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[PMID]:29437053
[Au] Autor:Tarabichi M; Shohat N; Goswami K; Parvizi J
[Ad] Endereço:The Rothman Institute at Thomas Jefferson University, 125 South 9th Street, Suite 1000, Philadelphia PA 19107, USA.
[Ti] Título:Can next generation sequencing play a role in detecting pathogens in synovial fluid?
[So] Source:Bone Joint J;100-B(2):127-133, 2018 02.
[Is] ISSN:2049-4408
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: The diagnosis of periprosthetic joint infection can be difficult due to the high rate of culture-negative infections. The aim of this study was to assess the use of next-generation sequencing for detecting organisms in synovial fluid. MATERIALS AND METHODS: In this prospective, single-blinded study, 86 anonymized samples of synovial fluid were obtained from patients undergoing aspiration of the hip or knee as part of the investigation of a periprosthetic infection. A panel of synovial fluid tests, including levels of C-reactive protein, human neutrophil elastase, total neutrophil count, alpha-defensin, and culture were performed prior to next-generation sequencing. RESULTS: Of these 86 samples, 30 were alpha-defensin-positive and culture-positive (Group I), 24 were alpha-defensin-positive and culture-negative (Group II) and 32 were alpha-defensin-negative and culture-negative (Group III). Next-generation sequencing was concordant with 25 results for Group I. In four of these, it detected antibiotic resistant bacteria whereas culture did not. In another four samples with relatively low levels of inflammatory biomarkers, culture was positive but next-generation sequencing was negative. A total of ten samples had a positive next-generation sequencing result and a negative culture. In five of these, alpha-defensin was positive and the levels of inflammatory markers were high. In the other five, alpha-defensin was negative and the levels of inflammatory markers were low. While next-generation sequencing detected several organisms in each sample, in most samples with a higher probability of infection, there was a predominant organism present, while in those presumed not to be infected, many organisms were identified with no predominant organism. CONCLUSION: Pathogens causing periprosthetic infection in both culture-positive and culture-negative samples of synovial fluid could be identified by next-generation sequencing. Cite this article: 2018;100-B:127-33.
[Mh] Termos MeSH primário: Artroplastia de Quadril
Artroplastia do Joelho
Infecções Bacterianas/microbiologia
Micoses/microbiologia
Infecções Relacionadas à Prótese/microbiologia
Análise de Sequência de DNA/métodos
Líquido Sinovial/química
Líquido Sinovial/microbiologia
[Mh] Termos MeSH secundário: Biomarcadores/análise
Proteína C-Reativa/análise
Seres Humanos
Elastase de Leucócito/análise
Reação em Cadeia da Polimerase
Estudos Prospectivos
Sensibilidade e Especificidade
Método Simples-Cego
alfa-Defensinas/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (alpha-Defensins); 9007-41-4 (C-Reactive Protein); EC 3.4.21.37 (Leukocyte Elastase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180214
[St] Status:MEDLINE
[do] DOI:10.1302/0301-620X.100B2.BJJ-2017-0531.R2


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[PMID]:28468826
[Au] Autor:Kerros C; Tripathi SC; Zha D; Mehrens JM; Sergeeva A; Philips AV; Qiao N; Peters HL; Katayama H; Sukhumalchandra P; Ruisaard KE; Perakis AA; St John LS; Lu S; Mittendorf EA; Clise-Dwyer K; Herrmann AC; Alatrash G; Toniatti C; Hanash SM; Ma Q; Molldrem JJ
[Ad] Endereço:From the University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030.
[Ti] Título:Neuropilin-1 mediates neutrophil elastase uptake and cross-presentation in breast cancer cells.
