The Experts below are selected from a list of 207 Experts worldwide ranked by ideXlab platform
Miklós Sahin-tóth - One of the best experts on this subject based on the ideXlab platform.
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Detection of human Elastase isoforms by the ScheBo Pancreatic Elastase 1 Test
American Journal of Physiology-gastrointestinal and Liver Physiology, 2017Co-Authors: Anna Zsófia Tóth, Eszter Hegyi, Peter Hegyi, András Szabó, Miklós Sahin-tóthAbstract:The ScheBo Pancreatic Elastase 1 stool test is widely used to assess Pancreatic exocrine function, yet its molecular targets have been poorly defined. We demonstrate that, among the human Pancreatic proteinases, the test measures the Elastase isoform chymotrypsin-like Elastase (CELA) 3B (CELA3B) and, to a lesser extent, CELA3A. Genetic variants of the human CELA3 isoforms have no significant effect on test performance.
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Detection of human Elastase isoforms by the ScheBo Pancreatic Elastase 1 Test
American journal of physiology. Gastrointestinal and liver physiology, 2017Co-Authors: Anna Zsófia Tóth, Eszter Hegyi, Peter Hegyi, András Szabó, Miklós Sahin-tóthAbstract:The ScheBo Pancreatic Elastase 1 stool test is widely used to assess Pancreatic exocrine function, yet its molecular targets have been poorly defined. We demonstrate that, among the human pancreati...
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Detection of human Elastase isoforms by the ScheBo Pancreatic Elastase 1 Test
American Journal of Physiology-gastrointestinal and Liver Physiology, 2017Co-Authors: Anna Zsófia Tóth, Eszter Hegyi, Peter Hegyi, András Szabó, Miklós Sahin-tóthAbstract:The ScheBo Pancreatic Elastase 1 stool test is widely used to assess Pancreatic exocrine function, yet its molecular targets have been poorly defined. We demonstrate that, among the human Pancreatic proteinases, the test measures the Elastase isoform chymotrypsin-like Elastase (CELA) 3B (CELA3B) and, to a lesser extent, CELA3A. Genetic variants of the human CELA3 isoforms have no significant effect on test performance.
Victor De Freitas - One of the best experts on this subject based on the ideXlab platform.
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Inhibition of Pancreatic Elastase by polyphenolic compounds.
Journal of Agricultural and Food Chemistry, 2010Co-Authors: Natércia F. Brás, Rui Gonçalves, Pedro A. Fernandes, Maria J. Ramos, Nuno Mateus, Victor De FreitasAbstract:Polyphenols are plant secondary metabolites commonly present in the human diet that possess the ability to bind and inhibit digestive proteins. In the present study, kinetic measurements of porcine Pancreatic Elastase (PPE) activity were determined using Suc-(Ala)3-p-nitroanilide as substrate and polyphenolic compounds as inhibitors. A positive relationship between the degree of polyphenol polymerization and the capacity of the polyphenols to inhibit PPE was observed. Procyanidins with a molecular weight of at least 1154 Da were necessary to observe a significant inhibitory ability. Kinetic parameters were also calculated and confirmed that the inhibition is reversible and competitive. Molecular docking and dynamics simulations demonstrated that the tetramer structure has a higher affinity to the enzyme due the establishment of more contact points with the amino acids present in its active site. Hydrogen bond interactions and hydrophobic effects established between the polyphenol groups and the side chain...
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Inhibition of Pancreatic Elastase by polyphenolic compounds.
Journal of Agricultural and Food Chemistry, 2010Co-Authors: Natércia F. Brás, Rui Gonçalves, Pedro A. Fernandes, Maria J. Ramos, Nuno Mateus, Victor De FreitasAbstract:Polyphenols are plant secondary metabolites commonly present in the human diet that possess the ability to bind and inhibit digestive proteins. In the present study, kinetic measurements of porcine Pancreatic Elastase (PPE) activity were determined using Suc-(Ala)3-p-nitroanilide as substrate and polyphenolic compounds as inhibitors. A positive relationship between the degree of polyphenol polymerization and the capacity of the polyphenols to inhibit PPE was observed. Procyanidins with a molecular weight of at least 1154 Da were necessary to observe a significant inhibitory ability. Kinetic parameters were also calculated and confirmed that the inhibition is reversible and competitive. Molecular docking and dynamics simulations demonstrated that the tetramer structure has a higher affinity to the enzyme due the establishment of more contact points with the amino acids present in its active site. Hydrogen bond interactions and hydrophobic effects established between the polyphenol groups and the side chain...
