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  1 / 2535 MEDLINE  
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[PMID]:28873661
[Au] Autor:Wang P; Zou M; Liu K; Gu Z; Yang R
[Ad] Endereço:College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: wangpei@njau.edu.cn.
[Ti] Título:Effect of mild thermal treatment on the polymerization behavior, conformation and viscoelasticity of wheat gliadin.
[So] Source:Food Chem;239:984-992, 2018 Jan 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The physicochemical properties of gliadin upon mild thermal treatment were studied in terms of polymerization behavior, conformation and viscoelasticity. Gliadin samples were heated at 40, 60 and 90°C for up to 20min. Results showed that α-gliadin started to polymerize via disulfide (SS) bonds before γ-gliadin at 90°C, resulting in the extractability loss in aqueous ethanol. ß-Turn and specific ß-sheet structures were partially conversed to α-helices during thermal treatment. Rearrangement of non-covalent forces might contribute to viscosity loss of gliadin at 40 and 60°C. However, the elevated elasticity at 90°C was mainly due to gliadin polymerization while the viscosity variation was resulted from combined effects of non-covalent forces and covalent SS bonds. This study could offer insight into the variation of gliadin characteristics during the early baking process.
[Mh] Termos MeSH primário: Triticum
[Mh] Termos MeSH secundário: Gliadina
Glutens
Polimerização
Viscosidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
8002-80-0 (Glutens); 9007-90-3 (Gliadin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE


  2 / 2535 MEDLINE  
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[PMID]:28771001
[Au] Autor:Zhou L; Kooy-Winkelaar YMC; Cordfunke RA; Dragan I; Thompson A; Drijfhout JW; van Veelen PA; Chen H; Koning F
[Ad] Endereço:State Key Laboratory of Food Science and Technology, Nanchang University , Nanchang 330047, China.
[Ti] Título:Abrogation of Immunogenic Properties of Gliadin Peptides through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor Dependent.
[So] Source:J Agric Food Chem;65(34):7542-7552, 2017 Aug 30.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Wheat gluten confers superior baking quality to wheat based products but elicits a pro-inflammatory immune response in patients with celiac disease. Transamidation of gluten by microbial transglutaminase (mTG) and tissue transglutaminase (tTG) reduces the immunogenicity of gluten; however, little information is available on the minimal modification sufficient to eliminate gliadin immunogenicity nor has the effectiveness of transamidation been studied with T-cell clones from patients. Here we demonstrate that mTG can efficiently couple three different acyl-acceptor molecules, l-lysine, glycine ethyl ester, and hydroxylamine, to gliadin peptides and protein. While all three acyl-acceptor molecules were cross-linked to the same Q-residues, not all modifications were equally effective in silencing T-cell reactivity. Finally, we observed that tTG can partially reverse the mTG-catalyzed transamidation by its isopeptidase activity. These results set the stage to determine the impact of these modifications on the baking quality of gluten proteins and in vivo immunogenicity of such food products.
[Mh] Termos MeSH primário: Gliadina/química
Gliadina/imunologia
Streptomyces/enzimologia
Transglutaminases/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Biocatálise
Glutens/química
Glutens/imunologia
Seres Humanos
Estrutura Molecular
Streptomyces/genética
Linfócitos T/imunologia
Ácido Tranexâmico/imunologia
Transglutaminases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 6T84R30KC1 (Tranexamic Acid); 8002-80-0 (Glutens); 9007-90-3 (Gliadin); EC 2.3.2.13 (Transglutaminases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02557


  3 / 2535 MEDLINE  
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[PMID]:28764003
[Au] Autor:Lexhaller B; Tompos C; Scherf KA
[Ad] Endereço:Deutsche Forschungsanstalt für Lebensmittelchemie, Leibniz Institut, Lise-Meitner-Straße 34, D-85354 Freising, Germany.
[Ti] Título:Fundamental study on reactivities of gluten protein types from wheat, rye and barley with five sandwich ELISA test kits.
