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[PMID]:29267658
[Au] Autor:Ferrúa CP; Centeno EGZ; Rosa LCD; Amaral CCD; Severo RF; Sarkis-Onofre R; Nascimento GG; Cordenonzi G; Bast RK; Demarco FF; Nedel F
[Ad] Endereço:Universidade Católica de Pelotas - UCPel, Program in Health and Behavior, Pelotas, RS, Brazil.
[Ti] Título:How has dental pulp stem cells isolation been conducted? A scoping review.
[So] Source:Braz Oral Res;31:e87, 2017 Dec 18.
[Is] ISSN:1807-3107
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:The objective of this study was to realize a scoping review the literature in order to identify the profile of DPSCs isolation and analyze the possible risk factors that could change the native behavior of these cells. An initial search was conducted using the following MeSH terms: "(dental pulp stem cell [MeSH])"; "(dental pulp [MeSH])" AND "(stem cell [MeSH])"; "("dental pulp stem cell" [MeSH]")". The electronic search was done without date restriction up to and including April 2014, in PubMed, Scopus, Scielo and ISI Web of Knowledge databases. Studies were submitted to inclusion and exclusion criteria and 222 articles were included. Data showed that over the past 15 years many studies have been conducted using DPSCs. However this is the first systematic review regarding the isolation of stem cell, and more specifically of dental pulp stem cells. The isolation of dental pulp stem cells showed great variability, hampering the development of standard protocols to achieve in vitro dental pulp stem cells with similar characteristics. This scoping review combined, for the first time, the methodologies used for dental pulp stem isolation, highlighting the most frequently used.
[Mh] Termos MeSH primário: Polpa Dentária/citologia
Células-Tronco/citologia
[Mh] Termos MeSH secundário: Técnicas de Cultura de Células
Colagenases
Meios de Cultura
Seres Humanos
Viés de Publicação
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Culture Media); EC 3.4.24.- (Collagenases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE


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[PMID]:29366749
[Au] Autor:Gonzalez EA; Martins GR; Tavares AMV; Viegas M; Poletto E; Giugliani R; Matte U; Baldo G
[Ad] Endereço:Gene Therapy Center, Hospital de Clínicas de Porto Alegre, Porto Alegre, Brazil; Post-Graduation Program in Genetics and Molecular Biology, UFRGS, Porto Alegre, Brazil.
[Ti] Título:Cathepsin B inhibition attenuates cardiovascular pathology in mucopolysaccharidosis I mice.
[So] Source:Life Sci;196:102-109, 2018 Mar 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mucopolysaccharidosis type I (MPS I) is a lysosomal storage disorder with multisystemic features, including heart enlargement, heart valve dysfunction, and aortic stiffness and dilatation. Previous studies have shown that MPS I mice overexpress cathepsin B (CtsB) in multiple tissues, including those from the cardiovascular system. Here, we hypothesized that inhibition of CtsB could ameliorate cardiac function parameters, as well as aorta and valve abnormalities found in MPS I. First, we found that total elastase activity in an MPS I aorta is elevated. Following that, we demonstrated that CtsB leaks from the lysosome in MPS I human fibroblasts, possibly acting as a degradative agent of extracellular matrix components from the aorta, cardiac muscle, and heart valves. We then used a CtsB inhibitor in vivo in the MPS I mouse model. After 4 months of treatment, partial inhibition of CtsB activity in treated mice reduced aortic dilatation, as well as heart valve thickening, and led to improvements in cardiac function parameters, although none of these were completely normalized. Based on these results, we conclude that lysosomal alterations in this disease promote leakage of CtsB to outside the organelle, where this protein can have multiple pathological roles. CtsB inhibition improved cardiovascular parameters in MPS I mice and can have a potential benefit in this disease.
