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[PMID]:29370193
[Au] Autor:Kalita D; Holm DG; LaBarbera DV; Petrash JM; Jayanty SS
[Ad] Endereço:San Luis Valley Research Center, Department of Horticulture and Landscape Architecture, Colorado State University, Center, United States of America.
[Ti] Título:Inhibition of α-glucosidase, α-amylase, and aldose reductase by potato polyphenolic compounds.
[So] Source:PLoS One;13(1):e0191025, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diabetes mellitus is a chronic disease that is becoming a serious global health problem. Diabetes has been considered to be one of the major risks of cataract and retinopathy. Synthetic and natural product inhibitors of carbohydrate degrading enzymes are able to reduce type 2 diabetes and its complications. For a long time, potatoes have been portrayed as unhealthy for diabetic patients by some nutritionist due to their high starch content. However, purple and red potato cultivars have received considerable attention from consumers because they have high levels of polyphenolic compounds that have potent antioxidant activities. In this study, we screened the total phenolics (TP) and total anthocyanins (TA) and analyzed the phenolic and anthocyanin compounds in selected potato cultivars and advanced selections with distinct flesh colors (purple, red, yellow and white). Purple and red potato cultivars had higher levels of TP and TA than tubers with other flesh colors. Chlorogenic acid is the predominant phenolic acid, and major anthocyanin is composed of the derivatives of petunidin, peonidin, malvidin and pelargonidin. We tested the potential inhibitory effect of potato extracts on the activities of α-amylase and α-glucosidase, which were targeted to develop antidiabetic therapeutic agents. We also measured inhibitory effect of potato extracts on aldose reductase (AR) which is a key enzyme that has been a major drug target for the development of therapies to treat diabetic complications. Purple flesh tubers extract showed the most effective inhibition of α-amylase, α-glucosidase, and aldose reductase with IC50 values 25, 42, and 32 µg/ml, respectively. Kinetic studies showed that anthocyanins are noncompetitive inhibitors of these enzymes, whereas phenolic acids behaved as mixed inhibitors for α-amylase and α-glucosidase and noncompetitive inhibitors for AR. This study supports the development of a positive and healthful image of potatoes, which is an important issue for consumers.
[Mh] Termos MeSH primário: Aldeído Redutase/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Polifenóis/farmacologia
Solanum tuberosum/química
alfa-Amilases/antagonistas & inibidores
alfa-Glucosidases/efeitos dos fármacos
[Mh] Termos MeSH secundário: Antocianinas/análise
Antocianinas/farmacologia
Cromatografia Líquida
Espectrometria de Massas
Polifenóis/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anthocyanins); 0 (Enzyme Inhibitors); 0 (Polyphenols); EC 1.1.1.21 (Aldehyde Reductase); EC 3.2.1.1 (alpha-Amylases); EC 3.2.1.20 (alpha-Glucosidases)
[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:180126
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191025


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[PMID]:28455256
[Au] Autor:Kim JH; Cho CW; Kim HY; Kim KT; Choi GS; Kim HH; Cho IS; Kwon SJ; Choi SK; Yoon JY; Yang SY; Kang JS; Kim YH
[Ad] Endereço:College of Pharmacy, Chungnam National University, Daejeon 34134, Republic of Korea; Department of Horticultural and Crop Environment, National Institute of Horticultural and Herbal Science, RDA, Wanju, 55365, Republic of Korea; Advanced Radiation Technology Institute, Korea Atomic Energy Research I
[Ti] Título:α-Glucosidase inhibition by prenylated and lavandulyl compounds from Sophora flavescens roots and in silico analysis.
[So] Source:Int J Biol Macromol;102:960-969, 2017 Sep.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The enzyme α-glucosidase is a good drug target for the treatment of diabetes mellitus. Four minor flavonoids (1-4) from roots of Sophora flavescens showed the inhibitory activity, with IC values ranging from 11.0±0.3 to 50.6±1.3µM, toward α-glucosidase. An enzyme kinetics analysis of them revealed that the compounds 1 and 4 were non-competitive, and compounds 2 and 3 were un-competitive inhibitors. For molecular docking, 3-dimensional structure of α-glucosidase was built by homology modeling. As the result, four compounds 1-4 were confirmed to interact into common binding site of α-glucosidase. In addition, all of the four prenylated and lavandulyl compounds (1-4) were abundant in an ethyl acetate fraction separated from a methanol extract, and the potential inhibitor (3) was extracted best using tetrahydrofuran.
