FBS or BSA Inhibits EGCG Induced Cell Death through Covalent Binding and the Reduction of Intracellular ROS Production
Previously we have shown that ( - )-epigallocatechin gallate (EGCG) can induce nonapoptotic cell death in human hepatoma HepG2 cells only under serum-free condition. However, the underlying mechanism for serum in determining the cell fate remains to be answered. The effects of fetal bovine serum (FB...
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| creator | Zhu, Xin-Qiang Shen, Han-Ming Zheng, Yi-Fan Zhang, Mo-Han Sun, Wen-Jie Xu, Yu-Ying Zhang, Yin Yang, Jun |
| description | Previously we have shown that ( - )-epigallocatechin gallate (EGCG) can induce nonapoptotic cell death in human hepatoma HepG2 cells only under serum-free condition. However, the underlying mechanism for serum in determining the cell fate remains to be answered. The effects of fetal bovine serum (FBS) and its major component bovine serum albumin (BSA) on EGCG-induced cell death were investigated in this study. It was found that BSA, just like FBS, can protect cells from EGCG-induced cell death in a dose-dependent manner. Detailed analysis revealed that both FBS and BSA inhibited generation of ROS to protect against toxicity of EGCG. Furthermore, EGCG was shown to bind to certain cellular proteins including caspase-3, PARP, and α-tubulin, but not LC3 nor β-actin, which formed EGCG-protein complexes that were inseparable by SDS-gel. On the other hand, addition of FBS or BSA to culture medium can block the binding of EGCG to these proteins. In silico docking analysis results suggested that BSA had a stronger affinity to EGCG than the other proteins. Taken together, these data indicated that the protective effect of FBS and BSA against EGCG-induced cell death could be due to (1) the decreased generation of ROS and (2) the competitive binding of BSA to EGCG. |
| doi_str_mv | 10.1155/2016/5013409 |
| format | Article |
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However, the underlying mechanism for serum in determining the cell fate remains to be answered. The effects of fetal bovine serum (FBS) and its major component bovine serum albumin (BSA) on EGCG-induced cell death were investigated in this study. It was found that BSA, just like FBS, can protect cells from EGCG-induced cell death in a dose-dependent manner. Detailed analysis revealed that both FBS and BSA inhibited generation of ROS to protect against toxicity of EGCG. Furthermore, EGCG was shown to bind to certain cellular proteins including caspase-3, PARP, and α-tubulin, but not LC3 nor β-actin, which formed EGCG-protein complexes that were inseparable by SDS-gel. On the other hand, addition of FBS or BSA to culture medium can block the binding of EGCG to these proteins. In silico docking analysis results suggested that BSA had a stronger affinity to EGCG than the other proteins. Taken together, these data indicated that the protective effect of FBS and BSA against EGCG-induced cell death could be due to (1) the decreased generation of ROS and (2) the competitive binding of BSA to EGCG.</description><identifier>ISSN: 2314-6133</identifier><identifier>EISSN: 2314-6141</identifier><identifier>DOI: 10.1155/2016/5013409</identifier><identifier>PMID: 27830147</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Albumin ; Analysis ; Animals ; Apoptosis ; Biochemistry ; Cancer ; Catechin ; Catechin - analogs & derivatives ; Catechin - pharmacology ; Cattle ; Cell culture ; Cell death ; Cell Death - drug effects ; Fourier transforms ; Hep G2 Cells ; Humans ; Immunoglobulins ; Infectious diseases ; Intracellular Space - metabolism ; Investigations ; Medical diagnosis ; Molecular Docking Simulation ; Polyphenols ; Protein binding ; Protein Binding - drug effects ; Proteins ; Public health ; Reactive Oxygen Species - metabolism ; Serum - metabolism ; Serum Albumin, Bovine - pharmacology ; Tea ; Toxicology ; Tubulins</subject><ispartof>BioMed research international, 2016-01, Vol.2016 (2016), p.1-8</ispartof><rights>Copyright © 2016 Yin Zhang et al.</rights><rights>COPYRIGHT 2016 John Wiley & Sons, Inc.</rights><rights>Copyright © 2016 Yin Zhang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2016 Yin Zhang et al. 