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[PMID]:29381773
[Au] Autor:Moradi N; Fadaei R; Emamgholipour S; Kazemian E; Panahi G; Vahedi S; Saed L; Fallah S
[Ad] Endereço:Department of Clinical Biochemistry, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran.
[Ti] Título:Association of circulating CTRP9 with soluble adhesion molecules and inflammatory markers in patients with type 2 diabetes mellitus and coronary artery disease.
[So] Source:PLoS One;13(1):e0192159, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:C1q/TNF-related protein 9 (CTRP9) is a paralogue of adiponectin with known favorable effects on lipid and glucose metabolism. A potential role of CTRP9 for regulation of endothelium function has been suggested by previous studies. However, no studies have examined the relation between serum CTRP9 levels and adhesion molecules in patients with type 2 diabetes mellitus (T2DM) and coronary artery disease (CAD). The present study was conducted on 337 subjects who underwent coronary angiography and were categorized into four groups according to the presence of CAD and T2DM (control, CAD, T2DM and CAD+T2DM). Serum levels of CTRP9, adiponectin, sICAM-1, sVCAM-1, sE-Selectin, IL-6 and TNF-α were measured. It was found that the circulating CTRP9 levels were independently associated with increased risk of CAD and T2DM in addition to elevated levels of serum CTRP9 in CAD, T2DM and CAD+T2DM groups. A significant association of serum CTRP9 levels with adhesion molecules in CAD and T2DM patients as well as serum TNF-α levels in CAD individuals was noted. A significant relation between the circulating levels of CTRP9 and HOMA-IR in T2DM subjects was also observed. The results revealed increased circulating levels of CTRP9 in T2DM and CAD individuals which suggests a compensatory response to insulin resistance, inflammatory milieu and endothelial dysfunction; however, more studies are needed to confirm this.
[Mh] Termos MeSH primário: Adiponectina/sangue
Biomarcadores/sangue
Moléculas de Adesão Celular/sangue
Doença da Artéria Coronariana/sangue
Diabetes Mellitus Tipo 2/sangue
Glicoproteínas/sangue
Mediadores da Inflamação/sangue
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Masculino
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adiponectin); 0 (Biomarkers); 0 (C1QTNF9B protein, human); 0 (Cell Adhesion Molecules); 0 (Glycoproteins); 0 (Inflammation Mediators)
[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:180131
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0192159


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[PMID]:28453664
[Au] Autor:Krag TO; Ruiz-Ruiz C; Vissing J
[Ad] Endereço:Copenhagen Neuromuscular Center, Department of Neurology, Rigshospitalet, University of Copenhagen, 2100 Copenhagen, Denmark.
[Ti] Título:Glycogen Synthesis in Glycogenin 1-Deficient Patients: A Role for Glycogenin 2 in Muscle.
[So] Source:J Clin Endocrinol Metab;102(8):2690-2700, 2017 Aug 01.
[Is] ISSN:1945-7197
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Context: Glycogen storage disease (GSD) type XV is a rare disease caused by mutations in the GYG1 gene that codes for the core molecule of muscle glycogen, glycogenin 1. Nonetheless, glycogen is present in muscles of glycogenin 1-deficient patients, suggesting an alternative for glycogen buildup. A likely candidate is glycogenin 2, an isoform expressed in the liver and heart but not in healthy skeletal muscle. Objective: We wanted to investigate the formation of glycogen and changes in glycogen metabolism in patients with GSD type XV. Design, Setting, and Patients: Two patients with mutations in the GYG1 gene were investigated for histopathology, ultrastructure, and expression of proteins involved in glycogen synthesis and metabolism. Results: Apart from occurrence of polyglucosan (PG) bodies in few fibers, glycogen appeared normal in most cells, and the concentration was normal in patients with GSD type XV. We found that glycogenin 1 was absent, but glycogenin 2 was present in the patients, whereas the opposite was the case in healthy controls. Electron microscopy revealed that glycogen was present between and not inside myofibrils in type II fibers, compromising the ultrastructure of these fibers, and only type I fibers contained PG bodies. We also found significant changes to the expression levels of several enzymes directly involved in glycogen and glucose metabolism. Conclusions: To our knowledge, this is the first report demonstrating expression of glycogenin 2 in glycogenin 1-deficient patients, suggesting that glycogenin 2 rescues the formation of glycogen in patients with glycogenin 1 deficiency.
