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Volumn 489, Issue 2, 2011, Pages 89-97

Gene transport and expression by arginine-rich cell-penetrating peptides in Paramecium

Author keywords

3 (4,5 Dimethylthiazol 2 yl) 2,5 diohenyltetrazolium bromide (MTT) assay; Cell penetrating peptide (CPP); Green fluorescent protein (GFP); Paramecium caudatum; Transformation; Transgenesis

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; ARGININE; CELL PENETRATING PEPTIDE; GREEN FLUORESCENT PROTEIN; HR9 PROTEIN; PLASMID DNA; PR9 PROTEIN; SYNTHETIC NONA ARGININE; UNCLASSIFIED DRUG;

EID: 80054869039     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2011.08.011     Document Type: Article
Times cited : (28)

References (47)
  • 1
    • 0033030282 scopus 로고    scopus 로고
    • Transformation of Paramecium tetraurelia by electroporation or particle bombardment
    • Boileau A.J., Kissmehl R., Kanabrocki J.A., Saimi Y. Transformation of Paramecium tetraurelia by electroporation or particle bombardment. J. Eukaryot. Microbiol. 1999, 46:56-65.
    • (1999) J. Eukaryot. Microbiol. , vol.46 , pp. 56-65
    • Boileau, A.J.1    Kissmehl, R.2    Kanabrocki, J.A.3    Saimi, Y.4
  • 2
    • 24144447302 scopus 로고    scopus 로고
    • Dye-free protein molecular weight markers
    • Chang M., Hsu H.Y., Lee H.J. Dye-free protein molecular weight markers. Electrophoresis 2005, 26:3062-3068.
    • (2005) Electrophoresis , vol.26 , pp. 3062-3068
    • Chang, M.1    Hsu, H.Y.2    Lee, H.J.3
  • 3
    • 17144368106 scopus 로고    scopus 로고
    • Cellular internalization of fluorescent proteins via arginine-rich intracellular delivery peptide in plant cells
    • Chang M., Chou J.C., Lee H.J. Cellular internalization of fluorescent proteins via arginine-rich intracellular delivery peptide in plant cells. Plant Cell Physiol. 2005, 46:482-488.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 482-488
    • Chang, M.1    Chou, J.C.2    Lee, H.J.3
  • 4
    • 33847351351 scopus 로고    scopus 로고
    • Noncovalent protein transduction in plant cells by macropinocytosis
    • Chang M., Chou J.C., Chen C.P., Liu B.R., Lee H.J. Noncovalent protein transduction in plant cells by macropinocytosis. New Phytol. 2007, 174:46-56.
    • (2007) New Phytol. , vol.174 , pp. 46-56
    • Chang, M.1    Chou, J.C.2    Chen, C.P.3    Liu, B.R.4    Lee, H.J.5
  • 5
    • 34247104947 scopus 로고    scopus 로고
    • Transfection and expression of plasmid DNA in plant cells by an arginine-rich intracellular delivery peptide without protoplast preparation
    • Chen C.P., Chou J.C., Liu B.R., Chang M., Lee H.J. Transfection and expression of plasmid DNA in plant cells by an arginine-rich intracellular delivery peptide without protoplast preparation. FEBS Lett. 2007, 581:1891-1897.
    • (2007) FEBS Lett. , vol.581 , pp. 1891-1897
    • Chen, C.P.1    Chou, J.C.2    Liu, B.R.3    Chang, M.4    Lee, H.J.5
  • 6
    • 33750525085 scopus 로고    scopus 로고
    • An insight into the gene delivery mechanism of the arginine peptide system: role of the peptide/DNA complex size
    • Choi H.S., Kim H.H., Yang J.M., Shin S. An insight into the gene delivery mechanism of the arginine peptide system: role of the peptide/DNA complex size. Biochim. Biophy. Acta 2006, 1760:1604-16112.
    • (2006) Biochim. Biophy. Acta , vol.1760 , pp. 1604-16112
    • Choi, H.S.1    Kim, H.H.2    Yang, J.M.3    Shin, S.4
  • 7
    • 77958152651 scopus 로고    scopus 로고
    • Structural polymorphism of non-covalent peptide-based delivery systems: highway to cellular uptake
    • Deshayes S., Konate K., Aldrian G., Crombez L., Heitz F., Divita G. Structural polymorphism of non-covalent peptide-based delivery systems: highway to cellular uptake. Biochim. Biophys. Acta 2010, 1798:2304-2314.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 2304-2314
    • Deshayes, S.1    Konate, K.2    Aldrian, G.3    Crombez, L.4    Heitz, F.5    Divita, G.6
  • 8
    • 0032214536 scopus 로고    scopus 로고
    • Introducing antisense oligodeoxynucleotides into Paramecium via electroporation
    • Fraga D., et al. Introducing antisense oligodeoxynucleotides into Paramecium via electroporation. J. Eukaryot. Microbiol. 1998, 45:582-588.
