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Pesquisa : D12.776.395.550.200.700.775 [Categoria DeCS]
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[PMID]:29377939
[Au] Autor:Budzyn M; Iskra M; Turkiewicz W; Krasinski Z; Gryszczynska B; Kasprzak MP
[Ad] Endereço:Department of General Chemistry, Chair of Chemistry and Clinical Biochemistry, Poznan University of Medical Sciences, Poznan, Poland.
[Ti] Título:Plasma concentration of selected biochemical markers of endothelial dysfunction in women with various severity of chronic venous insufficiency (CVI)-A pilot study.
[So] Source:PLoS One;13(1):e0191902, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Although the endothelial dysfunction is considered to be implicated in the pathogenesis of chronic venous insufficiency (CVI) the endothelial status in patients with venous disorders is still not fully evaluated. Therefore the aim of the study was to measure the concentration of selected markers of endothelial dysfunction: von Willebrand factor (vWf), soluble P-selectin (sP-selectin), soluble thrombomodulin (sTM) and soluble VE-cadherin (sVE-cadherin) in CVI women who constitute the most numerous group of patients suffering from venous disease. MATERIALS AND METHODS: Forty four women with CVI were involved in the study and divided into subgroups based on CEAP classification. Concentration of vWf, sP-selectin, sTM and sVE-cadherin were measured and compared with those obtained in 25 healthy age and sex-matched women. RESULTS: It was found that the concentration of sTM increased and sVEcadherin decreased along with disease severity in CVI women. A significant rise of sTM was observed especially in CVI women, with the highest inflammation status reflected by hsCRP or elastase concentration, and in CVI women with a high oxidative stress manifested by an increased plasma MDA. A significant fall of circulating sVE-cadherin was reported in CVI women with moderate to highest intensity of inflammation and oxidative stress. There was no change in vWF and sP-selectin concentration at any stage of CVI severity. CONCLUSIONS: The results of the present study demonstrate the presence of endothelial dysfunction in women suffering from CVI which seems to progress with the disease severity and may be associated with inflammation and enhanced oxidative stress.
[Mh] Termos MeSH primário: Biomarcadores/sangue
Endotélio Vascular/fisiopatologia
Insuficiência Venosa/sangue
[Mh] Termos MeSH secundário: Adulto
Antígenos CD/sangue
Caderinas/sangue
Doença Crônica
Feminino
Seres Humanos
Meia-Idade
Selectina-P/sangue
Projetos Piloto
Índice de Gravidade de Doença
Trombomodulina/sangue
Fator de von Willebrand/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Biomarkers); 0 (Cadherins); 0 (P-Selectin); 0 (Thrombomodulin); 0 (cadherin 5); 0 (von Willebrand Factor)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180130
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191902


  2 / 5792 MEDLINE  
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[PMID]:28467723
[Au] Autor:Diaz-Morales N; Rovira-Llopis S; Bañuls C; Lopez-Domenech S; Escribano-Lopez I; Veses S; Jover A; Rocha M; Hernandez-Mijares A; Victor VM
[Ad] Endereço:1 Service of Endocrinology and Nutrition, University Hospital Doctor Peset , Foundation for the Promotion of Health and Biomedical Research in the Valencian Region (FISABIO), Valencia, Spain .
[Ti] Título:Does Metformin Protect Diabetic Patients from Oxidative Stress and Leukocyte-Endothelium Interactions?
[So] Source:Antioxid Redox Signal;27(17):1439-1445, 2017 Dec 10.
