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[PMID]:29227084
[Au] Autor:Gudkova OO; Latyshko NV; Shandrenko SG
[Ti] Título:Amine oxidases as important agents of pathological processes of rhabdomyolysis in rats.
[So] Source:Ukr Biochem J;88(1):79-87, 2016 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:In this study we have tested an idea on the important role of amine oxidases (semicarbazide-sensitive amine oxidase, diamine oxidase, polyamine oxidase) as an additional source of oxidative/carbonyl stress under glycerol-induced rhabdomyolysis, since the enhanced formation of reactive oxygen species and reactive carbonyl species in a variety of tissues is linked to various diseases. In our experiments we used the sensitive fluorescent method devised for estimation of amine oxidases activity in the rat kidney and thymus as targeted organs under rhabdomyolysis. We have found in vivo the multiple rises in activity of semicarbazide-sensitive amine oxidase, diamine oxidase, polyamine oxidase (2-4.5 times) in the corresponding cell fractions, whole cells or their lysates at the 3-6th day after glycerol injection. Aberrant antioxidant activities depended on rhabdomyolysis stage and had organ specificity. Additional treatment of animals with metal chelator 'Unithiol' adjusted only the activity of antioxidant enzymes but not amine oxidases in both organs. Furthermore the in vitro experiment showed that Fenton reaction (hydrogen peroxide in the presence of iron) products alone had no effect on semicarbazide-sensitive amine oxidase activity in rat liver cell fraction whereas supplementation with methylglyoxal resulted in its significant 2.5-fold enhancement. Combined action of the both agents had additive effect on semicarbazide-sensitive amine oxidase activity. We can assume that biogenic amine and polyamine catabolism by amine oxidases is upregulated by oxidative and carbonyl stress factors directly under rhabdomyolysis progression, and the increase in catabolic products concentration contributes to tissue damage in glycerol-induced acute renal failure and apoptosis stimulation in thymus.
[Mh] Termos MeSH primário: Amina Oxidase (contendo Cobre)/metabolismo
Monoaminoxidase/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Rabdomiólise/enzimologia
[Mh] Termos MeSH secundário: Animais
Quelantes/farmacologia
Glicerol
Hepatócitos/efeitos dos fármacos
Hepatócitos/enzimologia
Hepatócitos/patologia
Peróxido de Hidrogênio/antagonistas & inibidores
Peróxido de Hidrogênio/farmacologia
Rim/efeitos dos fármacos
Rim/enzimologia
Rim/patologia
Fígado/efeitos dos fármacos
Fígado/enzimologia
Fígado/patologia
Masculino
Especificidade de Órgãos
Oxirredução
Carbonilação Proteica
Aldeído Pirúvico/antagonistas & inibidores
Aldeído Pirúvico/farmacologia
Ratos
Ratos Wistar
Rabdomiólise/induzido quimicamente
Rabdomiólise/tratamento farmacológico
Rabdomiólise/patologia
Semicarbazidas/antagonistas & inibidores
Semicarbazidas/farmacologia
Timo/efeitos dos fármacos
Timo/enzimologia
Timo/patologia
Unitiol/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chelating Agents); 0 (Reactive Oxygen Species); 0 (Semicarbazides); 37QUC23K2X (carbamylhydrazine); 4076-02-2 (Unithiol); 722KLD7415 (Pyruvaldehyde); BBX060AN9V (Hydrogen Peroxide); EC 1.4.3.21 (Amine Oxidase (Copper-Containing)); EC 1.4.3.4 (Monoamine Oxidase); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.3.- (polyamine oxidase); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.079


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[PMID]:28716979
[Au] Autor:Bustamante A; López-Cancio E; Pich S; Penalba A; Giralt D; García-Berrocoso T; Ferrer-Costa C; Gasull T; Hernández-Pérez M; Millan M; Rubiera M; Cardona P; Cano L; Quesada H; Terceño M; Silva Y; Castellanos M; Garces M; Reverté S; Ustrell X; Marés R; Baiges JJ; Serena J; Rubio F; Salas E; Dávalos A; Montaner J
[Ad] Endereço:From the Neurovascular Research Laboratory, Vall d'Hebron Institut de Recerca (VHIR), Hospital Universitari Vall d'Hebron, Universitat Autònoma de Barcelona, Spain (A.B., A.P., D.G., T.G.-B., J.M.); Stroke Unit, Hospital Universitari Germans Trias i Pujol, Barcelona, Spain (E.L.-C., M.H.-P., M.M., A
[Ti] Título:Blood Biomarkers for the Early Diagnosis of Stroke: The Stroke-Chip Study.
