Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis
Identifieur interne : 001248 ( Istex/Corpus ); précédent : 001247; suivant : 001249Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis
Auteurs : Ernst Wagner ; David Curiel ; Matt CottenSource :
- Advanced Drug Delivery Reviews [ 0169-409X ] ; 1994.
English descriptors
- Teeft :
- Acad, Acta, Adenovirus, Adriamycin, Antitfr, Antitfr antibodies, Antitumor activity, Asialoglycoprotein receptor, Biochim, Biol, Biophys, Birnstiel, Bone marrow, Brain capillaries, Cancer inst, Cancer therapy, Cell lines, Chem, Chloroquine, Conjugate, Cotten, Cttfr, Curiel, Cytotoxic, Cytotoxic activity, Cytotoxicity, Delivery, Diphtheria, Diphtheria toxin, Drug delivery, Drug delivery reviews, Endocytosis, Endocytosis pathway, Endosomal, Endosomal membrane, Endosomes, Endothelial cells, Enhancement, Epidermal growth factor, Erythroid cells, Eukaryotic cells, Exotoxin, Fibroblast, Gene, Gene delivery, Gene expression, Gene transfer, Hawtrey, Hela cells, Hepatocytes, High levels, Immunotoxin, Immunotoxins, Influenza virus, Internal vesicles, Internalization, Intracellular, Leukemia, Leukemia cells, Leukemic, Leukemic cells, Ligand, Light units, Liposome, Mammalian cells, Methods enzymol, Monensin, Monoclonal, Monoclonal antibodies, Natl, Nucleic, Nucleic acids, Nude mice, Other groups, Pastan, Pathway, Peptide, Polycations, Polylysine, Primary cells, Proc, Protein toxins, Pseudomonas, Pseudomonas exotoxin, Raso, Receptor, Recombinant, Ricin, Toxicity, Toxin, Toxin conjugates, Toxin proteins, Transfected, Transfection, Transferrin, Transferrin receptor, Transferrin receptors, Trowbridge, Tumor cells, Unpublished results, Uptake, Various cell types, Vesicle, Viral, Viral genome, Virol, Vivo, Vivo gene transfer, Willingham, Youle, Zatloukal.
Abstract
Abstract: Transferrin, an iron-transporting serum glycoprotein, is efficiently taken up into cells by the process of receptor-mediated endocytosis. Transferrin receptors are found on the surface of most proliferating cells, in elevated numbers on erythroblasts and on many kinds of tumors. The efficient cellular mechanism for uptake of transferrin has been subverted for the delivery of low-molecular-weight drugs, protein toxins, and liposomes by linkage of these agents to transferrin or to anti-transferrin receptor antibodies. Linkage may be via chemical conjugation procedures or by the generation of chimeric fusion proteins. Transferrin conjugated to DNA-binding compounds (e.g. polycations or intercalating agents) has been successfully used for the import of DNA molecules into cells. High-level gene expression is obtained only if endosome-disruptive agents such as influenza hemagglutinin peptides or adenovirus particles are included which release the DNA complex from intracellular vesicles into the cytoplasm.
Url:
DOI: 10.1016/0169-409X(94)90008-6
Links to Exploration step
ISTEX:5DB1BDC31D405841AE5FDE79B2E890C26404D396Le document en format XML
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sortKey="Curiel, David" sort="Curiel, David" uniqKey="Curiel D" first="David" last="Curiel">David Curiel</name><affiliation><mods:affiliation>Gene Therapy Program, University of Alabama, Birmingham, AL, USA</mods:affiliation></affiliation></author><author><name sortKey="Cotten, Matt" sort="Cotten, Matt" uniqKey="Cotten M" first="Matt" last="Cotten">Matt Cotten</name><affiliation><mods:affiliation>Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Advanced Drug Delivery Reviews</title><title level="j" type="abbrev">ADR</title><idno type="ISSN">0169-409X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">14</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="113">113</biblScope><biblScope unit="page" to="135">135</biblScope></imprint><idno type="ISSN">0169-409X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0169-409X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Acta</term><term>Adenovirus</term><term>Adriamycin</term><term>Antitfr</term><term>Antitfr antibodies</term><term>Antitumor activity</term><term>Asialoglycoprotein receptor</term><term>Biochim</term><term>Biol</term><term>Biophys</term><term>Birnstiel</term><term>Bone marrow</term><term>Brain capillaries</term><term>Cancer inst</term><term>Cancer therapy</term><term>Cell lines</term><term>Chem</term><term>Chloroquine</term><term>Conjugate</term><term>Cotten</term><term>Cttfr</term><term>Curiel</term><term>Cytotoxic</term><term>Cytotoxic activity</term><term>Cytotoxicity</term><term>Delivery</term><term>Diphtheria</term><term>Diphtheria toxin</term><term>Drug delivery</term><term>Drug delivery reviews</term><term>Endocytosis</term><term>Endocytosis pathway</term><term>Endosomal</term><term>Endosomal membrane</term><term>Endosomes</term><term>Endothelial cells</term><term>Enhancement</term><term>Epidermal growth factor</term><term>Erythroid cells</term><term>Eukaryotic cells</term><term>Exotoxin</term><term>Fibroblast</term><term>Gene</term><term>Gene delivery</term><term>Gene expression</term><term>Gene transfer</term><term>Hawtrey</term><term>Hela cells</term><term>Hepatocytes</term><term>High levels</term><term>Immunotoxin</term><term>Immunotoxins</term><term>Influenza virus</term><term>Internal