[Is] ISSN:1557-7716
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Since metformin can exert beneficial vascular effects, we aimed at studying its effect on reactive oxygen species (ROS) production, antioxidant enzyme expression, levels of adhesion molecules, and leukocyte-endothelium interactions in the leukocytes from type 2 diabetic (T2D) patients. The study was carried out in 72 T2D patients (41 of whom were treated with metformin for at least 12 months at a dose of 1700 mg per day), and in 40 sex- and age-matched control subjects. Leukocytes from T2D patients exhibited enhanced levels of mitochondrial ROS and decreased mRNA levels of glutathione peroxidase 1 (gpx1) and sirtuin 3 (sirt3) with respect to controls, whereas metformin was shown to revert these effects. No changes were observed on total ROS production and the expression levels of superoxide dismutase 1 and catalase. Furthermore, increases in leukocyte-endothelial interactions and intercellular adhesion molecule-1 and P-selectin levels were found in T2D and were also restored in metformin-treated patients. Our findings raise the question of whether metformin could modulate the appearance of atherosclerosis in T2D patients and reduce vascular events by decreasing leukocyte oxidative stress through an increase in gpx1 and sirt3 expression, and undermining adhesion molecule levels and leukocyte-endothelium interactions. Antioxid. Redox Signal. 27, 1439-1445.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 2/tratamento farmacológico
Células Endoteliais/efeitos dos fármacos
Hipoglicemiantes/administração & dosagem
Leucócitos/efeitos dos fármacos
Metformina/administração & dosagem
Estresse Oxidativo/efeitos dos fármacos
[Mh] Termos MeSH secundário: Idoso
Catalase
Adesão Celular
Diabetes Mellitus Tipo 2/genética
Diabetes Mellitus Tipo 2/metabolismo
Células Endoteliais/metabolismo
Feminino
Glutationa Peroxidase/genética
Seres Humanos
Hipoglicemiantes/farmacologia
Molécula 1 de Adesão Intercelular/metabolismo
Leucócitos/metabolismo
Masculino
Metformina/farmacologia
Meia-Idade
Selectina-P/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Sirtuína 3/genética
Superóxido Dismutase-1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hypoglycemic Agents); 0 (ICAM1 protein, human); 0 (P-Selectin); 0 (Reactive Oxygen Species); 0 (SOD1 protein, human); 126547-89-5 (Intercellular Adhesion Molecule-1); 9100L32L2N (Metformin); EC 1.11.1.- (glutathione peroxidase GPX1); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.15.1.1 (Superoxide Dismutase-1); EC 3.5.1.- (SIRT3 protein, human); EC 3.5.1.- (Sirtuin 3)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1089/ars.2017.7122


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


  4 / 5792 MEDLINE  
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[PMID]:29244817
[Au] Autor:Montiel-Dávalos A; Silva Sánchez GJ; Huerta-García E; Rueda-Romero C; Soca Chafre G; Mitre-Aguilar IB; Alfaro-Moreno E; Pedraza-Chaverri J; López-Marure R
[Ad] Endereço:Subdirección de Investigación Básica, Instituto Nacional de Cancerología, Ciudad de México, México.
[Ti] Título:Curcumin inhibits activation induced by urban particulate material or titanium dioxide nanoparticles in primary human endothelial cells.
[So] Source:PLoS One;12(12):e0188169, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Curcumin has protective effects against toxic agents and shows preventive properties for various diseases. Particulate material with an aerodynamic diameter of ≤10 µm (PM10) and titanium dioxide nanoparticles (TiO2-NPs) induce endothelial dysfunction and activation. We explored whether curcumin is able to attenuate different events related to endothelial activation. This includes adhesion, expression of adhesion molecules and oxidative stress induced by PM10 and TiO2-NPs. Human umbilical vein endothelial cells (HUVEC) were treated with 1, 10 and 100 µM curcumin for 1 h and then exposed to PM10 at 3 µg/cm2 or TiO2-NPs at 10 µg/cm2. Cell adhesion was evaluated by co-culture with U937 human myelomonocytic cells. Adhesion molecules expression was measured by flow cytometry after 3 or 24 h of exposure. Oxidative stress was determined by 2,7-dichlorodihydrofluorescein (H2DCF) oxidation. PM10 and TiO2-NPs induced the adhesion of U937 cells and the expression of E- and P-selectins, intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1) and platelet-endothelial cell adhesion molecule-1 (PECAM-1). The expression of E- and P-selectins matched the adhesion of monocytes to HUVEC after 3 h. In HUVEC treated with 1 or 10 µM curcumin, the expression of adhesion molecules and monocytes adhesion was significantly diminished. Curcumin also partially reduced the H2DCF oxidation induced by PM10 and TiO2-NPs. Our results suggest an anti-inflammatory and antioxidant role by curcumin attenuating the activation caused on endothelial cells by exposure to particles. Therefore, curcumin could be useful in the treatment of diseases where an inflammatory process and endothelial activation are involved.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Curcumina/farmacologia
