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[PMID]:28551252
[Au] Autor:Colgrave ML; Byrne K; Howitt CA
[Ad] Endereço:CSIRO Agriculture and Food, 306 Carmody Rd, St Lucia, QLD 4067, Australia. Electronic address: michelle.colgrave@csiro.au.
[Ti] Título:Food for thought: Selecting the right enzyme for the digestion of gluten.
[So] Source:Food Chem;234:389-397, 2017 Nov 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gluten describes a complex mixture of proteins found in wheat, rye, barley and oats that pose a health risk to people affected by conditions such as coeliac disease and non-coeliac gluten sensitivity. Complete digestion of gluten proteins is of critical importance during quantitative analysis. To this end, chymotrypsin was investigated for its ability to efficiently and reproducibly digest specific classes of gluten in barley. Using proteomics a chymotryptic peptide marker panel was elucidated and subjected to relative quantification using LC-MRM-MS. Thorough investigation of peptide markers revealed robust and reproducible quantification with CVs <15% was possible, however a greater proportion of non-specific cleavage variants were observed relative to trypsin. The selected peptide markers were assessed to ensure their efficient liberation from their parent proteins. While trypsin remains the preferred enzyme for quantification of the avenin-like A proteins, the B-, D- and γ-hordeins, chymotrypsin was the enzyme of choice for the C-hordeins.
[Mh] Termos MeSH primário: Quimotripsina/química
Glutens/química
Hordeum/química
Tripsina/química
[Mh] Termos MeSH secundário: Cromatografia Líquida
Espectrometria de Massas
Prolaminas/química
Proteômica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prolamins); 8002-80-0 (Glutens); EC 3.4.21.1 (Chymotrypsin); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE


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[PMID]:28141922
[Au] Autor:Benoit L; Masiri J; Del Blanco IA; Meshgi M; Gendel SM; Samadpour M
[Ad] Endereço:IEH Laboratories and Consulting Group, Inc. (IEH) , 15300 Bothell Way N.E., Lake Forest Park, Washington 98155, United States.
[Ti] Título:Assessment of Avenins from Different Oat Varieties Using R5-Based Sandwich ELISA.
[So] Source:J Agric Food Chem;65(8):1467-1472, 2017 Mar 01.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gluten derived from wheat and related triticeae cereals possesses distinct amino acid sequences that provoke the immunopathogenic features of celiac disease (CD) in genetically susceptible individuals. However, the role of oat-derived gluten, or avenins, in CD pathogenesis remains a disputed matter, as evidenced by a lack in harmonized legislation regarding gluten classification in relation to gluten-free labeling. In this study, we have analyzed a panel of pure oat cultivars using a sandwich ELISA based on the R5 monoclonal antibody (mAb), which binds to canonical epitopes occurring within celiagenic peptides present in triticeae-derived gluten but reportedly not present in avenins. We have identified three varieties of oats that reproducibly bind R5 antibodies and levels indicating the presence of gluten at more than the 20 ppm gluten regulatory threshold. Nested assessment using Western blot analysis and alternative gluten detection systems corroborated these results. Collectively, these data suggest that select oat varieties may prove problematic to patients with CD and to food companies and regulatory agencies and will extend our basic understanding of current gluten detection systems.
[Mh] Termos MeSH primário: Avena/química
Ensaio de Imunoadsorção Enzimática/métodos
Prolaminas/análise
[Mh] Termos MeSH secundário: Avena/classificação
Western Blotting
Glutens/análise
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prolamins); 8002-80-0 (Glutens)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170530
[Lr] Data última revisão:
170530
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.6b05105


  3 / 294 MEDLINE  
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[PMID]:28028608
[Au] Autor:Sasou A; Shigemitsu T; Morita S; Masumura T
[Ad] Endereço:Laboratory of Genetic Engineering, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, Shimogamo, Kyoto, 606-8522, Japan.
[Ti] Título:Accumulation of foreign polypeptides to rice seed protein body type I using prolamin portion sequences.
[So] Source:Plant Cell Rep;36(3):481-491, 2017 Mar.
