Gene transfer into mammalian cells using histone-condensed plasmid DNA
A recombinant histone (NLS-H1) containing both the SV40 large T antigen nuclear localization signal and the carboxy-terminal domain of human histone H1(0) was produced in bacteria. NLS-H1-plasmid DNA complexes, in the presence of chloroquine, mediated reporter gene transfer into cultured cells with...
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Veröffentlicht in: | Human gene therapy 1996-08, Vol.7 (12), p.1395-1404 |
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container_title | Human gene therapy |
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creator | Fritz, J D Herweijer, H Zhang, G Wolff, J A |
description | A recombinant histone (NLS-H1) containing both the SV40 large T antigen nuclear localization signal and the carboxy-terminal domain of human histone H1(0) was produced in bacteria. NLS-H1-plasmid DNA complexes, in the presence of chloroquine, mediated reporter gene transfer into cultured cells with similar efficiencies as plasmid DNA-cationic lipid (lipofectin) complexes. NIH-3T3 or COS-7 cells transfected with NLS-H1-plasmid DNA-lipofectin complexes expressed at least 20 times more luciferase or had at least 2.5 times more beta-galactosidase-positive cells than those transfected with plasmid DNA-lipofectin complexes. Foreign gene expression was also improved by other DNA-binding proteins and cationic lipid formulations, yet the greatest enhancement was obtained with complexes containing either NLS-H1 or calf thymus histone H1. Histone H1-plasmid DNA-lipofectin complexes were internalized by a greater number of cells than plasmid DNA-lipofectin complexes. |
doi_str_mv | 10.1089/hum.1996.7.12-1395 |
format | Article |
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NLS-H1-plasmid DNA complexes, in the presence of chloroquine, mediated reporter gene transfer into cultured cells with similar efficiencies as plasmid DNA-cationic lipid (lipofectin) complexes. NIH-3T3 or COS-7 cells transfected with NLS-H1-plasmid DNA-lipofectin complexes expressed at least 20 times more luciferase or had at least 2.5 times more beta-galactosidase-positive cells than those transfected with plasmid DNA-lipofectin complexes. Foreign gene expression was also improved by other DNA-binding proteins and cationic lipid formulations, yet the greatest enhancement was obtained with complexes containing either NLS-H1 or calf thymus histone H1. Histone H1-plasmid DNA-lipofectin complexes were internalized by a greater number of cells than plasmid DNA-lipofectin complexes.</description><identifier>ISSN: 1043-0342</identifier><identifier>EISSN: 1557-7422</identifier><identifier>DOI: 10.1089/hum.1996.7.12-1395</identifier><identifier>PMID: 8844198</identifier><language>eng</language><publisher>United States</publisher><subject>3T3 Cells ; Animals ; Antigens, Polyomavirus Transforming - genetics ; Antigens, Polyomavirus Transforming - physiology ; Cattle ; Cell Line, Transformed ; Cells, Cultured ; Cercopithecus aethiops ; Chloroquine - pharmacology ; COS Cells ; DNA, Recombinant - chemistry ; DNA, Recombinant - genetics ; Gene Expression ; Gene Transfer Techniques ; Genes, Reporter ; Genetic Vectors - genetics ; Genetic Vectors - ultrastructure ; HeLa Cells ; Histones - genetics ; Humans ; Kidney - cytology ; Luciferases - biosynthesis ; Luciferases - genetics ; Mice ; Phosphatidylethanolamines ; Recombinant Fusion Proteins</subject><ispartof>Human gene therapy, 1996-08, Vol.7 (12), p.1395-1404</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c329t-570a177a1af3b10aa72e3c4bc06f3b1552bb74ae033f1235553d2decd12794f93</citedby><cites>FETCH-LOGICAL-c329t-570a177a1af3b10aa72e3c4bc06f3b1552bb74ae033f1235553d2decd12794f93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,3029,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8844198$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fritz, J D</creatorcontrib><creatorcontrib>Herweijer, H</creatorcontrib><creatorcontrib>Zhang, G</creatorcontrib><creatorcontrib>Wolff, J A</creatorcontrib><title>Gene transfer into mammalian cells using histone-condensed plasmid DNA</title><title>Human gene therapy</title><addtitle>Hum Gene Ther</addtitle><description>A recombinant histone (NLS-H1) containing both the SV40 large T antigen nuclear localization signal and the carboxy-terminal domain of human histone H1(0) was produced in bacteria. NLS-H1-plasmid DNA complexes, in the presence of chloroquine, mediated reporter gene transfer into cultured cells with similar efficiencies as plasmid DNA-cationic lipid (lipofectin) complexes. NIH-3T3 or COS-7 cells transfected with NLS-H1-plasmid DNA-lipofectin complexes expressed at least 20 times more luciferase or had at least 2.5 times more beta-galactosidase-positive cells than those transfected with plasmid DNA-lipofectin complexes. Foreign gene expression was also improved by other DNA-binding proteins and cationic lipid formulations, yet the greatest enhancement was obtained with complexes containing either NLS-H1 or calf thymus histone H1. Histone H1-plasmid DNA-lipofectin complexes were internalized by a greater number of cells than plasmid DNA-lipofectin complexes.