[So] Source:Stroke;48(9):2419-2425, 2017 Sep.
[Is] ISSN:1524-4628
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND PURPOSE: Stroke diagnosis could be challenging in the acute phase. We aimed to develop a blood-based diagnostic tool to differentiate between real strokes and stroke mimics and between ischemic and hemorrhagic strokes in the hyperacute phase. METHODS: The Stroke-Chip was a prospective, observational, multicenter study, conducted at 6 Stroke Centers in Catalonia. Consecutive patients with suspected stroke were enrolled within the first 6 hours after symptom onset, and blood samples were drawn immediately after admission. A 21-biomarker panel selected among previous results and from the literature was measured by immunoassays. Outcomes were differentiation between real strokes and stroke mimics and between ischemic and hemorrhagic strokes. Predictive models were developed by combining biomarkers and clinical variables in logistic regression models. Accuracy was evaluated with receiver operating characteristic curves. RESULTS: From August 2012 to December 2013, 1308 patients were included (71.9% ischemic, 14.8% stroke mimics, and 13.3% hemorrhagic). For stroke versus stroke mimics comparison, no biomarker resulted included in the logistic regression model, but it was only integrated by clinical variables, with a predictive accuracy of 80.8%. For ischemic versus hemorrhagic strokes comparison, NT-proBNP (N-Terminal Pro-B-Type Natriuretic Peptide) >4.9 (odds ratio, 2.40; 95% confidence interval, 1.55-3.71; <0.0001) and endostatin >4.7 (odds ratio, 2.02; 95% confidence interval, 1.19-3.45; =0.010), together with age, sex, blood pressure, stroke severity, atrial fibrillation, and hypertension, were included in the model. Predictive accuracy was 80.6%. CONCLUSIONS: The studied biomarkers were not sufficient for an accurate differential diagnosis of stroke in the hyperacute setting. Additional discovery of new biomarkers and improvement on laboratory techniques seem necessary for achieving a molecular diagnosis of stroke.
[Mh] Termos MeSH primário: Isquemia Encefálica/sangue
Hemorragia Cerebral/sangue
Acidente Vascular Cerebral/sangue
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Amina Oxidase (contendo Cobre)/sangue
Apolipoproteína C-III/sangue
Biomarcadores/sangue
Isquemia Encefálica/diagnóstico
Estudos de Casos e Controles
Caspase 3/sangue
Moléculas de Adesão Celular/sangue
Hemorragia Cerebral/diagnóstico
Quimiocina CXCL1/sangue
Endostatinas/sangue
Proteína Ligante Fas/sangue
Feminino
Produtos de Degradação da Fibrina e do Fibrinogênio/metabolismo
Fibronectinas/sangue
Proteínas de Choque Térmico HSC70/sangue
Seres Humanos
Proteína 3 de Ligação a Fator de Crescimento Semelhante à Insulina/sangue
Subunidade gama Comum de Receptores de Interleucina/sangue
Interleucina-17/sangue
Interleucina-6/sangue
Modelos Logísticos
Masculino
Metaloproteinase 9 da Matriz/sangue
Meia-Idade
Peptídeo Natriurético Encefálico/sangue
Fator de Crescimento Neural/sangue
Moléculas de Adesão de Célula Nervosa/sangue
Razão de Chances
Fragmentos de Peptídeos/sangue
Fosfopiruvato Hidratase/sangue
Estudos Prospectivos
Curva ROC
Receptores Tipo I de Fatores de Necrose Tumoral/sangue
Subunidade beta da Proteína Ligante de Cálcio S100/sangue
Acidente Vascular Cerebral/diagnóstico
