Histone deacetylase inhibitors such as sodium butyrate and trichostatin A induce apoptosis through an increase of the bcl-2-related protein Bad
The effects of sodium butyrate (SB) and trichostatin A (TSA) on cell proliferation andapoptosis against human glioma T98G, U251MG, and U877MG cells were investigated. Upon exposure to either SB or TSA, cell proliferation was reduced, and apoptosis detected by DNA fragmentation analysis and the cleav...
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| Veröffentlicht in: | Brain tumor pathology 2001-09, Vol.18 (2), p.109-114 |
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| creator | Sawa, H Murakami, H Ohshima, Y Sugino, T Nakajyo, T Kisanuki, T Tamura, Y Satone, A Ide, W Hashimoto, I Kamada, H |
| description | The effects of sodium butyrate (SB) and trichostatin A (TSA) on cell proliferation andapoptosis against human glioma T98G, U251MG, and U877MG cells were investigated. Upon exposure to either SB or TSA, cell proliferation was reduced, and apoptosis detected by DNA fragmentation analysis and the cleavage of CPP32 was induced. Previously, we reported that SB increased the expression levels of p21 (WAF-1) and inhibited G1-S transition of the cell cycle. In this study, we showed that TSA also increased p21 expression, suggesting that histone deacetylase (HDAC) inhibitors may up-regulate p21 protein in common and thus arrest proliferation in the G1 phase of the cell cycle. To further determine the underlying molecular mechanisms of apoptosis with either SB or TSA treatment, we studied the expression levels of apoptosis-related proteins in human glioma cells. SB increased the expression of the Bad protein, although the expression of Bcl-2, Bcl-xL, Bax, and Fas was not changed by theaddition of SB. TSA treatment also up-regulated the expression of Bad protein. The results suggest that HDAC inhibitors such as SB and TSA induce apoptosis through an increase in Bad protein in human glioma cells in vitro. |
| doi_str_mv | 10.1007/BF02479423 |
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Upon exposure to either SB or TSA, cell proliferation was reduced, and apoptosis detected by DNA fragmentation analysis and the cleavage of CPP32 was induced. Previously, we reported that SB increased the expression levels of p21 (WAF-1) and inhibited G1-S transition of the cell cycle. In this study, we showed that TSA also increased p21 expression, suggesting that histone deacetylase (HDAC) inhibitors may up-regulate p21 protein in common and thus arrest proliferation in the G1 phase of the cell cycle. To further determine the underlying molecular mechanisms of apoptosis with either SB or TSA treatment, we studied the expression levels of apoptosis-related proteins in human glioma cells. SB increased the expression of the Bad protein, although the expression of Bcl-2, Bcl-xL, Bax, and Fas was not changed by theaddition of SB. TSA treatment also up-regulated the expression of Bad protein. The results suggest that HDAC inhibitors such as SB and TSA induce apoptosis through an increase in Bad protein in human glioma cells in vitro.</description><identifier>ISSN: 1433-7398</identifier><identifier>EISSN: 1861-387X</identifier><identifier>DOI: 10.1007/BF02479423</identifier><identifier>PMID: 11908866</identifier><language>eng</language><publisher>Japan: Springer Nature B.V</publisher><subject>Apoptosis ; Apoptosis - drug effects ; Brain Neoplasms - pathology ; Butyrates - pharmacology ; Cell cycle ; Cell Division - drug effects ; Cell growth ; Cell Line, Tumor - drug effects ; Cell Line, Tumor - metabolism ; Enzyme Inhibitors - pharmacology ; Gene Expression Regulation, Neoplastic - drug effects ; Glioblastoma - pathology ; Histone Deacetylase Inhibitors - pharmacology ; Humans ; Hydroxamic Acids - pharmacology ; Neoplasm Proteins - biosynthesis ; Neoplasm Proteins - genetics ; Nerve Tissue Proteins - biosynthesis ; Nerve Tissue Proteins - genetics ; Proteins ; Sodium - pharmacology</subject><ispartof>Brain tumor pathology, 2001-09, Vol.18 (2), p.109-114</ispartof><rights>The Japan Society of Brain Tumor Pathology 2001.