Bcl-2 protein inhibits oxysterol-induced apoptosis through suppressing CPP32-mediated pathway
Oxysterols are presumed to mediate cytotoxicity of oxidized LDL in atherosclerotic lesions. To elucidate its molecular mechanism, we established murine macrophage-like P388-D1 cells which over-express Bcl-2 protein by retrovirus-mediated gene transfer. Oxysterols (7-ketocholesterol, 25-hydroxycholes...
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| Veröffentlicht in: | FEBS letters 1997-07, Vol.411 (1), p.63-66 |
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| creator | Harada, Kenji Ishibashi, Shun Miyashita, Toshiyuki Osuga, Jun-ichi Yagyu, Hiroaki Ohashi, Ken Yazaki, Yoshio Yamada, Nobuhiro |
| description | Oxysterols are presumed to mediate cytotoxicity of oxidized LDL in atherosclerotic lesions. To elucidate its molecular mechanism, we established murine macrophage-like P388-D1 cells which over-express Bcl-2 protein by retrovirus-mediated gene transfer. Oxysterols (7-ketocholesterol, 25-hydroxycholesterol) induced nuclear condensation and oligonucleosomal DNA fragmentation, which were partially inhibited by Bcl-2 over-expression. Though CPP32 inhibitor suppressed the cell death in control cells, it showed no additive protection in the cells over-expressing Bcl-2. These findings indicate that oxysterols induce apoptosis via Bcl-2-inhibitable and -uninhibitable pathways, and the former depends on CPP32 activation. |
| doi_str_mv | 10.1016/S0014-5793(97)00662-5 |
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To elucidate its molecular mechanism, we established murine macrophage-like P388-D1 cells which over-express Bcl-2 protein by retrovirus-mediated gene transfer. Oxysterols (7-ketocholesterol, 25-hydroxycholesterol) induced nuclear condensation and oligonucleosomal DNA fragmentation, which were partially inhibited by Bcl-2 over-expression. Though CPP32 inhibitor suppressed the cell death in control cells, it showed no additive protection in the cells over-expressing Bcl-2. These findings indicate that oxysterols induce apoptosis via Bcl-2-inhibitable and -uninhibitable pathways, and the former depends on CPP32 activation.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(97)00662-5</identifier><identifier>PMID: 9247143</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>3-hydroxy-3-methylglutalyl coenzyme A ; Ac-DEVD-CHO ; acetyl-Asp-Glu-Val-Asp-CHO ; Animals ; Apoptosis ; Bcl-2 ; Caspase 3 ; Caspases ; Cell Line ; Cysteine Endopeptidases - metabolism ; Cysteine Proteinase Inhibitors - pharmacology ; Cytotoxicity ; HMG-CoA ; Hydroxycholesterols - antagonists & inhibitors ; Hydroxycholesterols - pharmacology ; ICE ; interleukin-1β converting enzyme ; Ketocholesterols - antagonists & inhibitors ; Ketocholesterols - pharmacology ; LDL ; low density lipoprotein ; Macrophages - cytology ; Macrophages - drug effects ; Mice ; Oligopeptides - pharmacology ; Oxysterol ; Proto-Oncogene Proteins c-bcl-2 - genetics ; Proto-Oncogene Proteins c-bcl-2 - metabolism</subject><ispartof>FEBS letters, 1997-07, Vol.411 (1), p.63-66</ispartof><rights>1997 Federation of European Biochemical Societies</rights><rights>FEBS Letters 411 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5385-bed4d4e2037239f867bab1904f1e6fb58e59dc36e92281aafb1f6939548b8a6b3</citedby><cites>FETCH-LOGICAL-c5385-bed4d4e2037239f867bab1904f1e6fb58e59dc36e92281aafb1f6939548b8a6b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2897%2900662-5$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579397006625$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9247143$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Harada, Kenji</creatorcontrib><creatorcontrib>Ishibashi, Shun</creatorcontrib><creatorcontrib>Miyashita, Toshiyuki</creatorcontrib><creatorcontrib>Osuga, Jun-ichi</creatorcontrib><creatorcontrib>Yagyu, Hiroaki</creatorcontrib><creatorcontrib>Ohashi, Ken</creatorcontrib><creatorcontrib>Yazaki, Yoshio</creatorcontrib><creatorcontrib>Yamada, Nobuhiro</creatorcontrib><title>Bcl-2 protein inhibits oxysterol-induced apoptosis through suppressing CPP32-mediated pathway</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Oxysterols are presumed to mediate cytotoxicity of oxidized LDL in atherosclerotic lesions. To elucidate its molecular mechanism, we established murine macrophage-like P388-D1 cells which over-express Bcl-2 protein by retrovirus-mediated gene transfer. Oxysterols (7-ketocholesterol, 25-hydroxycholesterol) induced nuclear condensation and oligonucleosomal DNA fragmentation, which were partially inhibited by Bcl-2 over-expression. Though CPP32 inhibitor suppressed the cell death in control cells, it showed no additive protection in the cells over-expressing Bcl-2. These findings indicate that oxysterols induce apoptosis via Bcl-2-inhibitable and -uninhibitable pathways, and the former depends on CPP32 activation.