Proteomic investigation of anti-tumor activities exerted by sinularin against A2058 melanoma cells
The extracts from soft corals have been increasingly investigated for biomedical and therapeutic purposes. The aim of this study is to examine and analyze the anti‐tumor effects of the genus Sinularia extract sinularin on A2058 melanoma cells using MTT assay, cell migration assay, wound healing assa...
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| Veröffentlicht in: | Electrophoresis 2012-04, Vol.33 (7), p.1139-1152 |
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| creator | Su, Tzu-Rong Lin, Jen-Jie Chiu, Chien-Chih Chen, Jeff Yi-Fu Su, Jui-Hsin Cheng, Zhi-Jiao Hwang, Wen-Ing Huang, Han Hsiang Wu, Yu-Jen |
| description | The extracts from soft corals have been increasingly investigated for biomedical and therapeutic purposes. The aim of this study is to examine and analyze the anti‐tumor effects of the genus Sinularia extract sinularin on A2058 melanoma cells using MTT assay, cell migration assay, wound healing assay, flow cytometric analysis, and proteomic analysis. Sinularin dose‐dependently (1–5 μg/mL) inhibited melanoma cell proliferation while the treatment at identical concentrations suppressed cell migration. Sinularin dose‐dependently enhanced apoptotic melanoma cells and caused tumor cell accumulation at G2/M phase, indicating that sinularin exerts apoptosis‐induced and cell cycle‐delayed activities in A2058 melanoma cells. Comparative proteomic analysis was conducted to investigate the effects of sinularin at the molecular level by comparison between the protein profiling of melanoma cells treated with sinularin and without the treatment. Thirty‐five differential proteins (13 upregulated and 22 downregulated) concerning the treatment were identified by liquid chromatography‐tandem mass spectrometry. Proteomic data and Western blot displayed the levels of several tumor inhibitory or apoptosis‐associated proteins including annexin A1, voltage‐dependent anion‐selective channel protein 1 and prohibitin (upregulated), heat shock protein 60, heat shock protein beta‐1, and peroxiredoxin‐2 (downregulated) in A2058 melanoma cells exposed to sinularin. Increased expression of p53, cleaved‐caspase‐3, cleaved‐caspase‐8, cleaved‐caspase‐9, p21, and Bax and decreased expression of Bcl‐2 in sinularin‐treated melanoma cells suggest that the anti‐tumor activities of sinularin against melanoma cells are particularly correlated with these pro‐apoptotic factors. These data provide important information for the mechanisms of anti‐tumor effects of sinularin on melanoma cells and may be helpful for drug development and progression monitoring of human melanoma. |
| doi_str_mv | 10.1002/elps.201100462 |
| format | Article |
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The aim of this study is to examine and analyze the anti‐tumor effects of the genus Sinularia extract sinularin on A2058 melanoma cells using MTT assay, cell migration assay, wound healing assay, flow cytometric analysis, and proteomic analysis. Sinularin dose‐dependently (1–5 μg/mL) inhibited melanoma cell proliferation while the treatment at identical concentrations suppressed cell migration. Sinularin dose‐dependently enhanced apoptotic melanoma cells and caused tumor cell accumulation at G2/M phase, indicating that sinularin exerts apoptosis‐induced and cell cycle‐delayed activities in A2058 melanoma cells. Comparative proteomic analysis was conducted to investigate the effects of sinularin at the molecular level by comparison between the protein profiling of melanoma cells treated with sinularin and without the treatment. Thirty‐five differential proteins (13 upregulated and 22 downregulated) concerning the treatment were identified by liquid chromatography‐tandem mass spectrometry. Proteomic data and Western blot displayed the levels of several tumor inhibitory or apoptosis‐associated proteins including annexin A1, voltage‐dependent anion‐selective channel protein 1 and prohibitin (upregulated), heat shock protein 60, heat shock protein beta‐1, and peroxiredoxin‐2 (downregulated) in A2058 melanoma cells exposed to sinularin. Increased expression of p53, cleaved‐caspase‐3, cleaved‐caspase‐8, cleaved‐caspase‐9, p21, and Bax and decreased expression of Bcl‐2 in sinularin‐treated melanoma cells suggest that the anti‐tumor activities of sinularin against melanoma cells are particularly correlated with these pro‐apoptotic factors. These data provide important information for the mechanisms of anti‐tumor effects of sinularin on melanoma cells and may be helpful for drug development and progression monitoring of human melanoma.