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Epigallocatechin gallate (EGCG) inhibits type II phosphatidylinositol 4-kinases: A key component in pathways of phosphoinositide turnover
► EGCG inhibits type II Phosphatidylinositol (PtdIns) 4-kinase α and β isoforms. ► EGCG has differential interaction with both the isoforms revealed by spectroscopy. ► Autodock mapped the binding residues at ATP binding domain of PtdIns 4-kinase. Type II phosphatidylinositol (PtdIns) 4-kinases produ...
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Published in: | Archives of biochemistry and biophysics 2011-12, Vol.516 (1), p.45-51 |
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description | ► EGCG inhibits type II Phosphatidylinositol (PtdIns) 4-kinase α and β isoforms. ► EGCG has differential interaction with both the isoforms revealed by spectroscopy. ► Autodock mapped the binding residues at ATP binding domain of PtdIns 4-kinase.
Type II phosphatidylinositol (PtdIns) 4-kinases produce PtdIns 4-phosphate, an early key signaling molecule in phosphatidylinositol cycle, which is indispensable for T cell activation. Type II PtdIns 4-kinase alpha and beta have similar biochemical properties. To distinguish these isoforms Epigallocatechin gallate (EGCG) has been evaluated as a specific inhibitor. EGCG is the major active catechin in green tea having anti-inflammatory, antiatherogenic and cancer chemopreventive properties. The precise mechanism of actions and molecular targets of EGCG in early signaling cascades are not well understood. In the present study, we have shown that EGCG inhibits type II PtdIns 4-kinases (α and β isoforms) and PtdIns 3-kinase activity in vitro. EGCG directly bind to both alpha and beta isoforms of type II PtdIns 4-kinases with a Kd of 2.62
μM and 1.02
μM, respectively. Type II PtdIns 4-kinase-EGCG complex have different binding pattern at its excited state. Both isoforms showed significant change in helicity upon binding with EGCG. EGCG modulates its effect by interacting with ATP binding pocket; the residues likely to be involved in EGCG binding were predicted by Autodock. Our findings suggest that EGCG inhibits two isoforms and could be a key to regulate T cell activation. |
doi_str_mv | 10.1016/j.abb.2011.09.005 |
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Type II phosphatidylinositol (PtdIns) 4-kinases produce PtdIns 4-phosphate, an early key signaling molecule in phosphatidylinositol cycle, which is indispensable for T cell activation. Type II PtdIns 4-kinase alpha and beta have similar biochemical properties. To distinguish these isoforms Epigallocatechin gallate (EGCG) has been evaluated as a specific inhibitor. EGCG is the major active catechin in green tea having anti-inflammatory, antiatherogenic and cancer chemopreventive properties. The precise mechanism of actions and molecular targets of EGCG in early signaling cascades are not well understood. In the present study, we have shown that EGCG inhibits type II PtdIns 4-kinases (α and β isoforms) and PtdIns 3-kinase activity in vitro. EGCG directly bind to both alpha and beta isoforms of type II PtdIns 4-kinases with a Kd of 2.62
μM and 1.02
μM, respectively. Type II PtdIns 4-kinase-EGCG complex have different binding pattern at its excited state. Both isoforms showed significant change in helicity upon binding with EGCG. EGCG modulates its effect by interacting with ATP binding pocket; the residues likely to be involved in EGCG binding were predicted by Autodock. Our findings suggest that EGCG inhibits two isoforms and could be a key to regulate T cell activation.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2011.09.005</identifier><identifier>PMID: 21964243</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>1-Phosphatidylinositol 4-Kinase - antagonists & inhibitors ; 1-Phosphatidylinositol 4-Kinase - chemistry ; 1-Phosphatidylinositol 4-Kinase - metabolism ; adenosine triphosphate ; Amino Acid Sequence ; Anticarcinogenic Agents - pharmacology ; Binding Sites ; Camellia sinensis - chemistry ; catechin ; Catechin - analogs & derivatives ; Catechin - pharmacology ; chemoprevention ; Enzyme Inhibitors - pharmacology ; epigallocatechin ; Epigallocatechin gallate ; green tea ; Humans ; Jurkat Cells ; mechanism of action ; Models, Molecular ; Molecular Sequence Data ; Neoplasms - prevention & control ; Phosphatidylinositol 4-kinase ; Phosphatidylinositols - metabolism ; Protein Binding ; Protein Isoforms - antagonists & inhibitors ; Protein Isoforms - chemistry ; Protein Isoforms - metabolism ; Sequence Alignment ; T cell activation ; T-lymphocytes</subject><ispartof>Archives of biochemistry and biophysics, 2011-12, Vol.516 (1), p.45-51</ispartof><rights>2011</rights><rights>Published by Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c376t-61ed445be879e3ee784202b6526eff39a818506d5c8b95860f7264cd22ed39413</citedby><cites>FETCH-LOGICAL-c376t-61ed445be879e3ee784202b6526eff39a818506d5c8b95860f7264cd22ed39413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21964243$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sinha, Ranjeet K.</creatorcontrib><creatorcontrib>Patel, Ronak Y.</creatorcontrib><creatorcontrib>Bojjireddy, Naveen</creatorcontrib><creatorcontrib>Datta, Anindya</creatorcontrib><creatorcontrib>Subrahmanyam, Gosukonda</creatorcontrib><title>Epigallocatechin gallate (EGCG) inhibits type II phosphatidylinositol 4-kinases: A key component in pathways of phosphoinositide turnover</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>► EGCG inhibits type II Phosphatidylinositol (PtdIns) 4-kinase α and β isoforms. ► EGCG has differential interaction with both the isoforms revealed by spectroscopy. ► Autodock mapped the binding residues at ATP binding domain of PtdIns 4-kinase.