vesicles</term><term>Internalization</term><term>Intracellular</term><term>Leukemia</term><term>Leukemia cells</term><term>Leukemic</term><term>Leukemic cells</term><term>Ligand</term><term>Light units</term><term>Liposome</term><term>Mammalian cells</term><term>Methods enzymol</term><term>Monensin</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Natl</term><term>Nucleic</term><term>Nucleic acids</term><term>Nude mice</term><term>Other groups</term><term>Pastan</term><term>Pathway</term><term>Peptide</term><term>Polycations</term><term>Polylysine</term><term>Primary cells</term><term>Proc</term><term>Protein toxins</term><term>Pseudomonas</term><term>Pseudomonas exotoxin</term><term>Raso</term><term>Receptor</term><term>Recombinant</term><term>Ricin</term><term>Toxicity</term><term>Toxin</term><term>Toxin conjugates</term><term>Toxin proteins</term><term>Transfected</term><term>Transfection</term><term>Transferrin</term><term>Transferrin receptor</term><term>Transferrin receptors</term><term>Trowbridge</term><term>Tumor cells</term><term>Unpublished results</term><term>Uptake</term><term>Various cell types</term><term>Vesicle</term><term>Viral</term><term>Viral genome</term><term>Virol</term><term>Vivo</term><term>Vivo gene transfer</term><term>Willingham</term><term>Youle</term><term>Zatloukal</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Transferrin, an iron-transporting serum glycoprotein, is efficiently taken up into cells by the process of receptor-mediated endocytosis. Transferrin receptors are found on the surface of most proliferating cells, in elevated numbers on erythroblasts and on many kinds of tumors. The efficient cellular mechanism for uptake of transferrin has been subverted for the delivery of low-molecular-weight drugs, protein toxins, and liposomes by linkage of these agents to transferrin or to anti-transferrin receptor antibodies. Linkage may be via chemical conjugation procedures or by the generation of chimeric fusion proteins. Transferrin conjugated to DNA-binding compounds (e.g. polycations or intercalating agents) has been successfully used for the import of DNA molecules into cells. High-level gene expression is obtained only if endosome-disruptive agents such as influenza hemagglutinin peptides or adenovirus particles are included which release the DNA complex from intracellular vesicles into the cytoplasm.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>transferrin</json:string><json:string>receptor</json:string><json:string>endocytosis</json:string><json:string>adenovirus</json:string><json:string>gene transfer</json:string><json:string>natl</json:string><json:string>biol</json:string><json:string>acad</json:string><json:string>proc</json:string><json:string>chem</json:string><json:string>ricin</json:string><json:string>drug delivery reviews</json:string><json:string>immunotoxins</json:string><json:string>toxin</json:string><json:string>immunotoxin</json:string><json:string>pathway</json:string><json:string>liposome</json:string><json:string>intracellular</json:string><json:string>monensin</json:string><json:string>pastan</json:string><json:string>viral</json:string><json:string>chloroquine</json:string><json:string>birnstiel</json:string><json:string>transferrin receptor</json:string><json:string>cytotoxic</json:string><json:string>transfection</json:string><json:string>exotoxin</json:string><json:string>polylysine</json:string><json:string>endosomal</json:string><json:string>antitfr</json:string><json:string>gene 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mice</json:string><json:string>biophys</json:string><json:string>youle</json:string><json:string>gene</json:string><json:string>acta</json:string><json:string>adriamycin</json:string><json:string>hawtrey</json:string><json:string>cytotoxicity</json:string><json:string>virol</json:string><json:string>polycations</json:string><json:string>gene expression</json:string><json:string>biochim</json:string><json:string>willingham</json:string><json:string>fibroblast</json:string><json:string>pseudomonas</json:string><json:string>brain capillaries</json:string><json:string>light units</json:string><json:string>nucleic acids</json:string><json:string>unpublished results</json:string><json:string>antitfr antibodies</json:string><json:string>eukaryotic cells</json:string><json:string>diphtheria toxin</json:string><json:string>endocytosis pathway</json:string><json:string>methods enzymol</json:string><json:string>bone marrow</json:string><json:string>internal vesicles</json:string><json:string>various cell types</json:string><json:string>toxin conjugates</json:string><json:string>high levels</json:string><json:string>cell lines</json:string><json:string>antitumor activity</json:string><json:string>primary cells</json:string><json:string>endothelial cells</json:string><json:string>viral genome</json:string><json:string>monoclonal antibodies</json:string><json:string>leukemic cells</json:string><json:string>vivo</json:string><json:string>nucleic</json:string><json:string>leukemia</json:string><json:string>conjugate</json:string><json:string>influenza virus</json:string><json:string>erythroid cells</json:string><json:string>cytotoxic activity</json:string><json:string>mammalian