Iron chelation properties of green tea Epigallocatechin-3-Gallate (EGCG) in colorectal cancer cells: analysis on Tfr/Fth regulations and molecular docking
In many studies, green tea epigallocatechin-3-gallate (EGCG) has already shown its therapeutic effects in colorectal cancer cells (CRC). However, its mechanism of actions in CRC is poorly elucidated. Hence, this study attempts to elucidate the mechanism of actions of green tea ECGG via iron chelatio...
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| Format: | Article |
| Language: | English |
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Hindawi Publishing Corporation
2020
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| Online Access: | http://psasir.upm.edu.my/id/eprint/89467/1/TEA.pdf |
| _version_ | 1796982168427167744 |
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| author | Md Nesran, Zarith Nameyrra Shafie, Nurul Husna Md Tohid, Siti Farah Norhaizan, Mohd Esa Ismail, Amin |
| author_facet | Md Nesran, Zarith Nameyrra Shafie, Nurul Husna Md Tohid, Siti Farah Norhaizan, Mohd Esa Ismail, Amin |
| author_sort | Md Nesran, Zarith Nameyrra |
| collection | UPM |
| description | In many studies, green tea epigallocatechin-3-gallate (EGCG) has already shown its therapeutic effects in colorectal cancer cells (CRC). However, its mechanism of actions in CRC is poorly elucidated. Hence, this study attempts to elucidate the mechanism of actions of green tea ECGG via iron chelation activity in CRC. In order to investigate this property, HT-29 cell lines (CRC) were treated with EGCG for 24 h, 48 h, and 72 h. From western blot analysis, EGCG had upregulated transferrin receptor (TfR) protein and downregulated Ferritin-H (FtH) protein indicating that iron chelation activity has occurred in CRC. Meanwhile, the molecular docking study demonstrated that EGCG is able to strongly interact the ferritin protein with a high binding affinity (−7.3 kcal/mol) via strong hydrogen bindings to glutamic acid 64 and lysine 71; two moderate hydrogen bindings to asparagine 74 and a hydrophobic interaction to the hydrophobic pocket of lysine 71. The strong interaction predicted between EGCG to ferritin may lead to inhibition of ferritin by EGCG, thus supporting the downregulation of FtH observed in in vitro studies. Molecular docking study of TfR to EGCG cannot be modulated based on the in vitro results. In conclusion, EGCG possesses iron chelator property in CRC and this potential could be further exploited for CRC treatment. |
| first_indexed | 2024-03-06T10:48:02Z |
| format | Article |
| id | upm.eprints-89467 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T10:48:02Z |
| publishDate | 2020 |
| publisher | Hindawi Publishing Corporation |
| record_format | dspace |
| spelling | upm.eprints-894672021-08-19T08:23:25Z http://psasir.upm.edu.my/id/eprint/89467/ Iron chelation properties of green tea Epigallocatechin-3-Gallate (EGCG) in colorectal cancer cells: analysis on Tfr/Fth regulations and molecular docking Md Nesran, Zarith Nameyrra Shafie, Nurul Husna Md Tohid, Siti Farah Norhaizan, Mohd Esa Ismail, Amin In many studies, green tea epigallocatechin-3-gallate (EGCG) has already shown its therapeutic effects in colorectal cancer cells (CRC). However, its mechanism of actions in CRC is poorly elucidated. Hence, this study attempts to elucidate the mechanism of actions of green tea ECGG via iron chelation activity in CRC. In order to investigate this property, HT-29 cell lines (CRC) were treated with EGCG for 24 h, 48 h, and 72 h. From western blot analysis, EGCG had upregulated transferrin receptor (TfR) protein and downregulated Ferritin-H (FtH) protein indicating that iron chelation activity has occurred in CRC. Meanwhile, the molecular docking study demonstrated that EGCG is able to strongly interact the ferritin protein with a high binding affinity (−7.3 kcal/mol) via strong hydrogen bindings to glutamic acid 64 and lysine 71; two moderate hydrogen bindings to asparagine 74 and a hydrophobic interaction to the hydrophobic pocket of lysine 71. The strong interaction predicted between EGCG to ferritin may lead to inhibition of ferritin by EGCG, thus supporting the downregulation of FtH observed in in vitro studies. Molecular docking study of TfR to EGCG cannot be modulated based on the in vitro results. In conclusion, EGCG possesses iron chelator property in CRC and this potential could be further exploited for CRC treatment. Hindawi Publishing Corporation 2020 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/89467/1/TEA.pdf Md Nesran, Zarith Nameyrra and Shafie, Nurul Husna and Md Tohid, Siti Farah and Norhaizan, Mohd Esa and Ismail, Amin (2020) Iron chelation properties of green tea Epigallocatechin-3-Gallate (EGCG) in colorectal cancer cells: analysis on Tfr/Fth regulations and molecular docking. Evidence-based Complementary and Alternative Medicine, 2020. art. no. 7958041. pp. 1-8. ISSN 1741-427X; ESSN: 1741-4288 https://www.hindawi.com/journals/ecam/2020/7958041/ 10.1155/2020/7958041 |
| spellingShingle | Md Nesran, Zarith Nameyrra Shafie, Nurul Husna Md Tohid, Siti Farah Norhaizan, Mohd Esa Ismail, Amin Iron chelation properties of green tea Epigallocatechin-3-Gallate (EGCG) in colorectal cancer cells: analysis on Tfr/Fth regulations and molecular docking |
| title | Iron chelation properties of green tea Epigallocatechin-3-Gallate (EGCG) in colorectal cancer cells: analysis on Tfr/Fth regulations and molecular docking |
| title_full | Iron chelation properties of green tea Epigallocatechin-3-Gallate (EGCG) in colorectal cancer cells: analysis on Tfr/Fth regulations and molecular docking |
| title_fullStr | Iron chelation properties of green tea Epigallocatechin-3-Gallate (EGCG) in colorectal cancer cells: analysis on Tfr/Fth regulations and molecular docking |
| title_full_unstemmed | Iron chelation properties of green tea Epigallocatechin-3-Gallate (EGCG) in colorectal cancer cells: analysis on Tfr/Fth regulations and molecular docking |
| title_short | Iron chelation properties of green tea Epigallocatechin-3-Gallate (EGCG) in colorectal cancer cells: analysis on Tfr/Fth regulations and molecular docking |
| title_sort | iron chelation properties of green tea epigallocatechin 3 gallate egcg in colorectal cancer cells analysis on tfr fth regulations and molecular docking |
| url | http://psasir.upm.edu.my/id/eprint/89467/1/TEA.pdf |
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