[Mh] Termos MeSH primário: Glucosiltransferases/genética
Glucosiltransferases/metabolismo
Glicogênio/biossíntese
Glicoproteínas/genética
Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: Idoso
Metabolismo dos Carboidratos
Estudos de Casos e Controles
Feminino
Glucanos/metabolismo
Glucose/metabolismo
Glicogênio/metabolismo
Glicogênio/ultraestrutura
Doença de Depósito de Glicogênio/genética
Glicoproteínas/metabolismo
Seres Humanos
Microscopia Eletrônica
Meia-Idade
Fibras Musculares de Contração Rápida/ultraestrutura
Músculo Esquelético/patologia
Músculo Esquelético/ultraestrutura
Miofibrilas/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucans); 0 (Glycoproteins); 0 (glycogenin); 9005-79-2 (Glycogen); 9012-72-0 (polyglucosan); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.186 (GYG2 protein, human); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1210/jc.2017-00399


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[PMID]:29374925
[Au] Autor:Liu W; Chai JK
[Ad] Endereço:Burn Institute, the First Affiliated Hospital of PLA General Hospital, Beijing 100048, China.
[Ti] Título:[Influences of ulinastatin on acute lung injury and time phase changes of coagulation parameters in rats with burn-blast combined injuries].
[So] Source:Zhonghua Shao Shang Za Zhi;34(1):32-39, 2018 Jan 20.
[Is] ISSN:1009-2587
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:To explore the influences of ulinastatin on acute lung injury and time phase changes of coagulation parameters in rats with severe burn-blast combined injuries. One hundred and ninety-two Sprague-Dawley rats were divided into pure burn-blast combined injury group, ulinastatin+ burn-blast combined injury group, and sham injury group according to the random number table, with 64 rats in each group. Two groups of rats with combined burn-blast injuries were inflicted with moderate blast injuries with the newly self-made explosive device. Then the rats were inflicted with 25% total body surface area full-thickness scald (hereinafter referred to as burn) on the back by immersing in 94 ℃ hot water for 12 s. Rats in sham injury group were sham injured on the back by immersing in 37 ℃ warm water for 12 s. Immediately after injury, rats in the three groups were intraperitoneally injected with Ringer's lactate solution (40 mL/kg), meanwhile rats in ulinastatin+ burn-blast combined injury group were intraperitoneally injected with ulinastatin (4×10(4)U/kg), once every 12 hours, until post injury hour (PIH) 72. Before injury, at PIH 3, 6, 12, 24, 48, 72, and on post injury day (PID) 7, 8 rats in each group were selected to harvest abdominal aortic blood samples to detect plasma levels of activated partial thromboplastin time (APTT), prothrombin time (PT), fibrinogen, D-dimer, antithrombin â…¢ (AT-â…¢), and α2-antiplasmin (α2-AP). At PIH 24, three rats in each group which were used in detection of coagulation parameters were sacrificed to observe lung injury. At PIH 72, three rats in each group were sacrificed for histopathological observation of lung. Data were processed with analysis of variance of factorial design and least-significant difference test. (1) Compared with those of rats in sham injury group, APTT of rats in pure burn-blast combined injury group significantly prolonged at PIH 72 and on PID 7 ( <0.05 or <0.01). PT significantly prolonged at PIH 3 and 72 and significantly shortened at PIH 6 ( <0.05 or <0.01) . Fibrinogen level significantly increased from PIH 12 to PID 7 ( <0.01). AT-â…¢ level significantly decreased at PIH 6 and 12 ( <0.01), and α2-AP level significantly decreased at PIH 6 and significantly increased from PIH 24 to 72 ( <0.01). Compared with those of rats in pure burn-blast combined injury group, APTT of rats in ulinastatin+ burn-blast combined injury group significantly prolonged at PIH 3 and 6 ( <0.01) while PT significantly shortened at PIH 3, 12, and 72 ( <0.05 or <0.01). Fibrinogen level significantly decreased at PIH 6 and 12 and