[Mh] Termos MeSH primário: Simulação por Computador
Extratos Vegetais/farmacologia
Raízes de Plantas/química
Prenilação
Sophora/química
Terpenos/química
alfa-Glucosidases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Inibidores de Glicosídeo Hidrolases/química
Inibidores de Glicosídeo Hidrolases/metabolismo
Inibidores de Glicosídeo Hidrolases/farmacologia
Simulação de Acoplamento Molecular
Extratos Vegetais/química
Extratos Vegetais/metabolismo
Conformação Proteica
alfa-Glucosidases/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycoside Hydrolase Inhibitors); 0 (Plant Extracts); 0 (Terpenes); EC 3.2.1.20 (alpha-Glucosidases)
[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:170430
[St] Status:MEDLINE


  3 / 3854 MEDLINE  
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[PMID]:29315315
[Au] Autor:Lollert A; Stihl C; Hötker AM; Mengel E; König J; Laudemann K; Gökce S; Düber C; Staatz G
[Ad] Endereço:Department of Diagnostic and Interventional Radiology, Section of Pediatric Radiology, Medical Center of the Johannes Gutenberg University, Mainz, Germany.
[Ti] Título:Quantification of intramuscular fat in patients with late-onset Pompe disease by conventional magnetic resonance imaging for the long-term follow-up of enzyme replacement therapy.
[So] Source:PLoS One;13(1):e0190784, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: The objective of this study was to evaluate a quantitative method based on conventional T1-weighted magnetic resonance (MR) imaging to assess fatty muscular degeneration in patients with late-onset Pompe disease and to compare it with semi-quantitative visual evaluation (the Mercuri score). In addition, a long-term retrospective data analysis was performed to evaluate treatment response to enzyme replacement therapy with alglucosidase alfa. METHODS: MR images of the lumbar spine were acquired in 41 patients diagnosed with late-onset Pompe disease from 2006 through 2015. Two independent readers retrospectively evaluated fatty degeneration of the psoas and paraspinal muscles by applying the Mercuri score. Quantitative semi-automated muscle and fat tissue separation was performed, and inter-observer agreement and correlations with clinical parameters were assessed. Follow-up examinations were performed in 13 patients treated with alglucosidase alfa after a median of 39 months; in 7/13 patients, an additional follow-up examination was completed after a median of 63 months. RESULTS: Inter-observer agreement was high. Measurements derived from the quantitative method correlated well with Medical Research Council scores of muscle strength, with moderate correlations found for the 6-minute walk test, the 4-step stair climb test, and spirometry in the supine position. A significant increase in the MR-derived fat fraction of the psoas muscle was found between baseline and follow-up 1 (P = 0.016), as was a significant decrease in the performance on the 6-minute walk test (P = 0.006) and 4-step stair climb test (P = 0.034), as well as plasma creatine kinase (P = 0.016). No statistically significant difference in clinical or MR-derived parameters was found between follow-up 1 and follow-up 2. CONCLUSIONS: Quantification of fatty muscle degeneration using the semi-automated method can provide a more detailed overview of disease progression than semi-quantitative Mercuri scoring. MR-derived data correlated with clinical symptoms and patient exercise capacity. After an initial worsening, the fat fraction of the psoas muscle and performance on the 6-minute walk test stayed constant during long-term follow-up under enzyme replacement therapy.
[Mh] Termos MeSH primário: Tecido Adiposo/diagnóstico por imagem
Terapia de Reposição de Enzimas/métodos
Doença de Depósito de Glicogênio Tipo II/diagnóstico por imagem
Imagem por Ressonância Magnética/métodos
Músculo Esquelético/diagnóstico por imagem
alfa-Glucosidases/administração & dosagem
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idade de Início
Idoso
Criança
Feminino
Seguimentos
Doença de Depósito de Glicogênio Tipo II/etiologia
Seres Humanos
Masculino
Meia-Idade
Músculo Esquelético/patologia
Variações Dependentes do Observador
Estudos Retrospectivos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.2.1.20 (GAA protein, human); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190784


  4 / 3854 MEDLINE  
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[PMID]:29274340
[Au] Autor:Park H; Kim J; Lee YK; Kim W; You SK; Do J; Jang Y; Oh DB; Il Kim J; Kim HH
[Ad] Endereço:Biotherapeutics and Glycomics Laboratory, College of Pharmacy, Chung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul 06944, South Korea.
