Heat shock protein Hsp72 plays an essential role in Her2-induced mammary tumorigenesis
The major heat shock protein Hsp72 is expressed at elevated levels in many human cancers and its expression correlates with tumor progression. Here, we investigated the role of Hsp72 in Her2 oncogene-induced neoplastic transformation and tumorigenesis. Expression of Her2 in untransformed MCF10A mamm...
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| Veröffentlicht in: | Oncogene 2011-06, Vol.30 (25), p.2836-2845 |
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| creator | Meng, L Hunt, C Yaglom, J A Gabai, V L Sherman, M Y |
| description | The major heat shock protein Hsp72 is expressed at elevated levels in many human cancers and its expression correlates with tumor progression. Here, we investigated the role of Hsp72 in Her2 oncogene-induced neoplastic transformation and tumorigenesis. Expression of Her2 in untransformed MCF10A mammary epithelial cells caused transformation, as judged by foci formation in culture and tumorigenesis in xenografts. However, expression of Her2 in Hsp72-depleted cells failed to induce transformation. The anti-tumorigenic effects of Hsp72 downregulation were associated with cellular senescence because of accumulation of p21 and depletion of survivin. Accordingly, either knockdown of p21 or expression of survivin reversed this senescence process. Further, we developed an animal model of Hsp72-dependent breast cancer associated with expression of Her2. Knockout (KO) of Hsp72 almost completely suppressed tumorigenesis in the MMTVneu breast cancer mouse model. In young Hsp72 KO mice, expression of Her2 instead of mammary tissue hyperplasia led to suppression of duct development and blocked alveolar budding. These effects were due to massive cell senescence in mammary tissue, which was associated with upregulation of p21 and downregulation of survivin. Therefore, Hsp72 has an essential role in Her2-induced tumorigenesis by regulating oncogene-induced senescence pathways. |
| doi_str_mv | 10.1038/onc.2011.5 |
| format | Article |
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Here, we investigated the role of Hsp72 in Her2 oncogene-induced neoplastic transformation and tumorigenesis. Expression of Her2 in untransformed MCF10A mammary epithelial cells caused transformation, as judged by foci formation in culture and tumorigenesis in xenografts. However, expression of Her2 in Hsp72-depleted cells failed to induce transformation. The anti-tumorigenic effects of Hsp72 downregulation were associated with cellular senescence because of accumulation of p21 and depletion of survivin. Accordingly, either knockdown of p21 or expression of survivin reversed this senescence process. Further, we developed an animal model of Hsp72-dependent breast cancer associated with expression of Her2. Knockout (KO) of Hsp72 almost completely suppressed tumorigenesis in the MMTVneu breast cancer mouse model. In young Hsp72 KO mice, expression of Her2 instead of mammary tissue hyperplasia led to suppression of duct development and blocked alveolar budding. These effects were due to massive cell senescence in mammary tissue, which was associated with upregulation of p21 and downregulation of survivin. Therefore, Hsp72 has an essential role in Her2-induced tumorigenesis by regulating oncogene-induced senescence pathways.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/onc.2011.5</identifier><identifier>PMID: 21297664</identifier><identifier>CODEN: ONCNES</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/67/395 ; 631/80/509 ; 692/420/755 ; 692/699/67/1347 ; Alveoli ; Analysis ; Animal models ; Animals ; Apoptosis ; Biological and medical sciences ; Blotting, Western ; Breast cancer ; Cell Biology ; Cell culture ; Cell Line, Tumor ; Cell physiology ; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes ; Cyclin-dependent kinase inhibitor p21 ; Development and progression ; Epithelial cells ; ErbB-2 protein ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Genetic aspects ; Heat shock proteins ; HSP72 Heat-Shock Proteins - physiology ; Hsp72 protein ; Human Genetics ; Hyperplasia ; Immunohistochemistry ; Internal Medicine ; Mammary gland ; Mammary Neoplasms, Experimental - pathology ; Mammary Neoplasms, Experimental - physiopathology ; Mammography ; Medicine ; Medicine & Public Health ; Mice ; Mice, Knockout ; Molecular and cellular biology ; Oncology ; original-article ; Receptor, ErbB-2 - physiology ; Senescence ; Survivin ; Tumorigenesis ; Tumors ; Xenograft Model Antitumor Assays ; Xenografts</subject><ispartof>Oncogene, 2011-06, Vol.30 (25), p.2836-2845</ispartof><rights>Macmillan Publishers Limited 2011</rights><rights>2015 INIST-CNRS</rights><rights>COPYRIGHT 2011 Nature Publishing Group</rights><rights>Macmillan Publishers Limited 2011.