significantly increased at PIH 72 ( <0.05 or <0.01). AT-â…¢ level significantly increased at PIH 3, 12, 48, and 72 ( <0.05 or <0.01), and α2-AP level significantly decreased from PIH 12 to 72 ( <0.05 or <0.01). D-dimer level of rats in sham injury group, pure burn-blast combined injury group, and ulinastatin+ burn-blast combined injury group were respectively (0.084±0.013), (0.115±0.015), (0.158±0.022), (0.099±0.011), (0.099±0.012), (0.089±0.011), (0.124±0.014), and (0.116±0.018) µg/mL, (0.064±0.033), (0.114±0.016), (0.135±0.009), (0.060±0.008), (0.104±0.010), (0.124±0.020), (0.180±0.036), and (0.201±0.032) µg/mL, (0.074±0.013), (0.084±0.035), (0.101±0.050), (0.091±0.046), (0.096±0.034), (0.044±0.019), (0.106±0.049), and (0.118±0.047) µg/mL. Compared with that of rats in sham injury group, D-dimer level significantly decreased at PIH 6 and 12 and significantly increased from PIH 48 to PID 7 ( <0.05 or <0.01). Compared with that of rats in pure burn-blast combined injury group, D-dimer level of rats in ulinastatin+ burn-blast combined injury group significantly decreased at PIH 3, 48, and 72, and on PID 7 ( <0.05 or <0.01). (2) At PIH 24, there was a large amount of light red effusion in the thoracic cavity, and both lung lobes were hyperemic and edematous with a small amount of blood clots in the left and middle lobe of rats in pure burn-blast combined injury group. There was a small amount of yellowish effusion in the thoracic cavity of rats in ulinastatin+ burn-blast combined injury group, and the degree of hyperemic and edematous of bilateral lobes was lighter compared with rats in pure burn-blast combined injury group with no clot in the left lobe. No congestion, edema, or bleeding was observed in lungs of rats in sham injury group. (3) At PIH 72, disorganized alveolar structure, collapsed alveolar cavity, edematous and thickening pulmonary interstitium, infiltration of a large amount of inflammatory cells, obvious rupture of alveolar septum, and hyaline thrombus were observed in lungs of rats in pure burn-blast combined injury group. Significantly improved alveolar structure, less collapsed alveolar cavity, improved edematous pulmonary interstitium, less infiltration of inflammatory cells, rupture of alveolar septum, and no thrombus were observed in lungs of rats in ulinastatin+ burn-blast combined injury group. The lung tissue had a well-filled alveolar cavity with no interstitial edema or infiltration of inflammatory cells and no thrombosis in lungs of rats in sham injury group. Ulinastatin has positive therapeutic effects on acute lung injury in rats with severe burn-blast combined injuries through its good regulating effects on coagulation and fibrinolytic disorders caused by burn-blast combined injuries.
[Mh] Termos MeSH primário: Lesão Pulmonar Aguda/tratamento farmacológico
Traumatismos por Explosões/complicações
Queimaduras/complicações
Glicoproteínas/farmacologia
Inibidores da Tripsina/farmacologia
[Mh] Termos MeSH secundário: Lesão Pulmonar Aguda/complicações
Animais
Traumatismos por Explosões/sangue
Traumatismos por Explosões/patologia
Queimaduras/sangue
Queimaduras/patologia
Edema
Produtos de Degradação da Fibrina e do Fibrinogênio
Edema Pulmonar
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibrin Fibrinogen Degradation Products); 0 (Glycoproteins); 0 (Trypsin Inhibitors); 0 (fibrin fragment D); OR3S9IF86U (urinastatin)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180129
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1009-2587.2018.01.007


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[PMID]:29342381
[Au] Autor:Kyle RA; Larson DR; Therneau TM; Dispenzieri A; Kumar S; Cerhan JR; Rajkumar SV
[Ad] Endereço:From the Divisions of Hematology (R.A.K., A.D., S.K., S.V.R.), Biostatistics (D.R.L., T.M.T.), and Epidemiology (J.R.C.), Mayo Clinic, Rochester, MN.
[Ti] Título:Long-Term Follow-up of Monoclonal Gammopathy of Undetermined Significance.
[So] Source:N Engl J Med;378(3):241-249, 2018 01 18.