[Ti] Título:Four unreported types of glycans containing mannose-6-phosphate are heterogeneously attached at three sites (including newly found Asn 233) to recombinant human acid alpha-glucosidase that is the only approved treatment for Pompe disease.
[So] Source:Biochem Biophys Res Commun;495(4):2418-2424, 2018 01 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Myozyme is a recombinant human acid alpha-glucosidase (rhGAA) that is currently the only drug approved for treating Pompe disease, and its low efficacy means that a high dose is required. Mannose-6-phosphate (M6P) glycosylation on rhGAA is a key factor influencing lysosomal enzyme targeting and the efficacy of enzyme replacement therapy (ERT); however, its complex structure and relatively small quantity still remain to be characterized. This study investigated M6P glycosylation on rhGAA using liquid chromatography (LC)-electrospray ionization (ESI)-high-energy collisional dissociation (HCD) tandem mass spectrometry (MS/MS). The glycans released from rhGAA were labeled with procainamide to improve mass ionization efficiency and the sensitivity of MS/MS. The relative quantities (%) of 78 glycans were obtained, and 1.0% of them were glycans containing M6P (M6P glycans). These were categorized according to their structure into 4 types: 3 newly found ones, comprising high-mannose-type M6P glycans capped with N-acetylglucosamine (GlcNAc) (2 variants, 17.5%), hybrid-type M6P glycans (2 variants, 11.2%), and hybrid-type M6P glycans capped with GlcNAc (3 variants, 6.9%), as well as high-mannose-type M6P glycans (3 variants, 64.4%). HCD-MS/MS spectra identified six distinctive M6P-derived oxonium ions. The glycopeptides obtained from protease-digested rhGAA were analyzed using nano-LC-ESI-HCD-MS/MS, and the extracted-ion chromatograms of M6P-derived oxonium ions confirmed three M6P glycosylation sites comprising Asn 140, Asn 233 (newly found), and Asn 470 attached heterogeneously to nine M6P glycans (two types), eight M6P glycans (four types), and seven M6P glycans (two types), respectively. This is the first study of rhGAA to differentiate M6P glycans and identify their attachment sites, despite rhGAA already being an approved drug for Pompe disease.
[Mh] Termos MeSH primário: Doença de Depósito de Glicogênio Tipo II/tratamento farmacológico
Manosefosfatos/química
Manosefosfatos/uso terapêutico
Polissacarídeos/química
Polissacarídeos/uso terapêutico
alfa-Glucosidases/química
alfa-Glucosidases/uso terapêutico
[Mh] Termos MeSH secundário: Sítios de Ligação
Aprovação de Drogas
Seres Humanos
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mannosephosphates); 0 (Polysaccharides); 0 (Recombinant Proteins); 3672-15-9 (mannose-6-phosphate); EC 3.2.1.20 (GAA protein, human); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171224
[St] Status:MEDLINE


  5 / 3854 MEDLINE  
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[PMID]:29208524
[Au] Autor:Wang G; Chen M; Qiu J; Xie Z; Cao A
[Ad] Endereço:Provincial Key Laboratory of Pharmaceutics in Guizhou Province, Guizhou Medical University, 4 Beijing Road, Guiyang 550004, China; School of Pharmacy, Guizhou Medical University, 4 Beijing Road, Guiyang 550004, China; National Engineering Research Center of Miao's Medicines, 4 Beijing Road, Guiyang
[Ti] Título:Synthesis, in vitro α-glucosidase inhibitory activity and docking studies of novel chromone-isatin derivatives.