[So] Source:Food Chem;237:320-330, 2017 Dec 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Monitoring the compliance of gluten-free foods to the regulatory threshold of 20mg/kg of gluten is essential for celiac disease patients. The different enzyme-linked immunosorbent assays (ELISAs) for gluten detection each have specific characteristics, but there are only a few systematic comparisons. This fundamental study compared the specificities and sensitivities of the R5, G12 and Skerritt monoclonal and two polyclonal antibodies to well-defined gluten protein types (GPT) isolated from wheat, rye and barley flours. Quantitation of protein concentrations by reversed-phase high-performance liquid chromatography provided independent reference values. The ELISA responses showed high variability depending on the type of cereal, the GPT and the antibody used. Overall, ω1,2-gliadins and γ-75k-secalins were most reactive, whereas ω5-gliadins and γ-, B- and D-hordeins were detected with the lowest sensitivities. These results revealed which GPT each antibody is most sensitive to and provided novel insights that will be helpful for appropriate calibration of ELISAs.
[Mh] Termos MeSH primário: Glutens/análise
[Mh] Termos MeSH secundário: Doença Celíaca
Ensaio de Imunoadsorção Enzimática
Gliadina
Hordeum
Seres Humanos
Secale
Triticum
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
8002-80-0 (Glutens); 9007-90-3 (Gliadin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE


  4 / 2535 MEDLINE  
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[PMID]:28759621
[Au] Autor:Röckendorf N; Meckelein B; Scherf KA; Schalk K; Koehler P; Frey A
[Ad] Endereço:Division of Mucosal Immunology & Diagnostics, Priority Area Asthma and Allergy, Research Center Borstel, Borstel, Germany.
[Ti] Título:Identification of novel antibody-reactive detection sites for comprehensive gluten monitoring.
[So] Source:PLoS One;12(7):e0181566, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Certain cereals like wheat, rye or barley contain gluten, a protein mixture that can trigger celiac disease (CD). To make gluten-free diets available for affected individuals the gluten content of foodstuff must be monitored. For this purpose, antibody-based assays exist which rely on the recognition of certain linear gluten sequence motifs. Yet, not all CD-active gluten constituents and fragments formed during food processing/fermentation may be covered by those tests. In this study, we therefore assayed the coverage of reportedly CD-active gluten components by currently available detection antibodies and determined the antibody-inducing capacity of wheat gluten constituents in order to provide novel diagnostic targets for comprehensive gluten quantitation. Immunizations of outbred mice with purified gliadins and glutenins were conducted and the linear target recognition profile of the sera was recorded using synthetic peptide arrays that covered the sequence space of gluten constituents present in those preparations. The resulting murine immunorecognition profile of gluten demonstrated that further linear binding sites beyond those recognized by the monoclonal antibodies α20, R5 and G12 exist and may be exploitable as diagnostic targets. We conclude that the safety of foodstuffs for CD patients can be further improved by complementing current tests with antibodies directed against additional CD-active gluten components. Currently unrepresented linear gluten detection sites in glutenins and α-gliadins suggest sequences QQQYPS, PQQSFP, QPGQGQQG and QQPPFS as novel targets for antibody generation.
[Mh] Termos MeSH primário: Anticorpos/química
Doença Celíaca/imunologia
Dieta Livre de Glúten
Glutens/imunologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Anticorpos Monoclonais/química
Linfócitos B/citologia
Grãos Comestíveis/química
Epitopos/química
Feminino
Gliadina/química
Glutens/química
Imunoglobulina G/química
Camundongos
Análise de Sequência com Séries de Oligonucleotídeos
Triticum/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Antibodies, Monoclonal); 0 (Epitopes); 0 (Immunoglobulin G); 8002-80-0 (Glutens); 9007-90-3 (Gliadin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181566


  5 / 2535 MEDLINE  
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[PMID]:28721717
[Au] Autor:Heil A; Ohsam J; van Genugten B; Diez O; Yokoyama K; Kumazawa Y; Pasternack R; Hils M
[Ad] Endereço:Zedira GmbH , Roesslerstraße 83, 64293 Darmstadt, Germany.
