VP22 does not significantly enhance enzyme prodrug cancer gene therapy as a part of a VP22-HSVTk-GFP triple fusion construct

Background VP22 is a herpes simplex virus type 1 (HSV‐1) tegument protein that has been suggested to spread from cell to cell, alone or as a part of fusion proteins. Creating controversy, some reports indicate that VP22 cannot facilitate significant intercellular spreading. To study the capacity of...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The journal of gene medicine 2005-07, Vol.7 (7), p.898-907
Hauptverfasser: Hakkarainen, Tanja, Wahlfors, Tiina, Meriläinen, Outi, Loimas, Sami, Hemminki, Akseli, Wahlfors, Jarmo
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 907
container_issue 7
container_start_page 898
container_title The journal of gene medicine
container_volume 7
creator Hakkarainen, Tanja
Wahlfors, Tiina
Meriläinen, Outi
Loimas, Sami
Hemminki, Akseli
Wahlfors, Jarmo
description Background VP22 is a herpes simplex virus type 1 (HSV‐1) tegument protein that has been suggested to spread from cell to cell, alone or as a part of fusion proteins. Creating controversy, some reports indicate that VP22 cannot facilitate significant intercellular spreading. To study the capacity of VP22 to cause spreading and enhance thymidine kinase/ganciclovir cancer gene therapy, we constructed a novel triple fusion protein containing VP22, HSV thymidine kinase and green fluorescent protein (VP22‐Tk‐GFP). This fusion protein has three functional domains in the same polypeptide, thus making it possible to reliably compare the causality between transduction rate and cell killing efficiency in vitro and in vivo. Methods VP22‐Tk‐GFP was cloned into lenti‐ and adenoviral vectors and used for expression studies, analyses for VP22‐mediated protein spreading, and to study the effect of VP22 to thymidine kinase/ganciclovir‐mediated cytotoxicity. The function of VP22‐Tk‐GFP was also investigated in vivo. Results The triple fusion protein was expressed correctly in vitro, but intercellular trafficking was not observed in any of the studied cell lines. However, under certain conditions, VP22‐Tk‐GFP sensitized cells more efficiently to ganciclovir than Tk‐GFP. In vivo there was a trend for increased inhibition of tumor growth with VP22‐Tk‐GFP when ganciclovir was present, but the difference with Tk‐GFP was not statistically significant. Conclusions Based on our results, VP22 fusion proteins do not seem to traffic intercellularly at detectable levels in most tumor cell types. Even though VP22 enhanced cytotoxicity in one cell line in vitro, the effect in vivo was modest. Therefore, our results do not support the utility of VP22 as an enhancer of enzyme prodrug cancer gene therapy. Copyright © 2005 John Wiley & Sons, Ltd.
doi_str_mv 10.1002/jgm.737
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67975333</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>860905581</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4117-774f6b2665aa1de1783127e15fe007b8064fd89e6baedff291c9d711b9bc79143</originalsourceid><addsrcrecordid>eNqFkdGK1DAUhoMo7jqKbyDBC72Qrjlp00wuZXBmXFddcF29C2l6OtvZNq1Ji1Z8eDN0UBDE3JzD4eMLPz8hj4GdAWP85X7XnslU3iGnIDgknIvsbtyZUkmmll9OyIMQ9oyBXC7VfXICQgrFpTolP68vOadlh4G6bqCh3rm6qq1xQzNRdDfGWYzzx9Qi7X1X-nFH7eHo6Q4d0uEGveknagI1tDd-oF0Vt4M12X68vrpNNutLOvi6b5BWY6g7R23nwuBHOzwk9yrTBHx0nAvyaf36arVNLj5s3qxeXSQ2A5CJlFmVFzzPhTFQYgyRApcIokLGZLFkeVaVS4V5YbCsKq7AqlICFKqwUkGWLsiz2RsTfB0xDLqtg8WmMQ67MehcKinS-P4HghSQivj_gjz9C9x3o3cxhAaVKy5SBhF6PkPWdyF4rHTv69b4SQPTh9p0rE3H2iL55KgbixbLP9yxpwi8mIFvdYPTvzz6fPNu1iUzXYcBv_-mjb-NUVMp9Of3G73i_C1j660-T38BjPauVw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>196925301</pqid></control><display><type>article</type><title>VP22 does not significantly enhance enzyme prodrug cancer gene therapy as a part of a VP22-HSVTk-GFP triple fusion construct</title><source>MEDLINE</source><source>Wiley Online