Interactions of the sweet-tasting proteins thaumatin and lysozyme with the human sweet-taste receptor.
Identifieur interne : 000314 ( Main/Corpus ); précédent : 000313; suivant : 000315Interactions of the sweet-tasting proteins thaumatin and lysozyme with the human sweet-taste receptor.
Auteurs : Nobuyuki Ide ; Eriko Sato ; Keisuke Ohta ; Tetsuya Masuda ; Naofumi KitabatakeSource :
- Journal of agricultural and food chemistry [ 1520-5118 ] ; 2009.
English descriptors
- KwdEn :
- Benzene Derivatives (pharmacology), Cell Line (MeSH), Cloning, Molecular (MeSH), Cyclic AMP (analysis), Gene Expression (MeSH), Humans (MeSH), Kidney (MeSH), Muramidase (pharmacology), Plant Proteins (pharmacology), Receptors, G-Protein-Coupled (drug effects), Receptors, G-Protein-Coupled (genetics), Receptors, G-Protein-Coupled (physiology), Sodium Chloride (pharmacology), Sweetening Agents (pharmacology), Transfection (MeSH).
- MESH :
- chemical , analysis : Cyclic AMP.
- chemical , drug effects : Receptors, G-Protein-Coupled.
- chemical , genetics : Receptors, G-Protein-Coupled.
- chemical , pharmacology : Benzene Derivatives, Muramidase, Plant Proteins, Sodium Chloride, Sweetening Agents.
- chemical , physiology : Receptors, G-Protein-Coupled.
- Cell Line, Cloning, Molecular, Gene Expression, Humans, Kidney, Transfection.
Abstract
This study investigated the sweetness of the sweet-tasting protein thaumatin and lysozyme by both an in vitro cell-based assay and an in vivo sensory analysis to elucidate the differences between in vitro and in vivo response profiles. Hek293 cells were constructed that stably expressed the human T1R2+T1R3 sweet-taste receptor, and their responses to thaumatin and lysozyme were analyzed by monitoring the levels of intracellular cAMP. The results indicated that thaumatin and lysozyme as well as aspartame induced a decrease in the intracellular cAMP accumulation of the T1R2+T1R3-transfected cells and that EC(50) values of thaumatin and lysozyme determined by cell-based assay are well-consistent with the results of the sweetness threshold value determined by sensory analysis in the presence of 140 mM NaCl. The results of both in vitro and in vivo experiments confirmed that the sweetness inhibitor lactisole significantly suppressed the sweetness of thaumatin and lysozyme.
DOI: 10.1021/jf803956f
PubMed: 19489607
Links to Exploration step
pubmed:19489607Le document en format XML
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<author><name sortKey="Ide, Nobuyuki" sort="Ide, Nobuyuki" uniqKey="Ide N" first="Nobuyuki" last="Ide">Nobuyuki Ide</name>
<affiliation><nlm:affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Sato, Eriko" sort="Sato, Eriko" uniqKey="Sato E" first="Eriko" last="Sato">Eriko Sato</name>
</author>
<author><name sortKey="Ohta, Keisuke" sort="Ohta, Keisuke" uniqKey="Ohta K" first="Keisuke" last="Ohta">Keisuke Ohta</name>
</author>
<author><name sortKey="Masuda, Tetsuya" sort="Masuda, Tetsuya" uniqKey="Masuda T" first="Tetsuya" last="Masuda">Tetsuya Masuda</name>
</author>
<author><name sortKey="Kitabatake, Naofumi" sort="Kitabatake, Naofumi" uniqKey="Kitabatake N" first="Naofumi" last="Kitabatake">Naofumi Kitabatake</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Interactions of the sweet-tasting proteins thaumatin and lysozyme with the human sweet-taste receptor.</title>
<author><name sortKey="Ide, Nobuyuki" sort="Ide, Nobuyuki" uniqKey="Ide N" first="Nobuyuki" last="Ide">Nobuyuki Ide</name>
<affiliation><nlm:affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.</nlm:affiliation>
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<author><name sortKey="Sato, Eriko" sort="Sato, Eriko" uniqKey="Sato E" first="Eriko" last="Sato">Eriko Sato</name>
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<author><name sortKey="Ohta, Keisuke" sort="Ohta, Keisuke" uniqKey="Ohta K" first="Keisuke" last="Ohta">Keisuke Ohta</name>
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<author><name sortKey="Masuda, Tetsuya" sort="Masuda, Tetsuya" uniqKey="Masuda T" first="Tetsuya" last="Masuda">Tetsuya Masuda</name>