[So] Source:J Biol Chem;292(24):10295-10305, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neutrophil elastase (NE) can be rapidly taken up by tumor cells that lack endogenous NE expression, including breast cancer, which results in cross-presentation of PR1, an NE-derived HLA-A2-restricted peptide that is an immunotherapy target in hematological and solid tumor malignancies. The mechanism of NE uptake, however, remains unknown. Using the mass spectrometry-based approach, we identify neuropilin-1 (NRP1) as a NE receptor that mediates uptake and PR1 cross-presentation in breast cancer cells. We demonstrated that soluble NE is a specific, high-affinity ligand for NRP1 with a calculated of 38.7 nm Furthermore, we showed that NRP1 binds to the RR R motif in NE. Notably, NRP1 knockdown with interfering RNA or CRISPR-cas9 system and blocking using anti-NRP1 antibody decreased NE uptake and, subsequently, susceptibility to lysis by PR1-specific cytotoxic T cells. Expression of NRP1 in NRP1-deficient cells was sufficient to induce NE uptake. Altogether, because NRP1 is broadly expressed in tumors, our findings suggest a role for this receptor in immunotherapy strategies that target cross-presented antigens.
[Mh] Termos MeSH primário: Absorção Fisiológica
Neoplasias da Mama/metabolismo
Apresentação Cruzada
Elastase de Leucócito/metabolismo
Proteínas de Neoplasias/metabolismo
Neuropilina-1/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Anticorpos Bloqueadores/metabolismo
Neoplasias da Mama/imunologia
Neoplasias da Mama/patologia
Sistemas CRISPR-Cas
Linhagem Celular Tumoral
Feminino
Seres Humanos
Cinética
Elastase de Leucócito/química
Elastase de Leucócito/imunologia
Ligantes
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/química
Proteínas de Neoplasias/genética
Neuropilina-1/antagonistas & inibidores
Neuropilina-1/química
Neuropilina-1/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Domínios e Motivos de Interação entre Proteínas
Interferência de RNA
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Solubilidade
Linfócitos T Citotóxicos/imunologia
Linfócitos T Citotóxicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antibodies, Blocking); 0 (Ligands); 0 (Neoplasm Proteins); 0 (Peptide Fragments); 0 (Recombinant Proteins); 144713-63-3 (Neuropilin-1); EC 3.4.21.37 (Leukocyte Elastase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.773051


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[PMID]:28922398
[Au] Autor:Chung HS; Kim JS; Lee SM; Park SJ
[Ad] Endereço:Alteogen Inc., Yuseong-gu, Daejeon, South Korea.
[Ti] Título:Role of the P2 residue of human alpha 1-antitrypsin in determining target protease specificity.
[So] Source:PLoS One;12(9):e0185074, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alpha 1-antitrypsin (A1AT) is a serine protease inhibitor that mainly inhibits neutrophil elastase in the lungs. A variant of A1AT at the P1 position with methionine 358 to arginine (A1AT-Pittsburgh) is a rapid inhibitor of thrombin with greatly diminished anti-elastase activity. The P2 residue (position 357) of A1AT-Pittsburgh has been shown to play an important role in interactions with thrombin and kallikrein, but the role of P2 residue in wild-type A1AT has largely been unraveled. Here, we investigated the effects of P2 proline substitutions in wild-type A1AT on interactions with porcine pancreatic elastase (PPE) and human neutrophil elastase (HNE). The mutant A1AT proteins (P357A, P357D, P357K, P357L, P357N, P357S, and P357W) were less efficient than the wild-type A1AT at inhibiting PPE and HNE. Among the mutants, P357D did not form a complex with PPE, whereas P357L, P357N, and P357W showed significantly reduced complex formation with PPE. Surprisingly, mass spectrometry analysis revealed that P357D had two cleavage sites after the P9 alanine and the P3 isoleucine residues. Our results indicate that the size and negative charge of the R group of the P2 residue influence the interaction with elastases. Specifically, the negative charge at the P2 residue is disfavored and the resulting conformational changes in the reactive center loop upon interaction with PPE lead to cleavage at new sites. Overall, the results of this study demonstrate a previously unknown role for P2 residue in determining inhibitory specificity of A1AT.