[Mh] Termos MeSH primário: Sistema Cardiovascular/patologia
Catepsina B/antagonistas & inibidores
Inibidores de Cisteína Proteinase/uso terapêutico
Dipeptídeos/uso terapêutico
Mucopolissacaridose I/diagnóstico por imagem
Mucopolissacaridose I/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Aorta/patologia
Aorta/fisiopatologia
Sistema Cardiovascular/diagnóstico por imagem
Catepsina B/metabolismo
Colagenases/metabolismo
Feminino
Fibroblastos/metabolismo
Testes de Função Cardíaca
Doenças das Valvas Cardíacas/diagnóstico por imagem
Doenças das Valvas Cardíacas/tratamento farmacológico
Doenças das Valvas Cardíacas/patologia
Seres Humanos
Lisossomos/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Mucopolissacaridose I/patologia
Elastase Pancreática/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cysteine Proteinase Inhibitors); 0 (Dipeptides); 134448-10-5 (N-(3-propylcarbamoyloxirane-2-carbonyl)-isoleucyl-proline); EC 3.4.21.36 (Pancreatic Elastase); EC 3.4.22.1 (Cathepsin B); EC 3.4.24.- (Collagenases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE


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[PMID]:27771138
[Au] Autor:Hiraishi N; Maruno T; Tochio N; Sono R; Otsuki M; Takatsuka T; Tagami J; Kobayashi Y
[Ad] Endereço:Cariology and Operative Dentistry, Department of Oral Health Sciences, Graduate School, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8549, Japan. Electronic address: hiraope@tmd.ac.jp.
[Ti] Título:Hesperidin interaction to collagen detected by physico-chemical techniques.
[So] Source:Dent Mater;33(1):33-42, 2017 01.
[Is] ISSN:1879-0097
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Dentin collagen can be modified by some plant-derived flavonoids to improve properties of dentin organic matrix. Hesperidin (HPN), a hesperetin-7-O-rutinoside flavonoid, has a potential of dentin modification for being based on evidence that a treatment with HPN may resist collagenase degradation and arrest demineralization of human dentin. In this study, biophysical and molecular-level information on the interaction of HPN and collagen was investigated. METHODS: HPN is extracted from citrus fruits. Sample collagenous solution was prepared using atelocollagen (ATCL) as a triple-helical peptide model. We have performed circular dichroism spectroscopic analysis, sedimentation velocity measurement by ultracentrifuge and saturation transfer difference measurement (STD) by NMR on HPN-collagen in solution state. RESULTS: The circular dichroism and sedimentation velocity measurement showed the evidence for the molecular interaction between ATCL and HPN, while HPN did not induce any conformational change of ATCL. The STD-NMR study further confirmed this interaction and suggested that HPN interacted with ATCL through its aromatic part, not through its disaccharide moiety. SIGNIFICANCE: These findings indicated that HPN is weakly bound to ATCL not causing structural modification of collagen. This interaction may contribute to the preservation of collagen by protecting from collagenase degradation.
[Mh] Termos MeSH primário: Colágeno/metabolismo
Dentina/metabolismo
Hesperidina/farmacologia
[Mh] Termos MeSH secundário: Colagenases/metabolismo
Seres Humanos
Espectroscopia de Ressonância Magnética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9007-34-5 (Collagen); E750O06Y6O (Hesperidin); EC 3.4.24.- (Collagenases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:D
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


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[PMID]:29246219
[Au] Autor:Jessberger S; Högger P; Genest F; Salter DM; Seefried L
[Ad] Endereço:Institut für Pharmazie und Lebensmittelchemie, Universität Würzburg, Am Hubland C7, 97074, Würzburg, Germany.
[Ti] Título:Cellular pharmacodynamic effects of Pycnogenol® in patients with severe osteoarthritis: a randomized controlled pilot study.
[So] Source:BMC Complement Altern Med;17(1):537, 2017 Dec 16.
[Is] ISSN:1472-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The standardized maritime pine bark extract (Pycnogenol®) has previously shown symptom alleviating effects in patients suffering from moderate forms of knee osteoarthritis (OA). The cellular mechanisms for this positive impact are so far unknown. The purpose of the present randomized pilot controlled study was to span the knowledge gap between the reported clinical effects of Pycnogenol® and its in vivo mechanism of action in OA patients. METHODS: Thirty three patients with severe OA scheduled for a knee arthroplasty either received 100 mg of Pycnogenol® twice daily or no treatment (control group) three weeks before surgery. Cartilage, synovial fluid and serum samples were collected during surgical intervention. Relative gene expression of cartilage homeostasis markers were analyzed in the patients' chondrocytes. Inflammatory and cartilage metabolism mediators were investigated in serum and synovial fluid samples. RESULTS: The oral intake of Pycnogenol® downregulated the gene expression of various cartilage degradation markers in the patients' chondrocytes, the decrease of MMP3, MMP13 and the pro-inflammatory cytokine IL1B were statistically significant (p ≤ 0.05). Additionally, protein concentrations of ADAMTS-5 in serum were reduced significantly (p ≤ 0.05) after three weeks intake of the pine bark extract. CONCLUSIONS: This is the first report about positive cellular effects of a dietary supplement on key catabolic and inflammatory markers in patients with severe OA. The results provide a rational basis for understanding previously reported clinical effects of Pycnogenol® on symptom scores of patients suffering from OA. TRIAL REGISTRATION: ISRCTN10754119 . Retrospectively registered 08/10/2015.