[Ti] Título:Microbial Transglutaminase Used in Bread Preparation at Standard Bakery Concentrations Does Not Increase Immunodetectable Amounts of Deamidated Gliadin.
[So] Source:J Agric Food Chem;65(32):6982-6990, 2017 Aug 16.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The effect of standard bakery concentrations of microbial transglutaminase (MTG) in wheat bread preparation on the immunoreactivity of sera of celiac disease (CD) patients was investigated. Immunoblotting using monoclonal antibodies specific to unmodified and/or deamidated gliadin showed no differences between control bread and MTG bread. Deamidation of gliadin could not be detected at standard MTG concentrations. Sera of CD patients were characterized using anti-gliadin and anti-deamidated gliadin peptide (DGP) enzyme-linked immunosorbent assay and grouped into DGP high- and low-titer pools. The recognition pattern obtained after using both CD sera pools for immunoblotting did not reveal differences between control and MTG-treated bread protein extracts. Our results indicate that MTG treatment of wheat bread prepared with typical MTG concentrations used in standard bakery processes does not lead to immunodetectable amounts of CD immunotoxic deamidated gliadins.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Pão/análise
Manipulação de Alimentos/métodos
Gliadina/imunologia
Streptomyces/enzimologia
Transglutaminases/química
Transglutaminases/imunologia
[Mh] Termos MeSH secundário: Doença Celíaca/imunologia
Ensaio de Imunoadsorção Enzimática
Gliadina/análise
Seres Humanos
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 9007-90-3 (Gliadin); EC 2.3.2.13 (Transglutaminases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170720
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02414


  6 / 2535 MEDLINE  
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[PMID]:28700675
[Au] Autor:Haupt-Jorgensen M; Nielsen E; Engkilde K; Lerche M; Larsen J; Buschard K
[Ad] Endereço:The Bartholin Institute, Rigshospitalet, Copenhagen, Denmark.
[Ti] Título:Occupation with grain crops is associated with lower type 1 diabetes incidence: Registry-based case-control study.
[So] Source:PLoS One;12(7):e0181143, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Intranasal administration of gliadin prevents autoimmune diabetes in non-obese diabetic mice. The current study was designed to investigate if bakers are intranasally exposed to gluten during work and whether occupation as baker is inversely associated with type 1 diabetes. Gliadin was measured in nasal swabs from eight bakers and butchers. The odds ratio of type 1 diabetes in selected profession groups was analysed in a registry-based case-control study with data from 1980 to 2010 derived from Statistics Denmark. The cohort included 1,210,017 Danish individuals, thereof 15,451 with type 1 diabetes (1.28%). Average nasal gliadin swab content after full working days was 6.3 µg (confidence interval (CI): 2.8 to 9.7) among bakers, while no nasal gliadin was detected among butchers. The odds ratio of type 1 diabetes was lower among bakers (OR = 0.57; CI: 0.52 to 0.62) and agriculture workers occupied with production of grains (OR = 0.65; CI: 0.56 to 0.75). Bakers had a lower odds ratio of type 1 diabetes, which potentially could be attributed to exposure of nasal mucosal gluten during work, as observed in this study. If other studies confirm the present observations, intranasal gliadin administration could possibly be an easy and safe approach for the prevention of type 1 diabetes in high-risk individuals or prediabetic subjects.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 1/epidemiologia
Grãos Comestíveis/química
Gliadina/análise
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Produtos Agrícolas
Glutens
Seres Humanos
Mucosa Nasal/metabolismo
Ocupações
Razão de Chances
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
8002-80-0 (Glutens); 9007-90-3 (Gliadin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181143


  7 / 2535 MEDLINE  
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[PMID]:28687275
[Au] Autor:Hyytinen M; Savilahti E; Virtanen SM; Härkönen T; Ilonen J; Luopajärvi K; Uibo R; Vaarala O; Åkerblom HK; Knip M; Finnish TRIGR Pilot Study Group
[Ad] Endereço:Children's Hospital, University of Helsinki and Helsinki University Hospital, Helsinki, Finland; Research Programs Unit, Diabetes and Obesity, University of Helsinki, Helsinki, Finland.