[Is] ISSN:1432-203X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: Rice prolamins are accumulated in endoplasmic reticulum (ER)-derived proteins bodies, although conserved sequences retained in ER are not confirmed. We investigated portion sequences of prolamins that must accumulate in PB-Is. Rice seed prolamins are accumulated in endoplasmic reticulum (ER)-derived protein body type I (PB-I), but ER retention sequences in rice prolamin polypeptides have not been confirmed. Here we investigated the lengths of the prolamin portion sequences required for accumulation in PB-Is. Of the rice prolamins, we compared 13a and 13b prolamins because the amino acid sequences of these prolamins are quite similar except for the presence or absence of Cys-residues. We also generated and analyzed transgenic rice expressing several prolamin portion sequence-GFP fusion proteins. We observed that in 13a prolamin, when the portion sequences were extended more than the 68th amino acid residue from the initiating methionine, the prolamin portion sequence-GFP fusion proteins were accumulated in PB-Is. In 13b prolamin, when the portion sequences were extended by more than the 82nd amino acid residue from the initiating methionine, the prolamin portion sequence-GFP fusion proteins were accumulated in PB-Is. When those fusion proteins were extracted under non-reduced or reduced conditions, the 13a prolamin portion sequence-GFP fusion proteins in PB-Is were soluble under only the reduced condition. In contrast, 13b prolamin portion sequence-GFP fusion proteins were soluble under both non-reduced and reduced conditions. These results suggest that the accumulation of 13a prolamin in PB-Is is associated with the formation of disulfide bonds and/or hydrophobicity in 13a prolamin polypeptide, whereas the accumulation of 13b prolamin in PB-Is was less involved in the formation of disulfide bonds.
[Mh] Termos MeSH primário: Oryza/metabolismo
Peptídeos/metabolismo
Prolaminas/química
Prolaminas/metabolismo
Sementes/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Tampões (Química)
Proteínas de Fluorescência Verde/metabolismo
Interações Hidrofóbicas e Hidrofílicas
Peptídeos/química
Plantas Geneticamente Modificadas
Proteínas Recombinantes de Fusão/metabolismo
Sementes/genética
Dodecilsulfato de Sódio/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Buffers); 0 (Peptides); 0 (Prolamins); 0 (Recombinant Fusion Proteins); 147336-22-9 (Green Fluorescent Proteins); 368GB5141J (Sodium Dodecyl Sulfate)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170327
[Lr] Data última revisão:
170327
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161229
[St] Status:MEDLINE
[do] DOI:10.1007/s00299-016-2097-5


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[PMID]:28071042
[Au] Autor:Mickowska B; Litwinek D; Gambus H
[Ad] Endereço:Malopolska Centre of Food Monitoring, University of Agriculture in Krakow, Poland.
[Ti] Título:Oat raw materials and bakery products - amino acid composition and celiac immunoreactivity.
[So] Source:Acta Sci Pol Technol Aliment;15(1):89-97, 2016 Jan-Mar.
[Is] ISSN:1898-9594
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The aim of this study was to compare the biochemical and immunochemical properties of avenins in some special oat raw materials and additionally the possibility of using them as a raw material for the gluten-free bakery products. METHODS: The compared oat raw materials were - oat flakes, commercial oat flours (including gluten-free oat flour) and residual oat flour, which is by-product of ß-glucan preparation. Biochemical characteristic included amino acid compositions and SDS-PAGE profiles of extracted avenins. The immunochemical reactivity with polyclonal anti-gluten and monoclonal anti-gliadin antibodies was evaluated qualitatively and quantitatively by immunoblotting and ELISA methods. Additionally, experimental bakery products made of examined raw materials were assessed according to their suitability for the celiac patients' diet. RESULTS: The highest protein content was measured in the ß-glucan preparation "Betaven" and gluten-free oat flour. Proteins of all materials are rich in glutamic and aspartic acid, leucine and arginine. Proportions of amino acids in avenins extracted from most of oat raw materials are similar, excluding gluten-free oat flour, which has a very low avenin content and proportions of individual amino acids are different. The SDS-PAGE protein pattern consisted of proteins with molecular weight of about 25-35 kDa. Polyclonal anti-gluten anti-body recognized all protein fractions of molecular weight higher than 20 kDa. Quantitative ELISA analysis shows that the majority of samples has a gliadin-like protein content within the range of 80-260 mg/kg, excluding gluten-free flours and corresponding bakery products. Altogether, ß-glucan preparation has extremely high level of gliadin-like proteins. CONCLUSIONS: In the examined oat raw materials and foods the contents of immunoreactive amino acid sequences exceeded the limit of 20 mg/kg (considered as gluten-free) except for gluten-free flours (oat and  the prepared mixture) and the bakery products based on gluten-free flours. Unfortunately, the rest of oat raw materials and products cannot be considered gluten-free.