[Mh] Termos MeSH primário: Cartilagem/efeitos dos fármacos
Flavonoides/farmacologia
Osteoartrite do Joelho/tratamento farmacológico
Osteoartrite do Joelho/metabolismo
Líquido Sinovial/efeitos dos fármacos
[Mh] Termos MeSH secundário: Idoso
Biomarcadores/análise
Cartilagem/química
Colagenases/sangue
Feminino
Flavonoides/administração & dosagem
Flavonoides/uso terapêutico
Seres Humanos
Interleucina-1beta/sangue
Masculino
Meia-Idade
Projetos Piloto
Líquido Sinovial/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
[Nm] Nome de substância:
0 (Biomarkers); 0 (Flavonoids); 0 (IL1B protein, human); 0 (Interleukin-1beta); 0 (pycnogenols); EC 3.4.24.- (Collagenases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE
[do] DOI:10.1186/s12906-017-2044-1


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[PMID]:28963928
[Au] Autor:Chang Y; Wang X; Sun Z; Jin Z; Chen M; Wang X; Lammi MJ; Guo X
[Ad] Endereço:Department of Orthopaedics, The Third Affiliated Hospital (Shaanxi Provincial People's Hospital), Health Science Center of Xi'an Jiaotong University, Xi'an 710061, Shaanxi, PR China.
[Ti] Título:Inflammatory cytokine of IL-1ß is involved in T-2 toxin-triggered chondrocyte injury and metabolism imbalance by the activation of Wnt/ß-catenin signaling.
[So] Source:Mol Immunol;91:195-201, 2017 11.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mycotoxin T-2 exerts a causative role in Kashin-Beck disease (KBD) suffering chondrocyte apoptosis and cartilage matrix homeostasis disruption. Recent research corroborated the aberrant levels of pro-inflammatory cytokine IL-1ß in KBD patients and mycotoxin environment. In the present study, we investigated the relevance of IL-1ß in T-2 toxin-evoked chondrocyte cytotoxic injury and aberrant catabolism. High levels of IL-1ß were detected in serum and cartilages from KBD patients and in T-2-stimulated chondrocytes. Moreover, knockdown of IL-1ß antagonized the adverse effects of T-2 on cytotoxic injury by enhancing cell viability and inhibiting apoptosis. However, exogenous supplementation of IL-1ß further aggravated cell damage in response to T-2. Additionally, cessation of IL-1ß rescued T-2-elicited tilt of matrix homeostasis toward catabolism by elevating the transcription of collagen II and aggrecan, promoting release of sulphated glycosaminoglycans (sGAG) and TIMP1, and suppressing matrix metalloproteinases production including MMP-1, MMP-3 and MMP-13. Conversely, IL-1ß stimulation deteriorated T-2-induced disruption of matrix metabolism balance toward catabolism. Mechanistic analysis found the high activation of Wnt/ß-catenin in KBD patients and chondrocytes upon T-2. Furthermore, this activation was mitigated after IL-1ß inhibition, but further enhanced following IL-1ß precondition. Importantly, blocking this pathway by transfection with ß-catenin alleviated the adverse roles of IL-1ß on cytotoxic injury and metabolism disorders under T-2 conditioning. Together, this study elucidates a new insight into how T-2 deteriorates the pathological progression of KBD by regulating inflammation-related pathways, indicating a promising anti-inflammation strategy for KBD therapy.
