Specific gene transfer mediated by lactosylated poly-L-lysine into hepatoma cells
Plasmid DNA/glycosylated polylysine complexes were used to transfer in vitro a luciferase reporter gene into human hepatoma cells by a receptor-mediated endocytosis process. HepG2 cells which express a galactose specific membrane lectin were efficiently and selectively transfected with pSV2Luc/lacto...
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| Veröffentlicht in: | Nucleic acids research 1993-02, Vol.21 (4), p.871-878 |
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| creator | Midoux, Patrick Mendes, Christina Legrand, Alain Raimond, Jacques Mayer, Roger Monsigny, Michel Roche, Annie Claude |
| description | Plasmid DNA/glycosylated polylysine complexes were used to transfer in vitro a luciferase reporter gene into human hepatoma cells by a receptor-mediated endocytosis process. HepG2 cells which express a galactose specific membrane lectin were efficiently and selectively transfected with pSV2Luc/lactosylated polylysine complexes in a sugar dependent manner: I) HepG2 cells which do not express membrane lectin specific for mannose were quite poorly transfected with pSV2Luc/mannosylated polylysine complexes, II) HeLa cells which do not express membrane lectin specific for galactose were not transfected with pSV2Luc/lactosylated polylysine complexes. The transfection efficiency of HepG2 cells with pSV2Luc/lactosylated polylysine complexes was greatly enhanced either in the presence of chloroquine or in the presence of a fusogenic peptide. A 22-residue peptide derived from the influenza virus hemagglutinin HA2 N-terminal polypeptide that mimics the fusogenic activity of the virus, was selected. In the presence of the fusogenic peptide, the luciferase activity in HepG2 cells was 10 fold larger than that of cells transfected with pSV2Luc/lactosylated polylysine complexes in the presence of chloroquine. |
| doi_str_mv | 10.1093/nar/21.4.871 |
| format | Article |
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HepG2 cells which express a galactose specific membrane lectin were efficiently and selectively transfected with pSV2Luc/lactosylated polylysine complexes in a sugar dependent manner: I) HepG2 cells which do not express membrane lectin specific for mannose were quite poorly transfected with pSV2Luc/mannosylated polylysine complexes, II) HeLa cells which do not express membrane lectin specific for galactose were not transfected with pSV2Luc/lactosylated polylysine complexes. The transfection efficiency of HepG2 cells with pSV2Luc/lactosylated polylysine complexes was greatly enhanced either in the presence of chloroquine or in the presence of a fusogenic peptide. A 22-residue peptide derived from the influenza virus hemagglutinin HA2 N-terminal polypeptide that mimics the fusogenic activity of the virus, was selected. In the presence of the fusogenic peptide, the luciferase activity in HepG2 cells was 10 fold larger than that of cells transfected with pSV2Luc/lactosylated polylysine complexes in the presence of chloroquine.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/21.4.871</identifier><identifier>PMID: 8383843</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Amino Acid Sequence ; Biological and medical sciences ; Carcinoma, Hepatocellular ; Chloroquine ; Diverse techniques ; Fluorescein ; Fluoresceins ; Fundamental and applied biological sciences. Psychology ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral ; Humans ; Influenza virus ; Lactose ; Life Sciences ; Microscopy, Fluorescence ; Molecular and cellular biology ; Molecular Sequence Data ; Plasmids - metabolism ; Polylysine ; Transfection - methods ; Tumor Cells, Cultured ; Viral Fusion Proteins</subject><ispartof>Nucleic acids research, 1993-02, Vol.21 (4), p.871-878</ispartof><rights>1993 