[Ti] Título:Avoidance of Cow's Milk-Based Formula for At-Risk Infants Does Not Reduce Development of Celiac Disease: A Randomized Controlled Trial.
[So] Source:Gastroenterology;153(4):961-970.e3, 2017 Oct.
[Is] ISSN:1528-0012
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND & AIMS: Feeding during the first months of life might affect risk for celiac disease. Individuals with celiac disease or type 1 diabetes have been reported to have high titers of antibodies against cow's milk proteins. Avoidance of cow's milk-based formula for infants with genetic susceptibility for type 1 diabetes reduced the cumulative incidence of diabetes-associated autoantibodies. We performed a randomized controlled trial in the same population to study whether weaning to an extensively hydrolyzed formula reduced the risk of celiac disease autoimmunity or celiac disease. METHODS: We performed a double-blind controlled trial of 230 infants with HLA-defined predisposition to type 1 diabetes and at least 1 family member with type 1 diabetes. The infants were randomly assigned to groups fed a casein hydrolysate formula (n = 113) or a conventional formula (control, n = 117) whenever breast milk was not available during the first 6-8 months of life. Serum samples were collected over a median time period of 10 years and analyzed for antibodies to tissue transglutaminase (anti-TG2A) using a radiobinding assay, to endomysium using an immunofluorescence assay, and antibodies to a deamidated gliadine peptide using an immunofluorometry assay. Duodenal biopsies were collected if levels of anti-TG2A exceeded 20 relative units. Cow's milk antibodies were measured during the first 2 years of life. RESULTS: Of the 189 participants analyzed for anti-TG2A, 25 (13.2%) tested positive. Of the 230 study participants observed, 10 (4.3%) were diagnosed with celiac disease. We did not find any significant differences at the cumulative incidence of anti-TG2A positivity (hazard ratio, 1.14; 95% confidence interval, 0.51-2.54) or celiac disease (hazard ratio, 4.13; 95% confidence interval, 0.81-21.02) between the casein hydrolysate and cow's milk groups. Children who developed celiac disease had increased titers of cow's milk antibodies before the appearance of anti-TG2A or celiac disease. CONCLUSIONS: In a randomized controlled trial of 230 infants with genetic risk factors for celiac disease, we did not find evidence that weaning to a diet of extensively hydrolyzed formula compared with cow's milk-based formula would decrease the risk for celiac disease later in life. Increased titers of cow's milk antibody before anti-TG2A and celiac disease indicates that subjects with celiac disease might have increased intestinal permeability in early life. ClinicalTrials.gov Number: NCT00570102.
[Mh] Termos MeSH primário: Autoanticorpos/sangue
Autoimunidade
Caseínas/uso terapêutico
Doença Celíaca/prevenção & controle
Diabetes Mellitus Tipo 1/imunologia
Proteínas de Ligação ao GTP/imunologia
Fórmulas Infantis/efeitos adversos
Hipersensibilidade a Leite/prevenção & controle
Proteínas do Leite/efeitos adversos
Transglutaminases/imunologia
[Mh] Termos MeSH secundário: Biópsia
Caseínas/efeitos adversos
Caseínas/imunologia
Doença Celíaca/diagnóstico
Doença Celíaca/imunologia
Criança
Pré-Escolar
Diabetes Mellitus Tipo 1/sangue
Diabetes Mellitus Tipo 1/diagnóstico
Diabetes Mellitus Tipo 1/genética
Método Duplo-Cego
Duodeno/imunologia
Duodeno/patologia
Finlândia
Gliadina/imunologia
Seres Humanos
Lactente
Hipersensibilidade a Leite/diagnóstico
Hipersensibilidade a Leite/imunologia
Proteínas do Leite/imunologia
Medição de Risco
Fatores de Risco
Testes Sorológicos
Fatores de Tempo
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Caseins); 0 (Milk Proteins); 65072-00-6 (casein hydrolysate); 9007-90-3 (Gliadin); EC 2.3.2.- (transglutaminase 2); EC 2.3.2.13 (Transglutaminases); EC 3.6.1.- (GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170709
[St] Status:MEDLINE


  8 / 2535 MEDLINE  
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[PMID]:28664699
[Au] Autor:Skoczowski A; Obtulowicz K; Czarnobilska E; Dyga W; Mazur M; Stawoska I; Waga J
[Ad] Endereço:Institute of Biology, Pedagogical University of Cracow, Kraków, Poland.