[Mh] Termos MeSH primário: Aminoácidos/análise
Avena/química
Pão/análise
Dieta Livre de Glúten
Farinha/análise
Prolaminas/análise
Sementes/química
[Mh] Termos MeSH secundário: Avena/efeitos adversos
Western Blotting
Pão/efeitos adversos
Pão/economia
Doença Celíaca/dietoterapia
Doença Celíaca/imunologia
Reações Cruzadas
Eletroforese em Gel de Poliacrilamida
Ensaio de Imunoadsorção Enzimática
Farinha/efeitos adversos
Farinha/economia
Indústria de Processamento de Alimentos/economia
Gliadina/efeitos adversos
Gliadina/análise
Gliadina/antagonistas & inibidores
Gliadina/química
Seres Humanos
Resíduos Industriais/análise
Resíduos Industriais/economia
Peso Molecular
Valor Nutritivo
Polônia
Prolaminas/efeitos adversos
Prolaminas/antagonistas & inibidores
Prolaminas/química
Sementes/efeitos adversos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Industrial Waste); 0 (Prolamins); 9007-90-3 (Gliadin)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170118
[Lr] Data última revisão:
170118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170111
[St] Status:MEDLINE
[do] DOI:10.17306/J.AFS.2016.1.9


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[PMID]:27580728
[Au] Autor:Takaiwa F; Yang L; Maruyama N; Wakasa Y; Ozawa K
[Ad] Endereço:Institute of Agrobiological Sciences, National Agriculture and Food Research Organization, Kannondai 2-1-2, Tsukuba, Ibaraki, 305-8602, Japan. takaiwa@affrc.go.jp.
[Ti] Título:Deposition mode of transforming growth factor-ß expressed in transgenic rice seed.
[So] Source:Plant Cell Rep;35(12):2461-2473, 2016 Dec.
[Is] ISSN:1432-203X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: Mouse TGF-ß highly accumulated by expressing as a secretory homodimeric protein in transgenic rice endosperm. It was tightly deposited in ER-derived PBs by interaction with cysteine-rich prolamins. TGF-ß is one of the key players involved in the induction and maintenance of mucosal immune tolerance to dietary proteins through the induction of regulatory T cells. In order to utilize rice-based TGF-ß as a tool to promote oral immune tolerance induction, high production of TGF-ß is essentially required. When the codon-optimized mTGF-ß was expressed as a secretory protein by ligating an N-terminal signal peptide and C-terminal KDEL ER retention signal under the control of the endosperm-specific rice storage protein glutelin GluB-1 promoter, accumulation level was low in stable transgenic rice seeds. Then, to increase the accumulation level of mTGF-ß, it was expressed as fusion proteins by inserting into the C terminus of acidic subunit of glutelin GluA and the variable region of 26 kDa globulin. When fused with the glutelin, it could accumulate well as visible bands by CBB staining gel, but not for the 26 kDa globulin. Unexpectedly, expression of homodimeric mTGF-ß linked by a 6×Gly1×Ser linker as secretory protein resulted in higher level of accumulation. This expression level was further enhanced by reduction of some endogenous prolamins by RNA interference. The monomeric and dimeric mTGF-ßs were deposited in ER-derived PBs containing prolamins. When highly produced in rice seed, it is notable that most of ER-derived PBs were distorted and granulated. Step-wise extraction of storage proteins from rice seeds suggested that the mTGF-ß strongly interacted with cysteine-rich prolamins via disulfide bonds. This result was also supported by the finding that reducing agent was absolutely required for mTGF-ß extraction.
