A receptor for green tea polyphenol EGCG

Tachibana, Hirofumi; Koga, Kohachiro; Fujimura, Yoshinori; Yamada, Koji

doi:10.1038/nsmb743

Cited by 633 publications

(546 citation statements)

References 8 publications

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“…Tachibana et al have identified a receptor protein for EGCg. [28] EGCg must interact with the cell membrane before binding to the receptor. Since our results indicate that EGCg interacts with membrane surface and moves freely on the membrane surface, it would be able to bind to its target receptor.…”

Section: Resultsmentioning

confidence: 99%

Solid‐state NMR analysis of the orientation and dynamics of epigallocatechin gallate, a green tea polyphenol, incorporated into lipid bilayers

Kajiya

Kumazawa

Naito

et al. 2007

Magnetic Reson in Chemistry

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Catechins are the principle polyphenolic compounds in green tea; the four major compounds identified are epicatechin (EC), epigallocatechin (EGC), epicatechin gallate (ECg) and epigallocatechin gallate (EGCg). Tea catechins tend to attach externally to their targets, such as viral envelopes, cell membranes, or the surface of low-density lipoproteins. In order to further our understanding of the molecular mobility of these compounds in cells, we examined the interaction of tea catechins with lipid membranes using solid-state NMR techniques. Our previous work indicated that the EGCg molecule is incorporated into lipid bilayers in a unique orientation. However, the detailed configuration, orientation, and dynamics of EGCg in lipid bilayers have not been well-characterized. Here, we investigated the orientation and dynamics of EGCg incorporated into multi-lamellar vesicles (MLVs) and bicelles using solid-state NMR spectroscopy.

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Section: Resultsmentioning

confidence: 99%

Solid‐state NMR analysis of the orientation and dynamics of epigallocatechin gallate, a green tea polyphenol, incorporated into lipid bilayers

Kajiya

Kumazawa

Naito

et al. 2007

Magnetic Reson in Chemistry

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“…Inhibition of telomerase and matrix metalloproteinases has been demonstrated with rather low concentrations of EGCG (IC 50 in the range of 0.5-1 μM). EGCG has also been found to bind to 67-kDa laminin receptor, Bcl-2, vimentin, and glucose-regulated protein 78 with high affinity [50][51][52][53]. However, there are big differences between the effective concentrations determined with pure enzymes and those in cell lines or tissues, possibly due to the nonspecific binding of EGCG to many proteins and the limited amount of EGCG that can enter the cells.…”

Section: Mechanistic Studies On the Activities Of Egcg In Cell Linesmentioning

confidence: 99%

“…the IC 50 observed in a cell-free system was 0.1-0.2 μM, but it was 1-40 μM in tumor cell lines [54]. EGCG was reported to bind to the 67-kDa laminin receptor with a K d of 0.04 μM, to vimentin with a K d of 3.3 nM, and interact with Bcl-2 with a K i of 0.33 μM [50][51][52]. In all these studies, there were experiments demonstrating the biological relevance of the effects in their specific experimental systems, but it required much higher concentrations of EGCG to cause growth inhibition and induce apoptosis.…”

Section: Mechanistic Studies On the Activities Of Egcg In Cell Linesmentioning

confidence: 99%

Inhibition of carcinogenesis by tea constituents

Lǚ

Lambert

et al. 2007

Seminars in Cancer Biology

130

104

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The possible cancer preventive activity of tea has received much attention in recent years. The inhibitory activities of tea and tea constituents against carcinogenesis at different organ sites have been demonstrated in many animal models. The effect of tea consumption on human cancers, however, remains inconclusive. The mechanisms of action of tea polyphenols, especially EGCG, the most abundant and active catechin, have been extensively investigated. Most of the studies, however, were based on cell culture systems, and these mechanisms need to be evaluated and verified in animal models or humans in order to gain more understanding on the effect of tea consumption on human cancer. Human intervention trials are warranted to determine the possible prevention of cancer of specific sites by preparation of tea constituents.

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“…Syncytiotrophoblast formation was monitored in nearly confluent TS cells differentiated for 6 days. In some cases, TS cells were differentiated in the presence of HDAC inhibitor [100 nM trichostatin A (TSA) or 2.5 mM sodium butyrate] (Maltepe et al, 2005) or HAT inhibitor (30 nM curcumin or 5 M EGCG) (Balasubramanyam et al, 2004;Tachibana et al, 2004). For quantification of syncytiotrophoblast formation, cells were incubated with 2.5 m CellMask Deep Red (Invitrogen) for 5 minutes at 37°C and then fixed for 3 minutes in 3.75% formaldehyde at room temperature.…”

Section: Mouse Trophoblast Cell Culture and In Vitro Syncytium Formationmentioning

confidence: 99%

p45NF-E2 represses Gcm1 in trophoblast cells to regulate syncytium formation, placental vascularization and embryonic growth

et al. 2011

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SUMMARYAbsence of the leucine zipper transcription factor p45NF-E2 results in thrombocytopenia, impaired placental vascularization and intrauterine growth restriction (IUGR) in mice. The mechanism underlying the p45NF-E2-dependent placental defect and IUGR remains unknown. Here, we show that the placental defect and IUGR of p45NF-E2 (Nfe2) null mouse embryos is unrelated to thrombocytopenia, establishing that embryonic platelets and platelet-released mediators are dispensable for placentation. Rather, p45NF-E2, which was hitherto thought to be specific to hematopoietic cells, is expressed in trophoblast cells, where it is required for normal syncytiotrophoblast formation, placental vascularization and embryonic growth. Expression of p45NF-E2 in labyrinthine trophoblast cells colocalizes with that of Gcm1, a transcription factor crucial for syncytiotrophoblast formation. In the absence of p45NF-E2, the width of syncytiotrophoblast layer 2 and the expression of Gcm1 and Gcm1-dependent genes (Synb and Cebpa) are increased. In vitro, p45NF-E2 deficiency results in spontaneous syncytiotrophoblast formation, which can be reversed by Gcm1 knockdown. Increased Gcm1 expression in the absence of p45NF-E2 is dependent on enhanced protein acetylation, including post-translational modification of Gcm1. Increasing and inhibiting acetylation in the placenta of wild-type control embryos phenocopies and corrects, respectively, the changes observed in p45NF-E2-deficient embryos. These studies identify a novel function of p45NF-E2 during placental development: in trophoblast cells, p45NF-E2 represses Gcm1 and syncytiotrophoblast formation via acetylation.

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A receptor for green tea polyphenol EGCG

Cited by 633 publications

References 8 publications

Solid‐state NMR analysis of the orientation and dynamics of epigallocatechin gallate, a green tea polyphenol, incorporated into lipid bilayers

Solid‐state NMR analysis of the orientation and dynamics of epigallocatechin gallate, a green tea polyphenol, incorporated into lipid bilayers

Inhibition of carcinogenesis by tea constituents

p45NF-E2 represses Gcm1 in trophoblast cells to regulate syncytium formation, placental vascularization and embryonic growth

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