[Mh] Termos MeSH primário: Elastase de Leucócito/química
alfa 1-Antitripsina/química
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Seres Humanos
Elastase de Leucócito/metabolismo
Mutação de Sentido Incorreto
Suínos
alfa 1-Antitripsina/genética
alfa 1-Antitripsina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (SERPINA1 protein, human); 0 (alpha 1-Antitrypsin); EC 3.4.21.37 (Leukocyte Elastase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185074


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[PMID]:28800474
[Au] Autor:Lee JW; Park HA; Kwon OK; Park JW; Lee G; Lee HJ; Lee SJ; Oh SR; Ahn KS
[Ad] Endereço:Natural Medicine Research Center, Korea Research Institute of Bioscience and Biotechnology, 30 Yeongudanji-ro, Ochang-eup, Cheongwon-gu, Chungju-si, Chungbuk, 363-883, Republic of Korea.
[Ti] Título:NPS 2143, a selective calcium-sensing receptor antagonist inhibits lipopolysaccharide-induced pulmonary inflammation.
[So] Source:Mol Immunol;90:150-157, 2017 Oct.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:NPS 2143, a novel and selective antagonist of calcium-sensing receptor (CaSR) has been reported to possess anti-inflammatory activity. In the present study, we examined the protective effect of NPS 2143 on lipopolysaccharide (LPS)-induced acute lung injury (ALI). NPS 2143 pretreatment significantly inhibited the influx of inflammatory cells and the expression of monocyte chemoattractant protein-1 (MCP-1) in the lung of mice with LPS-induced ALI. NPS 2143 decreased the levels of neutrophil elastase (NE) and protein concentration in the bronchoalveolar lavage fluid (BALF). NPS 2143 also reduced the production of inflammatory cytokines such as tumor necrosis factor-α (TNF-α) and interleukin-6 (IL-6) in the BALF and serum. In addition, NPS 2143 attenuated the expression of inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2), and increased the activation of AMP-activated protein kinase (AMPK) in the lung. NPS 2143 also downregulated the activation of nuclear factor-kappa B (NF-κB) in the lung. In LPS-stimulated H292 airway epithelial cells, NPS 2143 attenuated the releases of IL-6 and MCP-1. Furthermore, NPS 2143 upregulated the activation of AMPK and downregulated the activation of NF-κB. These results suggest that NPS 2143 could be potential agent for the treatment of inflammatory diseases including ALI.
[Mh] Termos MeSH primário: Lesão Pulmonar Aguda/prevenção & controle
Anti-Inflamatórios/farmacologia
Naftalenos/farmacologia
Pneumonia/prevenção & controle
Receptores de Detecção de Cálcio/antagonistas & inibidores
Mucosa Respiratória/efeitos dos fármacos
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/metabolismo
Lesão Pulmonar Aguda/induzido quimicamente
Animais
Líquido da Lavagem Broncoalveolar/química
Linhagem Celular
Quimiocina CCL2/biossíntese
Ciclo-Oxigenase 2/biossíntese
Ativação Enzimática/efeitos dos fármacos
Células Epiteliais/efeitos dos fármacos
Seres Humanos
Interleucina-6/metabolismo
Elastase de Leucócito/metabolismo
Lipopolissacarídeos
Pulmão/patologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
NF-kappa B/biossíntese
Óxido Nítrico Sintase Tipo II/biossíntese
Pneumonia/induzido quimicamente
Mucosa Respiratória/citologia
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Ccl2 protein, mouse); 0 (Chemokine CCL2); 0 (Interleukin-6); 0 (Lipopolysaccharides); 0 (N-(2-hydroxy-3-(2-cyano-3-chlorophenoxy)propyl)-1,1-dimethyl-2-(2-nephthyl)ethylamine); 0 (NF-kappa B); 0 (Naphthalenes); 0 (Receptors, Calcium-Sensing); 0 (Tumor Necrosis Factor-alpha); 0 (interleukin-6, mouse); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 1.14.99.- (Ptgs2 protein, mouse); EC 1.14.99.1 (Cyclooxygenase 2); EC 2.7.11.31 (AMP-Activated Protein Kinases); EC 3.4.21.37 (Leukocyte Elastase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE


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[PMID]:28796788
[Au] Autor:Cruz-Baquero A; Cárdenas Jaramillo LM; Gutiérrez-Meza M; Jarillo-Luna RA; Campos-Rodríguez R; Rivera-Aguilar V; Miliar-García A; Pacheco-Yepez J
[Ad] Endereço:Sección de Estudios de Posgrado e Investigación, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luís y Díaz Mirón, CP, Ciudad de México, México.