</rights><rights>Copyright Nature Publishing Group Jun 23, 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c686t-bedbc03f89564eba548ac723368239a1ebae2f28c0ce9816a66ca1a45be448c93</citedby><cites>FETCH-LOGICAL-c686t-bedbc03f89564eba548ac723368239a1ebae2f28c0ce9816a66ca1a45be448c93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,781,785,886,2728,27926,27927</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24302777$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21297664$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meng, L</creatorcontrib><creatorcontrib>Hunt, C</creatorcontrib><creatorcontrib>Yaglom, J A</creatorcontrib><creatorcontrib>Gabai, V L</creatorcontrib><creatorcontrib>Sherman, M Y</creatorcontrib><title>Heat shock protein Hsp72 plays an essential role in Her2-induced mammary tumorigenesis</title><title>Oncogene</title><addtitle>Oncogene</addtitle><addtitle>Oncogene</addtitle><description>The major heat shock protein Hsp72 is expressed at elevated levels in many human cancers and its expression correlates with tumor progression. Here, we investigated the role of Hsp72 in Her2 oncogene-induced neoplastic transformation and tumorigenesis. Expression of Her2 in untransformed MCF10A mammary epithelial cells caused transformation, as judged by foci formation in culture and tumorigenesis in xenografts. However, expression of Her2 in Hsp72-depleted cells failed to induce transformation. The anti-tumorigenic effects of Hsp72 downregulation were associated with cellular senescence because of accumulation of p21 and depletion of survivin. Accordingly, either knockdown of p21 or expression of survivin reversed this senescence process. Further, we developed an animal model of Hsp72-dependent breast cancer associated with expression of Her2. Knockout (KO) of Hsp72 almost completely suppressed tumorigenesis in the MMTVneu breast cancer mouse model. In young Hsp72 KO mice, expression of Her2 instead of mammary tissue hyperplasia led to suppression of duct development and blocked alveolar budding. These effects were due to massive cell senescence in mammary tissue, which was associated with upregulation of p21 and downregulation of survivin. Therefore, Hsp72 has an essential role in Her2-induced tumorigenesis by regulating oncogene-induced senescence pathways.</description><subject>631/67/395</subject><subject>631/80/509</subject><subject>692/420/755</subject><subject>692/699/67/1347</subject><subject>Alveoli</subject><subject>Analysis</subject><subject>Animal models</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Breast cancer</subject><subject>Cell Biology</subject><subject>Cell culture</subject><subject>Cell Line, Tumor</subject><subject>Cell physiology</subject><subject>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</subject><subject>Cyclin-dependent kinase inhibitor p21</subject><subject>Development and progression</subject><subject>Epithelial cells</subject><subject>ErbB-2 protein</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Genetic aspects</subject><subject>Heat shock proteins</subject><subject>HSP72 Heat-Shock Proteins - physiology</subject><subject>Hsp72 protein</subject><subject>Human Genetics</subject><subject>Hyperplasia</subject><subject>Immunohistochemistry</subject><subject>Internal Medicine</subject><subject>Mammary gland</subject><subject>Mammary Neoplasms, Experimental - pathology</subject><subject>Mammary Neoplasms, Experimental - physiopathology</subject><subject>Mammography</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Molecular and cellular biology</subject><subject>Oncology</subject><subject>original-article</subject><subject>Receptor, ErbB-2 - physiology</subject><subject>Senescence</subject><subject>Survivin</subject><subject>Tumorigenesis</subject><subject>Tumors</subject><subject>Xenograft Model Antitumor Assays</subject><subject>Xenografts</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkkuLFDEQx4Mo7uzoxQ8gjSKC0mPeSV-EZVkdYcGLeg3pTPVs1u5kTLqF_fammXHHFR_kUFD1q9c_hdATglcEM_0mBreimJCVuIcWhCtZC9Hw-2iBG4HrhjJ6gk5zvsYYqwbTh-iEEtooKfkCfVmDHat8Fd3XapfiCD5U67xTtNr19iZXNlSQM4TR275KsYdqBiDR2ofN5GBTDXYYbLqpxmmIyW8hQPb5EXrQ2T7D44Ndos_vLj6dr-vLj-8_nJ9d1k5qOdYtbFqHWacbITm0VnBtnaKMSU1ZY0lxAe2odthBo4m0UjpLLBctcK5dw5bo7b7ubmoH2LgyaLK92SU_z2Si9eZuJPgrs43fDeOMKSFLgZeHAil-myCPZvDZQd_bAHHKRmuGqaRE_J9UTGHOhS7ks9_I6zilUHSYIcZVU8wSPf8bRCUnHDMsyZHa2h6MD10sW7i5sTmjElMhlZqp1R-o8jYweBcDdL747yS82ie4FHNO0N0qRrCZb8qUmzLzTZl58ae_anyL_jyiArw4ADY723fJBufzkeNFQqXmlV_vuVxCYQvpuPK_2gY7TgmOfxrcTAj2A7Ag6xA</recordid><startdate>20110623</startdate><enddate>20110623</enddate><creator>Meng, L</creator><creator>Hunt, C</creator><creator>Yaglom, J A</creator><creator>Gabai, V L</creator><creator>Sherman, M Y</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>IQODW</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>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</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>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110623</creationdate><title>Heat shock protein Hsp72 plays an essential role in Her2-induced mammary tumorigenesis</title><author>Meng, L ; Hunt, C ; Yaglom, J A ; Gabai, V L ; Sherman, M Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c686t-bedbc03f89564eba548ac723368239a1ebae2f28c0ce9816a66ca1a45be448c93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>631/67/395</topic><topic>631/80/509</topic><topic>692/420/755</topic><topic>692/699/67/1347</topic><topic>Alveoli</topic><topic>Analysis</topic><topic>Animal models</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Breast cancer</topic><topic>Cell Biology</topic><topic>Cell culture</topic><topic>Cell