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  1 / 1406 MEDLINE  
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[PMID]:29187444
[Au] Autor:Pei JS; Chou AK; Hsu PC; Tsai CW; Chang WS; Wu MF; Wu MH; Hsia TC; Cheng SP; Bau DT
[Ad] Endereço:Department of Pediatrics, Taoyuan General Hospital, Ministry of Health and Welfare, Taoyuan, Taiwan, R.O.C.
[Ti] Título:Contribution of Matrix Metalloproteinase-7 Genotypes to the Risk of Non-solid Tumor, Childhood Leukemia.
[So] Source:Anticancer Res;37(12):6679-6684, 2017 12.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: The matrix metalloproteinases (MMPs) are important in inflammation and carcinogenesis, and the genotypic role of MMP7 has never been examined in leukemia to date. Therefore, in this study we aimed to evaluate the contribution of the genotypic variants in the promoter region of MMP7 (A-181G and C-153T) to childhood acute lymphoblastic leukemia (ALL) risk in Taiwan. MATERIALS AND METHODS: In this case-control study, 266 patients with childhood ALL and 266 non-cancer controls were genotyped by polymerase chain reaction-restriction fragment length polymorphism methodology. RESULTS: The distribution of AA, AG and GG for MMP7 promoter A-181G genotype was 83.5, 12.0 and 4.5% in the childhood ALL group and 89.8%, 9.4 and 0.8% in the non-cancer control group, respectively (p for trend=0.0134), significantly differentially distributed between childhood ALL and control groups. The comparisons in allelic frequency distribution also support the findings that G appears to be the risky allele in childhood ALL. In genotype and gender interaction analysis, it was found that boys carrying the MMP7 A-181G GG and AG+GG genotypes had 9.05- and 2.45-fold odds ratios (ORs) (p=0.0135 and 0.0142, respectively) for childhood ALL compared to those carrying wild-type AA genotype. But these differences were not found in girls. Analysis of genotype interaction with age of onset age showed those aged less than 3.5 years at onset carrying the GG or AG+GG genotypes also had elevated ORs of 8.79- and 2.04-fold (p=0.0150 and 0.0413, respectively) for childhood ALL, but there was no such difference for those having an age at onset of 3.5 years or more. CONCLUSION: Our results indicate that the MMP7 A-181G genotype interacts with age and gender and may serve as an early and predictive biomarker for childhood ALL.
[Mh] Termos MeSH primário: Predisposição Genética para Doença/genética
Metaloproteinase 7 da Matriz/genética
Leucemia-Linfoma Linfoblástico de Células Precursoras/genética
Regiões Promotoras Genéticas/genética
[Mh] Termos MeSH secundário: Grupo com Ancestrais do Continente Asiático/genética
Estudos de Casos e Controles
Criança
Feminino
Frequência do Gene
Predisposição Genética para Doença/etnologia
Genótipo
Seres Humanos
Masculino
Razão de Chances
Polimorfismo de Nucleotídeo Único
Leucemia-Linfoma Linfoblástico de Células Precursoras/etnologia
Fatores de Risco
Taiwan
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.24.23 (Matrix Metalloproteinase 7)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE


  2 / 1406 MEDLINE  
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[PMID]:28982905
[Au] Autor:Yoshida K; Matsuyama R; Mori R; Kumamoto T; Matsuo K; Takeda K; Sugita M; Fujii Y; Tanaka K; Shimada H; Endo I
[Ad] Endereço:Department of Gastroenterological Surgery, Yokohama City University Graduate School of Medicine, Yokohama, Japan kenichi@rd5.so-net.ne.jp.
[Ti] Título:Immunohistochemical Comparison of Malignancy Between Radial Invasion and Mucosal Extension in Hilar Cholangiocarcinoma.