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c572t-b96227e3d6fdf73361947485d1855af33a5f02f6b620027858a39a5cc86992f13</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC309219/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC309219/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4603333$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8383843$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02138456$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Midoux, Patrick</creatorcontrib><creatorcontrib>Mendes, Christina</creatorcontrib><creatorcontrib>Legrand, Alain</creatorcontrib><creatorcontrib>Raimond, Jacques</creatorcontrib><creatorcontrib>Mayer, Roger</creatorcontrib><creatorcontrib>Monsigny, Michel</creatorcontrib><creatorcontrib>Roche, Annie Claude</creatorcontrib><title>Specific gene transfer mediated by lactosylated poly-L-lysine into hepatoma cells</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Plasmid DNA/glycosylated polylysine complexes were used to transfer in vitro a luciferase reporter gene into human hepatoma cells by a receptor-mediated endocytosis process. HepG2 cells which express a galactose specific membrane lectin were efficiently and selectively transfected with pSV2Luc/lactosylated polylysine complexes in a sugar dependent manner: I) HepG2 cells which do not express membrane lectin specific for mannose were quite poorly transfected with pSV2Luc/mannosylated polylysine complexes, II) HeLa cells which do not express membrane lectin specific for galactose were not transfected with pSV2Luc/lactosylated polylysine complexes. The transfection efficiency of HepG2 cells with pSV2Luc/lactosylated polylysine complexes was greatly enhanced either in the presence of chloroquine or in the presence of a fusogenic peptide. A 22-residue peptide derived from the influenza virus hemagglutinin HA2 N-terminal polypeptide that mimics the fusogenic activity of the virus, was selected. In the presence of the fusogenic peptide, the luciferase activity in HepG2 cells was 10 fold larger than that of cells transfected with pSV2Luc/lactosylated polylysine complexes in the presence of chloroquine.</description><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Carcinoma, Hepatocellular</subject><subject>Chloroquine</subject><subject>Diverse techniques</subject><subject>Fluorescein</subject><subject>Fluoresceins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycosylation</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus</subject><subject>Hemagglutinins, Viral</subject><subject>Humans</subject><subject>Influenza virus</subject><subject>Lactose</subject><subject>Life Sciences</subject><subject>Microscopy, Fluorescence</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Plasmids - metabolism</subject><subject>Polylysine</subject><subject>Transfection - methods</subject><subject>Tumor Cells, Cultured</subject><subject>Viral Fusion Proteins</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNks1rFDEYxoNY6nb15lWYgwgFZ5vvj4OHUrUrDIpVUbyEbCbpRmcn42S2OP99M91lUS81OYTk-b15P3gAeIrgAkFFzlrTn2G0oAsp0AMwQ4TjkiqOH4IZJJCVCFL5CJyk9ANCRBGjx-BYkrwpmYGPnzpngw-2uHatK4betMm7vti4OpjB1cVqLBpjh5jG5u7exWYsq7IZU8h8aIdYrF1nhrgxhXVNkx6DI2-a5J7szzn48vbN54tlWX24fHdxXpWWCTyUq1whFo7U3NdeEMKRooJKViPJmPGEGOYh9nzFMYRYSCYNUYZZK7lS2CMyB692_3bbVa7WujYX3-iuDxvTjzqaoP9W2rDW1_FGE6gwUjn-dBe__idqeV7p6Q1ilGfE-M2U68U-Vx9_bV0a9CakqVvTurhNWjBOGBPiXhApKYmS6D9AIank-H6QUykk4hl8uQNtH1PqnT80haCejKKzUTRGmupslIw_-3N8B3jvjKw_3-smWdP4bAwb0gGjHJJpzUG5w0Ia3O-DbPqfmgsimF5--67FVaWuvr5-rzm5Bf5r1Dk</recordid><startdate>19930225</startdate><enddate>19930225</enddate><creator>Midoux, Patrick</creator><creator>Mendes, Christina</creator><creator>Legrand, Alain</creator><creator>Raimond, Jacques</creator><creator>Mayer, Roger</creator><creator>Monsigny, Michel</creator><creator>Roche, Annie Claude</creator><general>Oxford University Press</general><scope>BSCLL</scope><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>7QO</scope><scope>7T3</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7U9</scope><scope>H94</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>5PM</scope></search><sort><creationdate>19930225</creationdate><title>Specific gene transfer mediated by lactosylated poly-L-lysine into hepatoma