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c598t-5b1c7cfc7188f0ebbbb82e44522c065b3d15dcd0a97e1c783cffb7a0298307c53</citedby><cites>FETCH-LOGICAL-c598t-5b1c7cfc7188f0ebbbb82e44522c065b3d15dcd0a97e1c783cffb7a0298307c53</cites><orcidid>0000-0002-9088-7906</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5088332/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5088332/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27830147$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Mudgal, Jayesh</contributor><creatorcontrib>Zhu, Xin-Qiang</creatorcontrib><creatorcontrib>Shen, Han-Ming</creatorcontrib><creatorcontrib>Zheng, Yi-Fan</creatorcontrib><creatorcontrib>Zhang, Mo-Han</creatorcontrib><creatorcontrib>Sun, Wen-Jie</creatorcontrib><creatorcontrib>Xu, Yu-Ying</creatorcontrib><creatorcontrib>Zhang, Yin</creatorcontrib><creatorcontrib>Yang, Jun</creatorcontrib><title>FBS or BSA Inhibits EGCG Induced Cell Death through Covalent Binding and the Reduction of Intracellular ROS Production</title><title>BioMed research international</title><addtitle>Biomed Res Int</addtitle><description>Previously we have shown that ( - )-epigallocatechin gallate (EGCG) can induce nonapoptotic cell death in human hepatoma HepG2 cells only under serum-free condition. However, the underlying mechanism for serum in determining the cell fate remains to be answered. The effects of fetal bovine serum (FBS) and its major component bovine serum albumin (BSA) on EGCG-induced cell death were investigated in this study. It was found that BSA, just like FBS, can protect cells from EGCG-induced cell death in a dose-dependent manner. Detailed analysis revealed that both FBS and BSA inhibited generation of ROS to protect against toxicity of EGCG. Furthermore, EGCG was shown to bind to certain cellular proteins including caspase-3, PARP, and α-tubulin, but not LC3 nor β-actin, which formed EGCG-protein complexes that were inseparable by SDS-gel. On the other hand, addition of FBS or BSA to culture medium can block the binding of EGCG to these proteins. In silico docking analysis results suggested that BSA had a stronger affinity to EGCG than the other proteins. Taken together, these data indicated that the protective effect of FBS and BSA against EGCG-induced cell death could be due to (1) the decreased generation of ROS and (2) the competitive binding of BSA to EGCG.</description><subject>Albumin</subject><subject>Analysis</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Biochemistry</subject><subject>Cancer</subject><subject>Catechin</subject><subject>Catechin - analogs & derivatives</subject><subject>Catechin - pharmacology</subject><subject>Cattle</subject><subject>Cell culture</subject><subject>Cell death</subject><subject>Cell Death - drug effects</subject><subject>Fourier transforms</subject><subject>Hep G2 Cells</subject><subject>Humans</subject><subject>Immunoglobulins</subject><subject>Infectious diseases</subject><subject>Intracellular Space - metabolism</subject><subject>Investigations</subject><subject>Medical diagnosis</subject><subject>Molecular Docking Simulation</subject><subject>Polyphenols</subject><subject>Protein binding</subject><subject>Protein Binding - drug effects</subject><subject>Proteins</subject><subject>Public health</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>Serum - metabolism</subject><subject>Serum Albumin, Bovine - pharmacology</subject><subject>Tea</subject><subject>Toxicology</subject><subject>Tubulins</subject><issn>2314-6133</issn><issn>2314-6141</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkc1v1DAQxSMEolXpjTOyxAUJlvojjp0L0m5ol0qVirpwthzH2bjK2sVOtup_z4Rdti0nfLGt-c3TvHlZ9pbgz4RwfkYxKc44JizH5YvsmDKSzwqSk5eHN2NH2WlKtxiOJAUui9fZERWSYZKL42x7sVihENFiNUeXvnO1GxI6X1ZL-DWjsQ2qbN-jr1YPHRq6GMZ1h6qw1b31A1o43zi_Rto3ULToxkLP4IJHoQWBIWoD3WOvI7q5XqHvMezrb7JXre6TPd3fJ9nPi_Mf1bfZ1fXysppfzQwv5TDjNTHCtEYQKVtsaziS2jznlBpc8Jo1hDemwboUFkjJTNvWQmNagj9hODvJvux078Z6Yxtjp5l6dRfdRscHFbRTzyvedWodtopjKRmjIPBhLxDDr9GmQW1cmkxpb8OYFJF5kWPBZA7o-3_Q2zBGD_b-UCAoy_KRWsMKlfNtmLY0iao5p1gQTjgG6tOOMjGkFG17GJlgNSWvpuTVPnnA3z21eYD_5gzAxx3QQWL63v2nnAXGtvoJXYpScPYb6zq9qQ</recordid><startdate>20160101</startdate><enddate>20160101</enddate><creator>Zhu, Xin-Qiang</creator><creator>Shen, Han-Ming</creator><creator>Zheng, Yi-Fan</creator><creator>Zhang, Mo-Han</creator><creator>Sun, Wen-Jie</creator><creator>Xu, Yu-Ying</creator><creator>Zhang, Yin</creator><creator>Yang, Jun</creator><general>Hindawi Publishing Corporation</general><general>John Wiley & Sons, Inc</general><general>Hindawi Limited</general><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</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>3V.