[So] Source:Bioorg Med Chem Lett;28(2):113-116, 2018 01 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A novel series of chromone-isatin derivatives 6a-6p were designed, synthesized and characterized by H NMR, C NMR and HRMS. These novel synthetic compounds were evaluated for inhibitory activity against yeast α-glucosidase enzyme. The results of biological test have shown that all tested compounds exhibited excellent to potent inhibitory activity in the range of IC = 3.18 ±â€¯0.12-16.59 ±â€¯0.17 µM as compared to the standard drug acarbose (IC = 817.38 ±â€¯6.27 µM). Compound 6j (IC = 3.18 ±â€¯0.12 µM) with a hydroxyl group at the 7-position of chromone and a 4-bromobenzyl group at the N1-positions of isatin, was found to be the most active compound among the series. Furthermore, molecular docking study was performed to help understand binding interactions of the most active analogs with α-glucosidase enzyme. These results indicated that this class of compounds had potential for the development of anti-diabetic agents.
[Mh] Termos MeSH primário: Cromonas/farmacologia
Inibidores de Glicosídeo Hidrolases/farmacologia
Isatina/farmacologia
Simulação de Acoplamento Molecular
alfa-Glucosidases/metabolismo
[Mh] Termos MeSH secundário: Cromonas/química
Relação Dose-Resposta a Droga
Inibidores de Glicosídeo Hidrolases/síntese química
Inibidores de Glicosídeo Hidrolases/química
Isatina/química
Estrutura Molecular
Saccharomyces cerevisiae/enzimologia
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromones); 0 (Glycoside Hydrolase Inhibitors); 82X95S7M06 (Isatin); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


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[PMID]:29390460
[Au] Autor:Martínez M; Romero MG; Guereta LG; Cabrera M; Regojo RM; Albajara L; Couce ML; Pipaon MS
[Ad] Endereço:Department of Neonatology-Pediatrics.
[Ti] Título:Infantile-onset Pompe disease with neonatal debut: A case report and literature review.
[So] Source:Medicine (Baltimore);96(51):e9186, 2017 Dec.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RATIONALE: Infantile-onset Pompe disease, also known as glycogen storage disease type II, is a progressive and fatal disorder without treatment. Enzyme replacement therapy with recombinant human acid alpha-glucosidase (GAA) enhances survival; however, the best outcomes have been achieved with early treatment. PATIENT CONCERNS: We report a case of a newborn with infantile-onset Pompe disease diagnosed in the first days of life who did not undergo universal neonatal screening. The patient was asymptomatic, with a general physical examination revealing only a murmur. The clinical presentation was dominated by the neonatal detection of hypertrophic cardiomyopathy, without hypotonia or macroglossia. DIAGNOSES: Pompe disease was confirmed in the first week of life by GAA activity in dried blood spots, and a GAA genetic study showed the homozygous mutation p.Arg854X. INTERVENTIONS: Parents initially refused replacement therapy. OUTCOMES: The patient experienced recurrent episodes of ventricular fibrillation during central line placement and could not be resuscitated. LESSONS: Although Pompe disease is rare, and universal screening has not been established, neonatologists should be alerted to the diagnosis of Pompe in the presence of hypertrophic cardiomyopathy. Diagnosis is achieved in a few days with the aid of dried blood spots.
[Mh] Termos MeSH primário: Cardiomiopatia Hipertrófica/etiologia
Doença de Depósito de Glicogênio Tipo II/diagnóstico
Doença de Depósito de Glicogênio Tipo II/genética
Fibrilação Ventricular/diagnóstico
alfa-Glucosidases/genética
[Mh] Termos MeSH secundário: Biópsia por Agulha
Cardiomiopatia Hipertrófica/fisiopatologia
Cardiomiopatia Hipertrófica/terapia
Progressão da Doença
Evolução Fatal
Doença de Depósito de Glicogênio Tipo II/complicações
Homozigoto
Seres Humanos
Imuno-Histoquímica
Recém-Nascido
Doenças do Recém-Nascido/diagnóstico
Doenças do Recém-Nascido/terapia
Masculino
Mutação
Doenças Raras
Medição de Risco
Índice de Gravidade de Doença
Fibrilação Ventricular/etiologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 3.2.1.20 (GAA protein, human); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180203
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000009186


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[PMID]:29374975
[Au] Autor:Wang B; Liu T; Wu Z; Zhang L; Sun J; Wang X
[Ad] Endereço:a School of Medicine and Life Sciences , University of Jinan-Shandong Academy of Medical Sciences , Jinan , China.