[Ti] Título:Antibody reactivity in patients with IgE-mediated wheat allergy to various subunits and fractions of gluten and non-gluten proteins from ω-gliadin-free wheat genotypes.
[So] Source:Ann Agric Environ Med;24(2):229-236, 2017 May 11.
[Is] ISSN:1898-2263
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:[b]Abstract Introduction and objective[/b]. Gluten proteins (gliadins and glutenins) are polymorphic wheat storage proteins of allergenic properties. Significant differences in chemical composition between both protein groups allow to expect highly specific immunological response of individual subunits and fractions in reactions with IgE sera of people allergic to wheat. The aim of these studies was to identify and characterize the most allergenic gluten proteins (GP) and nongluten proteins (NGP) occurred in two closely related wheat hybrid genotypes. [b]Materials and method.[/b] 3xC and 3xN wheat hybrids, which differ strongly in regard of gliadin composition, were analyzed. Seven people manifesting different symptoms of wheat allergy donated sera for the experiment. The technique of immunoblotting after SDS-PAGE was used for identification of allergenic subunits and fractions among GP and NGP. Immunologically active protein bands were visualized by chemiluminescence. [b]Results[/b]. Great variation of immunodetection spectra was observed. Results of immunoblotting showed LMW glutenins to be of highest, gliadins of medium, while NGP of lowest allergenicity for selected patients. The 43-kDa and 47-kDa LMW glutenin subunits, 40-kDa and 43-kDa γ-gliadin fractions and 49-kDa NGP can be considered as the most immunoreactive among all protein bands [b]separated by SDS-PAGE. CONCLUSION: [/b] The observed differentiation of immunodetection spectra allows to model highly specific IgE-binding profiles of allergenic wheat proteins attributed to individual patients with symptoms of gluten intolerance. Highly immunoreactive subunits and fractions among GP and NGP were identified. The observed immunoreactivity of 49 kDa NGP is worth to emphasize, as it has never been reported as wheat allergenic protein before.
[Mh] Termos MeSH primário: Gliadina/imunologia
Glutens/imunologia
Imunoglobulina E/imunologia
Triticum/genética
Triticum/imunologia
Hipersensibilidade a Trigo/imunologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Feminino
Genótipo
Gliadina/análise
Gliadina/genética
Glutens/análise
Glutens/genética
Seres Humanos
Masculino
Meia-Idade
Triticum/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
37341-29-0 (Immunoglobulin E); 8002-80-0 (Glutens); 9007-90-3 (Gliadin); FX065C7O71 (glutenin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170701
[St] Status:MEDLINE


  9 / 2535 MEDLINE  
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[PMID]:28660745
[Au] Autor:Tereshchenkova VF; Goptar IA; Zhuzhikov DP; Belozersky MA; Dunaevsky YE; Oppert B; Filippova IY; Elpidina EN
[Ad] Endereço:Chemical Faculty, Lomonosov Moscow State University, Moscow, Russia.
[Ti] Título:Prolidase is a critical enzyme for complete gliadin digestion in Tenebrio molitor larvae.
[So] Source:Arch Insect Biochem Physiol;95(4), 2017 Aug.