</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7TK</scope><scope>7U7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CWDGH</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-9088-7906</orcidid></search><sort><creationdate>20160101</creationdate><title>FBS or BSA Inhibits EGCG Induced Cell Death through Covalent Binding and the Reduction of Intracellular ROS Production</title><author>Zhu, Xin-Qiang ; Shen, Han-Ming ; Zheng, Yi-Fan ; Zhang, Mo-Han ; Sun, Wen-Jie ; Xu, Yu-Ying ; Zhang, Yin ; Yang, Jun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c598t-5b1c7cfc7188f0ebbbb82e44522c065b3d15dcd0a97e1c783cffb7a0298307c53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Albumin</topic><topic>Analysis</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Biochemistry</topic><topic>Cancer</topic><topic>Catechin</topic><topic>Catechin - analogs & derivatives</topic><topic>Catechin - pharmacology</topic><topic>Cattle</topic><topic>Cell culture</topic><topic>Cell death</topic><topic>Cell Death - drug effects</topic><topic>Fourier transforms</topic><topic>Hep G2 Cells</topic><topic>Humans</topic><topic>Immunoglobulins</topic><topic>Infectious diseases</topic><topic>Intracellular Space - metabolism</topic><topic>Investigations</topic><topic>Medical diagnosis</topic><topic>Molecular Docking Simulation</topic><topic>Polyphenols</topic><topic>Protein binding</topic><topic>Protein Binding - drug effects</topic><topic>Proteins</topic><topic>Public health</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>Serum - metabolism</topic><topic>Serum Albumin, Bovine - pharmacology</topic><topic>Tea</topic><topic>Toxicology</topic><topic>Tubulins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhu, Xin-Qiang</creatorcontrib><creatorcontrib>Shen, Han-Ming</creatorcontrib><creatorcontrib>Zheng, Yi-Fan</creatorcontrib><creatorcontrib>Zhang, Mo-Han</creatorcontrib><creatorcontrib>Sun, Wen-Jie</creatorcontrib><creatorcontrib>Xu, Yu-Ying</creatorcontrib><creatorcontrib>Zhang, Yin</creatorcontrib><creatorcontrib>Yang, Jun</creatorcontrib><collection>الدوريات العلمية والإحصائية - 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)-epigallocatechin gallate (EGCG) can induce nonapoptotic cell death in human hepatoma HepG2 cells only under serum-free condition. However, the underlying mechanism for serum in determining the cell fate remains to be answered. The effects of fetal bovine serum (FBS) and its major component bovine serum albumin (BSA) on EGCG-induced cell death were investigated in this study. It was found that BSA, just like FBS, can protect cells from EGCG-induced cell death in a dose-dependent manner. Detailed analysis revealed that both FBS and BSA inhibited generation of ROS to protect against toxicity of EGCG. Furthermore, EGCG was shown to bind to certain cellular proteins including caspase-3, PARP, and α-tubulin, but not LC3 nor β-actin, which formed EGCG-protein complexes that were inseparable by SDS-gel. On the other hand, addition of FBS or BSA to culture medium can block the binding of EGCG to these proteins. In silico docking analysis results suggested that BSA had a stronger affinity to EGCG than the other proteins. Taken together, these data indicated that the protective effect of FBS and BSA against EGCG-induced cell death could be due to (1) the decreased generation of ROS and (2) the competitive binding of BSA to EGCG.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Publishing Corporation</pub><pmid>27830147</pmid><doi>10.1155/2016/5013409</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-9088-7906</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; PubMed Central Open Access; Wiley Online Library Open Access; PubMed Central; Alma/SFX Local Collection |
| subjects | Albumin Analysis Animals Apoptosis Biochemistry Cancer Catechin Catechin - analogs & derivatives Catechin - pharmacology Cattle Cell culture Cell death Cell Death - drug effects Fourier transforms Hep G2 Cells Humans Immunoglobulins Infectious diseases Intracellular Space - metabolism Investigations Medical diagnosis Molecular Docking Simulation Polyphenols Protein binding Protein Binding - drug effects Proteins Public health Reactive Oxygen Species - metabolism Serum - metabolism Serum Albumin, Bovine - pharmacology Tea Toxicology Tubulins |
| title | FBS or BSA Inhibits EGCG Induced Cell Death through Covalent Binding and the Reduction of Intracellular ROS Production |
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