[Mh] Termos MeSH primário: Condrócitos/imunologia
Interleucina-1beta/imunologia
Toxina T-2/toxicidade
Via de Sinalização Wnt/efeitos dos fármacos
beta Catenina/imunologia
[Mh] Termos MeSH secundário: Adulto
Agrecanas/biossíntese
Agrecanas/genética
Agrecanas/imunologia
Animais
Apoptose/genética
Apoptose/imunologia
Condrócitos/metabolismo
Condrócitos/patologia
Colágeno Tipo II/biossíntese
Colágeno Tipo II/genética
Colágeno Tipo II/imunologia
Colagenases/biossíntese
Colagenases/genética
Colagenases/imunologia
Matriz Extracelular/genética
Matriz Extracelular/imunologia
Matriz Extracelular/metabolismo
Matriz Extracelular/patologia
Feminino
Seres Humanos
Interleucina-1beta/genética
Interleucina-1beta/metabolismo
Doença de Kashin-Bek/genética
Doença de Kashin-Bek/imunologia
Doença de Kashin-Bek/metabolismo
Doença de Kashin-Bek/patologia
Masculino
Meia-Idade
Ratos
Ratos Sprague-Dawley
Inibidor Tecidual de Metaloproteinase-1/biossíntese
Inibidor Tecidual de Metaloproteinase-1/genética
Inibidor Tecidual de Metaloproteinase-1/imunologia
Transcrição Genética/efeitos dos fármacos
Transcrição Genética/imunologia
Via de Sinalização Wnt/genética
Via de Sinalização Wnt/imunologia
beta Catenina/genética
beta Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aggrecans); 0 (Collagen Type II); 0 (IL1B protein, human); 0 (IL1B protein, rat); 0 (Interleukin-1beta); 0 (TIMP1 protein, human); 0 (Tissue Inhibitor of Metalloproteinase-1); 0 (beta Catenin); 0 (tissue inhibitor of metalloproteinase-1 protein, rat); EC 3.4.24.- (Collagenases); I3FL5NM3MO (T-2 Toxin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171120
[Lr] Data última revisão:
171120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171001
[St] Status:MEDLINE


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[PMID]:28961239
[Au] Autor:Dong S; Balaraman V; Kantor AM; Lin J; Grant DG; Held NL; Franz AWE
[Ad] Endereço:Department of Veterinary Pathobiology, University of Missouri, Columbia, Missouri, United States of America.
[Ti] Título:Chikungunya virus dissemination from the midgut of Aedes aegypti is associated with temporal basal lamina degradation during bloodmeal digestion.
[So] Source:PLoS Negl Trop Dis;11(9):e0005976, 2017 Sep.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the mosquito, the midgut epithelium is the initial tissue to become infected with an arthropod-borne virus (arbovirus) that has been acquired from a vertebrate host along with a viremic bloodmeal. Following its replication in midgut epithelial cells, the virus needs to exit the midgut and infect secondary tissues including the salivary glands before it can be transmitted to another vertebrate host. The viral exit mechanism from the midgut, the midgut escape barrier (MEB), is poorly understood although it is an important determinant of mosquito vector competence for arboviruses. Using chikungunya virus (CHIKV) as a model in Aedes aegypti, we demonstrate that the basal lamina (BL) of the extracellular matrix (ECM) surrounding the midgut constitutes a potential barrier for the virus. The BL, predominantly consisting of collagen IV and laminin, becomes permissive during bloodmeal digestion in the midgut lumen. Bloodmeal digestion, BL permissiveness, and CHIKV dissemination are coincident with increased collagenase activity, diminished collagen IV abundance, and BL shredding in the midgut between 24-32 h post-bloodmeal. This indicates that there may be a window-of-opportunity during which the MEB in Ae. aegypti becomes permissive for CHIKV. Matrix metalloproteinases (MMPs) are the principal extracellular endopeptidases responsible for the degradation/remodeling of the ECM including the BL. We focused on Ae. aegypti (Ae)MMP1, which is expressed in midgut epithelial cells, is inducible upon bloodfeeding, and shows collagenase (gelatinase) activity. However, attempts to inhibit AeMMP activity in general or specifically that of AeMMP1 did not seem to affect its function nor produce an altered midgut escape phenotype. As an alternative, we silenced and overexpressed the Ae. aegypti tissue inhibitor of metalloproteinases (AeTIMP) in the mosquito midgut. AeTIMP was highly upregulated in the midgut during bloodmeal digestion and was able to inhibit MMP activity in vitro. Bloodmeal-inducible, midgut-specific overexpression of AeTIMP or its expression via a recombinant CHIKV significantly increased midgut dissemination rates of the virus. Possibly, AeTIMP overexpression affected BL degradation and/or restoration thereby increasing the midgut dissemination efficiency of the virus.
