The Intermediate Filament Protein Vimentin Is a New Target for Epigallocatechin Gallate
Epigallocatechin gallate (EGCG) is the major active polyphenol in green tea. Protein interaction with EGCG is a critical step in the effects of EGCG on the regulation of various key proteins involved in signal transduction. We have identified a novel molecular target of EGCG using affinity chromatog...
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| Veröffentlicht in: | The Journal of biological chemistry 2005-04, Vol.280 (17), p.16882-16890 |
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| container_title | The Journal of biological chemistry |
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| creator | Ermakova, Svetlana Choi, Bu Young Choi, Hong Seok Kang, Bong Seok Bode, Ann M. Dong, Zigang |
| description | Epigallocatechin gallate (EGCG) is the major active polyphenol in green tea. Protein interaction with EGCG is a critical step in the effects of EGCG on the regulation of various key proteins involved in signal transduction. We have identified a novel molecular target of EGCG using affinity chromatography, two-dimensional electrophoresis, and mass spectrometry for protein identification. Spots of interest were identified as the intermediate filament, vimentin. The identification was confirmed by Western blot analysis using an anti-vimentin antibody. Experiments using a pull-down assay with [3H]EGCG demonstrate binding of EGCG to vimentin with a Kd of 3.3 nm. EGCG inhibited phosphorylation of vimentin at serines 50 and 55 and phosphorylation of vimentin by cyclin-dependent kinase 2 and cAMP-dependent protein kinase. EGCG specifically inhibits cell proliferation by binding to vimentin. Because vimentin is important for maintaining cellular functions and is essential in maintaining the structure and mechanical integration of the cellular space, the inhibitory effect of EGCG on vimentin may further explain its anti-tumor-promoting effect. |
| doi_str_mv | 10.1074/jbc.M414185200 |
| format | Article |
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Protein interaction with EGCG is a critical step in the effects of EGCG on the regulation of various key proteins involved in signal transduction. We have identified a novel molecular target of EGCG using affinity chromatography, two-dimensional electrophoresis, and mass spectrometry for protein identification. Spots of interest were identified as the intermediate filament, vimentin. The identification was confirmed by Western blot analysis using an anti-vimentin antibody. Experiments using a pull-down assay with [3H]EGCG demonstrate binding of EGCG to vimentin with a Kd of 3.3 nm. EGCG inhibited phosphorylation of vimentin at serines 50 and 55 and phosphorylation of vimentin by cyclin-dependent kinase 2 and cAMP-dependent protein kinase. EGCG specifically inhibits cell proliferation by binding to vimentin. Because vimentin is important for maintaining cellular functions and is essential in maintaining the structure and mechanical integration of the cellular space, the inhibitory effect of EGCG on vimentin may further explain its anti-tumor-promoting effect.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M414185200</identifier><identifier>PMID: 15713670</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Anticarcinogenic Agents - pharmacology ; Antineoplastic Agents - pharmacology ; Blotting, Western ; Catechin - analogs & derivatives ; Catechin - chemistry ; Cell Line ; Cell Proliferation ; Chromatography, Affinity ; Cyclic AMP-Dependent Protein Kinases - chemistry ; Dose-Response Relationship, Drug ; Electrophoresis, Gel, Two-Dimensional ; Flavonoids - chemistry ; Genetic Vectors ; Glutathione Transferase - metabolism ; Humans ; Immunoprecipitation ; Inhibitory Concentration 50 ; Kinetics ; Mice ; Microscopy, Fluorescence ; Models, Chemical ; Molecular Sequence Data ; Peptides - chemistry ; Phenols - chemistry ; Phosphorylation ; Polyphenols ; Protein Binding ; Protein Structure, Tertiary ; RNA, Small Interfering - metabolism ; Serine - chemistry ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Time Factors ; Vimentin - chemistry ; Vimentin - metabolism</subject><ispartof>The Journal of biological chemistry, 2005-04, Vol.280 (17), p.16882-16890</ispartof><rights>2005 © 2005 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-50e02c789db4444e5aa0c226f2eeaf7b4f8a21031ae33093190f84bb5fc242f13</citedby><cites>FETCH-LOGICAL-c411t-50e02c789db4444e5aa0c226f2eeaf7b4f8a21031ae33093190f84bb5fc242f13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15713670$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ermakova, Svetlana</creatorcontrib><creatorcontrib>Choi, Bu Young</creatorcontrib><creatorcontrib>Choi, Hong Seok</creatorcontrib><creatorcontrib>Kang, Bong Seok</creatorcontrib><creatorcontrib>Bode, Ann M.