cells</json:string><json:string>drug delivery</json:string><json:string>vivo gene transfer</json:string><json:string>protein toxins</json:string><json:string>epidermal growth factor</json:string><json:string>transferrin receptors</json:string><json:string>cancer therapy</json:string><json:string>asialoglycoprotein receptor</json:string><json:string>toxin proteins</json:string><json:string>leukemia cells</json:string><json:string>hela cells</json:string><json:string>other groups</json:string><json:string>cancer inst</json:string><json:string>endosomal membrane</json:string><json:string>uptake</json:string><json:string>delivery</json:string><json:string>cotten</json:string></teeft></keywords><author><json:item><name>Ernst Wagner</name><affiliations><json:string>Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria</json:string></affiliations></json:item><json:item><name>David Curiel</name><affiliations><json:string>Gene Therapy Program, University of Alabama, Birmingham, AL, USA</json:string></affiliations></json:item><json:item><name>Matt Cotten</name><affiliations><json:string>Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Tf = transferrin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>TfR = transferrin receptor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>αTfR = anti-transferrin receptor antibody</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>AdV = adenovirus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DT = diphtheria toxin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PE = Pseudomonas exotoxin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Adenovirus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DNA transfection</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Drug delivery</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Endocytosis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Endosome disruption</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Gene transfer</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Gene therapy</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Immunotoxin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Polylysine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Transferrin</value></json:item></subject><arkIstex>ark:/67375/6H6-2215WF0Z-W</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Review article</json:string></originalGenre><abstract>Abstract: Transferrin, an iron-transporting serum glycoprotein, is efficiently taken up into cells by the process of receptor-mediated endocytosis. Transferrin receptors are found on the surface of most proliferating cells, in elevated numbers on erythroblasts and on many kinds of tumors. The efficient cellular mechanism for uptake of transferrin has been subverted for the delivery of low-molecular-weight drugs, protein toxins, and liposomes by linkage of these agents to transferrin or to anti-transferrin receptor antibodies. Linkage may be via chemical conjugation procedures or by the generation of chimeric fusion proteins. Transferrin conjugated to DNA-binding compounds (e.g. polycations or intercalating agents) has been successfully used for the import of DNA molecules into cells. High-level gene expression is obtained only if endosome-disruptive agents such as influenza hemagglutinin peptides or adenovirus particles are included which release the DNA complex from intracellular vesicles into the cytoplasm.</abstract><qualityIndicators><score>8.68</score><pdfWordCount>12662</pdfWordCount><pdfCharCount>81258</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>23</pdfPageCount><pdfPageSize>540 x 720 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>140</abstractWordCount><abstractCharCount>1024</abstractCharCount><keywordCount>16</keywordCount></qualityIndicators><title>Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis</title><pii><json:string>0169-409X(94)90008-6</json:string></pii><genre><json:string>review-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>78</volume><pages><first>3039</first></pages></serie><host><title>Advanced Drug Delivery Reviews</title><language><json:string>unknown</json:string></language><publicationDate>1994</publicationDate><issn><json:string>0169-409X</json:string></issn><pii><json:string>S0169-409X(00)X0103-2</json:string></pii><volume>14</volume><issue>1</issue><pages><first>113</first><last>135</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1994</json:string></date><geogName></geogName><orgName><json:string>University of Alabama</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName></persName><placeName><json:string>Birmingham</json:string><json:string>Austria</json:string><json:string>USA</json:string><json:string>AL</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Accepted July 1, 1993</json:string><json:string>Received February 23,1993</json:string><json:string>E. Wagner et al.