[So] Source:Anticancer Res;37(10):5805-5812, 2017 10.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:AIM: To compare the cells of mucosal extension (ME) and radial invasion (RI) in hilar cholangiocarcinoma (HCCA) for optimal resection. MATERIALS AND METHODS: Forty-six patients underwent surgery for HCCA between 1992 and 2004. Immunohistochemical expressions of p53, Ki-67, matrix metalloproteinase-7 (MMP7), mucin 1 (MUC1), and E-cadherin were assessed at five different sites of the tumour and compared between the recurrence and non-recurrence groups. RESULTS: Expression of E-cadherin was significantly lower in RI cells than in ME cells, and that of MMP7 and MUC1 was significantly higher in RI cells than in ME cells. Ki-67 expression was higher in ME cells than in RI cells. During the 11-year follow-up, recurrence in patients with R0 resection was associated with significantly lower E-cadherin, higher MMP7, and higher Ki-67 expression. CONCLUSION: Removal of as many RI cells as possible should be a priority in resection of HCCA, followed by removal of ME cells. E-Cadherin appears to be associated with recurrence of HCCA.
[Mh] Termos MeSH primário: Neoplasias dos Ductos Biliares/química
Neoplasias dos Ductos Biliares/patologia
Biomarcadores Tumorais/análise
Imuno-Histoquímica
Tumor de Klatskin/química
Tumor de Klatskin/patologia
Membrana Mucosa/patologia
[Mh] Termos MeSH secundário: Idoso
Neoplasias dos Ductos Biliares/cirurgia
Caderinas/análise
Feminino
Seres Humanos
Antígeno Ki-67/análise
Tumor de Klatskin/cirurgia
Masculino
Metaloproteinase 7 da Matriz/análise
Meia-Idade
Mucina-1/análise
Invasividade Neoplásica
Recidiva Local de Neoplasia
Valor Preditivo dos Testes
Estudos Retrospectivos
Fatores de Risco
Fatores de Tempo
Resultado do Tratamento
Proteína Supressora de Tumor p53/análise
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (CDH1 protein, human); 0 (Cadherins); 0 (Ki-67 Antigen); 0 (MUC1 protein, human); 0 (Mucin-1); 0 (TP53 protein, human); 0 (Tumor Suppressor Protein p53); EC 3.4.24.23 (MMP7 protein, human); EC 3.4.24.23 (Matrix Metalloproteinase 7)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171007
[St] Status:MEDLINE


  3 / 1406 MEDLINE  
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[PMID]:28870920
[Au] Autor:Chou AK; Hsiao CL; Shih TC; Wang HC; Tsai CW; Chang WS; Liu LC; Way TD; Chung JG; Bau DT
[Ad] Endereço:Department of Anesthesiology, China Medical University Hospital, Taichung, Taiwan, R.O.C.
[Ti] Título:The Contribution of Matrix Metalloproteinase-7 Promoter Genotypes in Breast Cancer in Taiwan.
[So] Source:Anticancer Res;37(9):4973-4977, 2017 09.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: The matrix metalloproteinase (MMP) family of enzymes are in charge of degradation of various components of the extracellular matrix and their functional genetic polymorphisms may be associated with cancer susceptibility. The functional polymorphisms in the promoter region of MMP7 (A-181G and C-153T) have been reported to influence the binding capacity of nuclear proteins and may contribute to genetic susceptibility to cancer. In this study, we focused on investigating the contribution of the genotypes of MMP7 (A-181G and C-153T) to breast cancer in Taiwan. MATERIALS AND METHODS: These two polymorphisms were genotyped in 1,232 patients with breast cancer and 1,232 controls by polymerase chain reaction-restriction fragment length polymorphism methodology. RESULTS: The odds ratios (ORs) after adjusting for age, family history of cancer, smoking and alcohol drinking status for those carrying AG and GG genotypes at MMP7 promoter A-181G were 1.22 (95%CI=0.91-1.63, p=0.2235) and 2.84 (95%CI=1.64-7.48, p=0.0007) respectively, compared to those carrying the wild-type AA genotype. Supporting this finding, the adjusted OR for those carrying the G allele at MMP7 promoter A-181G was 1.57 (95%CI=1.29-1.93, p=0.0008), compared to those carrying the wild-type A allele. There was no polymorphic genotype at MMP7 C-153T found among any of the investigated individuals. CONCLUSION: Our findings suggest that the MMP7 A-181G polymorphisms may play a role in determining personal cancer susceptibility and GG genotype at MMP7 A-181G may serve as a biomarker for early detection and prediction of breast cancer in Taiwanese.