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c323t-b4c6ed2d50f765e6fb407444ba10771d0632601e4697fb3670f3bbab264f67253</citedby><cites>FETCH-LOGICAL-c323t-b4c6ed2d50f765e6fb407444ba10771d0632601e4697fb3670f3bbab264f67253</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.proquest.com/docview/2917927360?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,776,780,21367,27901,27902,33721,33722,43781</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11908866$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sawa, H</creatorcontrib><creatorcontrib>Murakami, H</creatorcontrib><creatorcontrib>Ohshima, Y</creatorcontrib><creatorcontrib>Sugino, T</creatorcontrib><creatorcontrib>Nakajyo, T</creatorcontrib><creatorcontrib>Kisanuki, T</creatorcontrib><creatorcontrib>Tamura, Y</creatorcontrib><creatorcontrib>Satone, A</creatorcontrib><creatorcontrib>Ide, W</creatorcontrib><creatorcontrib>Hashimoto, I</creatorcontrib><creatorcontrib>Kamada, H</creatorcontrib><title>Histone deacetylase inhibitors such as sodium butyrate and trichostatin A induce apoptosis through an increase of the bcl-2-related protein Bad</title><title>Brain tumor pathology</title><addtitle>Brain Tumor Pathol</addtitle><description>The effects of sodium butyrate (SB) and trichostatin A (TSA) on cell proliferation andapoptosis against human glioma T98G, U251MG, and U877MG cells were investigated. 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The results suggest that HDAC inhibitors such as SB and TSA induce apoptosis through an increase in Bad protein in human glioma cells in vitro.</description><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Brain Neoplasms - pathology</subject><subject>Butyrates - pharmacology</subject><subject>Cell cycle</subject><subject>Cell Division - drug effects</subject><subject>Cell growth</subject><subject>Cell Line, Tumor - drug effects</subject><subject>Cell Line, Tumor - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Gene Expression Regulation, Neoplastic - drug effects</subject><subject>Glioblastoma - pathology</subject><subject>Histone Deacetylase Inhibitors - pharmacology</subject><subject>Humans</subject><subject>Hydroxamic Acids - pharmacology</subject><subject>Neoplasm Proteins - biosynthesis</subject><subject>Neoplasm Proteins - genetics</subject><subject>Nerve Tissue Proteins - biosynthesis</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Proteins</subject><subject>Sodium - pharmacology</subject><issn>1433-7398</issn><issn>1861-387X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kclqHDEQhoVx8JZc_ABBEIgh0Im2kbqPYxPHAUMuCeTWaKn2yPS0JloO8xR55ZTxgCEHn0qovvpE6SfkkrPPnDHz5fqWCWUGJeQROeO95p3sze9jPCspOyOH_pScl_LImFLM8BNyyvnA-l7rM_L3LpaaFqABrIe6n20BGpdNdLGmXGhpfkMt1hRi21LX6j7bCtQugdYc_SaVamtc6BqnQvPY2aVdTSUWWjc5tQccX7DnMzyp04TXQJ2fO9FlmNEV6C6nCui4tuEteTPZucC7Q70gv26__ry56-5_fPt-s77vvBSydk55DUGEFZuMXoGeHG6mlHKWM2N4YFoKzTgoPZjJSW3YJJ2zTmg1aSNW8oJcPXvx7T8NSh23sXiYZ7tAamU0Uhqm-5VG8uOrpMAvFUIYBD_8Bz6mlhfcYhQDNwMimiH16ZnyOZWSYRp3OW5t3o-cjU9xji9xIvz-oGxuC-EFPeQn_wFXOpqe</recordid><startdate>20010901</startdate><enddate>20010901</enddate><creator>Sawa, H</creator><creator>Murakami, H</creator><creator>Ohshima, Y</creator><creator>Sugino, T</creator><creator>Nakajyo, T</creator><creator>Kisanuki, T</creator><creator>Tamura, Y</creator><creator>Satone, A</creator><creator>Ide, W</creator><creator>Hashimoto, I</creator><creator>Kamada, H</creator><general>Springer Nature B.V</general><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>7X7</scope><scope>7XB</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>M0S</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>7TK</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20010901</creationdate><title>Histone deacetylase inhibitors such as sodium butyrate and trichostatin A induce apoptosis through an increase of the bcl-2-related protein Bad</title><author>Sawa, H ; Murakami, H ; Ohshima, Y ; Sugino, T ; Nakajyo, T ; Kisanuki, T ; Tamura, Y ; Satone, A ; Ide, W ; Hashimoto, I ; Kamada, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c323t-b4c6ed2d50f765e6fb407444ba10771d0632601e4697fb3670f3bbab264f67253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Brain Neoplasms - pathology</topic><topic>Butyrates - pharmacology</topic><topic>Cell cycle</topic><topic>Cell Division - drug effects</topic><topic>Cell