Library</source><creator>Hakkarainen, Tanja ; Wahlfors, Tiina ; Meriläinen, Outi ; Loimas, Sami ; Hemminki, Akseli ; Wahlfors, Jarmo</creator><creatorcontrib>Hakkarainen, Tanja ; Wahlfors, Tiina ; Meriläinen, Outi ; Loimas, Sami ; Hemminki, Akseli ; Wahlfors, Jarmo</creatorcontrib><description>Background VP22 is a herpes simplex virus type 1 (HSV‐1) tegument protein that has been suggested to spread from cell to cell, alone or as a part of fusion proteins. Creating controversy, some reports indicate that VP22 cannot facilitate significant intercellular spreading. To study the capacity of VP22 to cause spreading and enhance thymidine kinase/ganciclovir cancer gene therapy, we constructed a novel triple fusion protein containing VP22, HSV thymidine kinase and green fluorescent protein (VP22‐Tk‐GFP). This fusion protein has three functional domains in the same polypeptide, thus making it possible to reliably compare the causality between transduction rate and cell killing efficiency in vitro and in vivo. Methods VP22‐Tk‐GFP was cloned into lenti‐ and adenoviral vectors and used for expression studies, analyses for VP22‐mediated protein spreading, and to study the effect of VP22 to thymidine kinase/ganciclovir‐mediated cytotoxicity. The function of VP22‐Tk‐GFP was also investigated in vivo. Results The triple fusion protein was expressed correctly in vitro, but intercellular trafficking was not observed in any of the studied cell lines. However, under certain conditions, VP22‐Tk‐GFP sensitized cells more efficiently to ganciclovir than Tk‐GFP. In vivo there was a trend for increased inhibition of tumor growth with VP22‐Tk‐GFP when ganciclovir was present, but the difference with Tk‐GFP was not statistically significant. Conclusions Based on our results, VP22 fusion proteins do not seem to traffic intercellularly at detectable levels in most tumor cell types. Even though VP22 enhanced cytotoxicity in one cell line in vitro, the effect in vivo was modest. Therefore, our results do not support the utility of VP22 as an enhancer of enzyme prodrug cancer gene therapy. Copyright © 2005 John Wiley &amp; Sons, Ltd.</description><identifier>ISSN: 1099-498X</identifier><identifier>EISSN: 1521-2254</identifier><identifier>DOI: 10.1002/jgm.737</identifier><identifier>PMID: 15759279</identifier><language>eng</language><publisher>Chichester, UK: John Wiley &amp; Sons, Ltd</publisher><subject>Adenoviridae - genetics ; Animals ; Cells, Cultured ; Feasibility Studies ; Female ; fusion protein ; ganciclovir ; Ganciclovir - pharmacology ; Gene therapy ; Genes, Transgenic, Suicide ; Genetic Therapy - methods ; Genetic Vectors ; Green Fluorescent Proteins - genetics ; Herpes simplex virus 1 ; HSV-Tk ; Humans ; intercellular trafficking ; Lentivirus - genetics ; Mice ; Mice, Nude ; Ovarian Neoplasms - therapy ; Prodrugs - metabolism ; Prodrugs - pharmacology ; protein transduction domain ; Protein Transport ; Rats ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; suicide gene therapy ; Thymidine Kinase - genetics ; Transduction, Genetic ; Transgenes ; Tumor Cells, Cultured ; Viral Structural Proteins - genetics ; Viral Structural Proteins - metabolism ; Viral Structural Proteins - pharmacology ; VP22 tegument protein</subject><ispartof>The journal of gene medicine, 2005-07, Vol.7 (7), p.898-907</ispartof><rights>Copyright © 2005 John Wiley &amp; Sons, Ltd.