[Is] ISSN:1533-4406
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Monoclonal gammopathy of undetermined significance (MGUS) occurs in approximately 3% of persons 50 years of age or older. METHODS: We studied 1384 patients who were residing in southeastern Minnesota and in whom MGUS was diagnosed at the Mayo Clinic in the period from 1960 through 1994; the median follow-up was 34.1 years (range, 0.0 to 43.6). The primary end point was progression to multiple myeloma or another plasma-cell or lymphoid disorder. RESULTS: During 14,130 person-years of follow-up, MGUS progressed in 147 patients (11%), a rate that was 6.5 times (95% confidence interval [CI], 5.5 to 7.7) as high as the rate in the control population. The risk of progression without accounting for death due to competing causes was 10% at 10 years, 18% at 20 years, 28% at 30 years, 36% at 35 years, and 36% at 40 years. Among patients with IgM MGUS, the presence of two adverse risk factors - namely, an abnormal serum free light-chain ratio (ratio of kappa to lambda free light chains) and a high serum monoclonal protein (M protein) level (≥1.5 g per deciliter) - was associated with a risk of progression at 20 years of 55%, as compared with 41% among patients who had one adverse risk factor and 19% among patients who had neither risk factor. Among patients with non-IgM MGUS, the risk of progression at 20 years was 30% among those who had the two risk factors, 20% among those who had one risk factor, and 7% among those who had neither risk factor. Patients with MGUS had shorter survival than was expected in the control population of Minnesota residents of matched age and sex (median, 8.1 vs. 12.4 years; P<0.001). CONCLUSIONS: Significant differences were noted in the risk of progression between patients with IgM MGUS and those with non-IgM MGUS. Overall survival was shorter among patients with MGUS than was expected in a matched control population. (Funded by the National Cancer Institute.).
[Mh] Termos MeSH primário: Progressão da Doença
Gamopatia Monoclonal de Significância Indeterminada/complicações
[Mh] Termos MeSH secundário: Adulto
Idoso
Exame de Medula Óssea
Feminino
Seguimentos
Glicoproteínas/sangue
Seres Humanos
Cadeias Leves de Imunoglobulina/sangue
Imunoglobulina M/sangue
Masculino
Meia-Idade
Gamopatia Monoclonal de Significância Indeterminada/mortalidade
Gamopatia Monoclonal de Significância Indeterminada/patologia
Mieloma Múltiplo/etiologia
Prognóstico
Modelos de Riscos Proporcionais
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Immunoglobulin Light Chains); 0 (Immunoglobulin M); 0 (protein M (glycoprotein))
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1056/NEJMoa1709974


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[PMID]:28460472
[Au] Autor:Å Urga S; Nanut MP; Kos J; Sabotic J
[Ad] Endereço:Department of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
[Ti] Título:Fungal lectin MpL enables entry of protein drugs into cancer cells and their subcellular targeting.
[So] Source:Oncotarget;8(16):26896-26910, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lectins have been recognized as promising carrier molecules for targeted drug delivery. They specifically bind carbohydrate moieties on cell membranes and trigger cell internalization. Fungal lectin MpL (Macrolepiota procera lectin) does not provoke cancer cell cytotoxicity but is able to bind aminopeptidase N (CD13) and integrin α3ß1, two glycoproteins that are overexpressed on the membrane of tumor cells. Upon binding, MpL is endocytosed in a clathrin-dependent manner and accumulates initially in the Golgi apparatus and, finally, in the lysosomes. For effective binding and internalization a functional binding site on the α-repeat is needed. To test the potential of MpL as a carrier for delivering protein drugs to cancer cells we constructed fusion proteins consisting of MpL and the cysteine peptidase inhibitors cystatin C and clitocypin. The fused proteins followed the same endocytic route as the unlinked MpL. Peptidase inhibitor-MpL fusions impaired both the intracellular degradation of extracellular matrix and the invasiveness of cancer cells. MpL is thus shown in vitro to be a lectin that can enable protein drugs to enter cancer cells, enhance their internalization and sort them to lysosomes and the Golgi apparatus.
[Mh] Termos MeSH primário: Portadores de Fármacos
Proteínas Fúngicas/metabolismo
Lectinas/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Membrana Celular/metabolismo
Colágeno Tipo IV/metabolismo
Endocitose
Glicoproteínas/metabolismo
Seres Humanos
Espaço Intracelular/metabolismo
Ligação Proteica
Transporte Proteico
Proteólise
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type IV); 0 (Drug Carriers); 0 (Fungal Proteins); 0 (Glycoproteins); 0 (Lectins); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15849


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[PMID]:28742884
[Au] Autor:Borzym-Kluczyk M; Radziejewska I; Cechowska-Pasko M; Darewicz B
[Ad] Endereço:Department of Pharmaceutical Biochemistry, Medical University of Bialystok, Bialystok, Poland.