Fator de von Willebrand/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Apolipoprotein C-III); 0 (Biomarkers); 0 (Cell Adhesion Molecules); 0 (Chemokine CXCL1); 0 (Endostatins); 0 (FASLG protein, human); 0 (Fas Ligand Protein); 0 (Fibrin Fibrinogen Degradation Products); 0 (Fibronectins); 0 (HSC70 Heat-Shock Proteins); 0 (HSPA8 protein, human); 0 (IGFBP3 protein, human); 0 (IL17A protein, human); 0 (IL2RG protein, human); 0 (IL6 protein, human); 0 (Insulin-Like Growth Factor Binding Protein 3); 0 (Interleukin Receptor Common gamma Subunit); 0 (Interleukin-17); 0 (Interleukin-6); 0 (NGF protein, human); 0 (Neural Cell Adhesion Molecules); 0 (Peptide Fragments); 0 (Receptors, Tumor Necrosis Factor, Type I); 0 (S100 Calcium Binding Protein beta Subunit); 0 (S100B protein, human); 0 (fibrin fragment D); 0 (pro-brain natriuretic peptide (1-76)); 0 (von Willebrand Factor); 114471-18-0 (Natriuretic Peptide, Brain); 9061-61-4 (Nerve Growth Factor); EC 1.4.3.21 (AOC3 protein, human); EC 1.4.3.21 (Amine Oxidase (Copper-Containing)); EC 3.4.22.- (CASP3 protein, human); EC 3.4.22.- (Caspase 3); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9); EC 4.2.1.11 (Phosphopyruvate Hydratase)
[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:170719
[St] Status:MEDLINE
[do] DOI:10.1161/STROKEAHA.117.017076


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[PMID]:28662230
[Au] Autor:Matsuda T; Noda K; Murata M; Kawasaki A; Kanda A; Mashima Y; Ishida S
[Ad] Endereço:Laboratory of Ocular Cell Biology & Visual Science, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo, Japan.
[Ti] Título:Vascular Adhesion Protein-1 Blockade Suppresses Ocular Inflammation After Retinal Laser Photocoagulation in Mice.
[So] Source:Invest Ophthalmol Vis Sci;58(7):3254-3261, 2017 Jun 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: To investigate the effect of the vascular adhesion protein-1 (VAP-1) inhibitor RTU-1096 on retinal morphologic changes and ocular inflammation after retinal laser photocoagulation in mice. Methods: C57BL/6JJcl mice were fed a diet containing RTU-1096, a specific inhibitor for VAP-1, or a control diet ad libitum for 7 days. Laser photocoagulation was performed on the peripheral retina of the animals. The semicarbazide sensitive amine oxidase (SSAO) activities in plasma and chorioretinal tissues were measured. Optical coherence tomography (OCT) images were acquired before and at 1, 3, and 7 days after laser photocoagulation, and thickness of the individual retinal layers was measured. Intravitreal leukocyte infiltration was assessed by histologic analysis. The expression level of intercellular adhesion molecule-1 (ICAM-1) in retinal tissues were examined by quantitative real-time PCR. Results: One day after laser photocoagulation, the thickness of the outer nuclear layer (ONL) increased in the laser group compared with in the control group, and RTU-1096 administration abrogated the ONL thickening. Histologic analysis and OCT observation revealed that laser photocoagulation caused infiltration of inflammatory cells and the appearance of hyperreflective foci at the vitreoretinal surface, both of which were suppressed by RTU-1096 administration. In addition, systemic administration of RTU-1096 reduced upregulation of the leukocyte adhesion molecules ICAM-1 in the retina. Conclusions: The current data indicate that VAP-1/SSAO inhibition may be a potential therapeutic strategy for the prevention of macular edema secondary to scatter laser photocoagulation in patients with ischemic retinal diseases such as diabetic retinopathy.