[Ti] Título:Different behavior of myeloperoxidase in two rodent amoebic liver abscess models.
[So] Source:PLoS One;12(8):e0182480, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The protozoan Entamoeba histolytica is the etiological agent of amoebiasis, which can spread to the liver and form amoebic liver abscesses. Histological studies conducted with resistant and susceptible models of amoebic liver abscesses (ALAs) have established that neutrophils are the first cells to contact invasive amoebae at the lesion site. Myeloperoxidase is the most abundant enzyme secreted by neutrophils. It uses hydrogen peroxide secreted by the same cells to oxidize chloride ions and produce hypochlorous acid, which is the most efficient microbicidal system of neutrophils. In a previous report, our group demonstrated that myeloperoxidase presents amoebicidal activity in vitro. The aim of the current contribution was to analyze in vivo the role of myeloperoxidase in a susceptible (hamsters) and resistant (Balb/c mice) animal models of ALAs. In liver samples of hamsters and mice inoculated intraportally with Entamoeba histolytica trophozoites, the number of neutrophils in ALAs was determined by enzymatic activity. The presence of myeloperoxidase was observed by staining, and its expression and activity were quantified in situ. A significant difference existed between the two animal models in the number of neutrophils and the expression and activity of myeloperoxidase, which may explain the distinct evolution of amoebic liver abscesses. Hamsters and mice were treated with an MPO inhibitor (4-aminobenzoic acid hydrazide). Hamsters treated with ABAH showed no significant differences in the percentage of lesions or in the percentage of amoebae damaged compared with the untreated hamsters. ABAH treated mice versus untreated mice showed larger abscesses and a decreased percentage of damaged amoebae in these lesion at all stages of evolution. Further studies are needed to elucidate the host and amoebic mechanisms involved in the adequate or inadequate activation and modulation of myeloperoxidase.
[Mh] Termos MeSH primário: Entamoeba histolytica/fisiologia
Abscesso Hepático Amebiano/enzimologia
Peroxidase/metabolismo
[Mh] Termos MeSH secundário: Animais
Cricetinae
Modelos Animais de Doenças
Resistência à Doença
Interações Hospedeiro-Patógeno
Elastase de Leucócito/metabolismo
Fígado/enzimologia
Fígado/imunologia
Fígado/parasitologia
Masculino
Camundongos Endogâmicos BALB C
Neutrófilos/enzimologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.11.1.7 (Peroxidase); EC 3.4.21.37 (Leukocyte Elastase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182480


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[PMID]:28754797
[Au] Autor:Makaryan V; Kelley ML; Fletcher B; Bolyard AA; Aprikyan AA; Dale DC
[Ad] Endereço:Department of Medicine, University of Washington, Seattle, Washington, USA.
[Ti] Título:Elastase inhibitors as potential therapies for -associated neutropenia.
[So] Source:J Leukoc Biol;102(4):1143-1151, 2017 Oct.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in , the gene for neutrophil elastase (NE), a protease expressed early in neutrophil development, are the most frequent cause of cyclic (CyN) and severe congenital neutropenia (SCN). We hypothesized that inhibitors of NE, acting either by directly inhibiting enzymatic activity or as chaperones for the mutant protein, might be effective as therapy for CyN and SCN. We investigated ß-lactam-based inhibitors of human NE (Merck Research Laboratories, Kenilworth, NJ, USA), focusing on 1 inhibitor called MK0339, a potent, orally absorbed agent that had been tested in clinical trials and shown to have a favorable safety profile. Because fresh, primary bone marrow cells are rarely available in sufficient quantities for research studies, we used 3 cellular models: patient-derived, induced pluripotent stem cells (iPSCs); HL60 cells transiently expressing mutant NE; and HL60 cells with regulated expression of the mutant enzyme. In all 3 models, the cells expressing the mutant enzyme had reduced survival as measured with annexin V and FACS. Coincubation with the inhibitors, particularly MK0339, promoted cell survival and increased formation of mature neutrophils. These studies suggest that cell-permeable inhibitors of neutrophil elastase show promise as novel therapies for -associated neutropenia.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Elastase de Leucócito
Mutação
Neutropenia/congênito
[Mh] Termos MeSH secundário: Sobrevivência Celular
Feminino
Células HL-60
Seres Humanos
Elastase de Leucócito/antagonistas & inibidores
Elastase de Leucócito/genética
Elastase de Leucócito/metabolismo
Masculino
Neutropenia/tratamento farmacológico
Neutropenia/enzimologia
Neutropenia/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); EC 3.4.21.37 (Leukocyte Elastase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170730
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.5A1016-445R


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[PMID]:28704150
[Au] Autor:Power G; Moore Z; O'Connor T
[Ad] Endereço:Community Registered General Nurse, HSE Carlow/Kilkenny, Ireland.
