p53 triggers apoptosis in oncogene-expressing fibroblasts by the induction of Noxa and mitochondrial Bax translocation
The mechanism of p53-dependent apoptosis is still only partly defined. Using early-passage embryonic fibroblasts (MEF) from wild-type (wt), p53 −/− and bax −/− mice, we observe a p53-dependent translocation of Bax to the mitochondria and a release of mitochondrial Cytochrome c during stress-induced...
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| Veröffentlicht in: | Cell death and differentiation 2003-04, Vol.10 (4), p.451-460 |
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| creator | Schuler, M Maurer, U Goldstein, J C Breitenbücher, F Hoffarth, S Waterhouse, N J Green, D R |
| description | The mechanism of p53-dependent apoptosis is still only partly defined. Using early-passage embryonic fibroblasts (MEF) from wild-type (wt), p53
−/−
and bax
−/−
mice, we observe a p53-dependent translocation of Bax to the mitochondria and a release of mitochondrial Cytochrome
c
during stress-induced apoptosis. These events proceed independent of zVAD-inhibitable caspase activation, are not prevented by dominant negative FADD (DN-FADD), but are negatively regulated by Mdm-2. Bcl-x
L
expression prevents the release of mitochondrial Cytochrome
c
and apoptosis, but not Bax translocation. At a single-cell level, enforced expression of p53 is sufficient to induce Bax translocation and Cytochrome
c
release. Real-time RT-PCR analysis reveals a significant induction of RNA expression of
Noxa
and
Bax
in p53
+/+
, but not in p53
−/−
MEF. Noxa protein expression becomes detectable prior to Bax translocation, and downregulation of endogenous
Noxa
by RNA interference protects wt MEF against p53-dependent apoptosis. Hence, in oncogene-expressing MEF p53 induces apoptosis by BH3 protein-dependent caspase activation. |
| doi_str_mv | 10.1038/sj.cdd.4401180 |
| format | Article |
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−/−
and bax
−/−
mice, we observe a p53-dependent translocation of Bax to the mitochondria and a release of mitochondrial Cytochrome
c
during stress-induced apoptosis. These events proceed independent of zVAD-inhibitable caspase activation, are not prevented by dominant negative FADD (DN-FADD), but are negatively regulated by Mdm-2. Bcl-x
L
expression prevents the release of mitochondrial Cytochrome
c
and apoptosis, but not Bax translocation. At a single-cell level, enforced expression of p53 is sufficient to induce Bax translocation and Cytochrome
c
release. Real-time RT-PCR analysis reveals a significant induction of RNA expression of
Noxa
and
Bax
in p53
+/+
, but not in p53
−/−
MEF. Noxa protein expression becomes detectable prior to Bax translocation, and downregulation of endogenous
Noxa
by RNA interference protects wt MEF against p53-dependent apoptosis. Hence, in oncogene-expressing MEF p53 induces apoptosis by BH3 protein-dependent caspase activation.</description><identifier>ISSN: 1350-9047</identifier><identifier>EISSN: 1476-5403</identifier><identifier>DOI: 10.1038/sj.cdd.4401180</identifier><identifier>PMID: 12719722</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adaptor Proteins, Signal Transducing ; Animals ; Apoptosis ; Apoptosis - genetics ; bcl-2-Associated X Protein ; Biochemistry ; Biomedical and Life Sciences ; Carrier Proteins - genetics ; Caspases - metabolism ; Cell Biology ; Cell cycle ; Cell Cycle Analysis ; Cell death ; Cells, Cultured ; Cytochrome ; Cytochrome c Group - metabolism ; Down-Regulation - drug effects ; Down-Regulation - genetics ; Enzyme Inhibitors - pharmacology ; Fas-Associated Death Domain Protein ; Fetus ; Fibroblasts ; Fibroblasts - cytology ; Fibroblasts - enzymology ; Gene Expression Regulation - genetics ; Genes ; Immunology ; Life Sciences ; Localization ; Mice ; Mice, Knockout ; Mitochondria ; Mitochondria - enzymology ; Mitochondria - genetics ; Mutation ; original-paper ; Protein Transport - drug effects ; Protein Transport - physiology ; Proteins ; Proto-Oncogene Proteins - deficiency ; Proto-Oncogene Proteins - genetics ; Proto-Oncogene Proteins c-bcl-2 - biosynthesis ; Proto-Oncogene Proteins c-bcl-2 - genetics ; Stem Cells ; Tumor Suppressor Protein p53 - deficiency ; Tumor Suppressor Protein p53 - genetics</subject><ispartof>Cell death and differentiation, 2003-04, Vol.10 (4), p.451-460</ispartof><rights>Springer Nature Limited 2003</rights><rights>Copyright Nature Publishing Group Apr 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c429t-efec7ed12eac902863187f7f1244b404724eba15c7d5e44dde201c679f20b22d3</citedby><cites>FETCH-LOGICAL-c429t-efec7ed12eac902863187f7f1244b404724eba15c7d5e44dde201c679f20b22d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/sj.cdd.4401180$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/sj.cdd.4401180$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12719722$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schuler, M</creatorcontrib><creatorcontrib>Maurer, U</creatorcontrib><creatorcontrib>Goldstein, J C</creatorcontrib><creatorcontrib>Breitenbücher, F</creatorcontrib><creatorcontrib>Hoffarth, S</creatorcontrib><creatorcontrib>Waterhouse, N J</creatorcontrib><creatorcontrib>Green, D R</creatorcontrib><title>p53 triggers apoptosis in oncogene-expressing fibroblasts by the induction of Noxa and mitochondrial Bax translocation</title><title>Cell death and differentiation</title><addtitle>Cell Death Differ</addtitle><addtitle>Cell Death Differ</addtitle><description>The mechanism of p53-dependent apoptosis is still only partly defined. Using early-passage embryonic fibroblasts (MEF) from wild-type (wt), p53
−/−
and bax
−/−
mice, we observe a p53-dependent translocation of Bax to the mitochondria and a release of mitochondrial Cytochrome
c
during stress-induced apoptosis. These events proceed independent of zVAD-inhibitable caspase activation, are not prevented by dominant negative FADD (DN-FADD), but are negatively regulated by Mdm-2. Bcl-x
L
expression prevents the release of mitochondrial Cytochrome
c
and apoptosis, but not Bax translocation. At a single-cell level, enforced expression of p53 is sufficient to induce Bax translocation and Cytochrome
c
release. Real-time RT-PCR analysis reveals a significant induction of RNA expression of
Noxa
and
Bax
in p53
+/+
, but not in p53
−/−
MEF. Noxa protein expression becomes detectable prior to Bax translocation, and downregulation of endogenous
Noxa
by RNA interference protects wt MEF against p53-dependent apoptosis. Hence, in oncogene-expressing MEF p53 induces apoptosis by BH3 protein-dependent caspase activation.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis - genetics</subject><subject>bcl-2-Associated X Protein</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Carrier Proteins - genetics</subject><subject>Caspases - metabolism</subject><subject>Cell Biology</subject><subject>Cell cycle</subject><subject>Cell Cycle Analysis</subject><subject>Cell death</subject><subject>Cells, Cultured</subject><subject>Cytochrome</subject><subject>Cytochrome c Group - metabolism</subject><subject>Down-Regulation - drug effects</subject><subject>Down-Regulation - genetics</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Fas-Associated Death Domain Protein</subject><subject>Fetus</subject><subject>Fibroblasts</subject><subject>Fibroblasts - cytology</subject><subject>Fibroblasts - enzymology</subject><subject>Gene Expression Regulation - genetics</subject><subject>Genes</subject><subject>Immunology</subject><subject>Life Sciences</subject><subject>Localization</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Mitochondria</subject><subject>Mitochondria - enzymology</subject><subject>Mitochondria - genetics</subject><subject>Mutation</subject><subject>original-paper</subject><subject>Protein