[Ti] Título:Reduced expression of E-cadherin and increased sialylation level in clear cell renal cell carcinoma.
[So] Source:Acta Biochim Pol;64(3):465-470, 2017.
[Is] ISSN:1734-154X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Cancer cells are characterized by an aberrant increase in protein N-glycosylation and by disruption of E-cadherin-mediated adherens junctions. However, the relationship between alterations in N-glycosylation process and loss of E-cadherin adhesion in cancer remains unclear. The mechanisms of altered expression of adhesive glycoproteins in cancer cells have not been fully elucidated. Thus, the aim of this study was to examine the expression of E-cadherin and sialyl Lewis / , NeuAcα2-3Gal, NeuAcα2-6Gal/GalNAc structures in the normal renal tissue and intermediate and cancerous tissues from patients with clear cell RCC. Moreover, we attempted to correlate the E-cadherin expression with some specific sugar residues of renal cancer tissue glycoproteins. The expression of E-cadherin was analysed using ELISA test and immunoblotting. Oligosaccharide structures and sialylation level were detected with ELISA test using specific biotinylated lectins or antibodies. A significant decrease of E-cadherin expression as well as a significant increase in sialylated oligosaccharides level in intermediate zone and renal cancer tissue in comparison to normal renal tissue are reported. Significant decrease in expression of cadherins and increase in sialylation of oligosaccharide structures in renal cancer tissue in comparison to normal renal tissue, and in renal cancer tissue in comparison to intermediate zone of renal tissue, are important for the future research concerning detection and quantification of cadherins and sialylated oligosaccharide structures in urine and cells of urinary sediment as possible non-invasive marker of early RCC.
[Mh] Termos MeSH primário: Caderinas/metabolismo
Carcinoma de Células Renais/metabolismo
Neoplasias Renais/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/metabolismo
Idoso
Carcinoma de Células Renais/patologia
Feminino
Glicoconjugados/metabolismo
Glicoproteínas/metabolismo
Seres Humanos
Rim/metabolismo
Neoplasias Renais/patologia
Antígeno Lewis X/metabolismo
Masculino
Meia-Idade
Valores de Referência
Ácidos Siálicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CDH1 protein, human); 0 (Cadherins); 0 (Glycoconjugates); 0 (Glycoproteins); 0 (Lewis X Antigen); 0 (Sialic Acids); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.18388/abp.2015_1215


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[PMID]:29381065
[Au] Autor:Lin N; Chen S; Zhang H; Li J; Fu L
[Ti] Título:Quantification of Major Royal Jelly Protein 1 in Fresh Royal Jelly by Ultraperformance Liquid Chromatography-Tandem Mass Spectrometry.
[So] Source:J Agric Food Chem;66(5):1270-1278, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Major royal jelly protein 1 (MRJP1) is the most abundant protein in royal jelly (RJ), and the level of MRJP1 has been suggested as a promising parameter for standardization and evaluation of RJ authenticity in quality. Here, a quantitative method was developed for the quantification of MRJP1 in RJ based on a signature peptide and a stable isotope-labeled internal standard peptide FFDYDFGSDER*(R*, C , N ) by ultraperformance liquid chromatography-tandem mass spectrometry. Recoveries of the established method ranged from 85.33 to 95.80%, and both the intra- and interday precision were RSD < 4.97%. Quantification results showed that content of MRJP1 in fresh RJ was 41.96-55.01 mg/g. Abnormal levels of MRJP1 were found in three commercial RJs and implied that these samples were of low quality and might be adulterated. Results of the present work suggested that the developed method could be successfully applied to quantify MRJP1 in RJ and also could evaluate the quality of RJ.
[Mh] Termos MeSH primário: Cromatografia Líquida/métodos
Ácidos Graxos/química
Glicoproteínas/análise
Proteínas de Insetos/análise
Espectrometria de Massas em Tandem/métodos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Isótopos de Carbono
Marcação por Isótopo
Isótopos de Nitrogênio
Fragmentos de Peptídeos/química
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carbon Isotopes); 0 (Fatty Acids); 0 (Glycoproteins); 0 (Insect Proteins); 0 (MRJP1 protein, Apis mellifera); 0 (Nitrogen Isotopes); 0 (Peptide Fragments); L497I37F0C (royal jelly)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180131
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05698


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[PMID]:27778439
[Au] Autor:Randi AM; Laffan MA
[Ad] Endereço:National Heart and Lung Institute, Imperial College, London, UK.