[Mh] Termos MeSH primário: Neoplasias da Mama/epidemiologia
Neoplasias da Mama/genética
Metaloproteinase 7 da Matriz/genética
Polimorfismo de Nucleotídeo Único/genética
Regiões Promotoras Genéticas/genética
[Mh] Termos MeSH secundário: Adulto
Estudos de Casos e Controles
Feminino
Predisposição Genética para Doença
Genótipo
Seres Humanos
Meia-Idade
Prevalência
Prognóstico
Taiwan/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.24.23 (MMP7 protein, human); EC 3.4.24.23 (Matrix Metalloproteinase 7)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE


  4 / 1406 MEDLINE  
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[PMID]:28821612
[Au] Autor:Jang B; Jung H; Choi S; Lee YH; Lee ST; Oh ES
[Ad] Endereço:From the Department of Life Sciences, Research Center for Cellular Homeostasis, Ewha Womans University, Seoul 03760 and.
[Ti] Título:Syndecan-2 cytoplasmic domain up-regulates matrix metalloproteinase-7 expression via the protein kinase Cγ-mediated FAK/ERK signaling pathway in colon cancer.
[So] Source:J Biol Chem;292(39):16321-16332, 2017 Sep 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The syndecan family of heparan sulfate proteoglycans contributes to cell adhesion and communication by serving as co-receptors for cell signaling and extracellular matrix molecules. Syndecan-2 is located at the cell surface, and we previously reported that it induces matrix metalloproteinase-7 (MMP-7) expression in colon cancer cells. However, the underlying regulatory mechanisms are unknown. Here, we report that overexpression of syndecan-2 in HT-29 colon cancer cells increases the phosphorylation of focal adhesion kinase (FAK) and ERK in parallel with up-regulated MMP-7 expression, but a syndecan-2 mutant lacking the cytoplasmic domain showed significant reductions in these effects. Consistent with this observation, FAK inhibition via FAK-related non-kinase expression or inhibition of ERK with the ERK1/2 inhibitor SCH772984 diminished the syndecan-2-mediated up-regulation of MMP-7. Activation of PKC enhanced syndecan-2-mediated MMP-7 expression, whereas inhibition of PKC had the opposite effect. Of note, the exogenous expression of syndecan-2 triggered localization of PKCγ to the membrane. Expression of syndecan-2 harboring a phosphomimetic (S198E) mutation of the variable region of the cytoplasmic domain enhanced MMP-7 expression and FAK phosphorylation. Finally, experimental suppression of shedding of the syndecan-2 extracellular domain did not significantly affect the syndecan-2-mediated up-regulation of MMP-7 in the early period after syndecan-2 overexpression. Taken together, these findings suggest that syndecan-2's cytoplasmic domain up-regulates MMP-7 expression in colon cancer cells via PKCγ-mediated activation of FAK/ERK signaling.
[Mh] Termos MeSH primário: Carcinoma/metabolismo
Neoplasias do Colo/metabolismo
Quinase 1 de Adesão Focal/metabolismo
Sistema de Sinalização das MAP Quinases
Proteína Quinase C/metabolismo
Processamento de Proteína Pós-Traducional
Sindecana-2/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Carcinoma/tratamento farmacológico
Carcinoma/enzimologia
Neoplasias do Colo/tratamento farmacológico
Neoplasias do Colo/enzimologia
Indução Enzimática/efeitos dos fármacos
Quinase 1 de Adesão Focal/química
Quinase 1 de Adesão Focal/genética
Seres Humanos
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Metaloproteinase 7 da Matriz/genética
Metaloproteinase 7 da Matriz/metabolismo
Mutação
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/química
Proteínas de Neoplasias/genética
Proteínas de Neoplasias/metabolismo
Fragmentos de Peptídeos/antagonistas & inibidores
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Fosforilação/efeitos dos fármacos
Domínios e Motivos de Interação entre Proteínas
Inibidores de Proteínas Quinases/farmacologia
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
Interferência de RNA
Ratos
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Sindecana-2/antagonistas & inibidores
Sindecana-2/química
Sindecana-2/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neoplasm Proteins); 0 (Peptide Fragments); 0 (Protein Kinase Inhibitors); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Sdc2 protein, rat); 149769-25-5 (Syndecan-2); EC 2.7.1.- (protein kinase C gamma); EC 2.7.10.2 (Focal Adhesion Kinase 1); EC 2.7.10.2 (PTK2 protein, human); EC 2.7.11.13 (Protein Kinase C); EC 3.4.24.23 (MMP7 protein, human); EC 3.4.24.23 (Matrix Metalloproteinase 7)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.793752


  5 / 1406 MEDLINE  
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[PMID]:28751006
[Au] Autor:Jayakar SK; Loudig O; Brandwein-Gensler M; Kim RS; Ow TJ; Ustun B; Harris TM; Prystowsky MB; Childs G; Segall JE; Belbin TJ
[Ad] Endereço:Department of Pathology, Albert Einstein College of Medicine, Bronx, New York.