</creatorcontrib><creatorcontrib>Dong, Zigang</creatorcontrib><title>The Intermediate Filament Protein Vimentin Is a New Target for Epigallocatechin Gallate</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Epigallocatechin gallate (EGCG) is the major active polyphenol in green tea. Protein interaction with EGCG is a critical step in the effects of EGCG on the regulation of various key proteins involved in signal transduction. We have identified a novel molecular target of EGCG using affinity chromatography, two-dimensional electrophoresis, and mass spectrometry for protein identification. Spots of interest were identified as the intermediate filament, vimentin. The identification was confirmed by Western blot analysis using an anti-vimentin antibody. Experiments using a pull-down assay with [3H]EGCG demonstrate binding of EGCG to vimentin with a Kd of 3.3 nm. EGCG inhibited phosphorylation of vimentin at serines 50 and 55 and phosphorylation of vimentin by cyclin-dependent kinase 2 and cAMP-dependent protein kinase. EGCG specifically inhibits cell proliferation by binding to vimentin. Because vimentin is important for maintaining cellular functions and is essential in maintaining the structure and mechanical integration of the cellular space, the inhibitory effect of EGCG on vimentin may further explain its anti-tumor-promoting effect.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anticarcinogenic Agents - pharmacology</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Blotting, Western</subject><subject>Catechin - analogs & derivatives</subject><subject>Catechin - chemistry</subject><subject>Cell Line</subject><subject>Cell Proliferation</subject><subject>Chromatography, Affinity</subject><subject>Cyclic AMP-Dependent Protein Kinases - chemistry</subject><subject>Dose-Response Relationship, Drug</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Flavonoids - chemistry</subject><subject>Genetic Vectors</subject><subject>Glutathione Transferase - metabolism</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Inhibitory Concentration 50</subject><subject>Kinetics</subject><subject>Mice</subject><subject>Microscopy, Fluorescence</subject><subject>Models, Chemical</subject><subject>Molecular Sequence Data</subject><subject>Peptides - chemistry</subject><subject>Phenols - chemistry</subject><subject>Phosphorylation</subject><subject>Polyphenols</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>RNA, Small Interfering - metabolism</subject><subject>Serine - chemistry</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Time Factors</subject><subject>Vimentin - chemistry</subject><subject>Vimentin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1vwjAQhq2qVaG0a8fKQ9dQn-MQZ6wQUCT6MdCPzXLMmRglBDlpUf99jYLE1Ft8Jz3vyfcQcgtsCCwVD5vcDJ8FCJAJZ-yM9IHJOIoT-DonfcY4RBlPZI9cNc2GhRIZXJIeJCnEo5T1yeeyQDrftugrXDndIp26Ule4bembr1t0W_rhDmNo5g3V9AX3dKn9Gltqa08nO7fWZVmbEDVFgGZhCv01ubC6bPDm-A7I-3SyHD9Fi9fZfPy4iIwAaKOEIeMmldkqF6Ew0ZoZzkeWI2qb5sJKzYHFoDGOWRZDxqwUeZ5YwwW3EA_IsNtrfN00Hq3aeVdp_6uAqYMhFQypk6EQuOsCu-88nHzCj0oCcN8BhVsXe-dR5a42BVaKy7AyVTCSkgdMdhiG634cetUYh1sTLHo0rVrV7r8v_AHnR3_r</recordid><startdate>20050429</startdate><enddate>20050429</enddate><creator>Ermakova, Svetlana</creator><creator>Choi, Bu Young</creator><creator>Choi, Hong Seok</creator><creator>Kang, Bong Seok</creator><creator>Bode, Ann M.