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[PMID]:28950267
[Au] Autor:Schocker F; Scharf A; Kull S; Jappe U
[Ad] Endereço:Division of Clinical and Molecular Allergology, Research Center Borstel, Priority Research Area Asthma and Allergy, Airway Research Center North (ARCN), German Center for Lung Research (DZL), Borstel, Germany.
[Ti] Título:Detection of the Peanut Allergens Ara h 2 and Ara h 6 in Human Breast Milk: Development of 2 Sensitive and Specific Sandwich ELISA Assays.
[So] Source:Int Arch Allergy Immunol;174(1):17-25, 2017.
[Is] ISSN:1423-0097
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Little is known about breast milk as a vehicle for tolerance development or sensitization to peanuts very early in life. Thus, well-characterized and highly sensitive detection systems for the reliable determination of peanut allergens in breast milk are mandatory. METHODS: For the quantification of the marker allergens Ara h 2 and Ara h 6 in the low nanogram per milliliter range in breast milk samples of a German cohort, sensitive and highly specific sandwich ELISAs were optimized and validated. RESULTS: The Ara h 2 ELISA revealed a limit of detection (LOD) of 1.3 ng Ara h 2/mL and a quantification range of 2.3-250 ng/mL, the Ara h 6 ELISA showed an LOD of 0.7 ng/mL and a working range of 1.1-14.4 ng/mL. The assays showed no relevant cross-reactivity against other potentially cross-reactive legume, seed, and tree nut extracts (<0.01%, except for Ara h 1 in the Ara h 2 ELISA <0.1%). Ara h 2 was detectable in breast milk samples from 14/40 (35%) of the participants in concentrations from 2.3 to 184 ng/mL, Ara h 6 appeared in 9/40 (22.5%) of the lactating mothers between 1.1 and 9.7 ng/mL, and 1 highly positive sample with 79 ng/mL. Both allergens appeared at the same time points, but Ara h 6 in lower concentrations than Ara h 2. CONCLUSIONS: Sensitive and specific diagnostic tools for the determination of Ara h 2 and Ara h 6 in human breast milk were established. The kinetics of secreted Ara h 2 and Ara h 6 seem to be similar but with a difference in concentration. Follow-up investigations on their tolerogenic or sensitizing properties in breast milk become now accessible.
[Mh] Termos MeSH primário: Albuminas 2S de Plantas/análise
Antígenos de Plantas/análise
Ensaio de Imunoadsorção Enzimática/métodos
Glicoproteínas/análise
Leite Humano/química
Hipersensibilidade a Amendoim/diagnóstico
Proteínas de Plantas/imunologia
[Mh] Termos MeSH secundário: Alérgenos/análise
Arachis/imunologia
Reações Cruzadas/imunologia
Feminino
Seres Humanos
Lactação/fisiologia
Limite de Detecção
Hipersensibilidade a Amendoim/prevenção & controle
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Allergens); 0 (Antigens, Plant); 0 (Ara h 2 allergen, Arachis hypogaea); 0 (Ara h 6 allergen, Arachis hypogaea); 0 (Glycoproteins); 0 (Plant Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE
[do] DOI:10.1159/000479388


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[PMID]:28268214
[Au] Autor:Price D; Ackland ML; Suphioglu C
[Ad] Endereço:Centre for Cellular and Molecular Biology (CCMB), School of Life and Environmental Sciences, Deakin University, Burwood, VIC, Australia.
[Ti] Título:Identifying Epithelial Endocytotic Mechanisms of the Peanut Allergens Ara h 1 and Ara h 2.
[So] Source:Int Arch Allergy Immunol;172(2):106-115, 2017.