[Ti] Título:Apolipoprotein E Promotes Invasion in Oral Squamous Cell Carcinoma.
[So] Source:Am J Pathol;187(10):2259-2272, 2017 Oct.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oral squamous cell carcinoma (OSCC) patients generally have a poor prognosis, because of the invasive nature of these tumors. In comparing transcription profiles between OSCC tumors with a more invasive (worst pattern of tumor invasion 5) versus a less invasive (worst pattern of tumor invasion 3) pattern of invasion, we identified a total of 97 genes that were overexpressed at least 1.5-fold in the more invasive tumor subtype. The most functionally relevant genes were assessed using in vitro invasion assays with an OSCC cell line (UM-SCC-1). Individual siRNA knockdown of 15 of these 45 genes resulted in significant reductions in tumor cell invasion compared to a nontargeting siRNA control. One gene whose knockdown had a strong effect on invasion corresponded to apolipoprotein E (APOE). Both matrix degradation and the number of mature invadopodia were significantly decreased with APOE knockdown. APOE knockdown also resulted in increased cellular cholesterol, consistent with APOE's role in regulating cholesterol efflux. APOE knockdown resulted in decreased levels of phospho-extracellular signal-regulated kinase 1/2, phospho-c-Jun N-terminal kinase, and phospho-cJun, as well as decreased activator protein 1 (AP-1) activity. Expression of matrix metalloproteinase 7 (MMP7), an AP-1 target, was also significantly decreased. Our findings suggest that APOE protein plays a significant role in OSCC tumor invasion because of its effects on cellular cholesterol and subsequent effects on cell signaling and AP-1 activity, leading to changes in the expression of invasion-related proteins, including MMP7.
[Mh] Termos MeSH primário: Apolipoproteínas E/metabolismo
Carcinoma de Células Escamosas/patologia
Neoplasias Bucais/patologia
[Mh] Termos MeSH secundário: Apolipoproteínas E/genética
Carcinoma de Células Escamosas/genética
Linhagem Celular Tumoral
Colesterol/metabolismo
Matriz Extracelular/metabolismo
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Regulação Neoplásica da Expressão Gênica
Técnicas de Silenciamento de Genes
Genoma Humano
Seres Humanos
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Metaloproteinase 7 da Matriz/metabolismo
Modelos Biológicos
Neoplasias Bucais/genética
Invasividade Neoplásica
Fosforilação
Podossomos/metabolismo
Proteínas Proto-Oncogênicas c-jun/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/metabolismo
Transdução de Sinais/genética
Fator de Transcrição AP-1/metabolismo
Transcriptoma/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoproteins E); 0 (Proto-Oncogene Proteins c-jun); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (Transcription Factor AP-1); 97C5T2UQ7J (Cholesterol); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 3.4.24.23 (Matrix Metalloproteinase 7)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170729
[St] Status:MEDLINE


  6 / 1406 MEDLINE  
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[PMID]:28700662
[Au] Autor:Kaufmann B; Wang B; Zhong S; Laschinger M; Patil P; Lu M; Assfalg V; Cheng Z; Friess H; Hüser N; von Figura G; Hartmann D
[Ad] Endereço:Department of Surgery, Klinikum rechts der Isar, Technische Universität München, Munich, Germany.
[Ti] Título:BRG1 promotes hepatocarcinogenesis by regulating proliferation and invasiveness.