Transport - drug effects</subject><subject>Protein Transport - physiology</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins - deficiency</subject><subject>Proto-Oncogene Proteins - genetics</subject><subject>Proto-Oncogene Proteins c-bcl-2 - biosynthesis</subject><subject>Proto-Oncogene Proteins c-bcl-2 - genetics</subject><subject>Stem Cells</subject><subject>Tumor Suppressor Protein p53 - deficiency</subject><subject>Tumor Suppressor Protein p53 - genetics</subject><issn>1350-9047</issn><issn>1476-5403</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkU2LFDEQhoMo7rp69SjBg7eerXz0pPuoi1-w6EXPIZ1Uz2boSdpUt8z-e7PMwIIgnhLIU2_x5mHstYCNANVd037jQ9hoDUJ08IRdCm22TatBPa131ULTgzYX7AXRHgC2pt8-ZxdCGtEbKS_Z77lVfClxt8NC3M15XjJF4jHxnHzeYcIGj3NBoph2fIxDycPkaCE-3PPlDisZVr_EXAdG_i0fHXcp8ENcsr_LKZToJv7BHesSl2jK3j2wL9mz0U2Er87nFfv56eOPmy_N7ffPX2_e3zZey35pcERvMAiJzvcgu60SnRnNKKTWg67FpMbBidab0KLWIaAE4WvJUcIgZVBX7N0pdy7514q02EMkj9PkEuaVrFHSQKfUf0HRdQAtmAq-_Qvc57WkWsJKYYwS9Y8rtDlBvmSigqOdSzy4cm8F2Advlva2erNnb3XgzTl1HQ4YHvGzqApcnwCqT6nKelz7j8g_k2alXw</recordid><startdate>20030401</startdate><enddate>20030401</enddate><creator>Schuler, M</creator><creator>Maurer, U</creator><creator>Goldstein, J C</creator><creator>Breitenbücher, F</creator><creator>Hoffarth, S</creator><creator>Waterhouse, N J</creator><creator>Green, D R</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</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>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</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>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7TO</scope><scope>7X8</scope></search><sort><creationdate>20030401</creationdate><title>p53 triggers apoptosis in oncogene-expressing fibroblasts by the induction of Noxa and mitochondrial Bax translocation</title><author>Schuler, M ; Maurer, U ; Goldstein, J C ; Breitenbücher, F ; Hoffarth, S ; Waterhouse, N J ; Green, D R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c429t-efec7ed12eac902863187f7f1244b404724eba15c7d5e44dde201c679f20b22d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Apoptosis - genetics</topic><topic>bcl-2-Associated X Protein</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Carrier Proteins - genetics</topic><topic>Caspases - metabolism</topic><topic>Cell Biology</topic><topic>Cell cycle</topic><topic>Cell Cycle Analysis</topic><topic>Cell death</topic><topic>Cells, Cultured</topic><topic>Cytochrome</topic><topic>Cytochrome c Group - metabolism</topic><topic>Down-Regulation - drug effects</topic><topic>Down-Regulation - genetics</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Fas-Associated Death Domain Protein</topic><topic>Fetus</topic><topic>Fibroblasts</topic><topic>Fibroblasts - cytology</topic><topic>Fibroblasts - enzymology</topic><topic>Gene Expression Regulation - genetics</topic><topic>Genes</topic><topic>Immunology</topic><topic>Life Sciences</topic><topic>Localization</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Mitochondria</topic><topic>Mitochondria - enzymology</topic><topic>Mitochondria - genetics</topic><topic>Mutation</topic><topic>original-paper</topic><topic>Protein Transport - drug effects</topic><topic>Protein Transport - physiology</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins - deficiency</topic><topic>Proto-Oncogene Proteins - genetics</topic><topic>Proto-Oncogene Proteins c-bcl-2 - biosynthesis</topic><topic>Proto-Oncogene Proteins c-bcl-2 - genetics</topic><topic>Stem Cells</topic><topic>Tumor Suppressor Protein p53 - deficiency</topic><topic>Tumor Suppressor Protein p53 - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schuler, M</creatorcontrib><creatorcontrib>Maurer, U</creatorcontrib><creatorcontrib>Goldstein, J C</creatorcontrib><creatorcontrib>Breitenbücher, F</creatorcontrib><creatorcontrib>Hoffarth, S</creatorcontrib><creatorcontrib>Waterhouse, N