</description><subject>3T3 Cells</subject><subject>Animals</subject><subject>Antigens, Polyomavirus Transforming - genetics</subject><subject>Antigens, Polyomavirus Transforming - physiology</subject><subject>Cattle</subject><subject>Cell Line, Transformed</subject><subject>Cells, Cultured</subject><subject>Cercopithecus aethiops</subject><subject>Chloroquine - pharmacology</subject><subject>COS Cells</subject><subject>DNA, Recombinant - chemistry</subject><subject>DNA, Recombinant - genetics</subject><subject>Gene Expression</subject><subject>Gene Transfer Techniques</subject><subject>Genes, Reporter</subject><subject>Genetic Vectors - genetics</subject><subject>Genetic Vectors - ultrastructure</subject><subject>HeLa Cells</subject><subject>Histones - genetics</subject><subject>Humans</subject><subject>Kidney - cytology</subject><subject>Luciferases - biosynthesis</subject><subject>Luciferases - genetics</subject><subject>Mice</subject><subject>Phosphatidylethanolamines</subject><subject>Recombinant Fusion Proteins</subject><issn>1043-0342</issn><issn>1557-7422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EKqXwB5CQPLGl-PwRx2NVaEGqYIHZcpILDYqdEicD_55ErViZ7nR63lenh5BbYEtgmXnYD34JxqRLvQSegDDqjMxBKZ1oyfn5uDMpEiYkvyRXMX4xBkKlekZmWSYlmGxONlsMSPvOhVhhR-vQt9Q7711Tu0ALbJpIh1iHT7qvY98GTIo2lBgilvTQuOjrkj6-rq7JReWaiDenuSAfm6f39XOye9u-rFe7pBDc9InSzIHWDlwlcmDOaY6ikHnB0umgFM9zLR0yISrgQiklSl5iUQLXRlZGLMj9sffQtd8Dxt76Ok5fuoDtEK3OJGNcyn9BUEZLpdIR5Eew6NoYO6zsoau9634sMDtZtqNlO1m22gK3k-UxdHdqH3KP5V_kpFX8ApH0eFc</recordid><startdate>19960801</startdate><enddate>19960801</enddate><creator>Fritz, J D</creator><creator>Herweijer, H</creator><creator>Zhang, G</creator><creator>Wolff, J A</creator><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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19960801</creationdate><title>Gene transfer into mammalian cells using histone-condensed plasmid DNA</title><author>Fritz, J D ; Herweijer, H ; Zhang, G ; Wolff, J A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c329t-570a177a1af3b10aa72e3c4bc06f3b1552bb74ae033f1235553d2decd12794f93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>3T3 Cells</topic><topic>Animals</topic><topic>Antigens, Polyomavirus Transforming - genetics</topic><topic>Antigens, Polyomavirus Transforming - physiology</topic><topic>Cattle</topic><topic>Cell Line, Transformed</topic><topic>Cells, Cultured</topic><topic>Cercopithecus aethiops</topic><topic>Chloroquine - pharmacology</topic><topic>COS Cells</topic><topic>DNA, Recombinant - chemistry</topic><topic>DNA, Recombinant - genetics</topic><topic>Gene Expression</topic><topic>Gene Transfer Techniques</topic><topic>Genes, Reporter</topic><topic>Genetic Vectors - genetics</topic><topic>Genetic Vectors - ultrastructure</topic><topic>HeLa Cells</topic><topic>Histones - genetics</topic><topic>Humans</topic><topic>Kidney - cytology</topic><topic>Luciferases - biosynthesis</topic><topic>Luciferases - genetics</topic><topic>Mice</topic><topic>Phosphatidylethanolamines</topic><topic>Recombinant Fusion Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fritz, J D</creatorcontrib><creatorcontrib>Herweijer, H</creatorcontrib><creatorcontrib>Zhang, G</creatorcontrib><creatorcontrib>Wolff, J A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Human gene therapy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fritz, J D</au><au>Herweijer, H</au><au>Zhang, G</au><au>Wolff, J A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gene transfer into mammalian cells using histone-condensed plasmid DNA</atitle><jtitle>Human gene therapy</jtitle><addtitle>Hum Gene Ther</addtitle><date>1996-08-01</date><risdate>1996</risdate><volume>7</volume><issue>12</issue><spage>1395</spage><epage>1404</epage><pages>1395-1404</pages><issn>1043-0342</issn><eissn>1557-7422</eissn><abstract>A recombinant histone (NLS-H1) containing both the SV40 large T antigen nuclear localization signal and the carboxy-terminal domain of human histone H1(0) was produced in bacteria. NLS-H1-plasmid DNA complexes, in the presence of chloroquine, mediated reporter gene transfer into cultured cells with similar efficiencies as plasmid DNA-cationic lipid (lipofectin) complexes. NIH-3T3 or COS-7 cells transfected with NLS-H1-plasmid DNA-lipofectin complexes expressed at least 20 times more luciferase or had at least 2.5 times more beta-galactosidase-positive cells than those transfected with plasmid DNA-lipofectin complexes. Foreign gene expression was also improved by other DNA-binding proteins and cationic lipid formulations, yet the greatest enhancement was obtained with complexes containing either NLS-H1 or calf thymus histone H1. Histone H1-plasmid DNA-lipofectin complexes were internalized by a greater number of cells than plasmid DNA-lipofectin complexes.</abstract><cop>United States</cop><pmid>8844198</pmid><doi>10.1089/hum.1996.7.12-1395</doi><tpages>10</tpages></addata></record> |
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source | Mary Ann Liebert Online Subscription; MEDLINE |
subjects | 3T3 Cells Animals Antigens, Polyomavirus Transforming - genetics Antigens, Polyomavirus Transforming - physiology Cattle Cell Line, Transformed Cells, Cultured Cercopithecus aethiops Chloroquine - pharmacology COS Cells DNA, Recombinant - chemistry DNA, Recombinant - genetics Gene Expression Gene Transfer Techniques Genes, Reporter Genetic Vectors - genetics Genetic Vectors - ultrastructure HeLa Cells Histones - genetics Humans Kidney - cytology Luciferases - biosynthesis Luciferases - genetics Mice Phosphatidylethanolamines Recombinant Fusion Proteins |
title | Gene transfer into mammalian cells using histone-condensed plasmid DNA |
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