[Ti] Título:Synthesis and biological evaluation of stilbene derivatives coupled to NO donors as potential antidiabetic agents.
[So] Source:J Enzyme Inhib Med Chem;33(1):416-423, 2018 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The work is focused on the design of drugs that prevent and treat diabetes and its complications. A novel class of stilbene derivatives were prepared by coupling NO donors of alkyl nitrate and were fully characterised by NMR and other techniques. These compounds were tested in vitro activity, including α-glucosidase inhibitory activity, aldose reductase (AR) inhibitory activity and advanced glycation end products (AGEs) formation inhibitory activity. A class of modified compounds could play a significant effect for treatment of diabetic complications. Target compounds 3e and 7c offered a potential drug design concept for the development of therapeutic or preventive agents for diabetes and its complications.
[Mh] Termos MeSH primário: Complicações do Diabetes/tratamento farmacológico
Diabetes Mellitus Experimental/tratamento farmacológico
Inibidores Enzimáticos/farmacologia
Hipoglicemiantes/farmacologia
Nitratos/farmacologia
Estilbenos/farmacologia
[Mh] Termos MeSH secundário: Aldeído Redutase/antagonistas & inibidores
Aldeído Redutase/metabolismo
Animais
Complicações do Diabetes/metabolismo
Diabetes Mellitus Experimental/induzido quimicamente
Diabetes Mellitus Experimental/metabolismo
Relação Dose-Resposta a Droga
Desenho de Drogas
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Produtos Finais de Glicação Avançada/antagonistas & inibidores
Produtos Finais de Glicação Avançada/metabolismo
Hipoglicemiantes/síntese química
Hipoglicemiantes/química
Camundongos
Camundongos Endogâmicos
Estrutura Molecular
Nitratos/química
Óxido Nítrico/metabolismo
Estilbenos/síntese química
Estilbenos/química
Estreptozocina
Relação Estrutura-Atividade
alfa-Glucosidases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Glycation End Products, Advanced); 0 (Hypoglycemic Agents); 0 (Nitrates); 0 (Stilbenes); 31C4KY9ESH (Nitric Oxide); 5W494URQ81 (Streptozocin); EC 1.1.1.21 (Aldehyde Reductase); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180130
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2018.1425686


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[PMID]:28456989
[Au] Autor:Sozmen EY; Sezer ED
[Ad] Endereço:Department of Medical Biochemistry and Metabolism Laboratory, Ege University Faculty of Medicine, Izmir, Turkey. eser.sozmen@ege.edu.tr.
[Ti] Título:Methods for Determination of α-Glycosidase, ß-Glycosidase, and α-Galactosidase Activities in Dried Blood Spot Samples.
[So] Source:Methods Mol Biol;1594:255-264, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The lysosomal storage diseases (LDSs) are a heterogeneous group of inherited genetic disorders caused by defects of lysosomal proteins. The accumulation of undigested substrates from different catabolic pathways leads to cellular dysfunction. LSDs generally presents during early childhood and have a devastating impact on the families and on public health. Over the years, approaches for treatment of some LSDs have been developed with different strategies. Increasing availability of treatments of these diseases has accelerated the development of new methods and techniques for rapid diagnosis in patients with clinical indication.The use of dried blood spot (DBS) test has been proposed as a first tier test to identify patients with Gaucher, Pompe, and Fabry diseases. DBS usage is advantageous for the purpose of screening as it is non-invasive, sensitive, has low-cost and fast turnaround time compared to measurements in leucocyte and/or fibroblast culture. This chapter focuses on the activity measurement of three lysosomal enzymes (α-glucosidase, ß-glucosidase, and α galactosidase) in DBS samples by using fluorescent substrates and by the LC-MS/MS (liquid chromatography-mass spectrometry) method. All steps of the methods, from preparation of the solutions to calculation of the enzyme activity, will be explained in detail.