[Is] ISSN:1423-0097
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Peanuts are still one of the highest contributors to anaphylactic deaths after ingestion of a food allergen. At the molecular level, interactions between peanut allergens and the intestinal epithelium are largely unexplored. Previous findings by our research group demonstrated that the major peanut allergens, i.e., Ara h 1, Ara h 2, Ara h 3, and Ara h 6, were able to cross the Caco-2 human cell culture model of the intestinal epithelium. This research broadened our investigation to identify the mechanisms by which the Caco-2 monolayers uptake peanut allergens, specifically by endocytosis. Here, we aim to increase our understanding of allergen-epithelial interactions and, more broadly, the pathway from allergen to allergy. METHODS: The human Caco-2 cell culture model was exposed to peanut extract and a combination of confocal microscopy and inhibition studies were used to identify the endocytotic mechanisms of peanut allergens in intestinal epithelia. RESULTS: Our findings demonstrate that the peanut allergens Ara h 1 and Ara h 2 are transported through intestinal epithelia initially via early endosomes using multiple endocytotic mechanisms. From there, they are then transported to late endosomes and ultimately to lysosomes. CONCLUSIONS: These novel findings provide insight into the allergen-epithelial interactions of peanut allergens with the intestinal epithelium. Consequently, this opens the possibility of the use of these endocytotic pathways as targets for inhibitors in therapeutic development and preventative measures for peanut allergy in the future.
[Mh] Termos MeSH primário: Albuminas 2S de Plantas/metabolismo
Antígenos de Plantas/metabolismo
Endossomos/metabolismo
Glicoproteínas/metabolismo
Mucosa Intestinal/metabolismo
Lisossomos/metabolismo
Hipersensibilidade a Amendoim/imunologia
Proteínas de Plantas/metabolismo
[Mh] Termos MeSH secundário: Antígenos de Plantas/imunologia
Células CACO-2
Endocitose
Glicoproteínas/imunologia
Seres Humanos
Mucosa Intestinal/ultraestrutura
Microscopia Confocal
Proteínas de Plantas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Antigens, Plant); 0 (Ara h 1 protein, Arachis hypogaea); 0 (Ara h 2 allergen, Arachis hypogaea); 0 (Glycoproteins); 0 (Plant Proteins)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170407
[Lr] Data última revisão:
170407
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE
[do] DOI:10.1159/000451085


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[PMID]:28224143
[Au] Autor:Wu Z; Lian J; Zhao R; Li K; Li X; Yang A; Tong P; Chen H
[Ad] Endereço:State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China. wuzhihua@ncu.edu.cn chbgjy@hotmail.com and Sino-German Joint Research Institute, Nanchang University, Nanchang 330047, China.
[Ti] Título:Ara h 2 cross-linking catalyzed by MTGase decreases its allergenicity.
[So] Source:Food Funct;8(3):1195-1203, 2017 Mar 22.
[Is] ISSN:2042-650X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Peanuts, whose major allergen is Ara h 2, are included among the eight major food allergens. After reduction using dithiothreitol (DTT), cross-linking of Ara h 2 could be catalyzed by microbial transglutaminase (MTGase), a widely used enzyme in the food industry. In this study, Ara h 2 cross-linking was catalyzed by MTGase after it was reduced by DTT. Using mass spectrometry and PLINK software, five cross-linkers were identified, and five linear allergen epitopes were found to be involved in the reactions. The IgE binding capacity of cross-linked Ara h 2 was found to be significantly lower compared to that of native and reduced Ara h 2. After simulated gastric fluid (SGF) digestion, the digested products of the cross-linked Ara h 2, again, had a significantly lower IgE binding capacity compared to untreated and reduced Ara h 2. Furthermore, reduced and cross-linked Ara h 2 (RC-Ara h 2) induced lower sensitization in mice, indicating its lower allergenicity. Reduction and MTGase-catalyzed cross-linking are effective methods to decrease the allergenicity of Ara h 2. The reactions involved linear allergen epitopes destroying the material basis of the allergenicity, and this might develop a new direction for protein desensitization processes.
[Mh] Termos MeSH primário: Albuminas 2S de Plantas/química
Albuminas 2S de Plantas/imunologia
Antígenos de Plantas/química
Antígenos de Plantas/imunologia
Glicoproteínas/química
Glicoproteínas/imunologia
Transglutaminases/química
[Mh] Termos MeSH secundário: Alérgenos/química
Alérgenos/imunologia
Animais
Arachis
Biocatálise
Reagentes para Ligações Cruzadas/química
Ditiotreitol/química
Feminino
Hipersensibilidade Alimentar/imunologia
Seres Humanos
Imunoglobulina E/imunologia
Camundongos
Camundongos Endogâmicos BALB C
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Allergens); 0 (Antigens, Plant); 0 (Ara h 2 allergen, Arachis hypogaea); 0 (Cross-Linking Reagents); 0 (Glycoproteins); 37341-29-0 (Immunoglobulin E); EC 2.3.2.13 (Transglutaminases); T8ID5YZU6Y (Dithiothreitol)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170707
[Lr] Data última revisão:
170707
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE
[do] DOI:10.1039/c6fo01365a


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[PMID]:28212503
[Au] Autor:Anzengruber J; Bublin M; Bönisch E; Janesch B; Tscheppe A; Braun ML; Varga EM; Hafner C; Breiteneder H; Schäffer C
[Ad] Endereço:Department of NanoBiotechnology, NanoGlycobiology Unit, Universität für Bodenkultur Wien, Muthgasse 11, 1190 Vienna, Austria.
