The Experts below are selected from a list of 6123 Experts worldwide ranked by ideXlab platform
Andrew Bradbury - One of the best experts on this subject based on the ideXlab platform.
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the analysis of the fine specificity of celiac disease antibodies using tissue transglutaminase fragments
FEBS Journal, 2002Co-Authors: Daniele Sblattero, Fiorella Florian, Alessandro Ventura, Andrew Bradbury, Elisabetta Azzoni, Trevin Zyla, Min Park, V Baldas, Tarcisio NotAbstract:Celiac disease is an intestinal malabsorption characterized by an intolerance to Cereal Proteins accompanied by immunological responses to dietary gliadins and an autoantigen located in the endomysium. The latter has been identified as the enzyme tissue transglutaminase which belongs to a family of enzymes that catalyze protein cross-linking reactions and is constitutively expressed in many tissues as well as being activated during apoptosis. In a recent paper, we described the selection and characterization of anti-transglutaminase Igs from phage antibody libraries created from intestinal lymphocytes from celiac disease patients. In this work, using transglutaminase gene fragments, we identify a region of tissue transglutaminase recognized by these antibodies as being conformational and located in the core domain of the enzyme. This is identical to the region recognized by anti-transglutaminase Igs found in the serum of celiac disease patients.
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molecular dissection of the tissue transglutaminase autoantibody response in celiac disease
Journal of Immunology, 2001Co-Authors: Roberto Marzari, Daniele Sblattero, Fiorella Florian, Enrico Tongiorgi, Alberto Tommasini, Alessandro Ventura, Andrew BradburyAbstract:Celiac disease (CD) is an intestinal malabsorption characterized by intolerance to Cereal Proteins accompanied by immunological responses to dietary gliadins and tissue transglutaminase, an autoantigen located in the endomysium. Tissue transglutaminase belongs to the family of enzymes that catalyze protein cross-linking reactions and is constitutively expressed in many tissues as well as being activated during apoptosis. The role of gliadins in eliciting the immune response in CD and how transglutaminase is linked to the primary reaction are still unclear. In this work, we report the production and analysis of six phage Ab libraries from the peripheral and intestinal lymphocytes of three CD patients. We were able to isolate Abs to transglutaminase from all intestinal lymphocytes libraries but not from those obtained from peripheral lymphocytes. This is in contrast to Abs against gliadin, which could be obtained from all libraries, indicating that the humoral response against transglutaminase occurs at the local level, whereas that against gliadin occurs both peripherally and centrally. Abs from all three patients recognized the same transglutaminase epitopes with a bias toward the use of the VH5 Ab variable region family. The possible role of these anti-transglutaminase Abs in the onset of CD and associated autoimmune pathologies is discussed.
Ananda S. Prasad - One of the best experts on this subject based on the ideXlab platform.
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discovery of human zinc deficiency 50 years later
Journal of Trace Elements in Medicine and Biology, 2012Co-Authors: Ananda S. PrasadAbstract:Essentiality of zinc for humans and its deficiency was recognized in 1963. During the past 50 years, it has become apparent that deficiency of zinc in humans is prevalent. Nutritional deficiency of zinc may affect nearly 2 billion subjects in the developing world. Consumption of Cereal Proteins high in phytate decreases the availability of zinc for absorption. Conditioned deficiency of zinc is also very common. Growth retardation, hypogonadism in males, rough skin, impaired immunity, neuro-sensory disorder and cognitive impairment are some of the clinical manifestations of zinc deficiency. Zinc is involved in many biochemical functions. Over 300 enzymes require zinc for their activation and nearly 2000 transcription factors require zinc for gene expression. Zinc is essential for cell mediated immunity. Zinc is also an effective antioxidant and anti-inflammatory agent. In therapeutic dosages, zinc has been used for the treatment of acute diarrhea in infants and children, common cold, Wilson's disease, sickle cell disease and for prevention of blindness in patients with age related macular degeneration.
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discovery of human zinc deficiency and studies in an experimental human model
The American Journal of Clinical Nutrition, 1991Co-Authors: Ananda S. PrasadAbstract:The importance of zinc for human health was first documented in 1963. During the past 25 y, deficiency of zinc in humans due to nutritional factors and several disease states has now been recognized. The high phytate content of Cereal Proteins is known to decrease the availability of zincn, thus the prevalence of zinc deficiency is likely to be high in a population consuming large quantities of Cereal Proteins. Alcoholism, malabsorption, sickle cell anemia, chronic renal disease, and chronically debilitating diseases are now known to be predisposing factors for zinc deficiency. A spectrum of clinical manifestations ranging from mild to sever degree have now been recognized in human zinc-deficiency states. Zinc is required for many biological functions including DNA systhesis, cell division, and gene expression. It is required for the activity of many enzymes in bilogical systems. Recent studies indicate that zinc is needed for cell-mediated immunity
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Discovery of human zinc deficiency and studies in an experimental human model.