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Nanopartículas/toxicidade
Material Particulado/antagonistas & inibidores
[Mh] Termos MeSH secundário: Biomarcadores/metabolismo
Adesão Celular/efeitos dos fármacos
Cidades
Técnicas de Cocultura
Selectina E/genética
Selectina E/metabolismo
Fluoresceínas/química
Expressão Gênica
Células Endoteliais da Veia Umbilical Humana/citologia
Células Endoteliais da Veia Umbilical Humana/metabolismo
Seres Humanos
Molécula 1 de Adesão Intercelular/genética
Molécula 1 de Adesão Intercelular/metabolismo
México
Estresse Oxidativo/efeitos dos fármacos
Selectina-P/genética
Selectina-P/metabolismo
Material Particulado/farmacologia
Molécula-1 de Adesão Celular Endotelial de Plaquetas/genética
Molécula-1 de Adesão Celular Endotelial de Plaquetas/metabolismo
Titânio/farmacologia
Células U937
Molécula 1 de Adesão de Célula Vascular/genética
Molécula 1 de Adesão de Célula Vascular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Biomarkers); 0 (E-Selectin); 0 (Fluoresceins); 0 (ICAM1 protein, human); 0 (P-Selectin); 0 (Particulate Matter); 0 (Platelet Endothelial Cell Adhesion Molecule-1); 0 (SELE protein, human); 0 (Vascular Cell Adhesion Molecule-1); 106070-31-9 (2',7'-dichlorodihydrofluorescein); 126547-89-5 (Intercellular Adhesion Molecule-1); 15FIX9V2JP (titanium dioxide); D1JT611TNE (Titanium); IT942ZTH98 (Curcumin)
[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:171216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188169


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[PMID]:28957360
[Au] Autor:Matus V; Valenzuela JG; Hidalgo P; Pozo LM; Panes O; Wozniak A; Mezzano D; Pereira J; Sáez CG
[Ad] Endereço:Department of Hematology-Oncology, School of Medicine, Pontificia Universidad Católica de Chile, Santiago, Chile.
[Ti] Título:Human platelet interaction with E. coli O111 promotes tissue-factor-dependent procoagulant activity, involving Toll like receptor 4.
[So] Source:PLoS One;12(9):e0185431, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Platelets have a major role in clotting activation and contribute to the innate immune response during systemic infections. Human platelets contain tissue factor (TF) and express functional Toll-like receptor 4 (TLR4). However, the role of TLR4 in triggering the procoagulant properties of platelets, upon challenge with bacteria, is yet unknown. Our hypothesis is that E. coli O111-TLR4 interaction activates platelets and elicits their procoagulant activity. We demonstrated that the strain, but not ultrapure LPS, increased surface P-selectin expression, platelet dependent TF procoagulant activity (TF-PCA) and prompted a faster thrombin generation (TG). Blockade of TLR4 resulted in decreased platelet activation, TF-PCA and TG, revealing the participation of this immune receptor on the procoagulant response of platelets. Our results provide a novel mechanism by which individuals with bacterial infections would have an increased incidence of blood clots. Furthermore, the identification of platelet TF and TLR4 as regulators of the effect of E. coli O111 might represent a novel therapeutic target to reduce the devastating consequences of the hemostatic disorder during sepsis.
[Mh] Termos MeSH primário: Coagulação Sanguínea
Plaquetas/metabolismo
Plaquetas/microbiologia
Escherichia coli/metabolismo
Tromboplastina/metabolismo
Receptor 4 Toll-Like/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Anticorpos Monoclonais/farmacologia
Coagulação Sanguínea/efeitos dos fármacos
Plaquetas/efeitos dos fármacos
Escherichia coli/efeitos dos fármacos
Seres Humanos
Lipoproteínas/farmacologia
Meia-Idade
Selectina-P/metabolismo
Ativação Plaquetária/efeitos dos fármacos
Plasma Rico em Plaquetas/metabolismo
Trombina/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Lipoproteins); 0 (P-Selectin); 0 (TLR4 protein, human); 0 (Toll-Like Receptor 4); 0 (lipoprotein-associated coagulation inhibitor); 9035-58-9 (Thromboplastin); EC 3.4.21.5 (Thrombin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185431


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[PMID]:28934202
[Au] Autor:Tunjungputri RN; Gasem MH; van der Does W; Sasongko PH; Isbandrio B; Urbanus RT; de Groot PG; van der Ven A; de Mast Q
[Ad] Endereço:Department of Internal Medicine, Radboud university medical center, Nijmegen, The Netherlands.