[Ti] Título:Measurement of pH, exudate composition and temperature in wound healing: a systematic review.
[So] Source:J Wound Care;26(7):381-397, 2017 Jul 02.
[Is] ISSN:0969-0700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To assess the potential of measurements of pH, exudate composition and temperature in wounds to predict healing outcomes and to identify the methods that are employed to measure them. METHOD: A systematic review based on the outcomes of a search strategy of quantitative primary research published in the English language was conducted. Inclusion criteria limited studies to those involving in vivo and human participants with an existing or intentionally provoked wound, defined as 'a break in the epithelial integrity of the skin', and excluded in vitro and animal studies. Data synthesis and analysis was performed using structured narrative summaries of each included study arranged by concept, pH, exudate composition and temperature. The Evidence Based Literature (EBL) Critical Appraisal Checklist was implemented to appraise the quality of the included studies. RESULTS: A total of 23 studies, three for pH (mean quality score 54.48%), 12 for exudate composition (mean quality score 46.54%) and eight for temperature (mean quality score 36.66%), were assessed as eligible for inclusion in this review. Findings suggest that reduced pH levels in wounds, from alkaline towards acidic, are associated with improvements in wound condition. Metalloproteinase-9 (MMP-9), matrix metalloproteinase-2 (MMP-2), tissue inhibitor of metalloproteinase (TIMP), neutrophil elastase (NE) and albumin, in descending order, were the most frequently measured analytes in wounds. MMP-9 emerged as the analyte which offers the most potential as a biomarker of wound healing, with elevated levels observed in acute or non-healing wounds and decreasing levels in wounds progressing in healing. Combined measures of different exudate components, such as MMP/TIMP ratios, also appeared to offer substantial potential to indicate wound healing. Finally, temperature measurements are highest in non-healing, worsening or acute wounds and decrease as wounds progress towards healing. Methods used to measure pH, exudate composition and temperature varied greatly and, despite noting some similarities, the studies often yielded significantly contrasting results. Furthermore, a limitation to the generalisability of the findings was the overall quality scores of the research studies, which appeared suboptimal. CONCLUSION: Despite some promising findings, there was insufficient evidence to confidently recommend the use of any of these measures as predictors of wound healing. pH measurement appeared as the most practical method for use in clinical practice to indicate wound healing outcomes. Further research is required to increase the strength of evidence and develop a greater understanding of wound healing dynamics.
[Mh] Termos MeSH primário: Biomarcadores/metabolismo
Exsudatos e Transudatos/metabolismo
Temperatura Cutânea
Cicatrização
Ferimentos e Lesões
[Mh] Termos MeSH secundário: Albuminas/metabolismo
Exsudatos e Transudatos/química
Seres Humanos
Concentração de Íons de Hidrogênio
Elastase de Leucócito/metabolismo
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 9 da Matriz/metabolismo
Temperatura Ambiente
Inibidores Teciduais de Metaloproteinases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Albumins); 0 (Biomarkers); 0 (Tissue Inhibitor of Metalloproteinases); EC 3.4.21.37 (Leukocyte Elastase); EC 3.4.24.24 (MMP2 protein, human); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:N
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.12968/jowc.2017.26.7.381


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[PMID]:28696508
[Au] Autor:Laridan E; Denorme F; Desender L; François O; Andersson T; Deckmyn H; Vanhoorelbeke K; De Meyer SF
[Ad] Endereço:Laboratory for Thrombosis Research, KU Leuven, Campus Kulak Kortrijk, Kortrijk, Belgium.