The American journal of clinical nutrition, 1991Co-Authors: Ananda S. PrasadAbstract:The importance of zinc for human health was first documented in 1963. During the past 25 y, deficiency of zinc in humans due to nutritional factors and several disease states has now been recognized. The high phytate content of Cereal Proteins is known to decrease the availability of zinc, thus the prevalence of zinc deficiency is likely to be high in a population consuming large quantities of Cereal Proteins. Alcoholism, malabsorption, sickle cell anemia, chronic renal disease, and chronically debilitating diseases are now known to be predisposing factors for zinc deficiency. A spectrum of clinical manifestations ranging from mild to severe degree have now been recognized in human zinc-deficiency states. Zinc is required for many biological functions including DNA synthesis, cell division, and gene expression. It is required for the activity of many enzymes in biological systems. Recent studies indicate that zinc is needed for cell-mediated immunity.
Jan A. Delcour - One of the best experts on this subject based on the ideXlab platform.
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The impact of alkaline conditions on storage Proteins of Cereals and pseudo-Cereals
Current Opinion in Food Science, 2019Co-Authors: Lomme J. Deleu, Marlies A. Lambrecht, Julie Van De Vondel, Jan A. DelcourAbstract:Alkaline conditions have different impacts on Proteins. Firstly, they can impact on the protein structure which then influences their solubility and other techno-functional properties. The former generally increases with the difference between pH and pI, and generally increases protein extraction yield. Secondly, chemical reactions can lead to negative nutritional effects by loss of essential amino acids such as lysine. Chemical reactions can also lead to additional crosslinks and to (un)desired color and flavor components. (Pseudo)Cereal Proteins are often exposed to alkaline conditions, for example, during pretzel production and extraction of rice and pseudo-Cereal protein.
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Cereal protein-based nanoparticles as agents stabilizing air–water and oil–water interfaces in food systems
Current Opinion in Food Science, 2019Co-Authors: Arno G.b. Wouters, Jan A. DelcourAbstract:There has been a recent surge of interest in the use of food-grade nanoparticles (NPs) for stabilizing food foams and emulsions. Cereal Proteins are a promising raw material class to produce such NPs. Studies thus far have focused mostly on wheat gliadin and maize zein-based NPs. The former are effective interfacial stabilizing agents, while the latter due to their high hydrophobicity generally result in poor interfacial stability. Several strategies to modify the surface properties of wheat gliadin and maize zein NPs have been followed. In many instances, this resulted in improved foam or emulsion stability. Nonetheless, future efforts should be undertaken to gain fundamental insights in the interfacial behavior of NPs, to further explore NP surface modification strategies, and to validate the use of NPs in actual food systems.
Ralf G. Berger - One of the best experts on this subject based on the ideXlab platform.
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A prolyl endopeptidase from Flammulina velutipes for the possible degradation of celiac disease provoking toxic peptides in Cereal Proteins
Process Biochemistry, 2018Co-Authors: Kathrin Schulz, Lucienne Giesler, Diana Linke, Ralf G. BergerAbstract:Abstract A prolyl endopeptidase, FvpP, was identified in the culture supernatant of the basidiomycete Flammulina velutipes and functionally expressed for gene verification in Aspergillus oryzae. The wild-type FvpP with a molecular mass of 50 kDa under denaturing conditions, exhibited optima at pH 5, and 45 °C and an isoelectric point of 3.8. Five mM Fe2+ and Fe3+ activated the prolyl endopeptidase, while it was not affected by 10 mM CaCl2, EDTA, and Pepstatin A. Five mM Cu2+, Mn2+, Zn2+, Ni2+, Co2+ and low Z-Pro-prolinal concentrations decreased the enzyme activity. Concluded from comparative RP-HPLC and high-resolution QTOF-MS/MS analyses of the hydrolytic cleavage products of gliadin, casein and gelatin, FvpP possessed a P1-P1′-substrate specificity similar to the prolyl endopeptidase from Aspergillus niger (An-Pep), although the sequence similarity was only 39%. FvpP and An-Pep (S28.004; MEROPS) are unique in the serine peptidase family S28, because they share more sequence similarity with Pro-X carboxypeptidase (S28.001; MEROPS) and dipeptidyl peptidase II (S28.002; MEROPS) than with prolyl oligopeptidases of the serine peptidase family S09. As a potential degrader of the antigenic epitopes of α-gliadin, FvpP might provide an efficient tool for the processing of wheat and other gluten containing Cereals to better digestible foods for celiac patients.