[Mh] Termos MeSH primário: Oryza/genética
Sementes/genética
Fator de Crescimento Transformador beta/metabolismo
[Mh] Termos MeSH secundário: Animais
Cisteína/metabolismo
Endosperma/citologia
Endosperma/metabolismo
Endosperma/ultraestrutura
Regulação da Expressão Gênica de Plantas
Espaço Intracelular/metabolismo
Camundongos
Oryza/citologia
Oryza/ultraestrutura
Pepsina A/metabolismo
Plantas Geneticamente Modificadas
Prolaminas/química
Prolaminas/metabolismo
Multimerização Proteica
Proteínas Recombinantes/metabolismo
Sementes/citologia
Sementes/ultraestrutura
Resposta a Proteínas não Dobradas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prolamins); 0 (Recombinant Proteins); 0 (Transforming Growth Factor beta); EC 3.4.23.1 (Pepsin A); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160902
[St] Status:MEDLINE


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[PMID]:27228577
[Au] Autor:Dong L; Huo N; Wang Y; Deal K; Wang D; Hu T; Dvorak J; Anderson OD; Luo MC; Gu YQ
[Ad] Endereço:United States Department of Agriculture-Agricultural Research Service, Western Regional Research Center, Albany, CA, 94710, USA.
[Ti] Título:Rapid evolutionary dynamics in a 2.8-Mb chromosomal region containing multiple prolamin and resistance gene families in Aegilops tauschii.
[So] Source:Plant J;87(5):495-506, 2016 Sep.
[Is] ISSN:1365-313X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Prolamin and resistance gene families are important in wheat food use and in defense against pathogen attacks, respectively. To better understand the evolution of these multi-gene families, the DNA sequence of a 2.8-Mb genomic region, representing an 8.8 cM genetic interval and harboring multiple prolamin and resistance-like gene families, was analyzed in the diploid grass Aegilops tauschii, the D-genome donor of bread wheat. Comparison with orthologous regions from rice, Brachypodium, and sorghum showed that the Ae. tauschii region has undergone dramatic changes; it has acquired more than 80 non-syntenic genes and only 13 ancestral genes are shared among these grass species. These non-syntenic genes, including prolamin and resistance-like genes, originated from various genomic regions and likely moved to their present locations via sequence evolution processes involving gene duplication and translocation. Local duplication of non-syntenic genes contributed significantly to the expansion of gene families. Our analysis indicates that the insertion of prolamin-related genes occurred prior to the separation of the Brachypodieae and Triticeae lineages. Unlike in Brachypodium, inserted prolamin genes have rapidly evolved and expanded to encode different classes of major seed storage proteins in Triticeae species. Phylogenetic analyses also showed that the multiple insertions of resistance-like genes and subsequent differential expansion of each R gene family. The high frequency of non-syntenic genes and rapid local gene evolution correlate with the high recombination rate in the 2.8-Mb region with nine-fold higher than the genome-wide average. Our results demonstrate complex evolutionary dynamics in this agronomically important region of Triticeae species.
[Mh] Termos MeSH primário: Cromossomos de Plantas/genética
Prolaminas/metabolismo
Triticum/genética
[Mh] Termos MeSH secundário: Evolução Molecular
Duplicação Gênica/genética
Genes de Plantas/genética
Genoma de Planta/genética
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prolamins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160527
[St] Status:MEDLINE
[do] DOI:10.1111/tpj.13214


  7 / 294 MEDLINE  
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[PMID]:27190000
[Au] Autor:Zhang W; Xu J; Bennetzen JL; Messing J
[Ad] Endereço:Waksman Institute of Microbiology, Rutgers University.
[Ti] Título:Teff, an Orphan Cereal in the Chloridoideae, Provides Insights into the Evolution of Storage Proteins in Grasses.
[So] Source:Genome Biol Evol;8(6):1712-21, 2016 06 13.
[Is] ISSN:1759-6653
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Seed storage proteins (SSP) in cereals provide essential nutrition for humans and animals. Genes encoding these proteins have undergone rapid evolution in different grass species. To better understand the degree of divergence, we analyzed this gene family in the subfamily Chloridoideae, where the genome of teff (Eragrostis tef) has been sequenced. We find gene duplications, deletions, and rapid mutations in protein-coding sequences. The main SSPs in teff, like other grasses, are prolamins, here called eragrostins. Teff has γ- and δ-prolamins, but has no ß-prolamins. One δ-type prolamin (δ1) in teff has higher methionine (33%) levels than in maize (23-25%). The other δ-type prolamin (δ2) has reduced methionine residues (<10%) and is phylogenetically closer to α prolamins. Prolamin δ2 in teff represents an intermediate between δ and α types that appears to have been lost in maize and other Panicoideae, and was replaced by the expansion of α-prolamins. Teff also has considerably larger numbers of α-prolamin genes, which we further divide into five sub-groups, where α2 and α5 represent the most abundant α-prolamins both in number and in expression. In addition, indolines that determine kernel softness are present in teff and the panicoid cereal called foxtail millet (Setaria italica) but not in sorghum or maize, indicating that these genes were only recently lost in some members of the Panicoideae Moreover, this study provides not only information on the evolution of SSPs in the grass family but also the importance of α-globulins in protein aggregation and germplasm divergence.