    • (1998) J. Eukaryot. Microbiol. , vol.45 , pp. 582-588
    • Fraga, D.1
  • 9
    • 33645120542 scopus 로고    scopus 로고
    • The particle inflow gun can be used to co-transform Paramecium using tungsten particles
    • Fraga D., Keenan E., Hendel E., Nair A., Schofield W. The particle inflow gun can be used to co-transform Paramecium using tungsten particles. J. Eukaryot. Microbiol. 2006, 53:16-19.
    • (2006) J. Eukaryot. Microbiol. , vol.53 , pp. 16-19
    • Fraga, D.1    Keenan, E.2    Hendel, E.3    Nair, A.4    Schofield, W.5
  • 10
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel A.D., Pabo C.O. Cellular uptake of the tat protein from human immunodeficiency virus. Cell 1988, 55:1189-1193.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 11
    • 0036804013 scopus 로고    scopus 로고
    • Arginine-rich peptides: potential for intracellular delivery of macromolecules and the mystery of the translocation mechanisms
    • Futaki S. Arginine-rich peptides: potential for intracellular delivery of macromolecules and the mystery of the translocation mechanisms. Int. J. Pharm. 2002, 245:1-7.
    • (2002) Int. J. Pharm. , vol.245 , pp. 1-7
    • Futaki, S.1
  • 12
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • Green M., Loewenstein P.M. Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell 1988, 55:1179-1188.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 13
    • 35248880092 scopus 로고    scopus 로고
    • TAT transduction: the molecular mechanism and the therapeutic prospects
    • Gump J.M., Dowdy S.F. TAT transduction: the molecular mechanism and the therapeutic prospects. Trends Mol. Med. 2007, 13:443-448.
    • (2007) Trends Mol. Med. , vol.13 , pp. 443-448
    • Gump, J.M.1    Dowdy, S.F.2
  • 15
    • 0029201538 scopus 로고
    • Induction of antibiotic resistance in Paramecium tetraurelia by the bacterial gene APH-3'-II
    • Haynes W.J., Ling K.Y., Saimi Y., Kung C. Induction of antibiotic resistance in Paramecium tetraurelia by the bacterial gene APH-3'-II. J. Eukaryot. Microbiol. 1995, 42:83-91.
    • (1995) J. Eukaryot. Microbiol. , vol.42 , pp. 83-91
    • Haynes, W.J.1    Ling, K.Y.2    Saimi, Y.3    Kung, C.4
  • 17
    • 2342627919 scopus 로고    scopus 로고
    • Factors controlling the efficiency of Tat-mediated plasmid DNA transfer
    • Hellgren I., Gorman J., Sylven C. Factors controlling the efficiency of Tat-mediated plasmid DNA transfer. J. Drug Target. 2004, 12:39-47.
    • (2004) J. Drug Target. , vol.12 , pp. 39-47
    • Hellgren, I.1    Gorman, J.2    Sylven, C.3
  • 18
    • 36448986388 scopus 로고    scopus 로고
    • Transdermal delivery of proteins mediated by non-covalently associated arginine-rich intracellular delivery peptides
    • Hou Y.W., et al. Transdermal delivery of proteins mediated by non-covalently associated arginine-rich intracellular delivery peptides. Exp. Dermatol. 2007, 16:999-1006.
    • (2007) Exp. Dermatol. , vol.16 , pp. 999-1006
    • Hou, Y.W.1
  • 19
    • 67849115975 scopus 로고    scopus 로고
    • Protein transport in human cells mediated by covalently and noncovalently conjugated arginine-rich intracellular delivery peptides
    • Hu J.W., Liu B.R., Wu C.Y., Lu S.W., Lee H.J. Protein transport in human cells mediated by covalently and noncovalently conjugated arginine-rich intracellular delivery peptides. Peptides 2009, 30:1669-1678.