</rights><rights>Copyright 2005 John Wiley &amp; Sons, Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4117-774f6b2665aa1de1783127e15fe007b8064fd89e6baedff291c9d711b9bc79143</citedby><cites>FETCH-LOGICAL-c4117-774f6b2665aa1de1783127e15fe007b8064fd89e6baedff291c9d711b9bc79143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjgm.737$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjgm.737$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15759279$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hakkarainen, Tanja</creatorcontrib><creatorcontrib>Wahlfors, Tiina</creatorcontrib><creatorcontrib>Meriläinen, Outi</creatorcontrib><creatorcontrib>Loimas, Sami</creatorcontrib><creatorcontrib>Hemminki, Akseli</creatorcontrib><creatorcontrib>Wahlfors, Jarmo</creatorcontrib><title>VP22 does not significantly enhance enzyme prodrug cancer gene therapy as a part of a VP22-HSVTk-GFP triple fusion construct</title><title>The journal of gene medicine</title><addtitle>J. Gene Med</addtitle><description>Background VP22 is a herpes simplex virus type 1 (HSV‐1) tegument protein that has been suggested to spread from cell to cell, alone or as a part of fusion proteins. Creating controversy, some reports indicate that VP22 cannot facilitate significant intercellular spreading. To study the capacity of VP22 to cause spreading and enhance thymidine kinase/ganciclovir cancer gene therapy, we constructed a novel triple fusion protein containing VP22, HSV thymidine kinase and green fluorescent protein (VP22‐Tk‐GFP). This fusion protein has three functional domains in the same polypeptide, thus making it possible to reliably compare the causality between transduction rate and cell killing efficiency in vitro and in vivo. Methods VP22‐Tk‐GFP was cloned into lenti‐ and adenoviral vectors and used for expression studies, analyses for VP22‐mediated protein spreading, and to study the effect of VP22 to thymidine kinase/ganciclovir‐mediated cytotoxicity. The function of VP22‐Tk‐GFP was also investigated in vivo. Results The triple fusion protein was expressed correctly in vitro, but intercellular trafficking was not observed in any of the studied cell lines. However, under certain conditions, VP22‐Tk‐GFP sensitized cells more efficiently to ganciclovir than Tk‐GFP. In vivo there was a trend for increased inhibition of tumor growth with VP22‐Tk‐GFP when ganciclovir was present, but the difference with Tk‐GFP was not statistically significant. Conclusions Based on our results, VP22 fusion proteins do not seem to traffic intercellularly at detectable levels in most tumor cell types. Even though VP22 enhanced cytotoxicity in one cell line in vitro, the effect in vivo was modest. Therefore, our results do not support the utility of VP22 as an enhancer of enzyme prodrug cancer gene therapy. Copyright © 2005 John Wiley &amp; Sons, Ltd.</description><subject>Adenoviridae - genetics</subject><subject>Animals</subject><subject>Cells, Cultured</subject><subject>Feasibility Studies</subject><subject>Female</subject><subject>fusion protein</subject><subject>ganciclovir</subject><subject>Ganciclovir - pharmacology</subject><subject>Gene therapy</subject><subject>Genes, Transgenic, Suicide</subject><subject>Genetic Therapy - methods</subject><subject>Genetic Vectors</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Herpes simplex virus 1</subject><subject>HSV-Tk</subject><subject>Humans</subject><subject>intercellular trafficking</subject><subject>Lentivirus - genetics</subject><subject>Mice</subject><subject>Mice, Nude</subject><subject>Ovarian Neoplasms - therapy</subject><subject>Prodrugs - metabolism</subject><subject>Prodrugs - pharmacology</subject><subject>protein transduction domain</subject><subject>Protein Transport</subject><subject>Rats</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>suicide gene therapy</subject><subject>Thymidine Kinase - genetics</subject><subject>Transduction, Genetic</subject><subject>Transgenes</subject><subject>Tumor Cells, Cultured</subject><subject>Viral Structural Proteins - genetics</subject><subject>Viral Structural Proteins - metabolism</subject><subject>Viral Structural Proteins - pharmacology</subject><subject>VP22 tegument