</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-2215WF0Z-W</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - pharmacology & pharmacy</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - clinical medicine</json:string><json:string>3 - pharmacology & pharmacy</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Pharmacology, Toxicology and Pharmaceutics</json:string><json:string>3 - Pharmaceutical Science</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1994</publicationDate><copyrightDate>1994</copyrightDate><doi><json:string>10.1016/0169-409X(94)90008-6</json:string></doi><id>5DB1BDC31D405841AE5FDE79B2E890C26404D396</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-2215WF0Z-W/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-2215WF0Z-W/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-2215WF0Z-W/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1994</date></publicationStmt><notesStmt><note type="review-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis</title><author xml:id="author-0000"><persName><forename type="first">Ernst</forename><surname>Wagner</surname></persName><note type="correspondence"><p>Corresponding author.</p></note><affiliation>Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria</affiliation></author><author xml:id="author-0001"><persName><forename type="first">David</forename><surname>Curiel</surname></persName><affiliation>Gene Therapy Program, University of Alabama, Birmingham, AL, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Matt</forename><surname>Cotten</surname></persName><affiliation>Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria</affiliation></author><idno type="istex">5DB1BDC31D405841AE5FDE79B2E890C26404D396</idno><idno type="ark">ark:/67375/6H6-2215WF0Z-W</idno><idno type="DOI">10.1016/0169-409X(94)90008-6</idno><idno type="PII">0169-409X(94)90008-6</idno></analytic><monogr><title level="j">Advanced Drug Delivery Reviews</title><title level="j" type="abbrev">ADR</title><idno type="pISSN">0169-409X</idno><idno type="PII">S0169-409X(00)X0103-2</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994"></date><biblScope unit="volume">14</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="113">113</biblScope><biblScope unit="page" to="135">135</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1994</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Transferrin, an iron-transporting serum glycoprotein, is efficiently taken up into cells by the process of receptor-mediated endocytosis. Transferrin receptors are found on the surface of most proliferating cells, in elevated numbers on erythroblasts and on many kinds of tumors. The efficient cellular mechanism for uptake of transferrin has been subverted for the delivery of low-molecular-weight drugs, protein toxins, and liposomes by linkage of these agents to transferrin or to anti-transferrin receptor antibodies. Linkage may be via chemical conjugation procedures or by the generation of chimeric fusion proteins. Transferrin conjugated to DNA-binding compounds (e.g. polycations or intercalating agents) has been successfully used for the import of DNA molecules into cells. High-level gene expression is obtained only if endosome-disruptive agents such as influenza hemagglutinin peptides or adenovirus particles are included which release the DNA complex from intracellular vesicles into the cytoplasm.</p></abstract><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>Tf = transferrin</term></item><item><term>TfR = transferrin receptor</term></item><item><term>αTfR = anti-transferrin receptor antibody</term></item><item><term>AdV = adenovirus</term></item><item><term>DT = diphtheria toxin</term></item><item><term>PE = Pseudomonas exotoxin</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Adenovirus</term></item><item><term>DNA transfection</term></item><item><term>Drug delivery</term></item><item><term>Endocytosis</term></item><item><term>Endosome disruption</term></item><item><term>Gene transfer</term></item><item><term>Gene therapy</term></item><item><term>Immunotoxin</term></item><item><term>Polylysine</term></item><item><term>Transferrin</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1994">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-2215WF0Z-W/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="rev"><item-info><jid>ADR</jid><aid>94900086</aid><ce:pii>0169-409X(94)90008-6</ce:pii><ce:doi>10.1016/0169-409X(94)90008-6</ce:doi><ce:copyright type="unknown" year="1994"></ce:copyright></item-info><head><ce:title>Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis</ce:title><ce:author-group><ce:author><ce:given-name>Ernst</ce:given-name><ce:surname>Wagner</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>David</ce:given-name><ce:surname>Curiel</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Matt</ce:given-name><ce:surname>Cotten</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Gene Therapy Program, University of Alabama, Birmingham, AL, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Corresponding author.