    • (2009) Peptides , vol.30 , pp. 1669-1678
    • Hu, J.W.1    Liu, B.R.2    Wu, C.Y.3    Lu, S.W.4    Lee, H.J.5
  • 20
    • 71749110589 scopus 로고    scopus 로고
    • Analysis of in vitro toxicity of five cell-penetrating peptides by metabolic profiling
    • Kilk K., Mahlapuu R., Soomets U., Langel U. Analysis of in vitro toxicity of five cell-penetrating peptides by metabolic profiling. Toxicol. 2009, 265:87-95.
    • (2009) Toxicol. , vol.265 , pp. 87-95
    • Kilk, K.1    Mahlapuu, R.2    Soomets, U.3    Langel, U.4
  • 21
    • 0016275946 scopus 로고
    • An improved microinjection technique in Paramecium aurelia: transfer of mitochondria conferring erythromycin-resistance
    • Knowles J.K. An improved microinjection technique in Paramecium aurelia: transfer of mitochondria conferring erythromycin-resistance. Exp. Cell Res. 1974, 88:79-87.
    • (1974) Exp. Cell Res. , vol.88 , pp. 79-87
    • Knowles, J.K.1
  • 22
    • 79959899351 scopus 로고    scopus 로고
    • A gene delivery system for human cells mediated by both a cell-penetrating peptide and a piggyBac transposase
    • Lee C.Y., Li J.F., Liou J.S., Charng Y.C., Huang Y.W., Lee H.J. A gene delivery system for human cells mediated by both a cell-penetrating peptide and a piggyBac transposase. Biomaterials 2011, 32:6264-6276.
    • (2011) Biomaterials , vol.32 , pp. 6264-6276
    • Lee, C.Y.1    Li, J.F.2    Liou, J.S.3    Charng, Y.C.4    Huang, Y.W.5    Lee, H.J.6
  • 23
    • 77955081861 scopus 로고    scopus 로고
    • Induction of apoptosis by gene transfer of human TRAIL mediated by arginine-rich intracellular delivery peptides
    • Li J.F., Huang Y., Chen R.L., Lee H.J. Induction of apoptosis by gene transfer of human TRAIL mediated by arginine-rich intracellular delivery peptides. Anticancer Res. 2010, 30:2193-2202.
    • (2010) Anticancer Res. , vol.30 , pp. 2193-2202
    • Li, J.F.1    Huang, Y.2    Chen, R.L.3    Lee, H.J.4
  • 24
    • 39149096277 scopus 로고    scopus 로고
    • Cell membrane diversity in noncovalent protein transduction
    • Liu B.R., Chou J.C., Lee H.J. Cell membrane diversity in noncovalent protein transduction. J. Membr. Biol. 2008, 222:1-15.
    • (2008) J. Membr. Biol. , vol.222 , pp. 1-15
    • Liu, B.R.1    Chou, J.C.2    Lee, H.J.3
  • 25
    • 79952004320 scopus 로고    scopus 로고
    • Cellular internalization of quantum dots noncovalently conjugated with arginine-rich cell-penetrating peptides
    • Liu B.R., et al. Cellular internalization of quantum dots noncovalently conjugated with arginine-rich cell-penetrating peptides. J. Nanosci. Nanotechnol. 2010, 10:6534-6543.
    • (2010) J. Nanosci. Nanotechnol. , vol.10 , pp. 6534-6543
    • Liu, B.R.1
  • 26
    • 79952008175 scopus 로고    scopus 로고
    • Cell-penetrating peptide-functionized quantum dots for intracellular delivery
    • Liu B.R., Huang Y.W., Chiang H.J., Lee H.J. Cell-penetrating peptide-functionized quantum dots for intracellular delivery. J. Nanosci. Nanotechnol. 2010, 10:7897-7905.
    • (2010) J. Nanosci. Nanotechnol. , vol.10 , pp. 7897-7905
    • Liu, B.R.1    Huang, Y.W.2    Chiang, H.J.3    Lee, H.J.4
  • 27
    • 79952009756 scopus 로고    scopus 로고
    • Intracellular delivery of quantum dots mediated by a histidine- and arginine-rich HR9 cell-penetrating peptide through the direct membrane translocation mechanism
    • Liu B.R., Huang Y.W., Winiarz J.G., Chiang H.J., Lee H.J. Intracellular delivery of quantum dots mediated by a histidine- and arginine-rich HR9 cell-penetrating peptide through the direct membrane translocation mechanism. Biomaterials 2011, 32:3520-3537.