[Mh] Termos MeSH primário: Amina Oxidase (contendo Cobre)/antagonistas & inibidores
Moléculas de Adesão Celular/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Molécula 1 de Adesão Intercelular/fisiologia
Fotocoagulação a Laser/efeitos adversos
Edema Macular/etiologia
Retina/patologia
[Mh] Termos MeSH secundário: Animais
Feminino
Molécula 1 de Adesão Intercelular/metabolismo
Edema Macular/patologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Reação em Cadeia da Polimerase em Tempo Real
Retina/metabolismo
Tomografia de Coerência Óptica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Enzyme Inhibitors); 126547-89-5 (Intercellular Adhesion Molecule-1); EC 1.4.3.21 (AOC3 protein, human); EC 1.4.3.21 (Amine Oxidase (Copper-Containing))
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-21555


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[PMID]:28409494
[Au] Autor:Koborová I; Gurecká R; Csongová M; Volkovová K; Szöko É; Tábi T; Sebeková K
[Ad] Endereço:Ivana Koborová, Institute of Molecular BioMedicine, Faculty of Medicine, Comenius University, Sasinkova 4, 811 08 Bratislava, Slovakia, koborova@gmail.com.
[Ti] Título:Association between metabolically healthy central obesity in women and levels of soluble receptor for advanced glycation end products, soluble vascular adhesion protein-1, and the activity of semicarbazide-sensitive amine oxidase.
[So] Source:Croat Med J;58(2):106-116, 2017 Apr 14.
[Is] ISSN:1332-8166
[Cp] País de publicação:Croatia
[La] Idioma:eng
[Ab] Resumo:AIM: To determine the levels of circulating soluble receptor for advanced glycation end products (sRAGE), as a biomarker of risk of metabolic syndrome and cardiovascular disease development in centrally obese (CO) women considered metabolically healthy (COH) in comparison with those metabolically unhealthy (COU). METHODS: 47 lean healthy, 17 COH (presenting waist-to-height ratio ≥0.5 but not elevated blood pressure, atherogenic lipid profile, and insulin resistance), and 50 COU (CO presenting ≥2 risk factors) women aged 40-45 years were included. Anthropometric characteristics, blood chemistry and hematology data, adipokines, markers of inflammation, sRAGE, soluble vascular adhesion protein-1 (sVAP-1), and the activity of semicarbazide sensitive amine oxidase (SSAO) were determined. RESULTS: Central obesity associated with low sRAGE levels (lean healthy: 1503±633 pg/mL; COH: 1103±339 pg/mL, P<0.05; COU: 1106±367 ng/mL, P<0.0.1), hyperleptinemia, and elevated markers of inflammation irrespective of the presence or absence of cardiometabolic risk factors. COU women presented high adiponectin levels. SVAP-1 concentrations and the activity of SSAO were similar in all 3 groups. CONCLUSION: COH women present abnormalities in non-standard markers of cardiometabolic risk (sRAGE, leptin, high sensitive C-reactive protein), supporting the view that there is no healthy pattern of obesity. The clinical impact of our findings for future prognosis of metabolically healthy obese subjects remains to be elucidated in longitudinal studies.
[Mh] Termos MeSH primário: Amina Oxidase (contendo Cobre)/metabolismo
Moléculas de Adesão Celular/metabolismo
Obesidade Abdominal/fisiopatologia
Complicações na Gravidez/fisiopatologia
Receptor para Produtos Finais de Glicação Avançada/sangue
[Mh] Termos MeSH secundário: Adulto
Antropometria
Biomarcadores
Proteína C-Reativa/metabolismo
Doenças Cardiovasculares/fisiopatologia
Feminino
Seres Humanos
Inflamação/sangue
Mediadores da Inflamação/metabolismo
Resistência à Insulina/fisiologia
Lipídeos/sangue
Síndrome Metabólica/fisiopatologia
Meia-Idade
Gravidez
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Cell Adhesion Molecules); 0 (Inflammation Mediators); 0 (Lipids); 0 (Receptor for Advanced Glycation End Products); 9007-41-4 (C-Reactive Protein); EC 1.4.3.21 (AOC3 protein, human); EC 1.4.3.21 (Amine Oxidase (Copper-Containing))
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170415
[St] Status:MEDLINE


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[PMID]:28367269
[Au] Autor:Ohashi K; Kageyama M; Shinomiya K; Fujita-Koyama Y; Hirai SI; Katsuta O; Nakamura M
[Ad] Endereço:Global Research and Development, Santen Pharmaceutical Co. Ltd., Ikoma-shi, Nara, Japan.