[Ti] Título:Platelet dysfunction contributes to bleeding complications in patients with probable leptospirosis.
[So] Source:PLoS Negl Trop Dis;11(9):e0005915, 2017 Sep.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Severe leptospirosis is frequently complicated by a hemorrhagic diathesis, of which the pathogenesis is still largely unknown. Thrombocytopenia is common, but often not to the degree that spontaneous bleeding is expected. We hypothesized that the hemorrhagic complications are not only related to thrombocytopenia, but also to platelet dysfunction, and that increased binding of von Willebrand factor (VWF) to platelets is involved in both platelet dysfunction and increased platelet clearance. METHODOLOGY/PRINCIPAL FINDINGS: A prospective study was carried out in Semarang, Indonesia, enrolling 33 hospitalized patients with probable leptospirosis, of whom 15 developed clinical bleeding, and 25 healthy controls. Platelet activation and reactivity were determined using flow cytometry by measuring the expression of P-selectin and activation of the αIIbß3 integrin by the binding of fibrinogen in unstimulated samples and after ex vivo stimulation by the platelet agonists adenosine-diphosphate (ADP) and thrombin-receptor activating peptide (TRAP). Platelet-VWF binding, before and after VWF stimulation by ristocetin, as well as plasma levels of VWF, active VWF, the VWF-inactivating enzyme ADAMTS13, thrombin-antithrombin complexes (TAT) and P-selectin were also measured. Bleeding complications were graded using the WHO bleeding scale. Our study revealed that platelet activation, with a secondary platelet dysfunction, is a feature of patients with probable leptospirosis, especially in those with bleeding manifestations. There was a significant inverse correlation of bleeding score with TRAP-stimulated P-selectin and platelet-fibrinogen binding (R = -0.72, P = 0.003 and R = -0.66, P = 0.01, respectively) but not with platelet count. Patients with bleeding also had a significantly higher platelet-VWF binding. Platelet counts were inversely correlated with platelet-VWF binding (R = -0.74; P = 0.0009. There were no correlations between platelet-VWF binding and the degree of platelet dysfunction, suggesting that increased platelet-VWF binding does not directly interfere with the platelet αIIbß3 signaling pathway in patients with probable leptospirosis. CONCLUSION/SIGNIFICANCE: Platelet dysfunction is common in probable leptospirosis patients with manifest bleeding. Increased VWF-platelet binding may contribute to the activation and clearance of platelets.
[Mh] Termos MeSH primário: Plaquetas/patologia
Hemorragia/etiologia
Hemorragia/patologia
Leptospirose/patologia
[Mh] Termos MeSH secundário: Adulto
Feminino
Fibrinogênio/metabolismo
Seres Humanos
Indonésia
Masculino
Meia-Idade
Selectina-P/análise
Ativação Plaquetária
Complexo Glicoproteico GPIIb-IIIa de Plaquetas/metabolismo
Estudos Prospectivos
Ligação Proteica
Fator de von Willebrand/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (P-Selectin); 0 (Platelet Glycoprotein GPIIb-IIIa Complex); 0 (von Willebrand Factor); 9001-32-5 (Fibrinogen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005915


  7 / 5792 MEDLINE  
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[PMID]:28855423
[Au] Autor:Yao Y; Chen Y; Adili R; McKeown T; Chen P; Zhu G; Li D; Ling W; Ni H; Yang Y
[Ad] Endereço:Department of Nutrition, School of Public Health, Sun Yat-Sen University, Guangzhou, People's Republic of China.
[Ti] Título:Plant-based Food Cyanidin-3-Glucoside Modulates Human Platelet Glycoprotein VI Signaling and Inhibits Platelet Activation and Thrombus Formation.
[So] Source:J Nutr;147(10):1917-1925, 2017 Oct.
