RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation
Abstract We previously identified Hop as over expressed in invasive pancreatic cancer cell lines and malignant tissues of pancreatic cancer patients, suggesting an important role for Hop in the biology of invasive pancreatic cancer. Hop is a co-chaperone protein that binds to both Hsp70/Hsp90. We hy...
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| Veröffentlicht in: | Cancer letters 2011-07, Vol.306 (2), p.180-189 |
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| creator | Walsh, Naomi Larkin, AnneMarie Swan, Niall Conlon, Kevin Dowling, Paul McDermott, Ray Clynes, Martin |
| description | Abstract We previously identified Hop as over expressed in invasive pancreatic cancer cell lines and malignant tissues of pancreatic cancer patients, suggesting an important role for Hop in the biology of invasive pancreatic cancer. Hop is a co-chaperone protein that binds to both Hsp70/Hsp90. We hypothesised that by targeting Hop, signalling pathways modulating invasion and client protein stabilisation involving Hsp90-dependent complexes may be altered. In this study, we show that Hop knockdown by small interfering (si)RNA reduces the invasion of pancreatic cancer cells, resulting in decreased expression of the downstream target gene, matrix metalloproteinases-2 (MMP-2). Hop in conditioned media co-immunoprecipitates with MMP-2, implicating a possible extracellular function for Hop. Knockdown of Hop expression also reduced expression levels of Hsp90 client proteins, HER2, Bcr-Abl, c-MET and v-Src. Furthermore, Hop is strongly expressed in high grade PanINs compared to lower PanIN grades, displaying differential localisation in invasive ductal pancreatic cancer, indicating that the localisation of Hop is an important factor in pancreatic tumours. Our data suggests that the attenuation of Hop expression inactivates key signal transduction proteins which may decrease the invasiveness of pancreatic cancer cells possibly through the modulation of Hsp90 activity. Therefore, targeting Hop in pancreatic cancer may constitute a viable strategy for targeted cancer therapy. |
| doi_str_mv | 10.1016/j.canlet.2011.03.004 |
| format | Article |
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Hop is a co-chaperone protein that binds to both Hsp70/Hsp90. We hypothesised that by targeting Hop, signalling pathways modulating invasion and client protein stabilisation involving Hsp90-dependent complexes may be altered. In this study, we show that Hop knockdown by small interfering (si)RNA reduces the invasion of pancreatic cancer cells, resulting in decreased expression of the downstream target gene, matrix metalloproteinases-2 (MMP-2). Hop in conditioned media co-immunoprecipitates with MMP-2, implicating a possible extracellular function for Hop. Knockdown of Hop expression also reduced expression levels of Hsp90 client proteins, HER2, Bcr-Abl, c-MET and v-Src. Furthermore, Hop is strongly expressed in high grade PanINs compared to lower PanIN grades, displaying differential localisation in invasive ductal pancreatic cancer, indicating that the localisation of Hop is an important factor in pancreatic tumours. Our data suggests that the attenuation of Hop expression inactivates key signal transduction proteins which may decrease the invasiveness of pancreatic cancer cells possibly through the modulation of Hsp90 activity. Therefore, targeting Hop in pancreatic cancer may constitute a viable strategy for targeted cancer therapy.</description><identifier>ISSN: 0304-3835</identifier><identifier>EISSN: 1872-7980</identifier><identifier>DOI: 10.1016/j.canlet.2011.03.004</identifier><identifier>PMID: 21470770</identifier><language>eng</language><publisher>Ireland: Elsevier Ireland Ltd</publisher><subject>Adenocarcinoma, Mucinous - metabolism ; Adenocarcinoma, Mucinous - prevention & control ; Adenocarcinoma, Mucinous - secondary ; Blotting, Western ; Cancer therapies ; Carcinoma, Pancreatic Ductal - metabolism ; Carcinoma, Pancreatic Ductal - prevention & control ; Carcinoma, Pancreatic Ductal - secondary ; Cell Adhesion ; Cell division ; Cell Movement ; Cloning ; Down-Regulation ; Gene Expression Regulation, Neoplastic ; genes ; Heat shock proteins ; Heat-Shock Proteins - antagonists & inhibitors ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - metabolism ; Hematology, Oncology and Palliative Medicine ; Hop/STIP1/STI1 (Hsp70/Hsp90-organising protein) ; HSP70 Heat-Shock Proteins - metabolism ; HSP90 Heat-Shock Proteins - metabolism ; Humans ; Immunoenzyme Techniques ; Immunohistochemistry ; Immunoprecipitation ; In vitro invasion ; Kinases ; Matrix Metalloproteinase 2 - metabolism ; Matrix Metalloproteinase Inhibitors ; Membranes ; MMP-2 ; Molecular Chaperones ; Neoplasm Invasiveness ; Pancreas ; Pancreatic cancer ; pancreatic neoplasms ; Pancreatic Neoplasms - metabolism ; Pancreatic Neoplasms - pathology ; Pancreatic Neoplasms - prevention & control ; patients ; Phosphorylation ; proteins ; RNA ; RNA, Small Interfering - genetics ; signal transduction ; therapeutics ; Tumor Cells, Cultured ; Tumors</subject><ispartof>Cancer letters, 2011-07, Vol.306 (2), p.180-189</ispartof><rights>Elsevier Ireland Ltd</rights><rights>2011 Elsevier Ireland Ltd</rights><rights>Copyright © 2011 Elsevier Ireland Ltd. All rights reserved.</rights><rights>Copyright Elsevier Limited Jul 28, 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c546t-659b5083d5f860c4c01e973684111feee8c5927379b48b1d6bb5c519c0a029373</citedby><cites>FETCH-LOGICAL-c546t-659b5083d5f860c4c01e973684111feee8c5927379b48b1d6bb5c519c0a029373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0304383511001534$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21470770$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Walsh, Naomi</creatorcontrib><creatorcontrib>Larkin, AnneMarie</creatorcontrib><creatorcontrib>Swan, Niall</creatorcontrib><creatorcontrib>Conlon, Kevin</creatorcontrib><creatorcontrib>Dowling, Paul</creatorcontrib><creatorcontrib>McDermott, Ray</creatorcontrib><creatorcontrib>Clynes, Martin</creatorcontrib><title>RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation</title><title>Cancer letters</title><addtitle>Cancer Lett</addtitle><description>Abstract We previously identified Hop as over expressed in invasive pancreatic cancer cell lines and malignant tissues of pancreatic cancer patients, suggesting an important role for Hop in the biology of invasive pancreatic cancer. Hop is a co-chaperone protein that binds to both Hsp70/Hsp90. We hypothesised that by targeting Hop, signalling pathways modulating invasion and client protein stabilisation involving Hsp90-dependent complexes may be altered. In this study, we show that Hop knockdown by small interfering (si)RNA reduces the invasion of pancreatic cancer cells, resulting in decreased expression of the downstream target gene, matrix metalloproteinases-2 (MMP-2). Hop in conditioned media co-immunoprecipitates with MMP-2, implicating a possible extracellular function for Hop. Knockdown of Hop expression also reduced expression levels of Hsp90 client proteins, HER2, Bcr-Abl, c-MET and v-Src. Furthermore, Hop is strongly expressed in high grade PanINs compared to lower PanIN grades, displaying differential localisation in invasive ductal pancreatic cancer, indicating that the localisation of Hop is an important factor in pancreatic tumours. Our data suggests that the attenuation of Hop expression inactivates key signal transduction proteins which may decrease the invasiveness of pancreatic cancer cells possibly through the modulation of Hsp90 activity. Therefore, targeting Hop in pancreatic cancer may constitute a viable strategy for targeted cancer therapy.</description><subject>Adenocarcinoma, Mucinous - metabolism</subject><subject>Adenocarcinoma, Mucinous - prevention & control</subject><subject>Adenocarcinoma, Mucinous - secondary</subject><subject>Blotting, Western</subject><subject>Cancer therapies</subject><subject>Carcinoma, Pancreatic Ductal - metabolism</subject><subject>Carcinoma, Pancreatic Ductal - prevention & control</subject><subject>Carcinoma, Pancreatic Ductal - secondary</subject><subject>Cell Adhesion</subject><subject>Cell division</subject><subject>Cell Movement</subject><subject>Cloning</subject><subject>Down-Regulation</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>genes</subject><subject>Heat shock proteins</subject><subject>Heat-Shock Proteins - antagonists & inhibitors</subject><subject>Heat-Shock Proteins - genetics</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Hematology, Oncology and Palliative Medicine</subject><subject>Hop/STIP1/STI1 (Hsp70/Hsp90-organising