[So] Source:PLoS One;12(7):e0180225, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The chromatin remodeler complex SWI/SNF plays an important role in physiological and pathological processes. Brahma related gene 1(BRG1), a catalytic subunit of the SWI/SNF complex, is known to be mutated in hepatocellular carcinoma (HCC). However, its role in HCC remains unclear. Here, we investigate the role of BRG1 on cell growth and invasiveness as well as its effect on the expression of putative target genes. Expression of BRG1 was examined in human liver tissue samples and in HCC cell lines. In addition, BRG1 was silenced in human HCC cell lines to analyse cell growth and invasiveness by growth curves, colony formation assay, invasion assay and the expression of putative target genes. BRG1 was found to be significantly increased in HCC samples compared to non-HCC samples. In addition, a declined proliferation rate of BRG1-silenced human HCC cell lines was associated with a decrease of expression of cyclin family members. In line with a decreased invasiveness of BRG1-siRNA-treated human HCC cell lines, down-regulation of MMP7 was detected. These results support the hypothesis that overexpression of BRG1 increases cell growth and invasiveness in HCC. Furthermore, the data highlight cyclin B, E and MMP7 to be associated with BRG1 during hepatocarcinogenesis.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/metabolismo
Proliferação Celular
DNA Helicases/genética
Neoplasias Hepáticas/metabolismo
Proteínas Nucleares/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Carcinogênese
Carcinoma Hepatocelular/genética
Carcinoma Hepatocelular/patologia
Ciclinas/genética
Ciclinas/metabolismo
DNA Helicases/metabolismo
Regulação Neoplásica da Expressão Gênica
Células Hep G2
Seres Humanos
Fígado/embriologia
Neoplasias Hepáticas/genética
Neoplasias Hepáticas/patologia
Metaloproteinase 7 da Matriz/genética
Metaloproteinase 7 da Matriz/metabolismo
Invasividade Neoplásica
Proteínas Nucleares/metabolismo
Fatores de Transcrição/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclins); 0 (Nuclear Proteins); 0 (Transcription Factors); EC 3.4.24.23 (MMP7 protein, human); EC 3.4.24.23 (Matrix Metalloproteinase 7); EC 3.6.1.- (SMARCA4 protein, human); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180225


  7 / 1406 MEDLINE  
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[PMID]:28698269
[Au] Autor:Yang X; Chen C; Teng S; Fu X; Zha Y; Liu H; Wang L; Tian J; Zhang X; Liu Y; Nie J; Hou FF
[Ad] Endereço:Division of Nephrology, Nanfang Hospital, Southern Medical University, National Clinical Research Center for Kidney Disease, State Key Laboratory of Organ Failure Research, Guangzhou, China.
[Ti] Título:Urinary Matrix Metalloproteinase-7 Predicts Severe AKI and Poor Outcomes after Cardiac Surgery.
[So] Source:J Am Soc Nephrol;28(11):3373-3382, 2017 Nov.
[Is] ISSN:1533-3450
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Urinary matrix metalloproteinase-7 (uMMP-7) levels consistently reflect the activity of intrarenal Wnt/ -catenin, which is activated in AKI models. To test the hypothesis that uMMP-7 is a predictor for severe AKI in patients after cardiac surgery, we performed a prospective, multicenter, two-stage cohort study in 721 patients undergoing cardiac surgery. In stage 1, we enrolled 323 children from three academic medical centers. In stage 2, we enrolled 398 adults at six centers. We analyzed levels of uMMP-7 and other injury biomarkers during the perioperative period. Severe AKI was defined as Kidney Disease Improving Global Outcomes stage 2 or 3. uMMP-7 level peaked within 6 hours after surgery in patients who subsequently developed severe AKI. After multivariate adjustment, the highest quintile of postoperative uMMP-7 level, compared with the lowest quintile, associated with 17-fold (in adults) and 36-fold (in children) higher odds of severe AKI. Elevated uMMP-7 level associated with increased risk of composite events (severe AKI, acute dialysis, and in-hospital death) and longer stay in the intensive care unit and hospital. For predicting severe AKI, uMMP-7 had an area under the receiver operating characteristic curve of 0.81 (in children) and 0.76 (in adults), outperforming urinary IL-18, angiotensinogen, neutrophil gelatinase-associated lipocalin, albumin-to-creatinine ratio, and tissue inhibitor of metalloproteinase-2·IGF-binding protein-7 and the clinical model. uMMP-7 significantly improved risk reclassification over the clinical model alone, as measured by net reclassification improvement and integrated discrimination improvement. In conclusion, uMMP-7 is a promising predictor for severe AKI and poor in-hospital outcomes in patients after cardiac surgery.