[Ti] Título:Lactobacillus buchneri S-layer as carrier for an Ara h 2-derived peptide for peanut allergen-specific immunotherapy.
[So] Source:Mol Immunol;85:81-88, 2017 May.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Peanut allergy is an IgE-mediated severe hypersensitivity disorder. The lack of a treatment of this potentially fatal allergy has led to intensive research on vaccine development. Here, we describe the design and initial characterization of a carrier-bound peptide derived from the most potent peanut allergen, Ara h 2, as a candidate vaccine. Based on the adjuvant capability of bacterial surface (S-) layers, a fusion protein of the S-layer protein SlpB from Lactobacillus buchneri CD034 and the Ara h 2-derived peptide AH3a42 was produced. This peptide comprised immunodominant B-cell epitopes as well as one T cell epitope. The fusion protein SlpB-AH3a42 was expressed in E. coli, purified, and tested for its IgE binding capacity as well as for its ability to activate sensitized rat basophil leukemia (RBL) cells. The capacity of Ara h 2-specific IgG rabbit-antibodies raised against SlpB-AH3a42 or Ara h 2 to inhibit IgE-binding was determined by ELISA inhibition assays using sera of peanut allergic patients sensitized to Ara h 2. IgE specific to the SlpB-AH3a42 fusion protein was detected in 69% (25 of 36) of the sera. Despite the recognition by IgE, the SlpB-AH3a42 fusion protein was unable to induce ß-hexosaminidase release from sensitized RBL cells at concentrations up to 100ng per ml. The inhibition of IgE-binding to the natural allergen observed after pre-incubation of the 20 sera with rabbit anti-SlpB-AH3a42 IgG was more than 30% for four sera, more than 20% for eight sera, and below 10% for eight sera. In comparison, anti-Ara h 2 rabbit IgG antibodies inhibited binding to Ara h 2 by 48% ±13.5%. Our data provide evidence for the feasibility of this novel approach towards the development of a peanut allergen peptide-based carrier-bound vaccine. Our experiments further indicate that more than one allergen-peptide will be needed to induce a broader protection of patients allergic to Ara h 2.
[Mh] Termos MeSH primário: Albuminas 2S de Plantas/imunologia
Antígenos de Plantas/imunologia
Dessensibilização Imunológica/métodos
Glicoproteínas/imunologia
Glicoproteínas de Membrana/imunologia
Hipersensibilidade a Amendoim/imunologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Criança
Pré-Escolar
Ensaio de Imunoadsorção Enzimática
Feminino
Seres Humanos
Immunoblotting
Lactobacillus
Masculino
Proteínas Recombinantes/imunologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Antigens, Plant); 0 (Ara h 2 allergen, Arachis hypogaea); 0 (Glycoproteins); 0 (Membrane Glycoproteins); 0 (Recombinant Proteins); 0 (S-layer proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170218
[St] Status:MEDLINE
[do] DOI:10.1016/j.molimm.2017.02.005


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[PMID]:28128054
[Au] Autor:Sharma A; Kumar P; Kesari P; Neetu; Katiki M; Mishra M; Singh PK; Gurjar BR; Sharma AK; Tomar S; Kumar P
[Ad] Endereço:Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand-247667. India.
[Ti] Título:Purification and Characterization of 2S Albumin from Seeds of Wrightia tinctoria Exhibiting Antibacterial and DNase Activity.