protein)</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>HSP90 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Immunoenzyme Techniques</subject><subject>Immunohistochemistry</subject><subject>Immunoprecipitation</subject><subject>In vitro invasion</subject><subject>Kinases</subject><subject>Matrix Metalloproteinase 2 - metabolism</subject><subject>Matrix Metalloproteinase Inhibitors</subject><subject>Membranes</subject><subject>MMP-2</subject><subject>Molecular Chaperones</subject><subject>Neoplasm Invasiveness</subject><subject>Pancreas</subject><subject>Pancreatic cancer</subject><subject>pancreatic neoplasms</subject><subject>Pancreatic Neoplasms - metabolism</subject><subject>Pancreatic Neoplasms - pathology</subject><subject>Pancreatic Neoplasms - prevention & control</subject><subject>patients</subject><subject>Phosphorylation</subject><subject>proteins</subject><subject>RNA</subject><subject>RNA, Small Interfering - genetics</subject><subject>signal transduction</subject><subject>therapeutics</subject><subject>Tumor Cells, Cultured</subject><subject>Tumors</subject><issn>0304-3835</issn><issn>1872-7980</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkkFv1DAQhSMEokvhHyCwxAF6yHYc23F8Qaoq6CK1gCg9W44zWXk3a2_tZFH_PV62gNRLD7YP_ubpzbwpitcU5hRofbqaW-MHHOcVUDoHNgfgT4oZbWRVStXA02IGDHjJGiaOihcprQBAcCmeF0cV5RKkhFlhf3w9c2Ttg1134ZcnoSeLsCUfFmkr4TTfCkiIS-Ndcn5JtjGM6PwJ6dBGNAkTcX5nkgue7JwhV1ffy4r8UYq4nAYz5p-XxbPeDAlf3b_Hxc3nTz_PF-Xlt4sv52eXpRW8HstaqFZAwzrRNzVYboGikqxuOKW0R8TGClVJJlXLm5Z2ddsKK6iyYKBSTLLj4v1BN7u8nTCNeuOSxWEwHsOUtALOayUkPEo2NZf5AM3kuwfkKkzR5zY0zcNkPI9YZYofKBtDShF7vY1uY-KdpqD3aemVPqSl92lpYDqnlcve3ItP7Qa7f0V_48nA2wPQm6DNMrqkb66zgshRsqqWe4mPBwLzYHcOo07WobfYuYh21F1wj3l4KGAH5501wxrvMP3vVqdKg77e79R-pSiF7CP3_xs__8Hi</recordid><startdate>20110728</startdate><enddate>20110728</enddate><creator>Walsh, Naomi</creator><creator>Larkin, AnneMarie</creator><creator>Swan, Niall</creator><creator>Conlon, Kevin</creator><creator>Dowling, Paul</creator><creator>McDermott, Ray</creator><creator>Clynes, Martin</creator><general>Elsevier Ireland Ltd</general><general>Elsevier Limited</general><scope>FBQ</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>7TO</scope><scope>7U9</scope><scope>H94</scope><scope>K9.</scope><scope>NAPCQ</scope><scope>7X8</scope><scope>7TM</scope></search><sort><creationdate>20110728</creationdate><title>RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation</title><author>Walsh, Naomi ; Larkin, AnneMarie ; Swan, Niall ; Conlon, Kevin ; Dowling, Paul ; McDermott, Ray ; Clynes, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c546t-659b5083d5f860c4c01e973684111feee8c5927379b48b1d6bb5c519c0a029373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adenocarcinoma, Mucinous - metabolism</topic><topic>Adenocarcinoma, Mucinous - prevention & control</topic><topic>Adenocarcinoma, Mucinous - secondary</topic><topic>Blotting, Western</topic><topic>Cancer therapies</topic><topic>Carcinoma, Pancreatic Ductal - metabolism</topic><topic>Carcinoma, Pancreatic Ductal - prevention & control</topic><topic>Carcinoma, Pancreatic Ductal - secondary</topic><topic>Cell Adhesion</topic><topic>Cell division</topic><topic>Cell Movement</topic><topic>Cloning</topic><topic>Down-Regulation</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>genes</topic><topic>Heat shock proteins</topic><topic>Heat-Shock Proteins - antagonists & inhibitors</topic><topic>Heat-Shock Proteins - genetics</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Hematology, Oncology and Palliative Medicine</topic><topic>Hop/STIP1/STI1 (Hsp70/Hsp90-organising protein)</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>HSP90 Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Immunoenzyme Techniques</topic><topic>Immunohistochemistry</topic><topic>Immunoprecipitation</topic><topic>In vitro invasion</topic><topic>Kinases</topic><topic>Matrix Metalloproteinase 2 - metabolism</topic><topic>Matrix Metalloproteinase Inhibitors</topic><topic>Membranes</topic><topic>MMP-2</topic><topic>Molecular Chaperones</topic><topic>Neoplasm Invasiveness</topic><topic>Pancreas</topic><topic>Pancreatic cancer</topic><topic>pancreatic neoplasms</topic><topic>Pancreatic Neoplasms - metabolism</topic><topic>Pancreatic Neoplasms - pathology</topic><topic>Pancreatic Neoplasms - prevention & control</topic><topic>patients</topic><topic>Phosphorylation</topic><topic>proteins</topic><topic>RNA</topic><topic>RNA, Small