[Mh] Termos MeSH primário: Aedes/fisiologia
Aedes/virologia
Membrana Basal/metabolismo
Sangue
Vírus Chikungunya/fisiologia
Inibidores Teciduais de Metaloproteinases/metabolismo
[Mh] Termos MeSH secundário: Aedes/anatomia & histologia
Animais
Membrana Basal/virologia
Febre de Chikungunya/virologia
Vírus Chikungunya/genética
Colagenases/metabolismo
Matriz Extracelular/metabolismo
Matriz Extracelular/virologia
Trato Gastrointestinal/anatomia & histologia
Trato Gastrointestinal/citologia
Trato Gastrointestinal/patologia
Trato Gastrointestinal/virologia
Metaloproteinase 1 da Matriz/genética
Metaloproteinase 1 da Matriz/metabolismo
Proteínas Recombinantes/metabolismo
Inibidores Teciduais de Metaloproteinases/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 0 (Tissue Inhibitor of Metalloproteinases); EC 3.4.24.- (Collagenases); EC 3.4.24.7 (Matrix Metalloproteinase 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170930
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005976


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[PMID]:28841617
[Au] Autor:Nordenskjöld J; Waldén M; Kjellin A; Franzén H; Atroshi I
[Ad] Endereço:Hässleholm, Lund, Linköping, and Ängelholm, Sweden From the Department of Orthopedics, Hässleholm-Kristianstad Hospitals; the Department of Clinical Sciences-Orthopedics, Lund University; the Department of Medical and Health Sciences, Linköping University; and the Department of Orthopedics Aleris, Ängelholm Hospital.
[Ti] Título:Benefit of Local Anesthesia in Reducing Pain during Collagenase Injection for Dupuytren's Contracture.
[So] Source:Plast Reconstr Surg;140(3):565-569, 2017 Sep.
[Is] ISSN:1529-4242
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Collagenase injection for Dupuytren's contracture is commonly administered without anesthesia. The authors studied the benefit of injecting local anesthesia before collagenase in reducing treatment-related pain. This prospective cohort study included 187 patients (mean age, 69 years; 80 percent men) at two orthopedic departments in Sweden. At one center, 161 consecutive patients scheduled for collagenase injection were assigned to two groups by alternating outpatient clinics; 78 received collagenase without local anesthesia using a modified method (injecting 0.80 mg in multiple spots in the cord) and 83 received local anesthesia injected in the proximal palm before collagenase. At the other center, 26 consecutive patients received collagenase using the standard method (0.58 mg injected in one spot) without local anesthesia. Immediately after the first injection (collagenase or local anesthesia), the patients rated the severity of injection-related pain on a visual analogue scale from 0 (no pain) to 10 (worst pain). Before finger manipulation 1 or 2 days after injection, the patients rated the pain experienced since injection. Mean score ± SD for pain experienced during modified collagenase injection was 4.3 ± 2.5 without local anesthesia and 2.3 ± 1.7 during injection of local anesthesia (before collagenase) (age- and sex-adjusted mean difference, 2.1; 95 percent CI, 1.5 to 2.7; p < 0.001). Mean pain score ± SD during standard collagenase injection without local anesthesia was 4.8 ± 1.8. Mean pain score ± SD during the injection-manipulation interval was 2.9 ± 1.9 in the group without local anesthesia and 2.9 ± 2.3 in the local anesthesia group (p = 0.79). This study shows that local anesthesia significantly reduces the patient's overall pain experience during collagenase treatment for Dupuytren's contracture. CLINICAL QUESTION/LEVEL OF EVIDENCE: Therapeutic, II.
[Mh] Termos MeSH primário: Anestesia Local/métodos
Anestésicos Locais/administração & dosagem
Colagenases/administração & dosagem
Contratura de Dupuytren/terapia
Injeções Intralesionais/efeitos adversos
Dor/tratamento farmacológico
[Mh] Termos MeSH secundário: Idoso
Feminino
Seres Humanos
Masculino
Meia-Idade
Dor/etiologia
Estudos Prospectivos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anesthetics, Local); EC 3.4.24.- (Collagenases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170826
[St] Status:MEDLINE
[do] DOI:10.1097/PRS.0000000000003583


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[PMID]:28759010
[Au] Autor:Plebani R; Tripaldi R; Lanuti P; Recchiuti A; Patruno S; Di Silvestre S; Simeone P; Anile M; Venuta F; Prioletta M; Mucilli F; Del Porto P; Marchisio M; Pandolfi A; Romano M
[Ad] Endereço:Department of Medical, Oral and Biotechnological Sciences, "G. d'Annunzio" University of Chieti-Pescara, Chieti, Italy.
[Ti] Título:Establishment and long-term culture of human cystic fibrosis endothelial cells.
[So] Source:Lab Invest;97(11):1375-1384, 2017 Nov.