</description><identifier>ISSN: 0173-0835</identifier><identifier>EISSN: 1522-2683</identifier><identifier>DOI: 10.1002/elps.201100462</identifier><identifier>PMID: 22539317</identifier><language>eng</language><publisher>Germany: Blackwell Publishing Ltd</publisher><subject>Animals ; Anthozoa - chemistry ; Antineoplastic Agents, Phytogenic - chemistry ; Antineoplastic Agents, Phytogenic - pharmacology ; Apoptosis - drug effects ; Blotting, Western ; Cell Line, Tumor ; Cell Movement - drug effects ; Diterpenes - chemistry ; Diterpenes - pharmacology ; Dose-Response Relationship, Drug ; Electrophoresis, Gel, Two-Dimensional ; Flow Cytometry ; Heterocyclic Compounds, 3-Ring - chemistry ; Heterocyclic Compounds, 3-Ring - pharmacology ; Humans ; Melanoma - drug therapy ; Melanoma - metabolism ; Melanoma cells ; Proteins - analysis ; Proteins - classification ; Proteins - metabolism ; Proteome - analysis ; Proteome - drug effects ; Proteome - metabolism ; Proteomic analysis ; Proteomics ; Reproducibility of Results ; Sinularin</subject><ispartof>Electrophoresis, 2012-04, Vol.33 (7), p.1139-1152</ispartof><rights>2012 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Felps.201100462$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Felps.201100462$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22539317$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Su, Tzu-Rong</creatorcontrib><creatorcontrib>Lin, Jen-Jie</creatorcontrib><creatorcontrib>Chiu, Chien-Chih</creatorcontrib><creatorcontrib>Chen, Jeff Yi-Fu</creatorcontrib><creatorcontrib>Su, Jui-Hsin</creatorcontrib><creatorcontrib>Cheng, Zhi-Jiao</creatorcontrib><creatorcontrib>Hwang, Wen-Ing</creatorcontrib><creatorcontrib>Huang, Han Hsiang</creatorcontrib><creatorcontrib>Wu, Yu-Jen</creatorcontrib><title>Proteomic investigation of anti-tumor activities exerted by sinularin against A2058 melanoma cells</title><title>Electrophoresis</title><addtitle>ELECTROPHORESIS</addtitle><description>The extracts from soft corals have been increasingly investigated for biomedical and therapeutic purposes. The aim of this study is to examine and analyze the anti‐tumor effects of the genus Sinularia extract sinularin on A2058 melanoma cells using MTT assay, cell migration assay, wound healing assay, flow cytometric analysis, and proteomic analysis. Sinularin dose‐dependently (1–5 μg/mL) inhibited melanoma cell proliferation while the treatment at identical concentrations suppressed cell migration. Sinularin dose‐dependently enhanced apoptotic melanoma cells and caused tumor cell accumulation at G2/M phase, indicating that sinularin exerts apoptosis‐induced and cell cycle‐delayed activities in A2058 melanoma cells. Comparative proteomic analysis was conducted to investigate the effects of sinularin at the molecular level by comparison between the protein profiling of melanoma cells treated with sinularin and without the treatment. Thirty‐five differential proteins (13 upregulated and 22 downregulated) concerning the treatment were identified by liquid chromatography‐tandem mass spectrometry. Proteomic data and Western blot displayed the levels of several tumor inhibitory or apoptosis‐associated proteins including annexin A1, voltage‐dependent anion‐selective channel protein 1 and prohibitin (upregulated), heat shock protein 60, heat shock protein beta‐1, and peroxiredoxin‐2 (downregulated) in A2058 melanoma cells exposed to sinularin. Increased expression of p53, cleaved‐caspase‐3, cleaved‐caspase‐8, cleaved‐caspase‐9, p21, and Bax and decreased expression of Bcl‐2 in sinularin‐treated melanoma cells suggest that the anti‐tumor activities of sinularin against melanoma cells are particularly correlated with these pro‐apoptotic factors. These data provide important information for the mechanisms of anti‐tumor effects of sinularin on melanoma cells and may be helpful for drug development and progression monitoring of human melanoma.