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Inhibition of Pancreatic Elastase by Polyphenolic Compounds
Journal of agricultural and food chemistry, 2010Co-Authors: Natércia F. Brás, Rui Gonçalves, Pedro A. Fernandes, Maria J. Ramos, Nuno Mateus, Victor De FreitasAbstract:Polyphenols are plant secondary metabolites commonly present in the human diet that possess the ability to bind and inhibit digestive proteins. In the present study, kinetic measurements of porcine Pancreatic Elastase (PPE) activity were determined using Suc-(Ala)(3)-p-nitroanilide as substrate and polyphenolic compounds as inhibitors. A positive relationship between the degree of polyphenol polymerization and the capacity of the polyphenols to inhibit PPE was observed. Procyanidins with a molecular weight of at least 1154 Da were necessary to observe a significant inhibitory ability. Kinetic parameters were also calculated and confirmed that the inhibition is reversible and competitive. Molecular docking and dynamics simulations demonstrated that the tetramer structure has a higher affinity to the enzyme due the establishment of more contact points with the amino acids present in its active site. Hydrogen bond interactions and hydrophobic effects established between the polyphenol groups and the side chain of residues stabilize and favor the binding mode of this procyanidin. This work is relevant to the study of the antinutritional effects caused by dietary tannins on the digestive enzymes' activity, reducing food digestibility and the absorption of nutrients. In general, the Elastase model studied herein allows a better understanding of the inhibitory ability of polyphenol compounds.
Anna Zsófia Tóth - One of the best experts on this subject based on the ideXlab platform.
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Detection of human Elastase isoforms by the ScheBo Pancreatic Elastase 1 Test
American Journal of Physiology-gastrointestinal and Liver Physiology, 2017Co-Authors: Anna Zsófia Tóth, Eszter Hegyi, Peter Hegyi, András Szabó, Miklós Sahin-tóthAbstract:The ScheBo Pancreatic Elastase 1 stool test is widely used to assess Pancreatic exocrine function, yet its molecular targets have been poorly defined. We demonstrate that, among the human Pancreatic proteinases, the test measures the Elastase isoform chymotrypsin-like Elastase (CELA) 3B (CELA3B) and, to a lesser extent, CELA3A. Genetic variants of the human CELA3 isoforms have no significant effect on test performance.
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Detection of human Elastase isoforms by the ScheBo Pancreatic Elastase 1 Test
American journal of physiology. Gastrointestinal and liver physiology, 2017Co-Authors: Anna Zsófia Tóth, Eszter Hegyi, Peter Hegyi, András Szabó, Miklós Sahin-tóthAbstract:The ScheBo Pancreatic Elastase 1 stool test is widely used to assess Pancreatic exocrine function, yet its molecular targets have been poorly defined. We demonstrate that, among the human pancreati...
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Detection of human Elastase isoforms by the ScheBo Pancreatic Elastase 1 Test
American Journal of Physiology-gastrointestinal and Liver Physiology, 2017Co-Authors: Anna Zsófia Tóth, Eszter Hegyi, Peter Hegyi, András Szabó, Miklós Sahin-tóthAbstract:The ScheBo Pancreatic Elastase 1 stool test is widely used to assess Pancreatic exocrine function, yet its molecular targets have been poorly defined. We demonstrate that, among the human Pancreatic proteinases, the test measures the Elastase isoform chymotrypsin-like Elastase (CELA) 3B (CELA3B) and, to a lesser extent, CELA3A. Genetic variants of the human CELA3 isoforms have no significant effect on test performance.
Natércia F. Brás - One of the best experts on this subject based on the ideXlab platform.
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Inhibition of Pancreatic Elastase by polyphenolic compounds.