[So] Source:Protein Pept Lett;24(4):368-378, 2017.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:2S albumin is a low-molecular-weight seed storage protein belonging to the prolamin superfamily. In the present work a small 2S albumin (WTA) protein of ~16 kDa has been purified from the seeds of Wrightia tinctoria. The WTA is a heterodimer protein with a small subunit of ~5 kDa and a larger subunit of ~11 kDa bridged together through disulphide bonds. The protein exhibits deoxyribonucleases activity against closed circular pBR322 plasmid DNA and linear BL21 genomic DNA. The protein also showed antibacterial activity against Morexalla catarrhalis. CD studies indicate a high α-helical content in the protein. The conserved disulphide bonds in the protein suggest that the WTA is highly stable under high pH and temperature like other 2S albumin.
[Mh] Termos MeSH primário: Albuminas 2S de Plantas/isolamento & purificação
Antibacterianos/isolamento & purificação
Apocynaceae/química
Desoxirribonucleases/isolamento & purificação
[Mh] Termos MeSH secundário: Albuminas 2S de Plantas/química
Albuminas 2S de Plantas/farmacologia
Antibacterianos/química
Antibacterianos/farmacologia
DNA/efeitos dos fármacos
DNA/metabolismo
Desoxirribonucleases/química
Desoxirribonucleases/farmacologia
Epitopos de Linfócito B
Moraxella (Branhamella) catarrhalis/efeitos dos fármacos
Sementes/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Anti-Bacterial Agents); 0 (Epitopes, B-Lymphocyte); 9007-49-2 (DNA); EC 3.1.- (Deoxyribonucleases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170128
[St] Status:MEDLINE
[do] DOI:10.2174/0929866524666170126144936


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[PMID]:28120602
[Au] Autor:Tontini C; Marinangeli L; Maiello N; Abbadessa S; Villalta D; Antonicelli L
[Ad] Endereço:Dipartimento di Medicina Interna, U.O. Allergologia, Azienda Ospedaliero-Universitaria Ospedali Riuniti Ancona, Ancona, Italy. Phone: +39 071 596 5693 E-mail: c.tontini@live.com.
[Ti] Título:Ara h 6 sensitization in peanut allergy: friend, foe or innocent bystander?
[So] Source:Eur Ann Allergy Clin Immunol;49(1):18-21, 2017 Jan.
[Is] ISSN:1764-1489
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:The clinical role of Ara h 6 sensitization in peanut allergy is a current matter of debate. We investigated the role of Ara h 6 sensitization patterns in a sample of young adults from different Italian cities. Sera of 33 patients with specific IgE against Ara h 6 were selected. According to clinical symptoms upon peanut ingestion, patients were divided into severe reaction (SR) and mild-tolerant (MT) subgroups. While the SR group mainly showed sensitization patterns involving Ara h 2 and other major allergenic components, a previously undescribed association between Ara h 6 and Ara h 9 was found in the MT group. This pattern seems to be clustered in Mediterranean Italy and associated with Pru p 3 sensitization. This finding might shed a new light on the role of Ara h 6 sensitization in peanut allergy.
[Mh] Termos MeSH primário: Albuminas 2S de Plantas/imunologia
Antígenos de Plantas/imunologia
Hipersensibilidade a Amendoim/etiologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Criança
Feminino
Seres Humanos
Masculino
Estudos Retrospectivos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Antigens, Plant); 0 (Ara h 6 allergen, Arachis hypogaea)
[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:170126
[St] Status:MEDLINE


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[PMID]:28117717
[Au] Autor:JanssenDuijghuijsen LM; van Norren K; Grefte S; Koppelman SJ; Lenaerts K; Keijer J; Witkamp RF; Wichers HJ
[Ad] Endereço:Wageningen Food and Biobased Research, Wageningen University and Research, P.O. Box 17, 6700 AA Wageningen, The Netherlands. lonneke.janssen@wur.nl.
[Ti] Título:Endurance Exercise Increases Intestinal Uptake of the Peanut Allergen Ara h 6 after Peanut Consumption in Humans.
[So] Source:Nutrients;9(1), 2017 Jan 21.