[Is] ISSN:1541-6100
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Platelets play an important role in hemostasis, thrombosis, and atherosclerosis. Glycoprotein VI (GPVI) is a major platelet receptor that interacts with exposed collagen on injured vessel walls. Our previous studies have shown that anthocyanins (a type of natural plant pigment) attenuate platelet function; however, whether anthocyanins affect collagen-induced GPVI signaling remains unknown. The objective of this study was to explore the effects of cyanidin-3-glucoside (Cy-3-g, one of the major bioactive compounds in anthocyanins) on platelet activation and thrombosis and the GPVI signaling pathway. Platelets from healthy men and women were isolated and incubated with different concentrations (0, 0.5, 5, and 50 µM) of Cy-3-g. The expression of activated integrin αIIbß3, P-selectin, CD63, and CD40L, fibrinogen binding to platelets, and platelet aggregation were evaluated in vitro. Platelet adhesion and aggregation in whole blood under flow conditions were assessed in collagen-coated perfusion chambers. Thrombosis and hemostasis were assessed in 3-4-wk-old male C57BL/6J mice through FeCl -induced intravital microscopy and tail bleeding time. The effect of Cy-3-g on collagen-induced human platelet GPVI signaling was explored with Western blot. Cy-3-g attenuated platelet function in a dose-dependent manner. The 0.5-µM dose of Cy-3-g inhibited ( < 0.05) human platelet adhesion and aggregation to collagen at both venous (-54.02%) and arterial (-22.90%) shear stresses. The 5-µM dose inhibited ( < 0.05) collagen-induced human platelet activation (PAC-1: -48.21%, P-selectin: -50.63%), secretion (CD63: -73.89%, CD40L: -43.70%), fibrinogen binding (-56.79%), and aggregation (-17.81%). The 5-µM dose attenuated ( < 0.01) thrombus growth (-66.67%) without prolonging bleeding time in mice. The 50-µM dose downregulated ( < 0.05) collagen-induced GPVI signaling in human platelets and significantly decreased phosphorylation of Syk-linker for activation of T cells (LAT)-SLP76 (Syk: -39.08%, LAT: -32.25%, SLP76: -40.00%) and the expression of Lyn (-31.89%), Fyn (-36.27%), and phospholipase C-γ2 (-39.08%). Cy-3-g inhibits human platelet activation, aggregation, secretion, and thrombus formation, and downregulates the collagen-GPVI signaling pathway. Supplementation of Cy-3-g may have protective effects against atherothrombosis.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Fitoterapia
Extratos Vegetais/farmacologia
Plantas Comestíveis/química
Agregação Plaquetária/efeitos dos fármacos
Glicoproteínas da Membrana de Plaquetas/metabolismo
Trombose/prevenção & controle
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/sangue
Adulto
Idoso
Animais
Antocianinas/farmacologia
Antocianinas/uso terapêutico
Antígenos CD/sangue
Aterosclerose/sangue
Aterosclerose/dietoterapia
Aterosclerose/etiologia
Colágeno/sangue
Feminino
Glucosídeos/farmacologia
Glucosídeos/uso terapêutico
Hemostasia/efeitos dos fármacos
Seres Humanos
Masculino
Camundongos Endogâmicos C57BL
Meia-Idade
Selectina-P/sangue
Fosfoproteínas/sangue
Extratos Vegetais/uso terapêutico
Ativação Plaquetária/efeitos dos fármacos
Transdução de Sinais
Trombose/sangue
Trombose/etiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Anthocyanins); 0 (Antigens, CD); 0 (Glucosides); 0 (P-Selectin); 0 (Phosphoproteins); 0 (Plant Extracts); 0 (Platelet Membrane Glycoproteins); 0 (SELP protein, human); 0 (SLP-76 signal Transducing adaptor proteins); 0 (platelet membrane glycoprotein VI); 7084-24-4 (cyanidin 3-O-glucoside); 9007-34-5 (Collagen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.3945/jn.116.245944


  8 / 5792 MEDLINE  
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[PMID]:28703861
[Au] Autor:Bontekoe IJ; van der Meer PF; van den Hurk K; Verhoeven AJ; de Korte D
[Ad] Endereço:Department of Product and Process Development, Sanquin Blood Bank, Amsterdam, the Netherlands.
[Ti] Título:Platelet storage performance is consistent by donor: a pilot study comparing "good" and "poor" storing platelets.
[So] Source:Transfusion;57(10):2373-2380, 2017 Oct.