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<author><name sortKey="Kitabatake, Naofumi" sort="Kitabatake, Naofumi" uniqKey="Kitabatake N" first="Naofumi" last="Kitabatake">Naofumi Kitabatake</name>
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<series><title level="j">Journal of agricultural and food chemistry</title>
<idno type="eISSN">1520-5118</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Benzene Derivatives (pharmacology)</term>
<term>Cell Line (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Cyclic AMP (analysis)</term>
<term>Gene Expression (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Kidney (MeSH)</term>
<term>Muramidase (pharmacology)</term>
<term>Plant Proteins (pharmacology)</term>
<term>Receptors, G-Protein-Coupled (drug effects)</term>
<term>Receptors, G-Protein-Coupled (genetics)</term>
<term>Receptors, G-Protein-Coupled (physiology)</term>
<term>Sodium Chloride (pharmacology)</term>
<term>Sweetening Agents (pharmacology)</term>
<term>Transfection (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Cyclic AMP</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Receptors, G-Protein-Coupled</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Receptors, G-Protein-Coupled</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Benzene Derivatives</term>
<term>Muramidase</term>
<term>Plant Proteins</term>
<term>Sodium Chloride</term>
<term>Sweetening Agents</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Receptors, G-Protein-Coupled</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cell Line</term>
<term>Cloning, Molecular</term>
<term>Gene Expression</term>
<term>Humans</term>
<term>Kidney</term>
<term>Transfection</term>
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<front><div type="abstract" xml:lang="en">This study investigated the sweetness of the sweet-tasting protein thaumatin and lysozyme by both an in vitro cell-based assay and an in vivo sensory analysis to elucidate the differences between in vitro and in vivo response profiles. Hek293 cells were constructed that stably expressed the human T1R2+T1R3 sweet-taste receptor, and their responses to thaumatin and lysozyme were analyzed by monitoring the levels of intracellular cAMP. The results indicated that thaumatin and lysozyme as well as aspartame induced a decrease in the intracellular cAMP accumulation of the T1R2+T1R3-transfected cells and that EC(50) values of thaumatin and lysozyme determined by cell-based assay are well-consistent with the results of the sweetness threshold value determined by sensory analysis in the presence of 140 mM NaCl. The results of both in vitro and in vivo experiments confirmed that the sweetness inhibitor lactisole significantly suppressed the sweetness of thaumatin and lysozyme.</div>
</front>
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<Title>Journal of agricultural and food chemistry</Title>
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<ArticleTitle>Interactions of the sweet-tasting proteins thaumatin and lysozyme with the human sweet-taste receptor.</ArticleTitle>
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<Abstract><AbstractText>This study investigated the sweetness of the sweet-tasting protein thaumatin and lysozyme by both an in vitro cell-based assay and an in vivo sensory analysis to elucidate the differences between in vitro and in vivo response profiles. Hek293 cells were constructed that stably expressed the human T1R2+T1R3 sweet-taste receptor, and their responses to thaumatin and lysozyme were analyzed by monitoring the levels of intracellular cAMP. The results indicated that thaumatin and lysozyme as well as aspartame induced a decrease in the intracellular cAMP accumulation of the T1R2+T1R3-transfected cells and that EC(50) values of thaumatin and lysozyme determined by cell-based assay are well-consistent with the results of the sweetness threshold value determined by sensory analysis in the presence of 140 mM NaCl. The results of both in vitro and in vivo experiments confirmed that the sweetness inhibitor lactisole significantly suppressed the sweetness of thaumatin and lysozyme.</AbstractText>
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