[Ti] Título:Neutrophil extracellular traps in ischemic stroke thrombi.
[So] Source:Ann Neurol;82(2):223-232, 2017 Aug.
[Is] ISSN:1531-8249
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Neutrophil extracellular traps (NETs) have been shown to promote thrombus formation. Little is known about the exact composition of thrombi that cause ischemic stroke. In particular, no information is yet available on the presence of NETs in cerebral occlusions. Such information is, however, essential to improve current thrombolytic therapy with tissue plasminogen activator (t-PA). This study aimed at investigating the presence of neutrophils and more specifically NETs in ischemic stroke thrombi. METHODS: Sixty-eight thrombi retrieved from ischemic stroke patients undergoing endovascular treatment were characterized by immunostaining using neutrophil markers (CD66b and neutrophil elastase) and NET markers (citrullinated histone H3 [H3Cit] and extracellular DNA). Neutrophils and NETs were quantified. In addition, extracellular DNA was targeted by performing ex vivo lysis of retrieved thrombi with DNase 1 and t-PA. RESULTS: Neutrophils were detected extensively throughout all thrombi. H3Cit, a hallmark of NETs, was observed in almost all thrombi. H3Cit-positive area varied up to 13.45% of total thrombus area. Colocalization of H3Cit with extracellular DNA released from neutrophils confirmed the specific presence of NETs. H3Cit was more abundant in thrombi of cardioembolic origin compared to other etiologies. Older thrombi contained significantly more neutrophils and H3Cit compared to fresh thrombi. Interestingly, ex vivo lysis of patient thrombi was more successful when adding DNase 1 to standard t-PA. INTERPRETATION: Neutrophils and NETs form important constituents of cerebral thrombi. Targeting of NETs with DNase 1 might have prothrombolytic potential in treatment of acute ischemic stroke. Ann Neurol 2017;82:223-232.
[Mh] Termos MeSH primário: Antígenos CD/metabolismo
Isquemia Encefálica/metabolismo
Moléculas de Adesão Celular/metabolismo
DNA/metabolismo
Armadilhas Extracelulares/metabolismo
Elastase de Leucócito/metabolismo
Acidente Vascular Cerebral/metabolismo
Trombose/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Biomarcadores
Isquemia Encefálica/complicações
Contagem de Células/estatística & dados numéricos
Feminino
Proteínas Ligadas por GPI/metabolismo
Seres Humanos
Masculino
Meia-Idade
Acidente Vascular Cerebral/complicações
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Biomarkers); 0 (CEACAM8 protein, human); 0 (Cell Adhesion Molecules); 0 (GPI-Linked Proteins); 9007-49-2 (DNA); EC 3.4.21.37 (Leukocyte Elastase)
[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:170712
[St] Status:MEDLINE
[do] DOI:10.1002/ana.24993


  9 / 3526 MEDLINE  
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[PMID]:28685539
[Au] Autor:Liu L; Liu DZ; Wang QP; Zhu ZL; Li HM; Lu XY
[Ad] Endereço:Xinxiang Central Hospital, Xinxiang City, China.
[Ti] Título:Respiratory training during rehabilitation of acute organic fluorine-poisoned patients treated by non-invasive positive pressure ventilation.
[So] Source:J Biol Regul Homeost Agents;31(2):371-376, 2017 Apr-Jun.
