Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo.
Identifieur interne : 003629 ( Main/Exploration ); précédent : 003628; suivant : 003630Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo.
Auteurs : Z. Mi [États-Unis] ; J. Mai ; X. Lu ; P D RobbinsSource :
- Molecular therapy : the journal of the American Society of Gene Therapy [ 1525-0016 ] ; 2000.
Descripteurs français
- KwdFr :
- Animaux, Articulation du genou (métabolisme), Cations, Cellules cultivées (enzymologie), Fibrosarcome (métabolisme), Fragments peptidiques (métabolisme), Fragments peptidiques (usage thérapeutique), Injections articulaires, Lapins, Microscopie confocale, Protéine G ran (métabolisme), Protéines de fusion recombinantes (métabolisme), Protéines du gène tat (), Protéines du gène tat (métabolisme), Protéines luminescentes (métabolisme), Souris, Souris de lignée C57BL, Séquence d'acides aminés, Techniques in vitro, Transduction génétique (), beta-Galactosidase (métabolisme).
- MESH :
- enzymologie : Cellules cultivées.
- métabolisme : Articulation du genou, Fibrosarcome, Fragments peptidiques, Protéine G ran, Protéines de fusion recombinantes, Protéines du gène tat, Protéines luminescentes, beta-Galactosidase.
- usage thérapeutique : Fragments peptidiques.
- Animaux, Cations, Injections articulaires, Lapins, Microscopie confocale, Protéines du gène tat, Souris, Souris de lignée C57BL, Séquence d'acides aminés, Techniques in vitro, Transduction génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cations, Cells, Cultured (enzymology), Fibrosarcoma (metabolism), Gene Products, tat (chemistry), Gene Products, tat (metabolism), In Vitro Techniques, Injections, Intra-Articular, Knee Joint (metabolism), Luminescent Proteins (metabolism), Mice, Mice, Inbred C57BL, Microscopy, Confocal, Peptide Fragments (metabolism), Peptide Fragments (therapeutic use), Rabbits, Recombinant Fusion Proteins (metabolism), Transduction, Genetic (methods), beta-Galactosidase (metabolism), ran GTP-Binding Protein (metabolism).
- MESH :
- chemical , chemistry : Gene Products, tat.
- chemical , metabolism : Gene Products, tat, Luminescent Proteins, Peptide Fragments, Recombinant Fusion Proteins, beta-Galactosidase, ran GTP-Binding Protein.
- chemical , therapeutic use : Peptide Fragments.
- chemical : Cations.
- enzymology : Cells, Cultured.
- metabolism : Fibrosarcoma, Knee Joint.
- methods : Transduction, Genetic.
- Amino Acid Sequence, Animals, In Vitro Techniques, Injections, Intra-Articular, Mice, Mice, Inbred C57BL, Microscopy, Confocal, Rabbits.
Abstract
Protein transduction domains (PTDs), such as the third helix of the Drosophila Antennapedia homeobox gene (Antp) and the HIV TAT PTD, possess a characteristic positive charge on the basis of their enrichment for arginine and lysine residues. To determine whether cationic peptides are able to function as protein transduction domains, 12-mer peptide sequences from an M13 phage library were selected for synthesis on the basis of their varying cationic charge content. In addition, polylysine and polyarginine peptides were synthesized in order to assess the effect of charge contribution in protein transduction. Coupling of the biotinylated peptides to avidin-beta-galactosidase facilitated transduction in a wide variety of cell lines and primary cells, including islet beta-cells, synovial cells, polarized airway epithelial cells, dendritic cells, myoblasts, and tumor cells. Two of the peptides, PTD-4 and PTD-5, mediated transduction nearly 600-fold more efficiently than a random control peptide, but with an efficiency similar to the TAT PTD and the 12 mers of polylysine and polyarginine. Furthermore, confocal analysis of biotinylated peptide-streptavidin-Cy3 conjugates demonstrated that the internalized PTDs are found in both the nuclei and the cytoplasm of treated cells. When tested in vivo, the PTDs were able to facilitate efficient and rapid protein delivery into rabbit synovium and mouse solid tumors following intraarticular and intratumoral administration, respectively. These novel PTDs can be used to transfer therapeutic proteins and DNA for the treatment of a wide variety of diseases, including arthritis and cancer.