Line, Tumor</topic><topic>Cell physiology</topic><topic>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</topic><topic>Cyclin-dependent kinase inhibitor p21</topic><topic>Development and progression</topic><topic>Epithelial cells</topic><topic>ErbB-2 protein</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Genetic aspects</topic><topic>Heat shock proteins</topic><topic>HSP72 Heat-Shock Proteins - physiology</topic><topic>Hsp72 protein</topic><topic>Human Genetics</topic><topic>Hyperplasia</topic><topic>Immunohistochemistry</topic><topic>Internal Medicine</topic><topic>Mammary gland</topic><topic>Mammary Neoplasms, Experimental - pathology</topic><topic>Mammary Neoplasms, Experimental - physiopathology</topic><topic>Mammography</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Molecular and cellular biology</topic><topic>Oncology</topic><topic>original-article</topic><topic>Receptor, ErbB-2 - physiology</topic><topic>Senescence</topic><topic>Survivin</topic><topic>Tumorigenesis</topic><topic>Tumors</topic><topic>Xenograft Model Antitumor Assays</topic><topic>Xenografts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meng, L</creatorcontrib><creatorcontrib>Hunt, C</creatorcontrib><creatorcontrib>Yaglom, J A</creatorcontrib><creatorcontrib>Gabai, V L</creatorcontrib><creatorcontrib>Sherman, M Y</creatorcontrib><collection>Pascal-Francis</collection><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>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS 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>Public Health Database (Proquest)</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>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest 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>Research Library Prep</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>PML(ProQuest Medical Library)</collection><collection>ProQuest research library</collection><collection>ProQuest Biological Science Journals</collection><collection>Research Library (Corporate)</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>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meng, L</au><au>Hunt, C</au><au>Yaglom, J A</au><au>Gabai, V L</au><au>Sherman, M Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heat shock protein Hsp72 plays an essential role in Her2-induced mammary tumorigenesis</atitle><jtitle>Oncogene</jtitle><stitle>Oncogene</stitle><addtitle>Oncogene</addtitle><date>2011-06-23</date><risdate>2011</risdate><volume>30</volume><issue>25</issue><spage>2836</spage><epage>2845</epage><pages>2836-2845</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><coden>ONCNES</coden><abstract>The major heat shock protein Hsp72 is expressed at elevated levels in many human cancers and its expression correlates with tumor progression. Here, we investigated the role of Hsp72 in Her2 oncogene-induced neoplastic transformation and tumorigenesis. Expression of Her2 in untransformed MCF10A mammary epithelial cells caused transformation, as judged by foci formation in culture and tumorigenesis in xenografts. However, expression of Her2 in Hsp72-depleted cells failed to induce transformation. The anti-tumorigenic effects of Hsp72 downregulation were associated with cellular senescence because of accumulation of p21 and depletion of survivin. Accordingly, either knockdown of p21 or expression of survivin reversed this senescence process. Further, we developed an animal model of Hsp72-dependent breast cancer associated with expression of Her2. Knockout (KO) of Hsp72 almost completely suppressed tumorigenesis in the MMTVneu breast cancer mouse model. In young Hsp72 KO mice, expression of Her2 instead of mammary tissue hyperplasia led to suppression of duct development and blocked alveolar budding. These effects were due to massive cell senescence in mammary tissue, which was associated with upregulation of p21 and downregulation of survivin. Therefore, Hsp72 has an essential role in Her2-induced tumorigenesis by regulating oncogene-induced senescence pathways.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>21297664</pmid><doi>10.1038/onc.2011.5</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/67/395 631/80/509 692/420/755 692/699/67/1347 Alveoli Analysis Animal models Animals Apoptosis Biological and medical sciences Blotting, Western Breast cancer Cell Biology Cell culture Cell Line, Tumor Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Cyclin-dependent kinase inhibitor p21 Development and progression Epithelial cells ErbB-2 protein Fundamental and applied biological sciences. Psychology Gene expression Genetic aspects Heat shock proteins HSP72 Heat-Shock Proteins - physiology Hsp72 protein Human Genetics Hyperplasia Immunohistochemistry Internal Medicine Mammary gland Mammary Neoplasms, Experimental - pathology Mammary Neoplasms, Experimental - physiopathology Mammography Medicine Medicine & Public Health Mice Mice, Knockout Molecular and cellular biology Oncology original-article Receptor, ErbB-2 - physiology Senescence Survivin Tumorigenesis Tumors Xenograft Model Antitumor Assays Xenografts |
| title | Heat shock protein Hsp72 plays an essential role in Her2-induced mammary tumorigenesis |
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