[Mh] Termos MeSH primário: Eragrostis/genética
Evolução Molecular
Prolaminas/genética
Proteínas de Armazenamento de Sementes/genética
[Mh] Termos MeSH secundário: Grãos Comestíveis/genética
Deleção de Genes
Duplicação Gênica/genética
Genoma de Planta
Mutação
Filogenia
Sorghum/genética
Zea mays/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prolamins); 0 (Seed Storage Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160519
[St] Status:MEDLINE
[do] DOI:10.1093/gbe/evw117


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[PMID]:27006211
[Au] Autor:Moreno Mde L; Muñoz-Suano A; López-Casado MÁ; Torres MI; Sousa C; Cebolla Á
[Ad] Endereço:Departamento de Microbiología y Parasitología, Facultad de Farmacia, Universidad de Seville, C/ Profesor García González S/N, 41012 Seville, Spain. Electronic address: lmoreno@us.es.
[Ti] Título:Selective capture of most celiac immunogenic peptides from hydrolyzed gluten proteins.
[So] Source:Food Chem;205:36-42, 2016 Aug 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The available immunomethods for gluten quantitation could underestimate or overestimate the net immunoactivity of foods and beverages if the chosen analytical antibody is not specific to the relevant gluten immunogenic peptides (GIP). Accurate detection of the most active GIP is desirable to assess the potential celiac toxicity of food. We evaluated the capacity of the G12 monoclonal antibody for selectively depleting GIP in samples from two different gluteomes. Samples of hydrolyzed gliadin from wheat and a barley beer were used. The input (starting peptide digest of prolamins), the flow-through (unbound peptides), and the output (captured peptides) were analyzed by G12 and R5 competitive ELISA as well as by stimulation assays of T-cells from celiac patients. Most of the GIP were retained by the G12-agarose and represented the largest part of the immunogenicity of the gluten peptidome. G12 immunodepletion experiments with hydrolyzed gluten showed that this antibody reacted with those with the highest immunoactivity for celiac patients.
[Mh] Termos MeSH primário: Antígenos/análise
Doença Celíaca/imunologia
Glutens/imunologia
Peptídeos/análise
Peptídeos/imunologia
[Mh] Termos MeSH secundário: Anticorpos Monoclonais/imunologia
Cerveja/análise
Ensaio de Imunoadsorção Enzimática/métodos
Alimentos
Gliadina/química
Gliadina/metabolismo
Glutens/metabolismo
Hordeum/química
Seres Humanos
Hidrólise
Prolaminas/metabolismo
Triticum/química
Triticum/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antigens); 0 (Peptides); 0 (Prolamins); 8002-80-0 (Glutens); 9007-90-3 (Gliadin)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160324
[St] Status:MEDLINE


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[PMID]:26507269
[Au] Autor:Sikdar MS; Bowra S; Schmidt D; Dionisio G; Holm PB; Vincze E
[Ad] Endereço:Science and Technology, Department of Molecular Biology and Genetics, Research Centre Flakkebjerg, Aarhus University, 4200, Slagelse, Denmark.
[Ti] Título:Targeted modification of storage protein content resulting in improved amino acid composition of barley grain.
[So] Source:Transgenic Res;25(1):19-31, 2016 Feb.
[Is] ISSN:1573-9368
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:C-hordein in barley and ω-gliadins in wheat are members of the prolamins protein families. Prolamins are the major component of cereal storage proteins and composed of non-essential amino acids (AA) such as proline and glutamine therefore have low nutritional value. Using double stranded RNAi silencing technology directed towards C-hordein we obtained transgenic barley lines with up to 94.7% reduction in the levels of C-hordein protein relative to the parental line. The composition of the prolamin fraction of the barley parental line cv. Golden Promise was resolved using SDS-PAGE electrophoresis, the protein band were excised and the proteins identified by quadrupole-time-of-flight mass spectrometry. Subsequent SDS-PAGE separation and analysis of the prolamin fraction of the transgenic lines revealed a reduction in the amounts of C-hordeins and increases in the content of other hordein family members. Analysis of the AA composition of the transgenic lines showed that the level of essential amino acids increased with a concomitant reduction in proline and glutamine. Both the barley C-hordein and wheat ω-gliadin genes proved successful for RNAi-gene mediated suppression of barley C-hordein level. All transgenic lines that exhibited a reduction for C-hordein showed off-target effects: the lines exhibited increased level of B/γ-hordein while D-hordein level was reduced. Furthermore, the multicopy insertions correlated negatively with silencing.