[Is] ISSN:1520-6327
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prolidase is a proline-specific metallopeptidase that cleaves imidodipeptides with C-terminal Pro residue. Prolidase was purified and characterized from the Tenebrio molitor larval midgut. The enzyme was localized in the soluble fraction of posterior midgut tissues, corresponding to a predicted cytoplasmic localization of prolidase according to the structure of the mRNA transcript. Expression of genes encoding prolidase and the major digestive proline-specific peptidase (PSP)-dipeptidyl peptidase 4-were similar. The pH optimum of T. molitor prolidase was 7.5, and the enzyme was inhibited by Z-Pro, indicating that it belongs to type I prolidases. In mammals, prolidase is particularly important in the catabolism of a proline-rich protein-collagen. We propose that T. molitor larval prolidase is a critical enzyme for the final stages of digestion of dietary proline-rich gliadins, providing hydrolysis of imidodipeptides in the cytoplasm of midgut epithelial cells. We propose that the products of hydrolysis are absorbed from the luminal contents by peptide transporters, which we have annotated in the T. molitor larval gut transcriptome. The origin of prolidase substrates in the insect midgut is discussed in the context of overall success of grain feeding insects.
[Mh] Termos MeSH primário: Dipeptidases/metabolismo
Gliadina/metabolismo
Proteínas de Insetos/metabolismo
Tenebrio/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Dipeptidases/antagonistas & inibidores
Dipeptidases/isolamento & purificação
Trato Gastrointestinal/enzimologia
Proteínas de Insetos/antagonistas & inibidores
Proteínas de Insetos/isolamento & purificação
Larva/enzimologia
Proteínas de Membrana Transportadoras/metabolismo
Especificidade por Substrato
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insect Proteins); 0 (Membrane Transport Proteins); 9007-90-3 (Gliadin); 97599-47-8 (peptide permease); EC 3.4.13.- (Dipeptidases); EC 3.4.13.9 (proline dipeptidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1002/arch.21395


  10 / 2535 MEDLINE  
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[PMID]:28651807
[Au] Autor:Ozuna CV; Barro F
[Ad] Endereço:Departamento de Mejora Genética, Instituto de Agricultura Sostenible (IAS), Consejo Superior de Investigaciones Científicas (CSIC), Córdoba E-14080, Spain.
[Ti] Título:Safety evaluation of transgenic low-gliadin wheat in Sprague Dawley rats: An alternative to the gluten free diet with no subchronic adverse effects.
[So] Source:Food Chem Toxicol;107(Pt A):176-185, 2017 Sep.
[Is] ISSN:1873-6351
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gluten-associated pathologies have increased in recent years and there is a greater demand for low or gluten-free products. Transgenic low-gliadin wheat lines showed low T-cell response, good bread-making properties, and excellent sensory assets. The aim of this study was to evaluate the safety of the whole-wheat flour from one transgenic low-gliadin line (named E82) in a 90-day feeding study. In this study males (n = 50) and females (n = 50) SD rats were used. They were fed with doses of 1.42, 2.83 and 5.67 g/kg/day of the transgenic E82 line, 5.67 g/kg/day of the WT and a blank group. We found that there were no significant differences in the development of animals. Biochemistry for liver and kidney function were similar for males and females of all groups. Other haematological and metabolic blood parameters, as well as organ weight did not show significant differences in the five groups of animals. In the histopathological study performed for the higher dose of transgenic E82 line, WT and blank group no abnormalities were observed. The whole-wheat flour of E82 line administered to rats at tested doses for 90 days did not have any adverse effects and there was no difference with the rats which ate WT wheat.
[Mh] Termos MeSH primário: Gliadina/análise
Plantas Geneticamente Modificadas/química
Triticum/química
[Mh] Termos MeSH secundário: Animais
Dieta Livre de Glúten
Feminino
Farinha/análise
Gliadina/genética
Gliadina/imunologia
Gliadina/metabolismo
Glutens/análise
Glutens/imunologia
Glutens/metabolismo
Masculino
Plantas Geneticamente Modificadas/genética
Plantas Geneticamente Modificadas/imunologia
Plantas Geneticamente Modificadas/metabolismo
Ratos
Ratos Sprague-Dawley
Triticum/genética
Triticum/imunologia
Triticum/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
8002-80-0 (Glutens); 9007-90-3 (Gliadin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE



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