Título:Interindividual variation, correlations, and sex-related differences in the salivary biochemistry of young healthy adults.
[So] Source:Eur J Oral Sci;123(3):149-57, 2015 Jun.
[Is] ISSN:1600-0722
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A cross-sectional observational study was conducted to evaluate interindividual biochemical variation in unstimulated whole saliva in a population of 268 systemically healthy young students, 18-30 yr of age, with no apparent caries lesions or periodontal disease. Salivary flow rate, protein content, pH, buffering capacity, mucins MUC5B and MUC7, albumin, secretory IgA, cystatin S, lactoferrin, chitinase, amylase, lysozyme, and proteases were measured using ELISAs and enzymatic activity assays. Significant differences were found between male and female subjects. Salivary pH, buffering capacity, protein content, MUC5B, secretory IgA, and chitinase activity were all lower in female subjects compared with male subjects, whereas MUC7 and lysozyme activity were higher in female subjects. There was no significant difference between sexes in salivary flow rate, albumin, cystatin S, amylase, and protease activity. Principal component analysis (PCA) and spectral clustering (SC) were used to assess intervariable relationships within the data set and to identify subgroups. Spectral clustering identified two clusters of participants, which were subsequently described. This study provides a comprehensive overview of the distribution and inter-relations of a set of important salivary biochemical variables in a systemically healthy young adult population, free of apparent caries lesions and periodontal disease. It highlights significant gender differences in salivary biochemistry.
[Mh] Termos MeSH primário: Saliva/química
[Mh] Termos MeSH secundário: Adolescente
Adulto
Albuminas/análise
Amilases/análise
Tampões (Química)
Quitinases/análise
Análise por Conglomerados
Estudos Transversais
Feminino
Seres Humanos
Concentração de Íons de Hidrogênio
Imunoglobulina A Secretora/análise
Lactoferrina/análise
Masculino
Mucina-5B/análise
Mucinas/análise
Muramidase/análise
Peptídeo Hidrolases/análise
Análise de Componente Principal
Saliva/fisiologia
Saliva/secreção
Cistatinas Salivares/análise
Proteínas e Peptídeos Salivares/análise
Taxa Secretória/fisiologia
Fatores Sexuais
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Albumins); 0 (Buffers); 0 (CST4 protein, human); 0 (Immunoglobulin A, Secretory); 0 (MUC5B protein, human); 0 (MUC7 protein, human); 0 (Mucin-5B); 0 (Mucins); 0 (Salivary Cystatins); 0 (Salivary Proteins and Peptides); EC 3.2.1.- (Amylases); EC 3.2.1.14 (Chitinases); EC 3.2.1.17 (Muramidase); EC 3.4.- (Peptide Hydrolases); EC 3.4.21.- (Lactoferrin)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170103
[Lr] Data última revisão:
170103
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:150327
[St] Status:MEDLINE
[do] DOI:10.1111/eos.12182


  8 / 118 MEDLINE  
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[PMID]:25648368
[Au] Autor:Cao X; Li Y; Luo RZ; Zhang L; Zhang SL; Zeng J; Han YJ; Wen ZS
[Ad] Endereço:Sun Yat-Sen University Cancer Center, State Key Laboratory of Oncology in South China, Collaborative Innovation Center of Cancer Medicine, Guangzhou, China.
[Ti] Título:Expression of Cystatin SN significantly correlates with recurrence, metastasis, and survival duration in surgically resected non-small cell lung cancer patients.
[So] Source:Sci Rep;5:8230, 2015 Feb 04.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cystatin SN has been considered to be involved in human cancer, but its clinical significance in non-small cell lung cancer (NSCLC) has not been elucidated. The aim of this study was to evaluate the clinical value of Cystatin SN expression in patients with surgically resected NSCLCs. A retrospective analysis of 174 patients with surgically resected NSCLCs from April 2002 to March 2005 was performed with immunohistochemistry and fluorescence in situ hybridization to analyze the protein expression and amplification of Cystatin SN. The associations between Cystatin SN expression and recurrence, metastasis, and survival were investigated. In recurrence and metastasis analysis, compared with low-Cystatin SN expression NSCLCs, high expression tumors were more likely to recur and metastasize (P < 0.001). Disease-free survival (DFS) and overall survival (OS) were significantly prolonged in the low-Cystatin SN expression subgroup compared with the high-Cystatin SN expression subgroup (DFS, P < 0.001; OS, P = 0.001). A multivariate analysis confirmed that high expression of Cystatin SN was associated with poor survival (DFS, P = 0.001; OS, P = 0.006) and was an independent prognostic indicator. The present study indicates that high expression of Cystatin SN is a significant prognostic indicator of a higher rate of recurrence, metastatic risk, and poor survival in patients with surgically resected NSCLCs.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/genética
Carcinoma Pulmonar de Células não Pequenas/patologia
Expressão Gênica
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/patologia
Cistatinas Salivares/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Carcinoma Pulmonar de Células não Pequenas/mortalidade
Carcinoma Pulmonar de Células não Pequenas/cirurgia
Progressão da Doença
Feminino
Amplificação de Genes
Seres Humanos
Neoplasias Pulmonares/mortalidade
Neoplasias Pulmonares/cirurgia
Masculino
Meia-Idade
Gradação de Tumores
Metástase Neoplásica
Recidiva Local de Neoplasia
Estadiamento de Neoplasias
Prognóstico
Cistatinas Salivares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CST1 protein, human); 0 (Salivary Cystatins)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150212
[Lr] Data última revisão:
150212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150205
[St] Status:MEDLINE
[do] DOI:10.1038/srep08230