[Mh] Termos MeSH primário: Aminoácidos/química
Glutens/genética
Hordeum/química
Hordeum/genética
Sementes/química
[Mh] Termos MeSH secundário: Aminoácidos/genética
Eletroforese em Gel de Poliacrilamida
Gliadina/genética
Glutens/metabolismo
Plantas Geneticamente Modificadas
Prolaminas/análise
Prolaminas/genética
Prolaminas/metabolismo
Interferência de RNA
Sementes/genética
Espectrometria de Massas em Tandem/métodos
Triticum/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Prolamins); 8002-80-0 (Glutens); 9007-90-3 (Gliadin)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151029
[St] Status:MEDLINE
[do] DOI:10.1007/s11248-015-9911-7


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[PMID]:26300126
[Au] Autor:Barro F; Iehisa JC; Giménez MJ; García-Molina MD; Ozuna CV; Comino I; Sousa C; Gil-Humanes J
[Ad] Endereço:Departamento de Mejora Genética, Instituto de Agricultura Sostenible (IAS), Consejo Superior de Investigaciones Científicas (CSIC), Córdoba, Spain.
[Ti] Título:Targeting of prolamins by RNAi in bread wheat: effectiveness of seven silencing-fragment combinations for obtaining lines devoid of coeliac disease epitopes from highly immunogenic gliadins.
[So] Source:Plant Biotechnol J;14(3):986-96, 2016 Mar.
[Is] ISSN:1467-7652
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gluten proteins are responsible for the viscoelastic properties of wheat flour but also for triggering pathologies in susceptible individuals, of which coeliac disease (CD) and noncoeliac gluten sensitivity may affect up to 8% of the population. The only effective treatment for affected persons is a strict gluten-free diet. Here, we report the effectiveness of seven plasmid combinations, encompassing RNAi fragments from α-, γ-, ω-gliadins, and LMW glutenin subunits, for silencing the expression of different prolamin fractions. Silencing patterns of transgenic lines were analysed by gel electrophoresis, RP-HPLC and mass spectrometry (LC-MS/MS), whereas gluten immunogenicity was assayed by an anti-gliadin 33-mer monoclonal antibody (moAb). Plasmid combinations 1 and 2 downregulated only γ- and α-gliadins, respectively. Four plasmid combinations were highly effective in the silencing of ω-gliadins and γ-gliadins, and three of these also silenced α-gliadins. HMW glutenins were upregulated in all but one plasmid combination, while LMW glutenins were downregulated in three plasmid combinations. Total protein and starch contents were unaffected regardless of the plasmid combination used. Six plasmid combinations provided strong reduction in the gluten content as measured by moAb and for two combinations, this reduction was higher than 90% in comparison with the wild type. CD epitope analysis in peptides identified in LC-MS/MS showed that lines from three plasmid combinations were totally devoid of CD epitopes from the highly immunogenic α- and ω-gliadins. Our findings raise the prospect of breeding wheat species with low levels of harmful gluten, and of achieving the important goal of developing nontoxic wheat cultivars.
[Mh] Termos MeSH primário: Pão
Doença Celíaca/imunologia
Epitopos/imunologia
Gliadina/imunologia
Prolaminas/metabolismo
Interferência de RNA
Triticum/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Anticorpos Monoclonais/imunologia
Cromatografia Líquida
Epitopos/química
Peptídeos/química
Peptídeos/imunologia
Plantas Geneticamente Modificadas
Plasmídeos/metabolismo
Característica Quantitativa Herdável
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Epitopes); 0 (Peptides); 0 (Prolamins); 9007-90-3 (Gliadin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150825
[St] Status:MEDLINE
[do] DOI:10.1111/pbi.12455



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