[Ti] Título:Spermidine Oxidation-Mediated Degeneration of Retinal Pigment Epithelium in Rats.
[So] Source:Oxid Med Cell Longev;2017:4128061, 2017.
[Is] ISSN:1942-0994
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Retinal pigment epithelium (RPE) degeneration is a crucial event in dry age-related macular degeneration and gyrate atrophy. The polyamine spermidine has been shown to induce RPE cell death in vitro. The present study aimed to establish a novel in vivo model of spermidine-induced RPE degeneration and to determine whether spermidine-induced RPE cell death involves oxidative mechanisms. In this study, spermidine caused ARPE-19 cell death in a concentration-dependent manner. This effect was prevented by removal of serum from the culture medium or treatment with amine oxidase inhibitors, N-acetylcysteine (NAC), or aldehyde dehydrogenase (ALDH). Intravitreal injection of spermidine into rats significantly increased the permeability of the blood-retinal barrier and decreased the amplitudes of scotopic electroretinogram a- and b-waves. Histological analysis revealed that spermidine induced vacuolation, atrophy, and dropout of RPE cells, leading to the disruption of photoreceptor outer segments. Simultaneous intravitreal administration of NAC and ALDH with spermidine prominently inhibited the functional and morphological changes induced by spermidine. In conclusion, this study demonstrated that the intravitreal administration of spermidine induced RPE cell dysfunction and death followed by photoreceptor degeneration in rats. These effects of spermidine are thought to be mediated by oxidative stress and a toxic aldehyde generated during spermidine oxidation.
[Mh] Termos MeSH primário: Espermidina/química
[Mh] Termos MeSH secundário: Acetilcisteína/química
Acetilcisteína/metabolismo
Acetilcisteína/farmacologia
Aldeído Desidrogenase/metabolismo
Amina Oxidase (contendo Cobre)/antagonistas & inibidores
Amina Oxidase (contendo Cobre)/metabolismo
Animais
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Feminino
Fluorofotometria
Seres Humanos
Imuno-Histoquímica
Microscopia Eletrônica de Transmissão
Oxirredução
Células Fotorreceptoras de Vertebrados/patologia
Ratos
Ratos Endogâmicos BN
Degeneração Retiniana/metabolismo
Degeneração Retiniana/patologia
Epitélio Pigmentado da Retina/citologia
Epitélio Pigmentado da Retina/metabolismo
Epitélio Pigmentado da Retina/patologia
Espermidina/metabolismo
Espermidina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.2.1.3 (Aldehyde Dehydrogenase); EC 1.4.3.21 (Amine Oxidase (Copper-Containing)); U87FK77H25 (Spermidine); WYQ7N0BPYC (Acetylcysteine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170420
[Lr] Data última revisão:
170420
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1155/2017/4128061


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[PMID]:28315108
[Au] Autor:Amani M; Barzegar A; Mazani M
[Ad] Endereço:Department of Biochemistry, Faculty of Medicine, Ardabil University of Medical Sciences (ArUMS), Daneshgah Street, Ardabil, 5618985991, Iran. m.amani@arums.ac.ir.
[Ti] Título:Osmolytic Effect of Sucrose on Thermal Denaturation of Pea Seedling Copper Amine Oxidase.
[So] Source:Protein J;36(2):147-153, 2017 Apr.
[Is] ISSN:1875-8355
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Protein stability is a subject of interest by many researchers. One of the common methods to increase the protein stability is using the osmolytes. Many studies and theories analyzed and explained osmolytic effect by equilibrium thermodynamic while most proteins undergo an irreversible denaturation. In current study we investigated the effect of sucrose as an osmolyte on the thermal denaturation of pea seedlings amine oxidase by the enzyme activity, fluorescence spectroscopy, circular dichroism, and differential scanning calorimetry. All experiments are in agreement that pea seedlings amine oxidase denaturation is controlled kinetically and its kinetic stability is increased in presence of sucrose. Differential scanning calorimetry experiments at different scanning rates showed that pea seedlings amine oxidase unfolding obeys two-state irreversible model. Fitting the differential scanning calorimetry data to two-state irreversible model showed that unfolding enthalpy and T , temperature at which rate constant equals unit per minute, are increased while activation energy is not affected by increase in sucrose concentration. We concluded that osmolytes decrease the molecular oscillation of irreversible proteins which leads to decline in unfolding rate constant.