[Is] ISSN:1530-0307
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Endothelial cell (EC) dysfunction has been reported in cystic fibrosis (CF) patients. Thus, the availability of CF EC is paramount to uncover mechanisms of endothelial dysfunction in CF. Using collagenase digestion, we isolated cells from small fragments of pulmonary artery dissected from non-CF lobes or explanted CF lungs. These cells were a heterogeneous mixture, containing variable percentages of EC. To obtain virtually pure pulmonary artery endothelial cells (PAEC), we developed an easy, inexpensive, and reliable method, based on the differential adhesion time of pulmonary artery cells collected after collagenase digestion. With this method, we obtained up to 95% pure non-CF and CF-PAEC. Moreover, we also succeed at immortalizing both PAEC and CF-PAEC, which remained viable and with unchanged phenotype and proliferation rate over the 30th passage. These cells recapitulated cystic fibrosis transmembrane conductance regulator expression and functions of the parental cells. Thus, we isolated for the first time endothelial cells from CF patients, providing a valuable tool to define the emerging role of EC in CF lung and vascular disease.
[Mh] Termos MeSH primário: Fibrose Cística/patologia
Endotélio Vascular/patologia
Pulmão/patologia
Artéria Pulmonar/patologia
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Biomarcadores/metabolismo
Adesão Celular
Linhagem Celular Transformada
Proliferação Celular
Separação Celular
Sobrevivência Celular
Células Cultivadas
Colagenases/metabolismo
Fibrose Cística/genética
Fibrose Cística/metabolismo
Fibrose Cística/cirurgia
Regulador de Condutância Transmembrana em Fibrose Cística/genética
Regulador de Condutância Transmembrana em Fibrose Cística/metabolismo
Impedância Elétrica
Endotélio Vascular/metabolismo
Seres Humanos
Imunofenotipagem
Pulmão/irrigação sanguínea
Pulmão/metabolismo
Pulmão/cirurgia
Mutação
Pneumonectomia
Artéria Pulmonar/metabolismo
Técnicas de Cultura de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (CFTR protein, human); 126880-72-6 (Cystic Fibrosis Transmembrane Conductance Regulator); EC 3.4.24.- (Collagenases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE
[do] DOI:10.1038/labinvest.2017.74


  9 / 6049 MEDLINE  
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[PMID]:28750062
[Au] Autor:Ochocka R; Hering A; Stefanowicz-Hajduk J; Cal K; Baranska H
[Ad] Endereço:Department of Biology and Pharmaceutical Botany, Medical University of Gdansk, Gdansk, Poland.
[Ti] Título:The effect of mangiferin on skin: Penetration, permeation and inhibition of ECM enzymes.
[So] Source:PLoS One;12(7):e0181542, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mangiferin (2-C-ß-D-glucopyranosyl-1,3,6,7-tetrahydroxyxanthone) is a polyphenol with strong antioxidant properties. Mangiferin is obtained from the mango tree (Mangifera indica L., Anacardiaceae). It has been proven that mangiferin exhibits many pharmacological activities. The aim of this study was to analyze the penetration of mangiferin into the human skin and through the skin. According to our knowledge, skin penetration and permeation studies of mangiferin have not been analyzed so far. Additionally, the influence of mangiferin on two Extracellular Matrix Enzymes (ECM): collagenase and elastase, was evaluated for the first time. It has been indicated that mangiferin is able to permeate the stratum corneum and penetrate into the epidermis and dermis in comparable amounts. For confirmation of the obtained results, fluorescence microscopy was successfully utilized. The analysis revealed the capability of mangiferin to reversibly inhibit elastase and collagenase activity. The mechanism of mangiferin interaction with both enzymes was estimated as a noncompetitive inhibition.
[Mh] Termos MeSH primário: Colagenases/metabolismo
Matriz Extracelular/enzimologia
Elastase Pancreática/metabolismo
Absorção Cutânea/efeitos dos fármacos
Pele/efeitos dos fármacos
Xantonas/farmacologia
[Mh] Termos MeSH secundário: Adulto
Inibidores Enzimáticos/farmacologia
Matriz Extracelular/efeitos dos fármacos
Seres Humanos
Cinética
Meia-Idade
Soluções
Xantonas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Solutions); 0 (Xanthones); 1M84LD0UMD (mangiferin); EC 3.4.21.36 (Pancreatic Elastase); EC 3.4.24.- (Collagenases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181542


  10 / 6049 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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