Journal of Agricultural and Food Chemistry, 2010Co-Authors: Natércia F. Brás, Rui Gonçalves, Pedro A. Fernandes, Maria J. Ramos, Nuno Mateus, Victor De FreitasAbstract:Polyphenols are plant secondary metabolites commonly present in the human diet that possess the ability to bind and inhibit digestive proteins. In the present study, kinetic measurements of porcine Pancreatic Elastase (PPE) activity were determined using Suc-(Ala)3-p-nitroanilide as substrate and polyphenolic compounds as inhibitors. A positive relationship between the degree of polyphenol polymerization and the capacity of the polyphenols to inhibit PPE was observed. Procyanidins with a molecular weight of at least 1154 Da were necessary to observe a significant inhibitory ability. Kinetic parameters were also calculated and confirmed that the inhibition is reversible and competitive. Molecular docking and dynamics simulations demonstrated that the tetramer structure has a higher affinity to the enzyme due the establishment of more contact points with the amino acids present in its active site. Hydrogen bond interactions and hydrophobic effects established between the polyphenol groups and the side chain...
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Inhibition of Pancreatic Elastase by polyphenolic compounds.
Journal of Agricultural and Food Chemistry, 2010Co-Authors: Natércia F. Brás, Rui Gonçalves, Pedro A. Fernandes, Maria J. Ramos, Nuno Mateus, Victor De FreitasAbstract:Polyphenols are plant secondary metabolites commonly present in the human diet that possess the ability to bind and inhibit digestive proteins. In the present study, kinetic measurements of porcine Pancreatic Elastase (PPE) activity were determined using Suc-(Ala)3-p-nitroanilide as substrate and polyphenolic compounds as inhibitors. A positive relationship between the degree of polyphenol polymerization and the capacity of the polyphenols to inhibit PPE was observed. Procyanidins with a molecular weight of at least 1154 Da were necessary to observe a significant inhibitory ability. Kinetic parameters were also calculated and confirmed that the inhibition is reversible and competitive. Molecular docking and dynamics simulations demonstrated that the tetramer structure has a higher affinity to the enzyme due the establishment of more contact points with the amino acids present in its active site. Hydrogen bond interactions and hydrophobic effects established between the polyphenol groups and the side chain...
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Inhibition of Pancreatic Elastase by Polyphenolic Compounds
Journal of agricultural and food chemistry, 2010Co-Authors: Natércia F. Brás, Rui Gonçalves, Pedro A. Fernandes, Maria J. Ramos, Nuno Mateus, Victor De FreitasAbstract:Polyphenols are plant secondary metabolites commonly present in the human diet that possess the ability to bind and inhibit digestive proteins. In the present study, kinetic measurements of porcine Pancreatic Elastase (PPE) activity were determined using Suc-(Ala)(3)-p-nitroanilide as substrate and polyphenolic compounds as inhibitors. A positive relationship between the degree of polyphenol polymerization and the capacity of the polyphenols to inhibit PPE was observed. Procyanidins with a molecular weight of at least 1154 Da were necessary to observe a significant inhibitory ability. Kinetic parameters were also calculated and confirmed that the inhibition is reversible and competitive. Molecular docking and dynamics simulations demonstrated that the tetramer structure has a higher affinity to the enzyme due the establishment of more contact points with the amino acids present in its active site. Hydrogen bond interactions and hydrophobic effects established between the polyphenol groups and the side chain of residues stabilize and favor the binding mode of this procyanidin. This work is relevant to the study of the antinutritional effects caused by dietary tannins on the digestive enzymes' activity, reducing food digestibility and the absorption of nutrients. In general, the Elastase model studied herein allows a better understanding of the inhibitory ability of polyphenol compounds.
Michael E. Zenilman - One of the best experts on this subject based on the ideXlab platform.