[Mh] Termos MeSH primário: Amina Oxidase (contendo Cobre)/química
Ervilhas/enzimologia
Desnaturação Proteica
Proteínas/química
Sacarose/química
[Mh] Termos MeSH secundário: Amina Oxidase (contendo Cobre)/metabolismo
Varredura Diferencial de Calorimetria
Dicroísmo Circular
Cinética
Proteínas/metabolismo
Plântulas/enzimologia
Temperatura Ambiente
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins); 57-50-1 (Sucrose); EC 1.4.3.21 (Amine Oxidase (Copper-Containing))
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170319
[St] Status:MEDLINE
[do] DOI:10.1007/s10930-017-9706-1


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[PMID]:28251930
[Au] Autor:Marttila-Ichihara F; Elima K; Auvinen K; Veres TZ; Rantakari P; Weston C; Miyasaka M; Adams D; Jalkanen S; Salmi M
[Ad] Endereço:MediCity Research Laboratory, University of Turku, Turku, Finland; fumiko.marttila@utu.fi.
[Ti] Título:Amine oxidase activity regulates the development of pulmonary fibrosis.
[So] Source:FASEB J;31(6):2477-2491, 2017 Jun.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In pulmonary fibrosis, an inflammatory reaction and differentiation of myofibroblasts culminate in pathologic deposition of collagen. Amine oxidase copper containing-3 (AOC3) is a cell-surface-expressed oxidase that regulates leukocyte extravasation. Here we analyzed the potential role of AOC3 using gene-modified and inhibitor-treated mice in a bleomycin-induced pulmonary fibrosis model. Inflammation and fibrosis of lungs were assessed by histologic, flow cytometric, and quantitative PCR analysis. AOC3-deficient mice showed a 30-50% reduction in fibrosis, collagen synthesis, numbers of myofibroblasts, and accumulation of CD4 lymphocytes, NK T cells, macrophages, and type 2 innate lymphoid cells compared with wild-type control mice. AOC3-knock-in mice, which express a catalytically inactive form of AOC3, were also protected from lung fibrosis. In wild-type mice, a small-molecule AOC3 inhibitor treatment reduced leukocyte infiltration, myofibroblast differentiation, and fibrotic injury both in prophylactic and early therapeutic settings by about 50% but was unable to reverse the established fibrosis. AOC3 was also induced in myofibroblasts in human idiopathic pulmonary fibrosis. Thus, the oxidase activity of AOC3 contributes to the development of lung fibrosis mainly by regulating the accumulation of pathogenic leukocyte subtypes, which drive the fibrotic response.-Marttila-Ichihara, F., Elima, K., Auvinen, K., Veres, T. Z., Rantakari, P., Weston, C., Miyasaka, M., Adams, D., Jalkanen, S., Salmi, M. Amine oxidase activity regulates the development of pulmonary fibrosis.
[Mh] Termos MeSH primário: Amina Oxidase (contendo Cobre)/metabolismo
Moléculas de Adesão Celular/metabolismo
Fibrose Pulmonar/enzimologia
[Mh] Termos MeSH secundário: Amina Oxidase (contendo Cobre)/genética
Animais
Antibióticos Antineoplásicos/toxicidade
Bleomicina/toxicidade
Ácidos Carboxílicos
Moléculas de Adesão Celular/genética
Regulação Enzimológica da Expressão Gênica/fisiologia
Seres Humanos
Pulmão/enzimologia
Pulmão/patologia
Linfócitos/fisiologia
Camundongos
Camundongos Knockout
Fibrose Pulmonar/induzido quimicamente
Fibrose Pulmonar/metabolismo
Pirrolidinas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibiotics, Antineoplastic); 0 (Carboxylic Acids); 0 (Cell Adhesion Molecules); 0 (Pyrrolidines); 0 (trans-4-hydroxy-N-methyl-L-proline(-)-(2S,4R)-4-hydroxy-1-methyl pyrrolidine-2-carboxylic acid); 11056-06-7 (Bleomycin); EC 1.4.3.21 (AOC3 protein, human); EC 1.4.3.21 (Amine Oxidase (Copper-Containing)); EC 1.4.3.21 (semicarbazide-sensitive amine oxidase-vascular adhesion protein-1, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170303
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201600935R


  8 / 2805 MEDLINE  
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[PMID]:28112368
[Au] Autor:Jeong C; Kim Y
[Ad] Endereço:Department of Biochemistry, Wonkwang University School of Medicine, Institute of Wonkwang Medical Science, Iksan, Jeonbuk 570-749, Republic of Korea.