[Is] ISSN:0393-974X
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:This paper aimed to analyze the effects of respiratory training on pulmonary function during the rehabilitation period for acute organic fluorine-poisoned patients treated by non-invasive positive pressure ventilation (NIPPV). Sixty-two acute organic fluorine-poisoned patients admitted to the Xinxiang Central Hospital, Xinxiang City, China, from May 2012 to March 2016 were selected and randomly divided into an observation group and a control group, with 31 cases in each. Both groups received NIPPV. The patients in the control group exercised daily, while the patients in the observation group received contracting lips-abdominal breathing training. The therapeutic effects, pulmonary ventilation function, serum levels of α-antitrypsin1 (α-AT1), surfactant protein D (SP-D), neutrophil elastase (NE), transforming growth factor beta 1 (TGF-ß1), and quality of life were analyzed and compared between the two groups both before and after the administration of treatment. The total effective rate of the observation group was 93.55%, which was significantly higher when compared with the control group (74.19%) (P less than 0.05). The levels of forced expiratory volume in one second (FEV1), FEV1/FVC ratio, vital capacity (VC), carbon monoxide diffusion capacity (DLco), and maximal voluntary ventilation (MVV) of the observation group were better when compared with the control group and had statistical significance (P less than 0.05). Before treatment, the serum levels of α-AT1, SP-D, NE, and TGF-ß1, and quality of life had no statistical significance in either group (P>0.05); after treatment, these indexes and the quality of life for the observation group were significantly higher when compared with the control group, with statistical significance (P less than 0.05). The respiratory training in acute organic fluorine-poisoned patients treated by NIPPV can improve the serum indexes, dilute toxicity, and recover pulmonary function, which play key roles in improving the therapeutic effects and quality of life of patients, and is worthy of clinical promotion.
[Mh] Termos MeSH primário: Exercícios Respiratórios
Hidrocarbonetos Fluorados/envenenamento
Elastase de Leucócito/sangue
Respiração com Pressão Positiva
Proteína D Associada a Surfactante Pulmonar/sangue
Fator de Crescimento Transformador beta1/sangue
alfa 1-Antitripsina/sangue
[Mh] Termos MeSH secundário: Adulto
Feminino
Seres Humanos
Masculino
Meia-Idade
[Pt] Tipo de publicação:CLINICAL TRIAL; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hydrocarbons, Fluorinated); 0 (Pulmonary Surfactant-Associated Protein D); 0 (TGFB1 protein, human); 0 (Transforming Growth Factor beta1); 0 (alpha 1-Antitrypsin); EC 3.4.21.37 (Leukocyte Elastase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE


  10 / 3526 MEDLINE  
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Texto completo
[PMID]:28612630
[Au] Autor:Vergelli C; Schepetkin IA; Crocetti L; Iacovone A; Giovannoni MP; Guerrini G; Khlebnikov AI; Ciattini S; Ciciani G; Quinn MT
[Ad] Endereço:a NEUROFARBA, Sezione di Farmaceutica e Nutraceutica , Università degli Studi di Firenze , Sesto Fiorentino , Italy.
[Ti] Título:Isoxazol-5(2H)-one: a new scaffold for potent human neutrophil elastase (HNE) inhibitors.
[So] Source:J Enzyme Inhib Med Chem;32(1):821-831, 2017 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human neutrophil elastase (HNE) is an important target for the development of novel and selective inhibitors to treat inflammatory diseases, especially pulmonary pathologies. Here, we report the synthesis, structure-activity relationship analysis, and biological evaluation of a new series of HNE inhibitors with an isoxazol-5(2H)-one scaffold. The most potent compound (2o) had a good balance between HNE inhibitory activity (IC value =20 nM) and chemical stability in aqueous buffer (t =8.9 h). Analysis of reaction kinetics revealed that the most potent isoxazolone derivatives were reversible competitive inhibitors of HNE. Furthermore, since compounds 2o and 2s contain two carbonyl groups (2-N-CO and 5-CO) as possible points of attack for Ser195, the amino acid of the active site responsible for the nucleophilic attack, docking studies allowed us to clarify the different roles played by these groups.
[Mh] Termos MeSH primário: Isoxazóis/farmacologia
Elastase de Leucócito/antagonistas & inibidores
Inibidores de Serino Proteinase/farmacologia
[Mh] Termos MeSH secundário: Relação Dose-Resposta a Droga
Seres Humanos
Isoxazóis/síntese química
Isoxazóis/química
Elastase de Leucócito/metabolismo
Estrutura Molecular
Inibidores de Serino Proteinase/síntese química
Inibidores de Serino Proteinase/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoxazoles); 0 (Serine Proteinase Inhibitors); EC 3.4.21.37 (Leukocyte Elastase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170615
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2017.1326915



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