growth</topic><topic>Cell Line, Tumor - drug effects</topic><topic>Cell Line, Tumor - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Gene Expression Regulation, Neoplastic - drug effects</topic><topic>Glioblastoma - pathology</topic><topic>Histone Deacetylase Inhibitors - pharmacology</topic><topic>Humans</topic><topic>Hydroxamic Acids - pharmacology</topic><topic>Neoplasm Proteins - biosynthesis</topic><topic>Neoplasm Proteins - genetics</topic><topic>Nerve Tissue Proteins - biosynthesis</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Proteins</topic><topic>Sodium - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sawa, H</creatorcontrib><creatorcontrib>Murakami, H</creatorcontrib><creatorcontrib>Ohshima, Y</creatorcontrib><creatorcontrib>Sugino, T</creatorcontrib><creatorcontrib>Nakajyo, T</creatorcontrib><creatorcontrib>Kisanuki, T</creatorcontrib><creatorcontrib>Tamura, Y</creatorcontrib><creatorcontrib>Satone, A</creatorcontrib><creatorcontrib>Ide, W</creatorcontrib><creatorcontrib>Hashimoto, I</creatorcontrib><creatorcontrib>Kamada, H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest One Psychology</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Brain tumor pathology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sawa, H</au><au>Murakami, H</au><au>Ohshima, Y</au><au>Sugino, T</au><au>Nakajyo, T</au><au>Kisanuki, T</au><au>Tamura, Y</au><au>Satone, A</au><au>Ide, W</au><au>Hashimoto, I</au><au>Kamada, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Histone deacetylase inhibitors such as sodium butyrate and trichostatin A induce apoptosis through an increase of the bcl-2-related protein Bad</atitle><jtitle>Brain tumor pathology</jtitle><addtitle>Brain Tumor Pathol</addtitle><date>2001-09-01</date><risdate>2001</risdate><volume>18</volume><issue>2</issue><spage>109</spage><epage>114</epage><pages>109-114</pages><issn>1433-7398</issn><eissn>1861-387X</eissn><abstract>The effects of sodium butyrate (SB) and trichostatin A (TSA) on cell proliferation andapoptosis against human glioma T98G, U251MG, and U877MG cells were investigated. Upon exposure to either SB or TSA, cell proliferation was reduced, and apoptosis detected by DNA fragmentation analysis and the cleavage of CPP32 was induced. Previously, we reported that SB increased the expression levels of p21 (WAF-1) and inhibited G1-S transition of the cell cycle. In this study, we showed that TSA also increased p21 expression, suggesting that histone deacetylase (HDAC) inhibitors may up-regulate p21 protein in common and thus arrest proliferation in the G1 phase of the cell cycle. To further determine the underlying molecular mechanisms of apoptosis with either SB or TSA treatment, we studied the expression levels of apoptosis-related proteins in human glioma cells. SB increased the expression of the Bad protein, although the expression of Bcl-2, Bcl-xL, Bax, and Fas was not changed by theaddition of SB. TSA treatment also up-regulated the expression of Bad protein. The results suggest that HDAC inhibitors such as SB and TSA induce apoptosis through an increase in Bad protein in human glioma cells in vitro.</abstract><cop>Japan</cop><pub>Springer Nature B.V</pub><pmid>11908866</pmid><doi>10.1007/BF02479423</doi><tpages>6</tpages></addata></record> |
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| ispartof | Brain tumor pathology, 2001-09, Vol.18 (2), p.109-114 |
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| subjects | Apoptosis Apoptosis - drug effects Brain Neoplasms - pathology Butyrates - pharmacology Cell cycle Cell Division - drug effects Cell growth Cell Line, Tumor - drug effects Cell Line, Tumor - metabolism Enzyme Inhibitors - pharmacology Gene Expression Regulation, Neoplastic - drug effects Glioblastoma - pathology Histone Deacetylase Inhibitors - pharmacology Humans Hydroxamic Acids - pharmacology Neoplasm Proteins - biosynthesis Neoplasm Proteins - genetics Nerve Tissue Proteins - biosynthesis Nerve Tissue Proteins - genetics Proteins Sodium - pharmacology |
| title | Histone deacetylase inhibitors such as sodium butyrate and trichostatin A induce apoptosis through an increase of the bcl-2-related protein Bad |
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