[Mh] Termos MeSH primário: Teste em Amostras de Sangue Seco/métodos
Doenças por Armazenamento dos Lisossomos/enzimologia
alfa-Galactosidase/sangue
alfa-Glucosidases/sangue
[Mh] Termos MeSH secundário: Seres Humanos
Recém-Nascido
Isoenzimas/sangue
Doenças por Armazenamento dos Lisossomos/sangue
Doenças por Armazenamento dos Lisossomos/diagnóstico
Triagem Neonatal
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 2HLC17MX9G (agalsidase alfa); EC 3.2.1.20 (alpha-Glucosidases); EC 3.2.1.22 (alpha-Galactosidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6934-0_17


  9 / 3854 MEDLINE  
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[PMID]:29210296
[Au] Autor:Zhu LJ; Yi S; Li X; Chen HF; Ming M; Zhang X; Yao XS
[Ad] Endereço:a Key Laboratory of Structure-Based Drug Design & Discovery of Ministry of Education, School of Traditional Chinese Materia Medica , Shenyang Pharmaceutical University , Shenyang 110016 , China.
[Ti] Título:C-glycosides from the stems of Calophyllum membranaceum.
[So] Source:J Asian Nat Prod Res;20(1):49-54, 2018 Jan.
[Is] ISSN:1477-2213
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Three new C-glycosides, calophymembransides D-F (1-3), were isolated from the stems of Calophyllum membranaceum Gardn. et Champ.. The structures were assigned on the basis of spectroscopic data. RXRα transcriptional inhibition and α-glucosidase inhibition assays indicated that all the isolates were inactive.
[Mh] Termos MeSH primário: Calophyllum/química
Inibidores de Glicosídeo Hidrolases/farmacologia
Monossacarídeos/isolamento & purificação
[Mh] Termos MeSH secundário: Inibidores de Glicosídeo Hidrolases/química
Inibidores de Glicosídeo Hidrolases/isolamento & purificação
Estrutura Molecular
Monossacarídeos/química
Caules de Planta/química
alfa-Glucosidases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (C-glycoside); 0 (Glycoside Hydrolase Inhibitors); 0 (Monosaccharides); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1080/10286020.2017.1409734


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Fotocópia
[PMID]:27775125
[Au] Autor:Cásedas G; Les F; Gómez-Serranillos MP; Smith C; López V
[Ad] Endereço:Department of Pharmacy, Faculty of Health Sciences, Universidad San Jorge, 50.830 Villanueva de Gállego, Zaragoza, Spain. ilopez@usj.es.
[Ti] Título:Bioactive and functional properties of sour cherry juice (Prunus cerasus).
[So] Source:Food Funct;7(11):4675-4682, 2016 Nov 09.
[Is] ISSN:2042-650X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sour cherry juice (Prunus cerasus) is consumed as a nutritional supplement claiming health effects. The aim of the study was to evaluate the different properties of sour cherry juice in terms of antioxidant activity and inhibition of target enzymes in the central nervous system and diabetes. The content of polyphenols and anthocyanins was quantified. Different experiments were carried out to determine the radical scavenging properties of the juice. The activity of sour cherry juice was also tested in physiological relevant enzymes of the central nervous system (acetylcholinesterase, monoamine oxidase A, tyrosinase) and others involved in type 2 diabetes (α-glucosidase, dipeptidyl peptidase-4). Sour cherry juice showed significant antioxidant effects but the activity of the lyophilized juice was not superior to compounds such as ascorbic, gallic or chlorogenic acid. Furthermore, sour cherry juice and one of its main polyphenols known as chlorogenic acid were also able to inhibit monoamine oxidase A and tyrosinase as well as enzymes involved in diabetes. This is the first time that sour cherry juice is reported to inhibit monoamine oxidase A, α-glucosidase and dipeptidyl peptidase-4 in a dose dependent manner, which may be of interest for human health and the prevention of certain diseases.
[Mh] Termos MeSH primário: Artemia/efeitos dos fármacos
Sucos de Frutas e Vegetais/análise
Prunus avium/química
[Mh] Termos MeSH secundário: Animais
Antioxidantes
Bioensaio
Sobrevivência Celular
Alimento Funcional
Células HeLa
Seres Humanos
Compostos Fitoquímicos/química
Compostos Fitoquímicos/metabolismo
Superóxidos/química
alfa-Glucosidases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Phytochemicals); 11062-77-4 (Superoxides); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE



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