</description><subject>3-hydroxy-3-methylglutalyl coenzyme A</subject><subject>Ac-DEVD-CHO</subject><subject>acetyl-Asp-Glu-Val-Asp-CHO</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Bcl-2</subject><subject>Caspase 3</subject><subject>Caspases</subject><subject>Cell Line</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>Cytotoxicity</subject><subject>HMG-CoA</subject><subject>Hydroxycholesterols - antagonists & inhibitors</subject><subject>Hydroxycholesterols - pharmacology</subject><subject>ICE</subject><subject>interleukin-1β converting enzyme</subject><subject>Ketocholesterols - antagonists & inhibitors</subject><subject>Ketocholesterols - pharmacology</subject><subject>LDL</subject><subject>low density lipoprotein</subject><subject>Macrophages - cytology</subject><subject>Macrophages - drug effects</subject><subject>Mice</subject><subject>Oligopeptides - pharmacology</subject><subject>Oxysterol</subject><subject>Proto-Oncogene Proteins c-bcl-2 - genetics</subject><subject>Proto-Oncogene Proteins c-bcl-2 - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUtv1DAUhS0EKkPhJ1TKCsHC4Ef8WiE6ailSJSoBS2TZyU3HKBMH26HMv8fzULewsuxz7rn3fkbogpJ3lFD5_ishtMVCGf7GqLeESMmweIJWVCuOeSv1U7R6tDxHL3L-SepdU3OGzgxrFW35Cv247EbMmjnFAmFqwrQJPpTcxD-7XCDFEYepXzroGzfHucQcclM2KS73myYv85wg5zDdN-u7O87wFvrgSjXPrmwe3O4leja4McOr03mOvl9ffVvf4Nsvnz6vP97iTnAtsIe-7VtghCvGzaCl8s5TQ9qBghy80CBM33EJhjFNnRs8HaThRrTaayc9P0evj7l1j18L5GK3IXcwjm6CuGSrDFWcc1aN4mjsUsw5wWDnFLYu7Swldo_VHrDaPTNrlD1gtaLWXZwaLL4u-Vh14lj1m6P-EEbY_V-ovb66ZAdlLxh1eN63-nCMggrsd4Bkcxdgql8QEnTF9jH8Y9i_uq-cPg</recordid><startdate>19970707</startdate><enddate>19970707</enddate><creator>Harada, Kenji</creator><creator>Ishibashi, Shun</creator><creator>Miyashita, Toshiyuki</creator><creator>Osuga, Jun-ichi</creator><creator>Yagyu, Hiroaki</creator><creator>Ohashi, Ken</creator><creator>Yazaki, Yoshio</creator><creator>Yamada, Nobuhiro</creator><general>Elsevier B.V</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><scope>7X8</scope></search><sort><creationdate>19970707</creationdate><title>Bcl-2 protein inhibits oxysterol-induced apoptosis through suppressing CPP32-mediated pathway</title><author>Harada, Kenji ; 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To elucidate its molecular mechanism, we established murine macrophage-like P388-D1 cells which over-express Bcl-2 protein by retrovirus-mediated gene transfer. Oxysterols (7-ketocholesterol, 25-hydroxycholesterol) induced nuclear condensation and oligonucleosomal DNA fragmentation, which were partially inhibited by Bcl-2 over-expression. Though CPP32 inhibitor suppressed the cell death in control cells, it showed no additive protection in the cells over-expressing Bcl-2. These findings indicate that oxysterols induce apoptosis via Bcl-2-inhibitable and -uninhibitable pathways, and the former depends on CPP32 activation.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9247143</pmid><doi>10.1016/S0014-5793(97)00662-5</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | 3-hydroxy-3-methylglutalyl coenzyme A Ac-DEVD-CHO acetyl-Asp-Glu-Val-Asp-CHO Animals Apoptosis Bcl-2 Caspase 3 Caspases Cell Line Cysteine Endopeptidases - metabolism Cysteine Proteinase Inhibitors - pharmacology Cytotoxicity HMG-CoA Hydroxycholesterols - antagonists & inhibitors Hydroxycholesterols - pharmacology ICE interleukin-1β converting enzyme Ketocholesterols - antagonists & inhibitors Ketocholesterols - pharmacology LDL low density lipoprotein Macrophages - cytology Macrophages - drug effects Mice Oligopeptides - pharmacology Oxysterol Proto-Oncogene Proteins c-bcl-2 - genetics Proto-Oncogene Proteins c-bcl-2 - metabolism |
| title | Bcl-2 protein inhibits oxysterol-induced apoptosis through suppressing CPP32-mediated pathway |
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