[Is] ISSN:2072-6643
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Controlled studies on the effect of exercise on intestinal uptake of protein are scarce and underlying mechanisms largely unclear. We studied the uptake of the major allergen Ara h 6 following peanut consumption in an exercise model and compared this with changes in markers of intestinal permeability and integrity. Ten overnight-fasted healthy non-allergic men ( = 4) and women ( = 6) (23 ± 4 years) ingested 100 g of peanuts together with a lactulose/rhamnose (L/R) solution, followed by rest or by 60 min cycling at 70% of their maximal workload. Significantly higher, though variable, levels of Ara h 6 in serum were found during exercise compared to rest (Peak = 0.03; area under the curve = 0.006), with individual fold changes ranging from no increase to an increase of over 150-fold in the uptake of Ara h 6. Similarly, uptake of lactulose (2-18 fold change, = 0.0009) and L/R ratios (0.4-7.9 fold change, = 0.04) were significantly increased which indicates an increase in intestinal permeability. Intestinal permeability and uptake of Ara h 6 were strongly correlated ( = 0.77, < 0.0001 for lactulose and Ara h 6). Endurance exercise after consumption may lead to increased paracellular intestinal uptake of food proteins.
[Mh] Termos MeSH primário: Albuminas 2S de Plantas/metabolismo
Antígenos de Plantas/metabolismo
Arachis
Exercício
Absorção Intestinal
Sementes
Regulação para Cima
[Mh] Termos MeSH secundário: Albuminas 2S de Plantas/sangue
Albuminas 2S de Plantas/toxicidade
Adulto
Algoritmos
Antígenos de Plantas/sangue
Antígenos de Plantas/toxicidade
Arachis/efeitos adversos
Arachis/química
Ciclismo
Biomarcadores/sangue
Desjejum
Feminino
Fármacos Gastrointestinais/sangue
Fármacos Gastrointestinais/farmacocinética
Seres Humanos
Lactulose/sangue
Lactulose/farmacocinética
Masculino
Permeabilidade
Resistência Física
Período Pós-Prandial
Reprodutibilidade dos Testes
Sementes/efeitos adversos
Sementes/química
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Antigens, Plant); 0 (Ara h 6 allergen, Arachis hypogaea); 0 (Biomarkers); 0 (Gastrointestinal Agents); 4618-18-2 (Lactulose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170125
[St] Status:MEDLINE


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[PMID]:27989798
[Au] Autor:Wu Z; Zhang Y; Zhan S; Lian J; Zhao R; Li K; Tong P; Li X; Yang A; Chen H
[Ad] Endereço:State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; Sino-German Joint Research Institute, Nanchang University, Nanchang 330047, China. Electronic address: wuzhihua@ncu.edu.cn.
[Ti] Título:Development of immunoaffinity chromatographic method for Ara h 2 isolation.
[So] Source:Protein Expr Purif;131:85-90, 2017 Mar.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ara h 2 is considered a major allergen in peanut. Due to the difficulty of separation, Ara h 2 had not been fully studied. Immunoaffinity chromatography (IAC) column can separate target protein with high selectivity, which made it possible to purify Ara h 2 from different samples. In this study, IAC method was developed to purify Ara h 2 and its effect was evaluated. By coupling polyclonal antibody (pAb) on CNBr-activated Sepharose 4B, the column for specific extraction was constructed. The coupling efficiency of the IAC column was higher than 90%, which made the capacity of column reached 0.56 mg per 0.15 g medium (dry weight). The recovery of Ara h 2 ranged from 93% to 100% for different concentrations of pure Ara h 2 solutions in 15 min. After using a column 10 times, about 88% of the column capacity remained. When applied to extract Ara h 2 from raw peanut protein extract and boiled peanut protein extract, the IAC column could recovery 94% and 88% target protein from the mixture. SDS-PAGE and Western blotting analysis confirmed the purified protein was Ara h 2, its purity reached about 90%. Significantly, the IAC column could capture dimer of Ara h 2, which made it feasible to prepared derivative of protein after processing.
[Mh] Termos MeSH primário: Albuminas 2S de Plantas/química
Albuminas 2S de Plantas/isolamento & purificação
Anticorpos/química
Antígenos de Plantas/química
Antígenos de Plantas/isolamento & purificação
Arachis/química
Cromatografia de Afinidade/métodos
Glicoproteínas/química
Glicoproteínas/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Antibodies); 0 (Antigens, Plant); 0 (Ara h 2 allergen, Arachis hypogaea); 0 (Glycoproteins)
[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:161220
[St] Status:MEDLINE


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[PMID]:27859359
[Au] Autor:Kleine-Tebbe J; Hamilton RG
[Ad] Endereço:Allergy & Asthma Center Westend, Outpatient Clinic Hanf, Ackermann & Kleine-Tebbe, Berlin, Germany.