[Ti] Título:Von Willebrand factor and angiogenesis: basic and applied issues.
[So] Source:J Thromb Haemost;15(1):13-20, 2017 01.
[Is] ISSN:1538-7836
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The recent discovery that von Willebrand factor (VWF) regulates blood vessel formation has opened a novel perspective on the function of this complex protein. VWF was discovered as a key component of hemostasis, capturing platelets at sites of endothelial damage and synthesized in megakaryocytes and endothelial cells (EC). In recent years, novel functions and binding partners have been identified for VWF. The finding that loss of VWF in EC results in enhanced, possibly dysfunctional, angiogenesis is consistent with the clinical observations that in some patients with von Willebrand disease (VWD), vascular malformations can cause severe gastrointestinal (GI) bleeding. In vitro and in vivo studies indicate that VWF can regulate angiogenesis through multiple pathways, both intracellular and extracellular, although their relative importance is still unclear. Investigation of these pathways has been greatly facilitated by the ability to isolate EC from progenitors circulating in the peripheral blood of normal controls and patients with VWD. In the next few years, these will yield further evidence on the molecular pathways controlled by VWF and shed light on this novel and fascinating area of vascular biology. In this article, we will review the evidence supporting a role for VWF in blood vessel formation, the link between VWF dysfunction and vascular malformations causing GI bleeding and how they may be causally related. Finally, we will discuss how these findings point to novel therapeutic approaches to bleeding refractory to VWF replacement therapy in VWD.
[Mh] Termos MeSH primário: Neovascularização Fisiológica
Fator de von Willebrand/metabolismo
[Mh] Termos MeSH secundário: Angiodisplasia/metabolismo
Animais
Coagulação Sanguínea
Plaquetas/metabolismo
Células Endoteliais/metabolismo
Hemorragia Gastrointestinal/sangue
Glicoproteínas/metabolismo
Hemorragia
Hemostasia
Seres Humanos
Megacariócitos/metabolismo
Camundongos
Neovascularização Patológica
Transdução de Sinais
Células-Tronco/metabolismo
Receptor 2 de Fatores de Crescimento do Endotélio Vascular/metabolismo
Doenças de von Willebrand/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Glycoproteins); 0 (von Willebrand Factor); EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-2)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE
[do] DOI:10.1111/jth.13551


  9 / 67084 MEDLINE  
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[PMID]:28470609
[Au] Autor:Strutton B; Jaffé SRP; Pandhal J; Wright PC
[Ad] Endereço:Department of Chemical and Biological Engineering, ChELSI Institute, University of Sheffield, Mappin Street, Sheffield, S1 3JD, UK.
[Ti] Título:Generation of Recombinant N-Linked Glycoproteins in E. coli.
[So] Source:Methods Mol Biol;1586:233-250, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The production of N-linked recombinant glycoproteins is possible in a variety of biotechnology host cells, and more recently in the bacterial workhorse, Escherichia coli. This methods chapter will outline the components and procedures needed to produce N-linked glycoproteins in E. coli, utilizing Campylobacter jejuni glycosylation machinery, although other related genes can be used with minimal tweaks to this methodology. To ensure a successful outcome, various methods will be highlighted that can confirm glycoprotein production to a high degree of confidence, including the gold standard of mass spectrometry analysis.
[Mh] Termos MeSH primário: Campylobacter jejuni/genética
Escherichia coli/genética
Glicoproteínas/genética
Interferon-alfa/genética
[Mh] Termos MeSH secundário: Far-Western Blotting/métodos
Clonagem Molecular/métodos
Eletroforese em Gel de Poliacrilamida/métodos
Genes Bacterianos
Glicoproteínas/química
Glicoproteínas/isolamento & purificação
Glicosilação
Interferon-alfa/química
Interferon-alfa/isolamento & purificação
Espectrometria de Massas/métodos
Plasmídeos/genética
Polissacarídeos/análise
Polissacarídeos/genética
Processamento de Proteína Pós-Traducional
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Interferon-alpha); 0 (Polysaccharides); 0 (Recombinant Proteins); 43K1W2T1M6 (interferon alfa-2b)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_15


  10 / 67084 MEDLINE  
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[PMID]:29317208
[Au] Autor:Xiao XH; Qi XY; Wang YD; Ran L; Yang J; Zhang HL; Xu CX; Wen GB; Liu JH
[Ad] Endereço:Department of Metabolism and Endocrinology, University of South China, Hengyang, 421001, Hunan Province, China.