[Is] ISSN:1537-2995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In retrospective studies, it has been shown that differences in storage variables of platelet (PLT) concentrates (PCs) are partially donor dependent. It was our aim to prospectively determine the donor effect on PLT quality. STUDY DESIGN AND METHODS: Based on quality control data of outdated apheresis PCs, male donors were selected with at least one PC with a pH value of more than 7.0 ("good," n = 6) or one PC with a pH value of less than 6.7 ("poor," n = 6) on Day 8. These donors donated a PC (Trima Accel, Terumo) and completed a short questionnaire about their health and lifestyle. PCs were stored for 12 days and analyzed at regular intervals for in vitro quality. RESULTS: Donor characteristics were comparable, except that zero of six good and four of six poor donors reported high blood pressure and/or high cholesterol/fat and/or use of medicines. Lactate production in good PCs was lower than that in poor PCs (0.09 ± 0.03 mmol/day/10 PLTs vs. 0.13 ± 0.04 mmol/day/10 PLTs, p < 0.05) resulting in a higher pH from Day 5 onward. At the end of storage, the good PCs showed lower CD62P expression, lower phosphatidylserine exposure, and higher mitochondrial membrane potential. PLT functional properties were only slightly different. Despite having lower pH, the poor PCs also fulfilled European Guidelines during 7-day storage. CONCLUSION: Platelet storage performance is consistent when donors are dichotomized as having good or poor storing PLTs. Metabolic differences are perhaps due to different functionality of the mitochondria. More research is needed to establish the underlying causes and the implications for donors and blood products.
[Mh] Termos MeSH primário: Doadores de Sangue
Plaquetas/citologia
Preservação de Sangue/normas
[Mh] Termos MeSH secundário: Adulto
Idoso
Seres Humanos
Concentração de Íons de Hidrogênio
Masculino
Potencial da Membrana Mitocondrial
Meia-Idade
Selectina-P/sangue
Fosfatidilserinas/metabolismo
Projetos Piloto
Controle de Qualidade
Estudos Retrospectivos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (P-Selectin); 0 (Phosphatidylserines); 0 (SELP protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1111/trf.14238


  9 / 5792 MEDLINE  
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[PMID]:28692478
[Au] Autor:Legaz Pérez I; Falcón M; Gimenez M; Diaz FM; Pérez-Cárceles MD; Osuna E; Nuno-Vieira D; Luna A
[Ad] Endereço:From the *Department of Legal and Forensic Medicine, Biomedical Research Institute, Regional Campus of International Excellence "Campus Mare Nostrum," Faculty of Medicine, University of Murcia, Murcia, Spain; †Institute for Legal Medicine, Sao Paulo, Brazil; and ‡Institute for Legal Medicine, Coimbra, Portugal.
[Ti] Título:Diagnosis of Vitality in Skin Wounds in the Ligature Marks Resulting From Suicide Hanging.
[So] Source:Am J Forensic Med Pathol;38(3):211-218, 2017 Sep.
[Is] ISSN:1533-404X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ascertaining the vital origin of skin wounds is one of the most challenging problems in forensic pathology. The forensic literature describes biomarkers and methods for differentiating vital and postmortem wounds, although no clear conclusions have been reached. The aim of this study was to characterize human vital wounds by analyzing the concentrations of metallic ions and the expression of P-selectin and cathepsin D in skin wounds in the ligature marks in a cohort of suicidal hangings for which vitality was previously demonstrated.A total of 71 skin wounds were analyzed within a postmortem interval of 19 to 36 hours. The concentration of Fe, Zn, Mg, and Ca and the expression of P-selectin and cathepsin D were analyzed together and separately. The majority of autopsied suicidal hangings were men (86%) with complete hanging mode (60.7%) in which there was a high frequency of subcutaneous injuries (78.3%). High concentrations of Ca and Mg compared with Fe and Zn were found. Ca and Zn concentrations decreased, and Fe concentration increased with the seriousness of the injury. A high percentage of moderately negative expression of both proteins was correlated with subcutaneous injury and low or medium concentrations of Fe.In conclusion, the joint study of metallic ions and proteins allows to characterize and to differentiate an injured vital wound of noninjured skin, especially when the damage in the tissue affects to the majority of the structures of the skin, but these results will need to be complemented with other biomarkers in time-controlled samples to further help in the differentiation of vital and postmortem wounds.