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A prolyl endopeptidase from Flammulina velutipes for the possible degradation of celiac disease provoking toxic peptides in Cereal Proteins
Process Biochemistry, 2018Co-Authors: Kathrin Schulz, Lucienne Giesler, Diana Linke, Ralf G. BergerAbstract:Abstract A prolyl endopeptidase, FvpP, was identified in the culture supernatant of the basidiomycete Flammulina velutipes and functionally expressed for gene verification in Aspergillus oryzae. The wild-type FvpP with a molecular mass of 50 kDa under denaturing conditions, exhibited optima at pH 5, and 45 °C and an isoelectric point of 3.8. Five mM Fe2+ and Fe3+ activated the prolyl endopeptidase, while it was not affected by 10 mM CaCl2, EDTA, and Pepstatin A. Five mM Cu2+, Mn2+, Zn2+, Ni2+, Co2+ and low Z-Pro-prolinal concentrations decreased the enzyme activity. Concluded from comparative RP-HPLC and high-resolution QTOF-MS/MS analyses of the hydrolytic cleavage products of gliadin, casein and gelatin, FvpP possessed a P1-P1′-substrate specificity similar to the prolyl endopeptidase from Aspergillus niger (An-Pep), although the sequence similarity was only 39%. FvpP and An-Pep (S28.004; MEROPS) are unique in the serine peptidase family S28, because they share more sequence similarity with Pro-X carboxypeptidase (S28.001; MEROPS) and dipeptidyl peptidase II (S28.002; MEROPS) than with prolyl oligopeptidases of the serine peptidase family S09. As a potential degrader of the antigenic epitopes of α-gliadin, FvpP might provide an efficient tool for the processing of wheat and other gluten containing Cereals to better digestible foods for celiac patients.
Daniele Sblattero - One of the best experts on this subject based on the ideXlab platform.
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the analysis of the fine specificity of celiac disease antibodies using tissue transglutaminase fragments
FEBS Journal, 2002Co-Authors: Daniele Sblattero, Fiorella Florian, Alessandro Ventura, Andrew Bradbury, Elisabetta Azzoni, Trevin Zyla, Min Park, V Baldas, Tarcisio NotAbstract:Celiac disease is an intestinal malabsorption characterized by an intolerance to Cereal Proteins accompanied by immunological responses to dietary gliadins and an autoantigen located in the endomysium. The latter has been identified as the enzyme tissue transglutaminase which belongs to a family of enzymes that catalyze protein cross-linking reactions and is constitutively expressed in many tissues as well as being activated during apoptosis. In a recent paper, we described the selection and characterization of anti-transglutaminase Igs from phage antibody libraries created from intestinal lymphocytes from celiac disease patients. In this work, using transglutaminase gene fragments, we identify a region of tissue transglutaminase recognized by these antibodies as being conformational and located in the core domain of the enzyme. This is identical to the region recognized by anti-transglutaminase Igs found in the serum of celiac disease patients.
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molecular dissection of the tissue transglutaminase autoantibody response in celiac disease
Journal of Immunology, 2001Co-Authors: Roberto Marzari, Daniele Sblattero, Fiorella Florian, Enrico Tongiorgi, Alberto Tommasini, Alessandro Ventura, Andrew BradburyAbstract:Celiac disease (CD) is an intestinal malabsorption characterized by intolerance to Cereal Proteins accompanied by immunological responses to dietary gliadins and tissue transglutaminase, an autoantigen located in the endomysium. Tissue transglutaminase belongs to the family of enzymes that catalyze protein cross-linking reactions and is constitutively expressed in many tissues as well as being activated during apoptosis. The role of gliadins in eliciting the immune response in CD and how transglutaminase is linked to the primary reaction are still unclear. In this work, we report the production and analysis of six phage Ab libraries from the peripheral and intestinal lymphocytes of three CD patients. We were able to isolate Abs to transglutaminase from all intestinal lymphocytes libraries but not from those obtained from peripheral lymphocytes. This is in contrast to Abs against gliadin, which could be obtained from all libraries, indicating that the humoral response against transglutaminase occurs at the local level, whereas that against gliadin occurs both peripherally and centrally. Abs from all three patients recognized the same transglutaminase epitopes with a bias toward the use of the VH5 Ab variable region family. The possible role of these anti-transglutaminase Abs in the onset of CD and associated autoimmune pathologies is discussed.