cells</title><author>Midoux, Patrick ; Mendes, Christina ; Legrand, Alain ; Raimond, Jacques ; Mayer, Roger ; Monsigny, Michel ; Roche, Annie Claude</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c572t-b96227e3d6fdf73361947485d1855af33a5f02f6b620027858a39a5cc86992f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Carcinoma, Hepatocellular</topic><topic>Chloroquine</topic><topic>Diverse techniques</topic><topic>Fluorescein</topic><topic>Fluoresceins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycosylation</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus</topic><topic>Hemagglutinins, Viral</topic><topic>Humans</topic><topic>Influenza virus</topic><topic>Lactose</topic><topic>Life Sciences</topic><topic>Microscopy, Fluorescence</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Plasmids - metabolism</topic><topic>Polylysine</topic><topic>Transfection - methods</topic><topic>Tumor Cells, Cultured</topic><topic>Viral Fusion Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Midoux, Patrick</creatorcontrib><creatorcontrib>Mendes, Christina</creatorcontrib><creatorcontrib>Legrand, Alain</creatorcontrib><creatorcontrib>Raimond, Jacques</creatorcontrib><creatorcontrib>Mayer, Roger</creatorcontrib><creatorcontrib>Monsigny, Michel</creatorcontrib><creatorcontrib>Roche, Annie Claude</creatorcontrib><collection>Istex</collection><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>Biotechnology Research Abstracts</collection><collection>Human Genome Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Midoux, Patrick</au><au>Mendes, Christina</au><au>Legrand, Alain</au><au>Raimond, Jacques</au><au>Mayer, Roger</au><au>Monsigny, Michel</au><au>Roche, Annie Claude</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific gene transfer mediated by lactosylated poly-L-lysine into hepatoma cells</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>1993-02-25</date><risdate>1993</risdate><volume>21</volume><issue>4</issue><spage>871</spage><epage>878</epage><pages>871-878</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>Plasmid DNA/glycosylated polylysine complexes were used to transfer in vitro a luciferase reporter gene into human hepatoma cells by a receptor-mediated endocytosis process. HepG2 cells which express a galactose specific membrane lectin were efficiently and selectively transfected with pSV2Luc/lactosylated polylysine complexes in a sugar dependent manner: I) HepG2 cells which do not express membrane lectin specific for mannose were quite poorly transfected with pSV2Luc/mannosylated polylysine complexes, II) HeLa cells which do not express membrane lectin specific for galactose were not transfected with pSV2Luc/lactosylated polylysine complexes. The transfection efficiency of HepG2 cells with pSV2Luc/lactosylated polylysine complexes was greatly enhanced either in the presence of chloroquine or in the presence of a fusogenic peptide. A 22-residue peptide derived from the influenza virus hemagglutinin HA2 N-terminal polypeptide that mimics the fusogenic activity of the virus, was selected. 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| identifier | ISSN: 0305-1048 |
| ispartof | Nucleic acids research, 1993-02, Vol.21 (4), p.871-878 |
| issn | 0305-1048 1362-4962 |
| language | eng |
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| source | MEDLINE; Oxford University Press Journals Digital Archive Legacy; PubMed Central |
| subjects | Amino Acid Sequence Biological and medical sciences Carcinoma, Hepatocellular Chloroquine Diverse techniques Fluorescein Fluoresceins Fundamental and applied biological sciences. Psychology Glycosylation Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral Humans Influenza virus Lactose Life Sciences Microscopy, Fluorescence Molecular and cellular biology Molecular Sequence Data Plasmids - metabolism Polylysine Transfection - methods Tumor Cells, Cultured Viral Fusion Proteins |
| title | Specific gene transfer mediated by lactosylated poly-L-lysine into hepatoma cells |
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