[Ti] Título:Cashew allergy, 2S albumins, and risk predictions based on IgE antibody levels.
[So] Source:Allergy;72(4):515-518, 2017 04.
[Is] ISSN:1398-9995
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Mh] Termos MeSH primário: Albuminas
Anacardium/imunologia
[Mh] Termos MeSH secundário: Albuminas 2S de Plantas/imunologia
Alérgenos/imunologia
Antígenos de Plantas/imunologia
Seres Humanos
Imunoglobulina E/imunologia
Hipersensibilidade a Noz/imunologia
Proteínas de Plantas/imunologia
[Pt] Tipo de publicação:EDITORIAL; COMMENT
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Albumins); 0 (Allergens); 0 (Antigens, Plant); 0 (Plant Proteins); 37341-29-0 (Immunoglobulin E)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1111/all.13084


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[PMID]:27845035
[Au] Autor:JanssenDuijghuijsen LM; Wichers HJ; van Norren K; Keijer J; Baumert JL; de Jong GA; Witkamp RF; Koppelman SJ
[Ad] Endereço:Wageningen Food and Biobased Research, Wageningen University and Research, The Netherlands; Nutrition and Pharmacology, Wageningen University and Reserach, The Netherlands; Human and Animal Physiology, Wageningen University and Research, The Netherlands.
[Ti] Título:Detection of peanut allergen in human blood after consumption of peanuts is skewed by endogenous immunoglobulins.
[So] Source:J Immunol Methods;440:52-57, 2017 Jan.
[Is] ISSN:1872-7905
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Some studies have suggested that allergens may appear in the circulation after ingestion of allergenic food sources. The reported levels of allergen in serum, however, are low, and conclusions between studies differ. Here, we investigated factors that determine the detection of allergens in serum after consumption of peanuts. Ten healthy volunteers ingested 100g of light-roasted peanuts. Serum samples were taken at regular intervals for six hours. A double monoclonal sandwich ELISA was used to analyse the presence and quantity of the major peanut allergen Ara h 6 in serum. In 4 out of 10 subjects, no Ara h 6 could be detected. Purified Ara h 6 that was digested in vitro was still reactive in the ELISA, rejecting the possibility that digestion leads to small peptides that could not be detected. Spiking of purified Ara h 6 in baseline serum showed that the pre-ingestion serum of these four subjects partially prevented Ara h 6 to react in the ELISA, with a reduction of reactivity of up to 3 orders of magnitude or more. Pre-ingestion serum of the other six subjects did not show such an effect. The reduction of reactivity of Ara h 6 coincided with high titres of IgG and IgG4, and removal of IgG from pre-ingestion serum abolished this effect completely, indicating that IgG and IgG4 inhibited the reactivity of Ara h6 in the ELISA. We conclude that some individuals have IgG and IgG4 against food allergens in their blood, which interferes with detection of such food allergens in serum. Because this effect does not occur for each individual, the possibility of such interference should be taken into consideration when interpreting immunochemical studies on the absorption of food allergens in serum.
[Mh] Termos MeSH primário: Albuminas 2S de Plantas/sangue
Antígenos de Plantas/sangue
Arachis/imunologia
Ensaio de Imunoadsorção Enzimática/métodos
Imunoglobulina G/sangue
Hipersensibilidade a Amendoim/diagnóstico
[Mh] Termos MeSH secundário: Albuminas 2S de Plantas/imunologia
Anticorpos Monoclonais/imunologia
Antígenos de Plantas/imunologia
Arachis/efeitos adversos
Biomarcadores/sangue
Digestão
Epitopos
Feminino
Voluntários Saudáveis
Seres Humanos
Hidrólise
Masculino
Hipersensibilidade a Amendoim/sangue
Hipersensibilidade a Amendoim/imunologia
Valor Preditivo dos Testes
Reprodutibilidade dos Testes
Fatores de Tempo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2S Albumins, Plant); 0 (Antibodies, Monoclonal); 0 (Antigens, Plant); 0 (Ara h 6 allergen, Arachis hypogaea); 0 (Biomarkers); 0 (Epitopes); 0 (Immunoglobulin G)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161116
[St] Status:MEDLINE



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