Type II phosphatidylinositol (PtdIns) 4-kinases produce PtdIns 4-phosphate, an early key signaling molecule in phosphatidylinositol cycle, which is indispensable for T cell activation. Type II PtdIns 4-kinase alpha and beta have similar biochemical properties. To distinguish these isoforms Epigallocatechin gallate (EGCG) has been evaluated as a specific inhibitor. EGCG is the major active catechin in green tea having anti-inflammatory, antiatherogenic and cancer chemopreventive properties. The precise mechanism of actions and molecular targets of EGCG in early signaling cascades are not well understood. In the present study, we have shown that EGCG inhibits type II PtdIns 4-kinases (α and β isoforms) and PtdIns 3-kinase activity in vitro. EGCG directly bind to both alpha and beta isoforms of type II PtdIns 4-kinases with a Kd of 2.62
μM and 1.02
μM, respectively. Type II PtdIns 4-kinase-EGCG complex have different binding pattern at its excited state. Both isoforms showed significant change in helicity upon binding with EGCG. EGCG modulates its effect by interacting with ATP binding pocket; the residues likely to be involved in EGCG binding were predicted by Autodock. Our findings suggest that EGCG inhibits two isoforms and could be a key to regulate T cell activation.</description><subject>1-Phosphatidylinositol 4-Kinase - antagonists & inhibitors</subject><subject>1-Phosphatidylinositol 4-Kinase - chemistry</subject><subject>1-Phosphatidylinositol 4-Kinase - metabolism</subject><subject>adenosine triphosphate</subject><subject>Amino Acid Sequence</subject><subject>Anticarcinogenic Agents - pharmacology</subject><subject>Binding Sites</subject><subject>Camellia sinensis - chemistry</subject><subject>catechin</subject><subject>Catechin - analogs & derivatives</subject><subject>Catechin - pharmacology</subject><subject>chemoprevention</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>epigallocatechin</subject><subject>Epigallocatechin gallate</subject><subject>green tea</subject><subject>Humans</subject><subject>Jurkat Cells</subject><subject>mechanism of action</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Neoplasms - prevention & control</subject><subject>Phosphatidylinositol 4-kinase</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Protein Binding</subject><subject>Protein Isoforms - antagonists & inhibitors</subject><subject>Protein Isoforms - chemistry</subject><subject>Protein Isoforms - metabolism</subject><subject>Sequence Alignment</subject><subject>T cell activation</subject><subject>T-lymphocytes</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNp9kUGP1CAYhonRuOPqD_Ci3NRDK1DKgJ42k3GcZBMPumdC6dcts51SgVnTn-C_lklHj56A5Hmf8H0vQq8pKSmh4uOhNE1TMkJpSVRJSP0ErShRoiCV5E_RihBSFUoKeoVexHggGeSCPUdXjCrBGa9W6Pd2cvdmGLw1CWzvRnx-5Tt-v91tdh-wG3vXuBRxmifA-z2eeh-n3iTXzoMbfXTJD5gXD240EeInfIMfYMbWHyc_wpiyAE8m9b_MHLHvLnG_JF0LOJ3C6B8hvETPOjNEeHU5r9Hdl-2Pzdfi9ttuv7m5LWy1FqkQFFrO6wbkWkEFsJacEdaImgnoukoZSWVNRFtb2ahaCtKtmeC2ZQzaSnFaXaN3i3cK_ucJYtJHFy3koUfwp6gVqYVkXMpM0oW0wccYoNNTcEcTZk2JPhegDzoXoM8FaKJ0LiBn3lzsp-YI7b_E341n4O0CdMZrcx9c1Hffs6EmhFFeibPi80JA3sKjg6CjdTBaaF0Am3Tr3X8-8Ac0FqCZ</recordid><startdate>20111201</startdate><enddate>20111201</enddate><creator>Sinha, Ranjeet K.</creator><creator>Patel, Ronak Y.</creator><creator>Bojjireddy, Naveen</creator><creator>Datta, Anindya</creator><creator>Subrahmanyam, Gosukonda</creator><general>Elsevier Inc</general><scope>FBQ</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><scope>7X8</scope></search><sort><creationdate>20111201</creationdate><title>Epigallocatechin gallate (EGCG) inhibits type II phosphatidylinositol 4-kinases: A key component in pathways of phosphoinositide turnover</title><author>Sinha, Ranjeet K. ; Patel, Ronak Y. ; Bojjireddy, Naveen ; Datta, Anindya ; Subrahmanyam, Gosukonda</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c376t-61ed445be879e3ee784202b6526eff39a818506d5c8b95860f7264cd22ed39413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>1-Phosphatidylinositol 4-Kinase - antagonists & inhibitors</topic><topic>1-Phosphatidylinositol 4-Kinase - chemistry</topic><topic>1-Phosphatidylinositol 4-Kinase - metabolism</topic><topic>adenosine triphosphate</topic><topic>Amino Acid Sequence</topic><topic>Anticarcinogenic Agents - pharmacology</topic><topic>Binding Sites</topic><topic>Camellia sinensis - chemistry</topic><topic>catechin</topic><topic>Catechin - analogs & derivatives</topic><topic>Catechin - pharmacology</topic><topic>chemoprevention</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>epigallocatechin</topic><topic>Epigallocatechin gallate</topic><topic>green tea</topic><topic>Humans</topic><topic>Jurkat Cells</topic><topic>mechanism of action</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Neoplasms - prevention & control</topic><topic>Phosphatidylinositol 4-kinase</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Protein Binding</topic><topic>Protein Isoforms - antagonists & inhibitors</topic><topic>Protein Isoforms - chemistry</topic><topic>Protein Isoforms - metabolism</topic><topic>Sequence Alignment</topic><topic>T cell activation</topic><topic>T-lymphocytes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sinha, Ranjeet K.</creatorcontrib><creatorcontrib>Patel, Ronak Y.</creatorcontrib><creatorcontrib>Bojjireddy, Naveen</creatorcontrib><creatorcontrib>Datta, Anindya</creatorcontrib><creatorcontrib>Subrahmanyam, Gosukonda</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sinha, Ranjeet K.</au><au>Patel, Ronak Y.</au><au>Bojjireddy, Naveen</au><au>Datta, Anindya</au><au>Subrahmanyam, Gosukonda</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Epigallocatechin gallate (EGCG) inhibits type II phosphatidylinositol 4-kinases: A key component in pathways of phosphoinositide turnover</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2011-12-01</date><risdate>2011</risdate><volume>516</volume><issue>1</issue><spage>45</spage><epage>51</epage><pages>45-51</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><notes>http://dx.doi.org/10.1016/j.abb.2011.09.005</notes><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>► EGCG inhibits type II Phosphatidylinositol (PtdIns) 4-kinase α and β isoforms. ► EGCG has differential interaction with both the isoforms revealed by spectroscopy. ► Autodock mapped the binding residues at ATP binding domain of PtdIns 4-kinase.
Type II phosphatidylinositol (PtdIns) 4-kinases produce PtdIns 4-phosphate, an early key signaling molecule in phosphatidylinositol cycle, which is indispensable for T cell activation. Type II PtdIns 4-kinase alpha and beta have similar biochemical properties. To distinguish these isoforms Epigallocatechin gallate (EGCG) has been evaluated as a specific inhibitor. EGCG is the major active catechin in green tea having anti-inflammatory, antiatherogenic and cancer chemopreventive properties. The precise mechanism of actions and molecular targets of EGCG in early signaling cascades are not well understood. In the present study, we have shown that EGCG inhibits type II PtdIns 4-kinases (α and β isoforms) and PtdIns 3-kinase activity in vitro. EGCG directly bind to both alpha and beta isoforms of type II PtdIns 4-kinases with a Kd of 2.62
μM and 1.02
μM, respectively. Type II PtdIns 4-kinase-EGCG complex have different binding pattern at its excited state. Both isoforms showed significant change in helicity upon binding with EGCG. EGCG modulates its effect by interacting with ATP binding pocket; the residues likely to be involved in EGCG binding were predicted by Autodock. Our findings suggest that EGCG inhibits two isoforms and could be a key to regulate T cell activation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21964243</pmid><doi>10.1016/j.abb.2011.09.005</doi><tpages>7</tpages></addata></record> |
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subjects | 1-Phosphatidylinositol 4-Kinase - antagonists & inhibitors 1-Phosphatidylinositol 4-Kinase - chemistry 1-Phosphatidylinositol 4-Kinase - metabolism adenosine triphosphate Amino Acid Sequence Anticarcinogenic Agents - pharmacology Binding Sites Camellia sinensis - chemistry catechin Catechin - analogs & derivatives Catechin - pharmacology chemoprevention Enzyme Inhibitors - pharmacology epigallocatechin Epigallocatechin gallate green tea Humans Jurkat Cells mechanism of action Models, Molecular Molecular Sequence Data Neoplasms - prevention & control Phosphatidylinositol 4-kinase Phosphatidylinositols - metabolism Protein Binding Protein Isoforms - antagonists & inhibitors Protein Isoforms - chemistry Protein Isoforms - metabolism Sequence Alignment T cell activation T-lymphocytes |
title | Epigallocatechin gallate (EGCG) inhibits type II phosphatidylinositol 4-kinases: A key component in pathways of phosphoinositide turnover |
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