</creator><creator>Dong, Zigang</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20050429</creationdate><title>The Intermediate Filament Protein Vimentin Is a New Target for Epigallocatechin Gallate</title><author>Ermakova, Svetlana ; Choi, Bu Young ; Choi, Hong Seok ; Kang, Bong Seok ; Bode, Ann M. ; Dong, Zigang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-50e02c789db4444e5aa0c226f2eeaf7b4f8a21031ae33093190f84bb5fc242f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Anticarcinogenic Agents - pharmacology</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Blotting, Western</topic><topic>Catechin - analogs & derivatives</topic><topic>Catechin - chemistry</topic><topic>Cell Line</topic><topic>Cell Proliferation</topic><topic>Chromatography, Affinity</topic><topic>Cyclic AMP-Dependent Protein Kinases - chemistry</topic><topic>Dose-Response Relationship, Drug</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Flavonoids - chemistry</topic><topic>Genetic Vectors</topic><topic>Glutathione Transferase - metabolism</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Inhibitory Concentration 50</topic><topic>Kinetics</topic><topic>Mice</topic><topic>Microscopy, Fluorescence</topic><topic>Models, Chemical</topic><topic>Molecular Sequence Data</topic><topic>Peptides - chemistry</topic><topic>Phenols - chemistry</topic><topic>Phosphorylation</topic><topic>Polyphenols</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>RNA, Small Interfering - metabolism</topic><topic>Serine - chemistry</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Time Factors</topic><topic>Vimentin - chemistry</topic><topic>Vimentin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ermakova, Svetlana</creatorcontrib><creatorcontrib>Choi, Bu Young</creatorcontrib><creatorcontrib>Choi, Hong Seok</creatorcontrib><creatorcontrib>Kang, Bong Seok</creatorcontrib><creatorcontrib>Bode, Ann M.</creatorcontrib><creatorcontrib>Dong, Zigang</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ermakova, Svetlana</au><au>Choi, Bu Young</au><au>Choi, Hong Seok</au><au>Kang, Bong Seok</au><au>Bode, Ann M.</au><au>Dong, Zigang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Intermediate Filament Protein Vimentin Is a New Target for Epigallocatechin Gallate</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2005-04-29</date><risdate>2005</risdate><volume>280</volume><issue>17</issue><spage>16882</spage><epage>16890</epage><pages>16882-16890</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Epigallocatechin gallate (EGCG) is the major active polyphenol in green tea. Protein interaction with EGCG is a critical step in the effects of EGCG on the regulation of various key proteins involved in signal transduction. We have identified a novel molecular target of EGCG using affinity chromatography, two-dimensional electrophoresis, and mass spectrometry for protein identification. Spots of interest were identified as the intermediate filament, vimentin. The identification was confirmed by Western blot analysis using an anti-vimentin antibody. Experiments using a pull-down assay with [3H]EGCG demonstrate binding of EGCG to vimentin with a Kd of 3.3 nm. EGCG inhibited phosphorylation of vimentin at serines 50 and 55 and phosphorylation of vimentin by cyclin-dependent kinase 2 and cAMP-dependent protein kinase. EGCG specifically inhibits cell proliferation by binding to vimentin. Because vimentin is important for maintaining cellular functions and is essential in maintaining the structure and mechanical integration of the cellular space, the inhibitory effect of EGCG on vimentin may further explain its anti-tumor-promoting effect.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15713670</pmid><doi>10.1074/jbc.M414185200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2005-04, Vol.280 (17), p.16882-16890 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Anticarcinogenic Agents - pharmacology Antineoplastic Agents - pharmacology Blotting, Western Catechin - analogs & derivatives Catechin - chemistry Cell Line Cell Proliferation Chromatography, Affinity Cyclic AMP-Dependent Protein Kinases - chemistry Dose-Response Relationship, Drug Electrophoresis, Gel, Two-Dimensional Flavonoids - chemistry Genetic Vectors Glutathione Transferase - metabolism Humans Immunoprecipitation Inhibitory Concentration 50 Kinetics Mice Microscopy, Fluorescence Models, Chemical Molecular Sequence Data Peptides - chemistry Phenols - chemistry Phosphorylation Polyphenols Protein Binding Protein Structure, Tertiary RNA, Small Interfering - metabolism Serine - chemistry Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Time Factors Vimentin - chemistry Vimentin - metabolism |
| title | The Intermediate Filament Protein Vimentin Is a New Target for Epigallocatechin Gallate |
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