[Mh] Termos MeSH primário: Asfixia/patologia
Lesões do Pescoço/patologia
Pele/metabolismo
Suicídio
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Cálcio/metabolismo
Catepsina D/metabolismo
Feminino
Seres Humanos
Imuno-Histoquímica
Ferro/metabolismo
Magnésio/metabolismo
Masculino
Meia-Idade
Selectina-P/metabolismo
Mudanças Depois da Morte
Pele/lesões
Adulto Jovem
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (P-Selectin); E1UOL152H7 (Iron); EC 3.4.23.5 (Cathepsin D); I38ZP9992A (Magnesium); J41CSQ7QDS (Zinc); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1097/PAF.0000000000000322


  10 / 5792 MEDLINE  
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[PMID]:28652742
[Au] Autor:Xu X; Wang Y; Wu J; Hu X; Zhu H; Zhang X; Wang Y; Gui L; Zhao M; Peng S
[Ad] Endereço:Beijing Area Major Laboratory of Peptide and Small Molecular Drugs, Engineering Research Center of Endogenous Prophylactic of Ministry of Education of China, Beijing Laboratory of Biomedical Materials, College of Pharmaceutical Sciences, Capital Medical University, Beijing, People's Republic of Chin
[Ti] Título:ATIQCTPC: a nanomedicine capable of targeting tumor and blocking thrombosis in vivo.
[So] Source:Int J Nanomedicine;12:4415-4431, 2017.
[Is] ISSN:1178-2013
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:To overcome the harmful side effects, low tolerance, and undesirable outcomes of the anticancer drugs, we used ethane-1,2-diamine to bridge antitumoral ( )-3-acetyl-4-oxo-tetrahydroindolo[2,3-a]quinolizine-6-carboxylic acid (ATIQC) and tumor-targeting d-glucuronic acid, thereby providing (6 )-3-acetyl-4-oxo- -(2-(3,4,5,6-tetrahydroxytetrahydro-2H-pyran-2-carboxamido)ethyl)-4,6,7,12-tetrahydroindolo[2,3-a]quinolizine-6-carboxamide (ATIQCTPC). Atomic force microscopy images visualized, that in serum, ATIQCTPC formed particles of height <81 nm. These particles effectively avoided phagocytosis of macrophages and were stable in blood circulation. Distribution analysis indicated that ATIQCTPC accumulated and released ATIQC in the tumor tissue through a targeting manner. Thus, the antitumor and the anti-thrombotic activities of ATIQCTPC were 100-fold higher than those of ATIQC, and ATIQCTPC was able to prevent cancer patients from suffering from thrombosis. Based on the observation that ATIQCTPC decreased serum tumor necrosis factor-α (TNF-α) and interleukin-8 (IL-8) in S180 mice, we hypothesized that this is the mechanism that ATIQCTPC utilized to slow tumor growth. Additionally, we observed that ATIQCTPC inhibited thrombosis by decreasing serum P-selectin of thrombotic rats. The intermolecular association and the hexamerization manner of ATIQCTPC were experimentally evidenced and correlated with the formation of the nanoparticles.
[Mh] Termos MeSH primário: Antineoplásicos/química
Antineoplásicos/farmacologia
Indóis/farmacologia
Nanopartículas/administração & dosagem
Quinolizinas/farmacologia
Trombose/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/administração & dosagem
Sistemas de Liberação de Medicamentos/métodos
Ácido Glucurônico/administração & dosagem
Ácido Glucurônico/química
Ácido Glucurônico/farmacologia
Indóis/química
Interleucina-8/metabolismo
Macrófagos/efeitos dos fármacos
Masculino
Camundongos
Camundongos Endogâmicos ICR
Microscopia de Força Atômica
Nanopartículas/química
Neoplasias Experimentais/tratamento farmacológico
Selectina-P/antagonistas & inibidores
Selectina-P/metabolismo
Fagocitose/efeitos dos fármacos
Quinolizinas/química
Ratos Sprague-Dawley
Ratos Wistar
Distribuição Tecidual
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATIQCTPC compound); 0 (Antineoplastic Agents); 0 (Indoles); 0 (Interleukin-8); 0 (P-Selectin); 0 (Quinolizines); 0 (Tumor Necrosis Factor-alpha); 8A5D83Q4RW (Glucuronic Acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE
[do] DOI:10.2147/IJN.S129989



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