[Ti] Título:Zinc alpha2 glycoprotein promotes browning in adipocytes.
[So] Source:Biochem Biophys Res Commun;496(2):287-293, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent studies have highlighted recruiting and activating brite adipocytes in WAT (so-called "browning") would be an attractive anti-obesity strategy. Zinc alpha2 glycoprotein (ZAG) as an important adipokine, is reported to ameliorate glycolipid metabolism and lose body weight in obese mice. However whether the body reducing effect mediated by browning programme remains unclear. Here, we show that overexpression of ZAG in 3T3-L1 adipocytes enhanced expression of brown fat-specific markers (UCP-1, PRDM16 and CIDEA), mitochondrial biogenesis genes (PGC-1α, NRF-1/2 and mtTFA) and the key lipid metabolism lipases (ATGL, HSL, CPT1-A and p-acyl-CoA carboxylase). Additionally, those effects were dramaticlly abolished by H89/SB203580, revealing ZAG-induced browning depend on PKA and p38 MAPK signaling. Overall, our findings suggest that ZAG is a candidate therapeutic agent against obesity via induction of brown fat-like phenotype in white adipocytes.
[Mh] Termos MeSH primário: Adipócitos Marrons/metabolismo
Proteínas de Transporte/genética
Regulação da Expressão Gênica
Glicoproteínas/genética
Metabolismo dos Lipídeos/genética
[Mh] Termos MeSH secundário: Células 3T3-L1
Adipócitos Marrons/citologia
Adipócitos Marrons/efeitos dos fármacos
Animais
Proteínas Reguladoras de Apoptose/genética
Proteínas Reguladoras de Apoptose/metabolismo
Carbono-Carbono Ligases/genética
Carbono-Carbono Ligases/metabolismo
Carnitina O-Palmitoiltransferase/genética
Carnitina O-Palmitoiltransferase/metabolismo
Proteínas de Transporte/metabolismo
Proteínas Quinases Dependentes de AMP Cíclico/genética
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Glicoproteínas/metabolismo
Imidazóis/farmacologia
Isoquinolinas/farmacologia
Lipase/genética
Lipase/metabolismo
Camundongos
Fator 2 Relacionado a NF-E2/genética
Fator 2 Relacionado a NF-E2/metabolismo
Fator 1 Nuclear Respiratório/genética
Fator 1 Nuclear Respiratório/metabolismo
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/genética
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/metabolismo
Piridinas/farmacologia
Transdução de Sinais
Sulfonamidas/farmacologia
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Proteína Desacopladora 1/genética
Proteína Desacopladora 1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AZGP1 protein, mouse); 0 (Apoptosis Regulatory Proteins); 0 (Carrier Proteins); 0 (Cidea protein, mouse); 0 (DNA-Binding Proteins); 0 (Glycoproteins); 0 (Imidazoles); 0 (Isoquinolines); 0 (NF-E2-Related Factor 2); 0 (Nfe2l2 protein, mouse); 0 (Nrf1 protein, mouse); 0 (Nuclear Respiratory Factor 1); 0 (Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha); 0 (Ppargc1a protein, mouse); 0 (Prdm16 protein, mouse); 0 (Pyridines); 0 (Sulfonamides); 0 (Transcription Factors); 0 (Ucp1 protein, mouse); 0 (Uncoupling Protein 1); EC 2.3.1.21 (CPT1B protein, mouse); EC 2.3.1.21 (Carnitine O-Palmitoyltransferase); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (PNPLA2 protein, mouse); EC 6.4.- (Carbon-Carbon Ligases); EC 6.4.1.- (acyl-CoA carboxylase); M876330O56 (N-(2-(4-bromocinnamylamino)ethyl)-5-isoquinolinesulfonamide); OU13V1EYWQ (SB 203580)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE



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