[Mh] Termos MeSH primário: Lesão Renal Aguda/urina
Procedimentos Cirúrgicos Cardíacos
Metaloproteinase 7 da Matriz/urina
[Mh] Termos MeSH secundário: Lesão Renal Aguda/diagnóstico
Adolescente
Adulto
Criança
Pré-Escolar
Feminino
Seres Humanos
Lactente
Masculino
Meia-Idade
Valor Preditivo dos Testes
Estudos Prospectivos
Índice de Gravidade de Doença
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; MULTICENTER STUDY
[Nm] Nome de substância:
EC 3.4.24.23 (Matrix Metalloproteinase 7)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1681/ASN.2017020142


  8 / 1406 MEDLINE  
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[PMID]:28646039
[Au] Autor:Brilha S; Wysoczanski R; Whittington AM; Friedland JS; Porter JC
[Ad] Endereço:Department of Infectious Diseases and Immunity, Imperial College London, London W12 0NN, United Kingdom.
[Ti] Título:Monocyte Adhesion, Migration, and Extracellular Matrix Breakdown Are Regulated by Integrin αVß3 in Infection.
[So] Source:J Immunol;199(3):982-991, 2017 Aug 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In tuberculosis (TB), the innate inflammatory immune response drives tissue destruction, morbidity, and mortality. Monocytes secrete matrix metalloproteinases (MMPs), which have key roles in local tissue destruction and cavitation. We hypothesized that integrin signaling might regulate monocyte MMP secretion in pulmonary TB during cell adhesion to the extracellular matrix (ECM). Adhesion to type I collagen and fibronectin by -stimulated monocytes increased MMP-1 gene expression by 2.6-fold and 4.3-fold respectively, and secretion by 60% (from 1208.1 ± 186 to 1934.4 ± 135 pg/ml; < 0.0001) and 63% (1970.3 ± 95 pg/ml; < 0.001). MMP-10 secretion increased by 90% with binding to type I collagen and 55% with fibronectin, whereas MMP-7 increased 57% with collagen. The ECM did not affect the secretion of tissue inhibitors of metalloproteinases-1 or -2. Integrin αVß3 surface expression was specifically upregulated in stimulated monocytes and was further increased after adhesion to type I collagen. Binding of either ß3 or αV integrin subunits increased MMP-1/10 secretion in -stimulated monocytes. In a cohort of TB patients, significantly increased integrin ß3 mRNA accumulation in induced sputum was detected, to our knowledge, for the first time, compared with control subjects ( < 0.05). Integrin αVß3 colocalized with areas of increased and functionally active MMP-1 on infected monocytes, and αVß3 blockade markedly decreased type I collagen breakdown, and impaired both monocyte adhesion and leukocyte migration in a transwell system ( < 0.0001). In summary, our data demonstrate that stimulation upregulates integrin αVß3 expression on monocytes, which upregulates secretion of MMP-1 and -10 on adhesion to the ECM. This leads to increased monocyte recruitment and collagenase activity, which will drive inflammatory tissue damage.
