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Green tea catechins can bind and modify ERp57/PDIA3 activity
L. Trnková, D. Ricci, C. Grillo, G. Colotti, F. Altieri,
Language English Country Netherlands
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- DNA chemistry MeSH
- Enzyme Assays MeSH
- Spectrometry, Fluorescence MeSH
- Catalytic Domain MeSH
- Catechin analogs & derivatives chemistry MeSH
- Kinetics MeSH
- Humans MeSH
- Ligands MeSH
- Models, Molecular MeSH
- Oxidation-Reduction MeSH
- Surface Plasmon Resonance MeSH
- Protein Disulfide-Isomerases chemistry MeSH
- Recombinant Proteins chemistry MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Structure-Activity Relationship MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
BACKGROUND: Green tea is a rich source of polyphenols, mainly catechins (flavanols), which significantly contribute to the beneficial health effects of green tea in the prevention and treatment of various diseases. In this study the effects of four green tea catechins on protein ERp57, also known as protein disulfide isomerase isoform A3 (PDIA3), have been investigated in an in vitro model. METHODS: The interaction of catechins with ERp57 was explored by fluorescence quenching and surface plasmon resonance techniques and their effect on ERp57 activities was investigated. RESULTS: A higher affinity was observed for galloylated cathechins, which bind close to the thioredoxin-like redox-sensitive active sites of the protein, with a preference for the oxidized form. The effects of these catechins on ERp57 properties were also investigated and a moderate inhibition of the reductase activity of ERp57 was observed as well as a strong inhibition of ERp57 DNA binding activity. CONCLUSIONS: Considering the high affinity of galloylated catechins for ERp57 and their capability to inhibit ERp57 binding to other macromolecular ligands, some effects of catechins interaction with this protein on eukaryotic cells may be expected. GENERAL SIGNIFICANCE: This study provides information to better understand the molecular mechanisms underlying the biological activities of catechins and to design new polyphenol-based ERp57-specific inhibitors.
References provided by Crossref.org
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- $a Trnková, Lucie $u 1 Department of Chemistry, Faculty of Science, University of Hradec Králové, Rokitanského 62, 500 03, Hradec Králové, Czech Republic; Department of Biochemical Sciences, Charles University in Prague, Faculty of Pharmacy, Heyrovského 1203, 500 05, Hradec Králové, Czech Republic.
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- $a BACKGROUND: Green tea is a rich source of polyphenols, mainly catechins (flavanols), which significantly contribute to the beneficial health effects of green tea in the prevention and treatment of various diseases. In this study the effects of four green tea catechins on protein ERp57, also known as protein disulfide isomerase isoform A3 (PDIA3), have been investigated in an in vitro model. METHODS: The interaction of catechins with ERp57 was explored by fluorescence quenching and surface plasmon resonance techniques and their effect on ERp57 activities was investigated. RESULTS: A higher affinity was observed for galloylated cathechins, which bind close to the thioredoxin-like redox-sensitive active sites of the protein, with a preference for the oxidized form. The effects of these catechins on ERp57 properties were also investigated and a moderate inhibition of the reductase activity of ERp57 was observed as well as a strong inhibition of ERp57 DNA binding activity. CONCLUSIONS: Considering the high affinity of galloylated catechins for ERp57 and their capability to inhibit ERp57 binding to other macromolecular ligands, some effects of catechins interaction with this protein on eukaryotic cells may be expected. GENERAL SIGNIFICANCE: This study provides information to better understand the molecular mechanisms underlying the biological activities of catechins and to design new polyphenol-based ERp57-specific inhibitors.
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- $a Ricci, Daniela $u 2 Department of Biochemical Sciences "A. Rossi Fanelli", Sapienza University, P. le A. Moro 5, 00185, Rome, Italy; Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza University, P. le A. Moro 5, 00185, Rome, Italy.
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- $a Grillo, Caterina $u 2 Department of Biochemical Sciences "A. Rossi Fanelli", Sapienza University, P. le A. Moro 5, 00185, Rome, Italy; Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza University, P. le A. Moro 5, 00185, Rome, Italy.
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- $a Colotti, Gianni $u 3 Institute of Molecular Biology and Pathology, CNR, National Research Council, c/o Department of Biochemical Sciences "A. Rossi Fanelli", Sapienza University, P. le A. Moro 5, 00185, Rome, Italy.
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