</description><subject>Animals</subject><subject>Anthozoa - chemistry</subject><subject>Antineoplastic Agents, Phytogenic - chemistry</subject><subject>Antineoplastic Agents, Phytogenic - pharmacology</subject><subject>Apoptosis - drug effects</subject><subject>Blotting, Western</subject><subject>Cell Line, Tumor</subject><subject>Cell Movement - drug effects</subject><subject>Diterpenes - chemistry</subject><subject>Diterpenes - pharmacology</subject><subject>Dose-Response Relationship, Drug</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Flow Cytometry</subject><subject>Heterocyclic Compounds, 3-Ring - chemistry</subject><subject>Heterocyclic Compounds, 3-Ring - pharmacology</subject><subject>Humans</subject><subject>Melanoma - drug therapy</subject><subject>Melanoma - metabolism</subject><subject>Melanoma cells</subject><subject>Proteins - analysis</subject><subject>Proteins - classification</subject><subject>Proteins - metabolism</subject><subject>Proteome - analysis</subject><subject>Proteome - drug effects</subject><subject>Proteome - metabolism</subject><subject>Proteomic analysis</subject><subject>Proteomics</subject><subject>Reproducibility of Results</subject><subject>Sinularin</subject><issn>0173-0835</issn><issn>1522-2683</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1PGzEQhi3UClLKlWPlYy9L7fHnHhGitFHaIhXE0bKdWeSyH2HtpeTfd6PQnEajed7RzEPIOWcXnDH4gu0mXwDjcyM1HJEFVwAVaCvekQXjRlTMCnVCPuT8h81MLeUxOQFQohbcLEi4HYeCQ5ciTf0L5pIefUlDT4eG-r6kqkzdMFIfS3pJJWGm-IpjwTUNW5pTP7V-TD31jz71udBLYMrSDlvfD52nEds2fyTvG99mPHurp-T-6_Xd1bdq9evm-9XlqkpQS16BWOtGIdiAKoCWwTIba0RZhxh5VOhZHZpGGROjWhujPRgTjAZmdaNNLU7J5_3ezTg8T_Mrrkt5d4HvcZiy44wzEGCtmdFPb-gUOly7zZg6P27dfy8zIPfA39Ti9jDnzO2su511d7Durle3vyXXfI5V-1jKBV8PMT8-OW2EUe7h542Td6sfy-VSOCv-AcVqhM0</recordid><startdate>201204</startdate><enddate>201204</enddate><creator>Su, Tzu-Rong</creator><creator>Lin, Jen-Jie</creator><creator>Chiu, Chien-Chih</creator><creator>Chen, Jeff Yi-Fu</creator><creator>Su, Jui-Hsin</creator><creator>Cheng, Zhi-Jiao</creator><creator>Hwang, Wen-Ing</creator><creator>Huang, Han Hsiang</creator><creator>Wu, Yu-Jen</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>201204</creationdate><title>Proteomic investigation of anti-tumor activities exerted by sinularin against A2058 melanoma cells</title><author>Su, Tzu-Rong ; Lin, Jen-Jie ; Chiu, Chien-Chih ; Chen, Jeff Yi-Fu ; Su, Jui-Hsin ; Cheng, Zhi-Jiao ; Hwang, Wen-Ing ; Huang, Han Hsiang ; Wu, Yu-Jen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i2941-23d6f5e28be5b264b808c9ee49bcc1c5ea09bff577cc5d776a277b762086f6793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Anthozoa - chemistry</topic><topic>Antineoplastic Agents, Phytogenic - chemistry</topic><topic>Antineoplastic Agents, Phytogenic - pharmacology</topic><topic>Apoptosis - drug effects</topic><topic>Blotting, Western</topic><topic>Cell Line, Tumor</topic><topic>Cell Movement - drug effects</topic><topic>Diterpenes - chemistry</topic><topic>Diterpenes - pharmacology</topic><topic>Dose-Response Relationship, Drug</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Flow Cytometry</topic><topic>Heterocyclic Compounds, 3-Ring - chemistry</topic><topic>Heterocyclic Compounds, 3-Ring - pharmacology</topic><topic>Humans</topic><topic>Melanoma - drug therapy</topic><topic>Melanoma - metabolism</topic><topic>Melanoma cells</topic><topic>Proteins - analysis</topic><topic>Proteins - classification</topic><topic>Proteins - metabolism</topic><topic>Proteome - analysis</topic><topic>Proteome - drug effects</topic><topic>Proteome - metabolism</topic><topic>Proteomic analysis</topic><topic>Proteomics</topic><topic>Reproducibility of Results</topic><topic>Sinularin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Su, Tzu-Rong</creatorcontrib><creatorcontrib>Lin, Jen-Jie</creatorcontrib><creatorcontrib>Chiu, Chien-Chih</creatorcontrib><creatorcontrib>Chen, Jeff