[Mh] Termos MeSH primário: Adesão Celular
Movimento Celular
Matriz Extracelular/metabolismo
Integrina alfaVbeta3/genética
Monócitos/imunologia
Mycobacterium tuberculosis/imunologia
[Mh] Termos MeSH secundário: Colágeno Tipo I/metabolismo
Colagenases/metabolismo
Matriz Extracelular/efeitos dos fármacos
Fibronectinas/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Integrina alfaVbeta3/antagonistas & inibidores
Integrina alfaVbeta3/imunologia
Metaloproteinase 1 da Matriz/genética
Metaloproteinase 1 da Matriz/metabolismo
Metaloproteinase 10 da Matriz/imunologia
Metaloproteinase 10 da Matriz/metabolismo
Metaloproteinase 7 da Matriz/imunologia
Metaloproteinase 7 da Matriz/metabolismo
Inibidores de Metaloproteinases de Matriz/farmacologia
Monócitos/microbiologia
Monócitos/fisiologia
Transdução de Sinais
Escarro/química
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type I); 0 (Fibronectins); 0 (Integrin alphaVbeta3); 0 (Matrix Metalloproteinase Inhibitors); EC 3.4.24.- (Collagenases); EC 3.4.24.22 (Matrix Metalloproteinase 10); EC 3.4.24.23 (Matrix Metalloproteinase 7); EC 3.4.24.7 (Matrix Metalloproteinase 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170625
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700128


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[PMID]:28635400
[Au] Autor:Xu YZ; Chen FF; Zhang Y; Zhao QF; Guan XL; Wang HY; Li A; Lv X; Song SS; Zhou Y; Li XJ
[Ad] Endereço:1 Institute of Clinical Laboratory Science, Jinling Hospital, Southern Medical University, Nanjing, China.
[Ti] Título:The long noncoding RNA FOXCUT promotes proliferation and migration by targeting FOXC1 in nasopharyngeal carcinoma.
[So] Source:Tumour Biol;39(6):1010428317706054, 2017 Jun.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Long noncoding RNAs play an important role in various biological processes, including tumorigenesis. FOXC1 (Forkhead box C1) is a member of the Forkhead box family of transcription factors and plays a crucial role in nasopharyngeal carcinoma. In this study, a novel long noncoding RNA (FOXCUT) located upstream of FOXC1 was investigated in 42 nasopharyngeal carcinoma patients. Our analysis revealed that the expression levels of FOXCUT and FOXC1 in nasopharyngeal carcinoma tissues were significantly higher than those observed in chronic nasopharyngitis tissues and that FOXCUT expression was positively correlated with FOXC1 expression. Additionally, knockdown of FOXCUT significantly inhibited proliferation and migration of nasopharyngeal carcinoma cell lines and resulted in downregulated expression of the matrix metalloproteinase 7 and matrix metalloproteinase 9, as well as vascular endothelial growth factor A and ß-catenin. Our findings suggested that FOXCUT expression contributed to the development and progression of nasopharyngeal carcinoma by targeting FOXC1 and that FOXCUT might be useful as a potential nasopharyngeal carcinoma biomarker and therapeutic target.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/genética
Carcinoma/genética
Fatores de Transcrição Forkhead/genética
Neoplasias Nasofaríngeas/genética
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Adulto
Biomarcadores Tumorais/biossíntese
Carcinoma/patologia
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Feminino
Fatores de Transcrição Forkhead/biossíntese
Regulação Neoplásica da Expressão Gênica
Técnicas de Silenciamento de Genes
Seres Humanos
Masculino
Metaloproteinase 7 da Matriz/biossíntese
Metaloproteinase 9 da Matriz/biossíntese
Meia-Idade
Neoplasias Nasofaríngeas/patologia
RNA Longo não Codificante/biossíntese
Fator A de Crescimento do Endotélio Vascular/biossíntese
beta Catenina/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (FOXC1 protein, human); 0 (Forkhead Transcription Factors); 0 (RNA, Long Noncoding); 0 (VEGFA protein, human); 0 (Vascular Endothelial Growth Factor A); 0 (beta Catenin); 0 (long non-coding RNA FOXCUT, human); EC 3.4.24.23 (MMP7 protein, human); EC 3.4.24.23 (Matrix Metalloproteinase 7); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317706054


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[PMID]:28626073
[Au] Autor:Li W; Cui N; Mazzuca MQ; Mata KM; Khalil RA
[Ad] Endereço:Vascular Surgery Research Laboratories, Division of Vascular and Endovascular Surgery, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts.
[Ti] Título:Increased vascular and uteroplacental matrix metalloproteinase-1 and -7 levels and collagen type I deposition in hypertension in pregnancy: role of TNF-α.