[Ti] Título:LOXL3-sv2, a novel variant of human lysyl oxidase-like 3 (LOXL3), functions as an amine oxidase.
[So] Source:Int J Mol Med;39(3):719-724, 2017 Mar.
[Is] ISSN:1791-244X
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Human lysyl oxidase-like 3 (LOXL3) functions as a copper-dependent amine oxidase toward collagen and elastin. The LOXL3 protein contains four scavenger receptor cysteine-rich (SRCR) domains in the N-terminus in addition to the C-terminal characteristic domains of the lysyl oxidase (LOX) family, such as a copper-binding domain, a cytokine receptor­like domain and residues for the lysyl-tyrosyl quinone cofactor. Using BLASTN searches, we identified a novel variant of LOXL3 (termed LOXL3-sv2), which lacked the sequences corresponding to exons 4 and 5 of LOXL3. The LOXL3-sv2 mRNA is at least 2,398 bp in length, encoding a 608 amino acid-long polypeptide with a calculated molecular mass of 67.4 kDa. The deletion of exons 4 and 5 do not change the open-reading frame of LOXL3 but results in deletion of the SRCR domain 2. The recombinant LOXL3-sv2 protein showed a ß-aminopropionitrile-inhibitable amine oxidase activity toward collagen type I. In RT-PCR analysis, LOXL3-sv2 was detected in all human tissues tested, along with LOXL3 and LOXL3-sv1, a previously identified variant of LOXL3. These findings indicate that the human LOXL3 gene encodes at least three variants, LOXL3, LOXL3-sv1 and LOXL3-sv2, all of which function as amine oxidases.
[Mh] Termos MeSH primário: Amina Oxidase (contendo Cobre)/metabolismo
Aminoácido Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Amina Oxidase (contendo Cobre)/química
Amina Oxidase (contendo Cobre)/genética
Aminoácido Oxirredutases/química
Aminoácido Oxirredutases/genética
Sequência de Aminoácidos
Ativação Enzimática
Éxons
Ordem dos Genes
Seres Humanos
Íntrons
Domínios Proteicos
RNA Mensageiro/genética
Proteínas Recombinantes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Recombinant Proteins); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (LOXL3 protein, human); EC 1.4.3.21 (Amine Oxidase (Copper-Containing))
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170124
[St] Status:MEDLINE
[do] DOI:10.3892/ijmm.2017.2862


  9 / 2805 MEDLINE  
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[PMID]:28108908
[Au] Autor:Jumarie C; Séïde M; Marcocci L; Pietrangeli P; Mateescu MA
[Ad] Endereço:Department of Biological Sciences and Centre TOXEN, Université du Québec à Montreal, CP 8888, Branch A, Montreal, Québec, H3C 3P8, Canada.
[Ti] Título:Diamine Oxidase from White Pea (Lathyrus sativus) Combined with Catalase Protects the Human Intestinal Caco-2 Cell Line from Histamine Damage.