Yi-Fu</creatorcontrib><creatorcontrib>Su, Jui-Hsin</creatorcontrib><creatorcontrib>Cheng, Zhi-Jiao</creatorcontrib><creatorcontrib>Hwang, Wen-Ing</creatorcontrib><creatorcontrib>Huang, Han Hsiang</creatorcontrib><creatorcontrib>Wu, Yu-Jen</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Electrophoresis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Su, Tzu-Rong</au><au>Lin, Jen-Jie</au><au>Chiu, Chien-Chih</au><au>Chen, Jeff Yi-Fu</au><au>Su, Jui-Hsin</au><au>Cheng, Zhi-Jiao</au><au>Hwang, Wen-Ing</au><au>Huang, Han Hsiang</au><au>Wu, Yu-Jen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteomic investigation of anti-tumor activities exerted by sinularin against A2058 melanoma cells</atitle><jtitle>Electrophoresis</jtitle><addtitle>ELECTROPHORESIS</addtitle><date>2012-04</date><risdate>2012</risdate><volume>33</volume><issue>7</issue><spage>1139</spage><epage>1152</epage><pages>1139-1152</pages><issn>0173-0835</issn><eissn>1522-2683</eissn><abstract>The extracts from soft corals have been increasingly investigated for biomedical and therapeutic purposes. The aim of this study is to examine and analyze the anti‐tumor effects of the genus Sinularia extract sinularin on A2058 melanoma cells using MTT assay, cell migration assay, wound healing assay, flow cytometric analysis, and proteomic analysis. Sinularin dose‐dependently (1–5 μg/mL) inhibited melanoma cell proliferation while the treatment at identical concentrations suppressed cell migration. Sinularin dose‐dependently enhanced apoptotic melanoma cells and caused tumor cell accumulation at G2/M phase, indicating that sinularin exerts apoptosis‐induced and cell cycle‐delayed activities in A2058 melanoma cells. Comparative proteomic analysis was conducted to investigate the effects of sinularin at the molecular level by comparison between the protein profiling of melanoma cells treated with sinularin and without the treatment. Thirty‐five differential proteins (13 upregulated and 22 downregulated) concerning the treatment were identified by liquid chromatography‐tandem mass spectrometry. Proteomic data and Western blot displayed the levels of several tumor inhibitory or apoptosis‐associated proteins including annexin A1, voltage‐dependent anion‐selective channel protein 1 and prohibitin (upregulated), heat shock protein 60, heat shock protein beta‐1, and peroxiredoxin‐2 (downregulated) in A2058 melanoma cells exposed to sinularin. Increased expression of p53, cleaved‐caspase‐3, cleaved‐caspase‐8, cleaved‐caspase‐9, p21, and Bax and decreased expression of Bcl‐2 in sinularin‐treated melanoma cells suggest that the anti‐tumor activities of sinularin against melanoma cells are particularly correlated with these pro‐apoptotic factors. These data provide important information for the mechanisms of anti‐tumor effects of sinularin on melanoma cells and may be helpful for drug development and progression monitoring of human melanoma.</abstract><cop>Germany</cop><pub>Blackwell Publishing Ltd</pub><pmid>22539317</pmid><doi>10.1002/elps.201100462</doi><tpages>14</tpages></addata></record> |
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| subjects | Animals Anthozoa - chemistry Antineoplastic Agents, Phytogenic - chemistry Antineoplastic Agents, Phytogenic - pharmacology Apoptosis - drug effects Blotting, Western Cell Line, Tumor Cell Movement - drug effects Diterpenes - chemistry Diterpenes - pharmacology Dose-Response Relationship, Drug Electrophoresis, Gel, Two-Dimensional Flow Cytometry Heterocyclic Compounds, 3-Ring - chemistry Heterocyclic Compounds, 3-Ring - pharmacology Humans Melanoma - drug therapy Melanoma - metabolism Melanoma cells Proteins - analysis Proteins - classification Proteins - metabolism Proteome - analysis Proteome - drug effects Proteome - metabolism Proteomic analysis Proteomics Reproducibility of Results Sinularin |
| title | Proteomic investigation of anti-tumor activities exerted by sinularin against A2058 melanoma cells |
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