[So] Source:Am J Physiol Heart Circ Physiol;313(3):H491-H507, 2017 Sep 01.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Preeclampsia is a pregnancy-related disorder manifested as maternal hypertension in pregnancy (HTN-Preg) and fetal growth restriction. Placental ischemia could be an initiating event that leads to abnormal vascular and uteroplacental remodeling in HTN-Preg; however, the molecular targets and intermediary mechanisms involved are unclear. We tested the hypothesis that placental ischemia could target vascular and uteroplacental matrix metalloproteinases (MMPs) through an inflammatory cytokine-mediated mechanism. MMP levels and distribution were measured in the aorta, uterus, and placenta of normal pregnant (Preg) rats and pregnant rats with reduced uterine perfusion pressure (RUPP). Maternal blood pressure was higher and the litter size and pup weight were lower in RUPP compared with Preg rats. Gelatin zymography showed prominent uterine MMP-2 and MMP-9 activity that was dependent on the amount of loaded protein. At saturating protein loading, both gelatin and casein zymography revealed two additional bands corresponding to MMP-1 and MMP-7 that were greater in the aorta, uterus, and placenta of RUPP compared with Preg rats. Western blots and immunohistochemistry confirmed increased MMP-1 and MMP-7 in the aorta, uterus, and placenta of RUPP versus Preg rats. The levels of MMP-1 and MMP-7 substrate collagen type I were greater in tissues of RUPP compared with Preg rats. In organ culture, TNF-α increased MMP-1 and MMP-7 in the aorta, uterus, and placenta of Preg rats, and a TNF-α antagonist prevented the increases in MMPs in tissues of RUPP rats. Thus, placental ischemia, possibly through TNF-α, increases vascular and uteroplacental MMP-1 and MMP-7, which, in turn, alter collagen deposition and cause inadequate tissue remodeling in HTN-Preg. Cytokine antagonists may reverse the increase in MMP-1 and MMP-7 expression/activity and, in turn, restore proper vascular and uteroplacental remodeling in HTN-Preg and preeclampsia. The molecular mechanisms of preeclampsia are unclear, making it difficult to predict, prevent, or manage the pregnancy-associated disorder. This study showed that placental ischemia, possibly through the release of TNF-α, causes increases in the levels of matrix metalloproteinase (MMP)-1 and MMP-7, which could alter collagen deposition and cause inadequate uteroplacental and vascular remodeling in hypertension in pregnancy. The data suggest that targeting MMP-1 and MMP-7 and their upstream modulators, such as TNF-α, could provide a new approach in the management of hypertension in pregnancy and preeclampsia.
[Mh] Termos MeSH primário: Colágeno Tipo I/metabolismo
Hipertensão Induzida pela Gravidez/enzimologia
Isquemia/enzimologia
Metaloproteinase 1 da Matriz/metabolismo
Metaloproteinase 7 da Matriz/metabolismo
Placenta/irrigação sanguínea
Placenta/enzimologia
Placentação
Fator de Necrose Tumoral alfa/metabolismo
Útero/irrigação sanguínea
Útero/enzimologia
Remodelação Vascular
[Mh] Termos MeSH secundário: Animais
Aorta/enzimologia
Pressão Sanguínea
Modelos Animais de Doenças
Feminino
Idade Gestacional
Hipertensão Induzida pela Gravidez/etiologia
Hipertensão Induzida pela Gravidez/fisiopatologia
Fragmentos Fc das Imunoglobulinas/farmacologia
Isquemia/etiologia
Isquemia/fisiopatologia
Técnicas de Cultura de Órgãos
Placenta/efeitos dos fármacos
Circulação Placentária
Placentação/efeitos dos fármacos
Gravidez
Ratos Sprague-Dawley
Transdução de Sinais
Fator de Necrose Tumoral alfa/antagonistas & inibidores
Fator de Necrose Tumoral alfa/farmacologia
Regulação para Cima
Útero/efeitos dos fármacos
Remodelação Vascular/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type I); 0 (Immunoglobulin Fc Fragments); 0 (Tumor Necrosis Factor-alpha); EC 3.4.24.23 (Matrix Metalloproteinase 7); EC 3.4.24.7 (MMP1 protein, rat); EC 3.4.24.7 (Matrix Metalloproteinase 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00207.2017



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