protein</subject><issn>1099-498X</issn><issn>1521-2254</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkdGK1DAUhoMo7jqKbyDBC72Qrjlp00wuZXBmXFddcF29C2l6OtvZNq1Ji1Z8eDN0UBDE3JzD4eMLPz8hj4GdAWP85X7XnslU3iGnIDgknIvsbtyZUkmmll9OyIMQ9oyBXC7VfXICQgrFpTolP68vOadlh4G6bqCh3rm6qq1xQzNRdDfGWYzzx9Qi7X1X-nFH7eHo6Q4d0uEGveknagI1tDd-oF0Vt4M12X68vrpNNutLOvi6b5BWY6g7R23nwuBHOzwk9yrTBHx0nAvyaf36arVNLj5s3qxeXSQ2A5CJlFmVFzzPhTFQYgyRApcIokLGZLFkeVaVS4V5YbCsKq7AqlICFKqwUkGWLsiz2RsTfB0xDLqtg8WmMQ67MehcKinS-P4HghSQivj_gjz9C9x3o3cxhAaVKy5SBhF6PkPWdyF4rHTv69b4SQPTh9p0rE3H2iL55KgbixbLP9yxpwi8mIFvdYPTvzz6fPNu1iUzXYcBv_-mjb-NUVMp9Of3G73i_C1j660-T38BjPauVw</recordid><startdate>200507</startdate><enddate>200507</enddate><creator>Hakkarainen, Tanja</creator><creator>Wahlfors, Tiina</creator><creator>Meriläinen, Outi</creator><creator>Loimas, Sami</creator><creator>Hemminki, Akseli</creator><creator>Wahlfors, Jarmo</creator><general>John Wiley &amp; Sons, Ltd</general><general>Wiley Periodicals Inc</general><scope>BSCLL</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>7QP</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>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>7QO</scope><scope>7X8</scope></search><sort><creationdate>200507</creationdate><title>VP22 does not significantly enhance enzyme prodrug cancer gene therapy as a part of a VP22-HSVTk-GFP triple fusion construct</title><author>Hakkarainen, Tanja ; Wahlfors, Tiina ; Meriläinen, Outi ; Loimas, Sami ; Hemminki, Akseli ; Wahlfors, Jarmo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4117-774f6b2665aa1de1783127e15fe007b8064fd89e6baedff291c9d711b9bc79143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adenoviridae - genetics</topic><topic>Animals</topic><topic>Cells, Cultured</topic><topic>Feasibility Studies</topic><topic>Female</topic><topic>fusion protein</topic><topic>ganciclovir</topic><topic>Ganciclovir - pharmacology</topic><topic>Gene therapy</topic><topic>Genes, Transgenic, Suicide</topic><topic>Genetic Therapy - methods</topic><topic>Genetic Vectors</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Herpes simplex virus 1</topic><topic>HSV-Tk</topic><topic>Humans</topic><topic>intercellular trafficking</topic><topic>Lentivirus - genetics</topic><topic>Mice</topic><topic>Mice, Nude</topic><topic>Ovarian Neoplasms - therapy</topic><topic>Prodrugs - metabolism</topic><topic>Prodrugs - pharmacology</topic><topic>protein transduction domain</topic><topic>Protein Transport</topic><topic>Rats</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>suicide gene therapy</topic><topic>Thymidine Kinase - genetics</topic><topic>Transduction, Genetic</topic><topic>Transgenes</topic><topic>Tumor Cells, Cultured</topic><topic>Viral Structural Proteins - genetics</topic><topic>Viral Structural Proteins - metabolism</topic><topic>Viral Structural Proteins - pharmacology</topic><topic>VP22 tegument protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hakkarainen, Tanja</creatorcontrib><creatorcontrib>Wahlfors, Tiina</creatorcontrib><creatorcontrib>Meriläinen, Outi</creatorcontrib><creatorcontrib>Loimas, Sami</creatorcontrib><creatorcontrib>Hemminki, Akseli</creatorcontrib><creatorcontrib>Wahlfors, Jarmo</creatorcontrib><collection>Istex</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>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest_Health &amp; 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>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</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>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</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>Biotechnology Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The journal of gene medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hakkarainen, Tanja</au><au>Wahlfors, Tiina</au><au>Meriläinen, Outi</au><au>Loimas, Sami</au><au>Hemminki, Akseli</au><au>Wahlfors, Jarmo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>VP22 does not significantly enhance enzyme prodrug cancer gene therapy as a part of a VP22-HSVTk-GFP triple fusion construct</atitle><jtitle>The journal of gene medicine</jtitle><addtitle>J. Gene