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Pancreatic Elastase is proven to be a mannose-binding protein—implications for the systemic response to pancreatitis
Surgery, 2003Co-Authors: Hong Zhang, Yin Yao Lin, Cathy M. Mueller, Sameer A Patel, Emad Kandil, Michael E. ZenilmanAbstract:Abstract Background. Mannose-binding proteins (MBPs) have been isolated from serum, liver, lung, and kidney and are believed to play an important role in first-line host defense during acute phase inflammatory response. Because of the inflammatory nature of pancreatitis, we postulate that the pancreas produces endogenous MBP. Methods. Pancreatic juice, from both human and rat, was collected by Pancreatic duct cannulation and subjected to mannose-Sepharose affinity chromatography to isolate Pancreatic MBP (pMBP). Protein eluates from the mannose-Sepharose column were analyzed using reverse-phase high-performance liquid chromatography, sodium dodeclysulfate-polyacrylamide gel electrophoresis, and, subsequently, by N-terminal protein sequencing. Western blot analysis was used to identify the pMBP, and reverse transcriptionase-polymerase chain reaction was used to examine its mRNA expression. Complement lysis was measured using red blood cells coated with yeast mannan. Tumor necrosis factor (TNF)-α mRNA expression in macrophages was measured using RNase protection assay. Results. A 30-kd MBP was isolated from both human and rat Pancreatic juice and a rat acinar cell line. Genetic analysis (using RT-PCR with known MBP primers) and protein analysis (using Western blot with a known anti-MBP antibody) suggest that the pMBP is different from any previously described MBP. Protein sequencing analysis of pMBP generated an N-terminus sequence of 12 residues, indicating that pMBP is human Pancreatic Elastase III. Western blot analysis using an anti-Elastase antibody confirms that the pMBP is a Pancreatic Elastase. Exposure of macrophages to Pancreatic Elastase resulted in an increased mRNA level of TNF-α, a potent proinflammatory cytokine in acute-phase response. Addition of mannan to Pancreatic Elastase further upregulated the TNF-α response. Conclusion. We isolated an MBP from the pancreas and identified it as Pancreatic Elastase. We characterized it as having properties different from that of any previously known MBP. We showed that pMBP or Pancreatic Elastase is involved in the activation of macrophages, and that this activation is potentiated by mannan. We postulate that the mannose-binding properties of Pancreatic Elastase identify this enzyme as a candidate catalyst for both Pancreatic and systemic inflammation. (Surgery 2003;133:678-88.)
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Pancreatic Elastase is proven to be a mannose-binding protein--implications for the systemic response to pancreatitis.
Surgery, 2003Co-Authors: Hong Zhang, Yin Yao Lin, Cathy M. Mueller, Sameer A Patel, Emad Kandil, Michael E. ZenilmanAbstract:Abstract Background. Mannose-binding proteins (MBPs) have been isolated from serum, liver, lung, and kidney and are believed to play an important role in first-line host defense during acute phase inflammatory response. Because of the inflammatory nature of pancreatitis, we postulate that the pancreas produces endogenous MBP. Methods. Pancreatic juice, from both human and rat, was collected by Pancreatic duct cannulation and subjected to mannose-Sepharose affinity chromatography to isolate Pancreatic MBP (pMBP). Protein eluates from the mannose-Sepharose column were analyzed using reverse-phase high-performance liquid chromatography, sodium dodeclysulfate-polyacrylamide gel electrophoresis, and, subsequently, by N-terminal protein sequencing. Western blot analysis was used to identify the pMBP, and reverse transcriptionase-polymerase chain reaction was used to examine its mRNA expression. Complement lysis was measured using red blood cells coated with yeast mannan. Tumor necrosis factor (TNF)-α mRNA expression in macrophages was measured using RNase protection assay. Results. A 30-kd MBP was isolated from both human and rat Pancreatic juice and a rat acinar cell line. Genetic analysis (using RT-PCR with known MBP primers) and protein analysis (using Western blot with a known anti-MBP antibody) suggest that the pMBP is different from any previously described MBP. Protein sequencing analysis of pMBP generated an N-terminus sequence of 12 residues, indicating that pMBP is human Pancreatic Elastase III. Western blot analysis using an anti-Elastase antibody confirms that the pMBP is a Pancreatic Elastase. Exposure of macrophages to Pancreatic Elastase resulted in an increased mRNA level of TNF-α, a potent proinflammatory cytokine in acute-phase response. Addition of mannan to Pancreatic Elastase further upregulated the TNF-α response. Conclusion. We isolated an MBP from the pancreas and identified it as Pancreatic Elastase. We characterized it as having properties different from that of any previously known MBP. We showed that pMBP or Pancreatic Elastase is involved in the activation of macrophages, and that this activation is potentiated by mannan. We postulate that the mannose-binding properties of Pancreatic Elastase identify this enzyme as a candidate catalyst for both Pancreatic and systemic inflammation. (Surgery 2003;133:678-88.)