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="23" month="2" year="1993"></ce:date-received><ce:date-accepted day="1" month="7" year="1993"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Transferrin, an iron-transporting serum glycoprotein, is efficiently taken up into cells by the process of receptor-mediated endocytosis. Transferrin receptors are found on the surface of most proliferating cells, in elevated numbers on erythroblasts and on many kinds of tumors. The efficient cellular mechanism for uptake of transferrin has been subverted for the delivery of low-molecular-weight drugs, protein toxins, and liposomes by linkage of these agents to transferrin or to anti-transferrin receptor antibodies. Linkage may be via chemical conjugation procedures or by the generation of chimeric fusion proteins. Transferrin conjugated to DNA-binding compounds (e.g. polycations or intercalating agents) has been successfully used for the import of DNA molecules into cells. High-level gene expression is obtained only if endosome-disruptive agents such as influenza hemagglutinin peptides or adenovirus particles are included which release the DNA complex from intracellular vesicles into the cytoplasm.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>Tf = transferrin</ce:text></ce:keyword><ce:keyword><ce:text>TfR = transferrin receptor</ce:text></ce:keyword><ce:keyword><ce:text>αTfR = anti-transferrin receptor antibody</ce:text></ce:keyword><ce:keyword><ce:text>AdV = adenovirus</ce:text></ce:keyword><ce:keyword><ce:text>DT = diphtheria toxin</ce:text></ce:keyword><ce:keyword><ce:text>PE = <ce:italic>Pseudomonas</ce:italic> exotoxin</ce:text></ce:keyword></ce:keywords><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Adenovirus</ce:text></ce:keyword><ce:keyword><ce:text>DNA transfection</ce:text></ce:keyword><ce:keyword><ce:text>Drug delivery</ce:text></ce:keyword><ce:keyword><ce:text>Endocytosis</ce:text></ce:keyword><ce:keyword><ce:text>Endosome disruption</ce:text></ce:keyword><ce:keyword><ce:text>Gene transfer</ce:text></ce:keyword><ce:keyword><ce:text>Gene therapy</ce:text></ce:keyword><ce:keyword><ce:text>Immunotoxin</ce:text></ce:keyword><ce:keyword><ce:text>Polylysine</ce:text></ce:keyword><ce:keyword><ce:text>Transferrin</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis</title></titleInfo><name type="personal"><namePart type="given">Ernst</namePart><namePart type="family">Wagner</namePart><affiliation>Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria</affiliation><description>Corresponding author.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David</namePart><namePart type="family">Curiel</namePart><affiliation>Gene Therapy Program, University of Alabama, Birmingham, AL, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Matt</namePart><namePart type="family">Cotten</namePart><affiliation>Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="Review article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1994</dateIssued><copyrightDate encoding="w3cdtf">1994</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Transferrin, an iron-transporting serum glycoprotein, is efficiently taken up into cells by the process of receptor-mediated endocytosis. Transferrin receptors are found on the surface of most proliferating cells, in elevated numbers on erythroblasts and on many kinds of tumors. The efficient cellular mechanism for uptake of transferrin has been subverted for the delivery of low-molecular-weight drugs, protein toxins, and liposomes by linkage of these agents to transferrin or to anti-transferrin receptor antibodies. Linkage may be via chemical conjugation procedures or by the generation of chimeric fusion proteins. Transferrin conjugated to DNA-binding compounds (e.g. polycations or intercalating agents) has been successfully used for the import of DNA molecules into cells. High-level gene expression is obtained only if endosome-disruptive agents such as influenza hemagglutinin peptides or adenovirus particles are included which release the DNA complex from intracellular vesicles into the cytoplasm.</abstract><subject><genre>Abbreviations</genre><topic>Tf = transferrin</topic><topic>TfR = transferrin receptor</topic><topic>αTfR = anti-transferrin receptor antibody</topic><topic>AdV = adenovirus</topic><topic>DT = diphtheria toxin</topic><topic>PE = Pseudomonas exotoxin</topic></subject><subject><genre>Keywords</genre><topic>Adenovirus</topic><topic>DNA transfection</topic><topic>Drug delivery</topic><topic>Endocytosis</topic><topic>Endosome disruption</topic><topic>Gene transfer</topic><topic>Gene therapy</topic><topic>Immunotoxin</topic><topic>Polylysine</topic><topic>Transferrin</topic></subject><relatedItem type="host"><titleInfo><title>Advanced Drug Delivery Reviews</title></titleInfo><titleInfo type="abbreviated"><title>ADR</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1994</dateIssued></originInfo><identifier type="ISSN">0169-409X</identifier><identifier type="PII">S0169-409X(00)X0103-2</identifier><part><date>1994</date><detail type="issue"><title>Drug and Gene Targeting with (glyco)-Proteins and Other Glycoconjugates </title></detail><detail type="volume"><number>14</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>156</end></extent><extent unit="pages"><start>113</start><end>135</end></extent></part></relatedItem><identifier type="istex">5DB1BDC31D405841AE5FDE79B2E890C26404D396</identifier><identifier type="ark">ark:/67375/6H6-2215WF0Z-W</identifier><identifier type="DOI">10.1016/0169-409X(94)90008-6</identifier><identifier type="PII">0169-409X(94)90008-6</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-2215WF0Z-W/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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