  9 / 118 MEDLINE  
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[PMID]:25577248
[Au] Autor:Jiang J; Liu HL; Liu ZH; Tan SW; Wu B
[Ad] Endereço:Department of Gastroenterology, The Third Affiliated Hospital of Sun Yat-Sen University, 600 Tianhe Road, Guangzhou, 510630, China.
[Ti] Título:Identification of cystatin SN as a novel biomarker for pancreatic cancer.
[So] Source:Tumour Biol;36(5):3903-10, 2015 May.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cystatin SN (cystatin 1, CST1) is a member of the cystatin superfamily that inhibits the proteolytic activity of cysteine proteases. CST1 is a tumor biomarker that provides useful information for the diagnosis of esophageal, gastric, and colorectal carcinomas. However, the significance of CST1 in pancreatic cancer is unknown. The aim of this study was to assess whether CST1 is a potential biomarker for early diagnosis of malignant pancreatic neoplasms. Microarray analysis of mRNA extracted from pancreatic cancer and pancreatic normal tissues was performed. Bioinformatics revealed that CST1 was one of the highest expressed genes on the array in pancreatic cancer, compared with normal tissue. In addition, the upregulation of CST1 in pancreatic cancer and several pancreatic cancer cell lines was confirmed using real-time PCR (RT-PCR), immunohistochemistry, and Western blotting. Next, CST1 knockdown using siRNA reduced the expression of the proliferation-related proteins p-AKT and PCNA significantly, as well as colony formation and xenograft development in vitro. Consistent with this, CST1 mRNA overexpression was correlated closely with malignancy-associated proteins such as PCNA, cyclin D1, cyclin A2, and cyclin E in pancreatic cancer cell lines. In conclusion, our data suggest that CST1 might contribute to the proliferation of pancreatic cancer cells and could be a potential biomarker for the early detection of pancreatic cancer.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/biossíntese
Carcinogênese
Detecção Precoce de Câncer
Neoplasias Pancreáticas/genética
Cistatinas Salivares/biossíntese
[Mh] Termos MeSH secundário: Biomarcadores Tumorais/genética
Linhagem Celular Tumoral
Proliferação Celular/genética
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Análise em Microsséries
Meia-Idade
Neoplasias Pancreáticas/diagnóstico
Neoplasias Pancreáticas/patologia
RNA Mensageiro/biossíntese
Cistatinas Salivares/genética
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (CST1 protein, human); 0 (RNA, Messenger); 0 (Salivary Cystatins)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150112
[St] Status:MEDLINE
[do] DOI:10.1007/s13277-014-3033-3


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[PMID]:25408129
[Au] Autor:Lieskovská J; Páleníková J; Sirmarová J; Elsterová J; Kotsyfakis M; Campos Chagas A; Calvo E; Ruzek D; Kopecký J
[Ad] Endereço:Faculty of Science, University of South Bohemia, Ceské Budejovice, Czech Republic; Institute of Parasitology, Biology Centre of the Academy of Sciences of the Czech Republic, Ceské Budejovice, Czech Republic.
[Ti] Título:Tick salivary cystatin sialostatin L2 suppresses IFN responses in mouse dendritic cells.
[So] Source:Parasite Immunol;37(2):70-8, 2015 Feb.
[Is] ISSN:1365-3024
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Type I interferon (IFN), mainly produced by dendritic cells (DCs), is critical in the host defence against tick-transmitted pathogens. Here, we report that salivary cysteine protease inhibitor from the hard tick Ixodes scapularis, sialostatin L2, affects IFN-ß mediated immune reactions in mouse dendritic cells. Following IFN receptor ligation, the Janus activated kinases/signal transducer and activator of transcription (JAK/STAT) pathway is activated. We show that sialostatin L2 attenuates phosphorylation of STATs in spleen dendritic cells upon addition of recombinant IFN-ß. LPS-stimulated dendritic cells release IFN-ß which in turn leads to the induction of IFN-stimulated genes (ISG) through JAK/STAT pathway activation. The induction of two ISG, interferon regulatory factor 7 (IRF-7) and IP-10, was suppressed by sialostatin L2 in LPS-stimulated dendritic cells. Finally, the interference of sialostatin L2 with IFN action led to the enhanced replication of tick-borne encephalitis virus in DC. In summary, we present here that tick salivary cystatin negatively affects IFN-ß responses which may consequently increase the pathogen load after transmission via tick saliva.
[Mh] Termos MeSH primário: Borrelia burgdorferi/fisiologia
Cistatinas/imunologia
Células Dendríticas/imunologia
Interferon beta/imunologia
Ixodes/imunologia
Cistatinas Salivares/imunologia
[Mh] Termos MeSH secundário: Animais
Feminino
Fator Regulador 7 de Interferon/imunologia
Ixodes/microbiologia
Lipopolissacarídeos/imunologia
Camundongos
Camundongos Endogâmicos C57BL
Fosforilação
Receptores de Citocinas/imunologia
Receptores de Interferon/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cystatins); 0 (IP10-Mig receptor); 0 (Interferon Regulatory Factor-7); 0 (Irf7 protein, mouse); 0 (Lipopolysaccharides); 0 (Receptors, Cytokine); 0 (Receptors, Interferon); 0 (Salivary Cystatins); 0 (sialostatin L, Ixodes scapularis); 77238-31-4 (Interferon-beta)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:150123
[Lr] Data última revisão:
150123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141120
[St] Status:MEDLINE
[do] DOI:10.1111/pim.12162



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