DOI: 10.1006/mthe.2000.0137
PubMed: 11020349
Affiliations:
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Le document en format XML
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<term>Animals</term>
<term>Cations</term>
<term>Cells, Cultured (enzymology)</term>
<term>Fibrosarcoma (metabolism)</term>
<term>Gene Products, tat (chemistry)</term>
<term>Gene Products, tat (metabolism)</term>
<term>In Vitro Techniques</term>
<term>Injections, Intra-Articular</term>
<term>Knee Joint (metabolism)</term>
<term>Luminescent Proteins (metabolism)</term>
<term>Mice</term>
<term>Mice, Inbred C57BL</term>
<term>Microscopy, Confocal</term>
<term>Peptide Fragments (metabolism)</term>
<term>Peptide Fragments (therapeutic use)</term>
<term>Rabbits</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Transduction, Genetic (methods)</term>
<term>beta-Galactosidase (metabolism)</term>
<term>ran GTP-Binding Protein (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Articulation du genou (métabolisme)</term>
<term>Cations</term>
<term>Cellules cultivées (enzymologie)</term>
<term>Fibrosarcome (métabolisme)</term>
<term>Fragments peptidiques (métabolisme)</term>
<term>Fragments peptidiques (usage thérapeutique)</term>
<term>Injections articulaires</term>
<term>Lapins</term>
<term>Microscopie confocale</term>
<term>Protéine G ran (métabolisme)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines du gène tat ()</term>
<term>Protéines du gène tat (métabolisme)</term>
<term>Protéines luminescentes (métabolisme)</term>
<term>Souris</term>
<term>Souris de lignée C57BL</term>
<term>Séquence d'acides aminés</term>
<term>Techniques in vitro</term>
<term>Transduction génétique ()</term>
<term>beta-Galactosidase (métabolisme)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Gene Products, tat</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Gene Products, tat</term>
<term>Luminescent Proteins</term>
<term>Peptide Fragments</term>
<term>Recombinant Fusion Proteins</term>
<term>beta-Galactosidase</term>
<term>ran GTP-Binding Protein</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cations</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cellules cultivées</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cells, Cultured</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fibrosarcoma</term>
<term>Knee Joint</term>
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<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Transduction, Genetic</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Articulation du genou</term>
<term>Fibrosarcome</term>
<term>Fragments peptidiques</term>
<term>Protéine G ran</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines du gène tat</term>
<term>Protéines luminescentes</term>
<term>beta-Galactosidase</term>
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</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>In Vitro Techniques</term>
<term>Injections, Intra-Articular</term>
<term>Mice</term>
<term>Mice, Inbred C57BL</term>
<term>Microscopy, Confocal</term>
<term>Rabbits</term>
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<term>Cations</term>
<term>Injections articulaires</term>
<term>Lapins</term>
<term>Microscopie confocale</term>
<term>Protéines du gène tat</term>
<term>Souris</term>
<term>Souris de lignée C57BL</term>
<term>Séquence d'acides aminés</term>
<term>Techniques in vitro</term>
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<front><div type="abstract" xml:lang="en">Protein transduction domains (PTDs), such as the third helix of the Drosophila Antennapedia homeobox gene (Antp) and the HIV TAT PTD, possess a characteristic positive charge on the basis of their enrichment for arginine and lysine residues. To determine whether cationic peptides are able to function as protein transduction domains, 12-mer peptide sequences from an M13 phage library were selected for synthesis on the basis of their varying cationic charge content. In addition, polylysine and polyarginine peptides were synthesized in order to assess the effect of charge contribution in protein transduction. Coupling of the biotinylated peptides to avidin-beta-galactosidase facilitated transduction in a wide variety of cell lines and primary cells, including islet beta-cells, synovial cells, polarized airway epithelial cells, dendritic cells, myoblasts, and tumor cells. Two of the peptides, PTD-4 and PTD-5, mediated transduction nearly 600-fold more efficiently than a random control peptide, but with an efficiency similar to the TAT PTD and the 12 mers of polylysine and polyarginine. Furthermore, confocal analysis of biotinylated peptide-streptavidin-Cy3 conjugates demonstrated that the internalized PTDs are found in both the nuclei and the cytoplasm of treated cells. When tested in vivo, the PTDs were able to facilitate efficient and rapid protein delivery into rabbit synovium and mouse solid tumors following intraarticular and intratumoral administration, respectively. These novel PTDs can be used to transfer therapeutic proteins and DNA for the treatment of a wide variety of diseases, including arthritis and cancer.</div>
</front>
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