Med</addtitle><date>2005-07</date><risdate>2005</risdate><volume>7</volume><issue>7</issue><spage>898</spage><epage>907</epage><pages>898-907</pages><issn>1099-498X</issn><eissn>1521-2254</eissn><abstract>Background VP22 is a herpes simplex virus type 1 (HSV‐1) tegument protein that has been suggested to spread from cell to cell, alone or as a part of fusion proteins. Creating controversy, some reports indicate that VP22 cannot facilitate significant intercellular spreading. To study the capacity of VP22 to cause spreading and enhance thymidine kinase/ganciclovir cancer gene therapy, we constructed a novel triple fusion protein containing VP22, HSV thymidine kinase and green fluorescent protein (VP22‐Tk‐GFP). This fusion protein has three functional domains in the same polypeptide, thus making it possible to reliably compare the causality between transduction rate and cell killing efficiency in vitro and in vivo. Methods VP22‐Tk‐GFP was cloned into lenti‐ and adenoviral vectors and used for expression studies, analyses for VP22‐mediated protein spreading, and to study the effect of VP22 to thymidine kinase/ganciclovir‐mediated cytotoxicity. The function of VP22‐Tk‐GFP was also investigated in vivo. Results The triple fusion protein was expressed correctly in vitro, but intercellular trafficking was not observed in any of the studied cell lines. However, under certain conditions, VP22‐Tk‐GFP sensitized cells more efficiently to ganciclovir than Tk‐GFP. In vivo there was a trend for increased inhibition of tumor growth with VP22‐Tk‐GFP when ganciclovir was present, but the difference with Tk‐GFP was not statistically significant. Conclusions Based on our results, VP22 fusion proteins do not seem to traffic intercellularly at detectable levels in most tumor cell types. Even though VP22 enhanced cytotoxicity in one cell line in vitro, the effect in vivo was modest. Therefore, our results do not support the utility of VP22 as an enhancer of enzyme prodrug cancer gene therapy. Copyright © 2005 John Wiley &amp; Sons, Ltd.</abstract><cop>Chichester, UK</cop><pub>John Wiley &amp; Sons, Ltd</pub><pmid>15759279</pmid><doi>10.1002/jgm.737</doi><tpages>10</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1099-498X
ispartof The journal of gene medicine, 2005-07, Vol.7 (7), p.898-907
issn 1099-498X
1521-2254
language eng
recordid cdi_proquest_miscellaneous_67975333
source MEDLINE; Wiley Online Library
subjects Adenoviridae - genetics
Animals
Cells, Cultured
Feasibility Studies
Female
fusion protein
ganciclovir
Ganciclovir - pharmacology
Gene therapy
Genes, Transgenic, Suicide
Genetic Therapy - methods
Genetic Vectors
Green Fluorescent Proteins - genetics
Herpes simplex virus 1
HSV-Tk
Humans
intercellular trafficking
Lentivirus - genetics
Mice
Mice, Nude
Ovarian Neoplasms - therapy
Prodrugs - metabolism
Prodrugs - pharmacology
protein transduction domain
Protein Transport
Rats
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
suicide gene therapy
Thymidine Kinase - genetics
Transduction, Genetic
Transgenes
Tumor Cells, Cultured
Viral Structural Proteins - genetics
Viral Structural Proteins - metabolism
Viral Structural Proteins - pharmacology
VP22 tegument protein
title VP22 does not significantly enhance enzyme prodrug cancer gene therapy as a part of a VP22-HSVTk-GFP triple fusion construct
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T05%3A22%3A21IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=VP22%20does%20not%20significantly%20enhance%20enzyme%20prodrug%20cancer%20gene%20therapy%20as%20a%20part%20of%20a%20VP22-HSVTk-GFP%20triple%20fusion%20construct&rft.jtitle=The%20journal%20of%20gene%20medicine&rft.au=Hakkarainen,%20Tanja&rft.date=2005-07&rft.volume=7&rft.issue=7&rft.spage=898&rft.epage=907&rft.pages=898-907&rft.issn=1099-498X&rft.eissn=1521-2254&rft_id=info:doi/10.1002/jgm.737&rft_dat=%3Cproquest_cross%3E860905581%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=196925301&rft_id=info:pmid/15759279&rfr_iscdi=true