[So] Source:Appl Biochem Biotechnol;182(3):1171-1181, 2017 Jul.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diamine oxidase (DAO) administration has been proposed to treat certain gastrointestinal dysfunctions induced by histamine, an immunomodulator, signaling, and pro-inflammatory factor. However, H O resulting from the oxidative deamination of histamine by DAO may be toxic. The purpose of this study was to investigate to which extent DAO from white pea (Lathyrus sativus), alone or in combination with catalase, may modulate histamine toxicity in the human intestinal Caco-2 cell line. The results show that histamine at concentrations higher than 1 mM is toxic to the Caco-2 cells, independently of the cell differentiation status, with a LC of ≅ 10 mM following a 24-h exposure. Depending on its concentration, DAO increased histamine toxicity to a greater extent in differentiated cells compared to undifferentiated cultures. In the presence of catalase, the DAO-induced increase in histamine toxicity was completely abolished in the undifferentiated cells and only partially decreased in differentiated cells, showing differences in the sensitivity of Caco-2 cells to the products resulting from histamine degradation by DAO (H O , NH , or imidazole aldehyde). It appears that treatment of food histaminosis using a combination of vegetal DAO and catalase would protect against histamine toxicity and prevent H O -induced damage that may occur during histamine oxidative deamination.
[Mh] Termos MeSH primário: Amina Oxidase (contendo Cobre)/farmacologia
Catalase/farmacologia
Histamina/efeitos adversos
Lathyrus/enzimologia
Proteínas de Plantas/farmacologia
[Mh] Termos MeSH secundário: Células CACO-2
Sobrevivência Celular/efeitos dos fármacos
Histamina/farmacologia
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 820484N8I3 (Histamine); EC 1.11.1.6 (Catalase); EC 1.4.3.21 (Amine Oxidase (Copper-Containing))
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170122
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-016-2390-3


  10 / 2805 MEDLINE  
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[PMID]:28089246
[Au] Autor:Xu B; Lei L; Zhu X; Zhou Y; Xiao Y
[Ad] Endereço:CAS Key Laboratory of Synthetic Biology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, 200032, China; University of Chinese Academy of Sciences, Beijing, 100039, Ch
[Ti] Título:Identification and characterization of L-lysine decarboxylase from Huperzia serrata and its role in the metabolic pathway of lycopodium alkaloid.
[So] Source:Phytochemistry;136:23-30, 2017 Apr.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lysine decarboxylation is the first biosynthetic step of Huperzine A (HupA). Six cDNAs encoding lysine decarboxylases (LDCs) were cloned from Huperzia serrata by degenerate PCR and rapid amplification of cDNA ends (RACE). One HsLDC isoform was functionally characterized as lysine decarboxylase. The HsLDC exhibited greatest catalytic efficiency (k /K , 2.11 s mM ) toward L-lysine in vitro among all reported plant-LDCs. Moreover, transient expression of the HsLDC in tobacco leaves specifically increased cadaverine content from zero to 0.75 mg per gram of dry mass. Additionally, a convenient and reliable method used to detect the two catalytic products was developed. With the novel method, the enzymatic products of HsLDC and HsCAO, namely cadaverine and 5-aminopentanal, respectively, were detected simultaneously both in assay with purified enzymes and in transgenic tobacco leaves. This work not only provides direct evidence of the first two-step in biosynthetic pathway of HupA in Huperzia serrata and paves the way for further elucidation of the pathway, but also enables engineering heterologous production of HupA.
[Mh] Termos MeSH primário: Alcaloides/metabolismo
Amina Oxidase (contendo Cobre)/metabolismo
Carboxiliases/metabolismo
Huperzia/enzimologia
Lycopodium/química
Sesquiterpenos/metabolismo
[Mh] Termos MeSH secundário: Alcaloides/biossíntese
Alcaloides/química
Cadaverina/análise
Carboxiliases/farmacocinética
DNA Complementar/metabolismo
Lisina/metabolismo
Redes e Vias Metabólicas
Estrutura Molecular
Folhas de Planta/química
Plantas Geneticamente Modificadas/metabolismo
Reação em Cadeia da Polimerase
Sesquiterpenos/análise
Sesquiterpenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alkaloids); 0 (DNA, Complementary); 0 (Sesquiterpenes); 0111871I23 (huperzine A); EC 1.4.3.21 (Amine Oxidase (Copper-Containing)); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.18 (lysine decarboxylase); K3Z4F929H6 (Lysine); L90BEN6OLL (Cadaverine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170321
[Lr] Data última revisão:
170321
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE



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