Interfering - genetics</topic><topic>signal transduction</topic><topic>therapeutics</topic><topic>Tumor Cells, Cultured</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Walsh, Naomi</creatorcontrib><creatorcontrib>Larkin, AnneMarie</creatorcontrib><creatorcontrib>Swan, Niall</creatorcontrib><creatorcontrib>Conlon, Kevin</creatorcontrib><creatorcontrib>Dowling, Paul</creatorcontrib><creatorcontrib>McDermott, Ray</creatorcontrib><creatorcontrib>Clynes, Martin</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Premium</collection><collection>MEDLINE - Academic</collection><collection>Nucleic Acids Abstracts</collection><jtitle>Cancer letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Walsh, Naomi</au><au>Larkin, AnneMarie</au><au>Swan, Niall</au><au>Conlon, Kevin</au><au>Dowling, Paul</au><au>McDermott, Ray</au><au>Clynes, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation</atitle><jtitle>Cancer letters</jtitle><addtitle>Cancer Lett</addtitle><date>2011-07-28</date><risdate>2011</risdate><volume>306</volume><issue>2</issue><spage>180</spage><epage>189</epage><pages>180-189</pages><issn>0304-3835</issn><eissn>1872-7980</eissn><abstract>Abstract We previously identified Hop as over expressed in invasive pancreatic cancer cell lines and malignant tissues of pancreatic cancer patients, suggesting an important role for Hop in the biology of invasive pancreatic cancer. Hop is a co-chaperone protein that binds to both Hsp70/Hsp90. We hypothesised that by targeting Hop, signalling pathways modulating invasion and client protein stabilisation involving Hsp90-dependent complexes may be altered. In this study, we show that Hop knockdown by small interfering (si)RNA reduces the invasion of pancreatic cancer cells, resulting in decreased expression of the downstream target gene, matrix metalloproteinases-2 (MMP-2). Hop in conditioned media co-immunoprecipitates with MMP-2, implicating a possible extracellular function for Hop. Knockdown of Hop expression also reduced expression levels of Hsp90 client proteins, HER2, Bcr-Abl, c-MET and v-Src. Furthermore, Hop is strongly expressed in high grade PanINs compared to lower PanIN grades, displaying differential localisation in invasive ductal pancreatic cancer, indicating that the localisation of Hop is an important factor in pancreatic tumours. Our data suggests that the attenuation of Hop expression inactivates key signal transduction proteins which may decrease the invasiveness of pancreatic cancer cells possibly through the modulation of Hsp90 activity. Therefore, targeting Hop in pancreatic cancer may constitute a viable strategy for targeted cancer therapy.</abstract><cop>Ireland</cop><pub>Elsevier Ireland Ltd</pub><pmid>21470770</pmid><doi>10.1016/j.canlet.2011.03.004</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cancer letters, 2011-07, Vol.306 (2), p.180-189 |
| issn | 0304-3835 1872-7980 |
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| subjects | Adenocarcinoma, Mucinous - metabolism Adenocarcinoma, Mucinous - prevention & control Adenocarcinoma, Mucinous - secondary Blotting, Western Cancer therapies Carcinoma, Pancreatic Ductal - metabolism Carcinoma, Pancreatic Ductal - prevention & control Carcinoma, Pancreatic Ductal - secondary Cell Adhesion Cell division Cell Movement Cloning Down-Regulation Gene Expression Regulation, Neoplastic genes Heat shock proteins Heat-Shock Proteins - antagonists & inhibitors Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism Hematology, Oncology and Palliative Medicine Hop/STIP1/STI1 (Hsp70/Hsp90-organising protein) HSP70 Heat-Shock Proteins - metabolism HSP90 Heat-Shock Proteins - metabolism Humans Immunoenzyme Techniques Immunohistochemistry Immunoprecipitation In vitro invasion Kinases Matrix Metalloproteinase 2 - metabolism Matrix Metalloproteinase Inhibitors Membranes MMP-2 Molecular Chaperones Neoplasm Invasiveness Pancreas Pancreatic cancer pancreatic neoplasms Pancreatic Neoplasms - metabolism Pancreatic Neoplasms - pathology Pancreatic Neoplasms - prevention & control patients Phosphorylation proteins RNA RNA, Small Interfering - genetics signal transduction therapeutics Tumor Cells, Cultured Tumors |
| title | RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation |
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