J</creatorcontrib><creatorcontrib>Green, D R</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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</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)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</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 Central China</collection><collection>Genetics Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell death and differentiation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schuler, M</au><au>Maurer, U</au><au>Goldstein, J C</au><au>Breitenbücher, F</au><au>Hoffarth, S</au><au>Waterhouse, N J</au><au>Green, D R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>p53 triggers apoptosis in oncogene-expressing fibroblasts by the induction of Noxa and mitochondrial Bax translocation</atitle><jtitle>Cell death and differentiation</jtitle><stitle>Cell Death Differ</stitle><addtitle>Cell Death Differ</addtitle><date>2003-04-01</date><risdate>2003</risdate><volume>10</volume><issue>4</issue><spage>451</spage><epage>460</epage><pages>451-460</pages><issn>1350-9047</issn><eissn>1476-5403</eissn><abstract>The mechanism of p53-dependent apoptosis is still only partly defined. Using early-passage embryonic fibroblasts (MEF) from wild-type (wt), p53
−/−
and bax
−/−
mice, we observe a p53-dependent translocation of Bax to the mitochondria and a release of mitochondrial Cytochrome
c
during stress-induced apoptosis. These events proceed independent of zVAD-inhibitable caspase activation, are not prevented by dominant negative FADD (DN-FADD), but are negatively regulated by Mdm-2. Bcl-x
L
expression prevents the release of mitochondrial Cytochrome
c
and apoptosis, but not Bax translocation. At a single-cell level, enforced expression of p53 is sufficient to induce Bax translocation and Cytochrome
c
release. Real-time RT-PCR analysis reveals a significant induction of RNA expression of
Noxa
and
Bax
in p53
+/+
, but not in p53
−/−
MEF. Noxa protein expression becomes detectable prior to Bax translocation, and downregulation of endogenous
Noxa
by RNA interference protects wt MEF against p53-dependent apoptosis. Hence, in oncogene-expressing MEF p53 induces apoptosis by BH3 protein-dependent caspase activation.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>12719722</pmid><doi>10.1038/sj.cdd.4401180</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1350-9047 |
| ispartof | Cell death and differentiation, 2003-04, Vol.10 (4), p.451-460 |
| issn | 1350-9047 1476-5403 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73270833 |
| source | MEDLINE; Springer Nature - Complete Springer Journals; EZB Electronic Journals Library |
| subjects | Adaptor Proteins, Signal Transducing Animals Apoptosis Apoptosis - genetics bcl-2-Associated X Protein Biochemistry Biomedical and Life Sciences Carrier Proteins - genetics Caspases - metabolism Cell Biology Cell cycle Cell Cycle Analysis Cell death Cells, Cultured Cytochrome Cytochrome c Group - metabolism Down-Regulation - drug effects Down-Regulation - genetics Enzyme Inhibitors - pharmacology Fas-Associated Death Domain Protein Fetus Fibroblasts Fibroblasts - cytology Fibroblasts - enzymology Gene Expression Regulation - genetics Genes Immunology Life Sciences Localization Mice Mice, Knockout Mitochondria Mitochondria - enzymology Mitochondria - genetics Mutation original-paper Protein Transport - drug effects Protein Transport - physiology Proteins Proto-Oncogene Proteins - deficiency Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins c-bcl-2 - biosynthesis Proto-Oncogene Proteins c-bcl-2 - genetics Stem Cells Tumor Suppressor Protein p53 - deficiency Tumor Suppressor Protein p53 - genetics |
| title | p53 triggers apoptosis in oncogene-expressing fibroblasts by the induction of Noxa and mitochondrial Bax translocation |
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