    • (2011) Biomaterials , vol.32 , pp. 3520-3537
    • Liu, B.R.1    Huang, Y.W.2    Winiarz, J.G.3    Chiang, H.J.4    Lee, H.J.5
  • 28
    • 77249178234 scopus 로고    scopus 로고
    • Arginine-rich intracellular delivery peptides synchronously deliver covalently and noncovalently linked proteins into plant cells
    • Lu S.W., et al. Arginine-rich intracellular delivery peptides synchronously deliver covalently and noncovalently linked proteins into plant cells. J. Agricult. Food Chem. 2010, 58:2288-2294.
    • (2010) J. Agricult. Food Chem. , vol.58 , pp. 2288-2294
    • Lu, S.W.1
  • 29
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 1983, 65:55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 30
    • 77956561675 scopus 로고    scopus 로고
    • CPP-ZFN: a potential DNA-targeting anti-malarial drug
    • Nain V., Sahi S., Verma A. CPP-ZFN: a potential DNA-targeting anti-malarial drug. Malaria J. 2010, 9:258.
    • (2010) Malaria J. , vol.9 , pp. 258
    • Nain, V.1    Sahi, S.2    Verma, A.3
  • 31
    • 0030068995 scopus 로고    scopus 로고
    • Identification of a human immunodeficiency virus type 1 Tat epitope that is neuroexcitatory and neurotoxic
    • Nath A., et al. Identification of a human immunodeficiency virus type 1 Tat epitope that is neuroexcitatory and neurotoxic. J. Virol. 1996, 70:1475-1480.
    • (1996) J. Virol. , vol.70 , pp. 1475-1480
    • Nath, A.1
  • 33
    • 33745698016 scopus 로고    scopus 로고
    • Use of penetratin-linked peptide in Dictyostelium
    • Ryves W.J., Harwood A.J. Use of penetratin-linked peptide in Dictyostelium. Mol. Biotechnol. 2006, 33:123-131.
    • (2006) Mol. Biotechnol. , vol.33 , pp. 123-131
    • Ryves, W.J.1    Harwood, A.J.2
  • 36
    • 75549083574 scopus 로고    scopus 로고
    • Gene transfer using self-assembled ternary complexes of cationic magnetic nanoparticles, plasmid DNA and cell-penetrating Tat peptide
    • Song H.P., et al. Gene transfer using self-assembled ternary complexes of cationic magnetic nanoparticles, plasmid DNA and cell-penetrating Tat peptide. Biomaterials 2010, 31:769-778.
    • (2010) Biomaterials , vol.31 , pp. 769-778
    • Song, H.P.1
  • 37
    • 0028222581 scopus 로고
    • The effects of nucleoside analogs on telomerase and telomeres in Tetrahymena
    • Strahl C., Blackburn E.H. The effects of nucleoside analogs on telomerase and telomeres in Tetrahymena. Nucl. Acids Res. 1994, 22:893-900.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 893-900
    • Strahl, C.1    Blackburn, E.H.2
  • 38
    • 0035925057 scopus 로고    scopus 로고
    • Expression of telomerase reverse transcriptase and telomere elongation during sexual maturation in Paramecium caudatum
    • Takenaka Y., Matsuura T., Haga N., Mitsui Y. Expression of telomerase reverse transcriptase and telomere elongation during sexual maturation in Paramecium caudatum. Gene 2001, 264:153-161.
    • (2001) Gene , vol.264 , pp. 153-161
    • Takenaka, Y.1    Matsuura, T.2    Haga, N.3    Mitsui, Y.4
  • 39
    • 0037028491 scopus 로고    scopus 로고
    • Transformation of Paramecium caudatum with a novel expression vector harboring codon-optimized GFP gene
    • Takenaka Y., Haga N., Harumoto T., Matsuura T., Mitsui Y. Transformation of Paramecium caudatum with a novel expression vector harboring codon-optimized GFP gene. Gene 2002, 284:233-240.
    • (2002) Gene , vol.284 , pp. 233-240
    • Takenaka, Y.1    Haga, N.2    Harumoto, T.3    Matsuura, T.4    Mitsui, Y.5
  • 40
    • 34247574165 scopus 로고    scopus 로고
    • Direct observation of histone H2B-YFP fusion proteins and transport of their mRNA between conjugating Paramecia
    • Takenaka Y., Yanagi A., Masuda H., Mitsui Y., Mizuno H., Haga N. Direct observation of histone H2B-YFP fusion proteins and transport of their mRNA between conjugating Paramecia. Gene 2007, 395:108-115.
    • (2007) Gene , vol.395 , pp. 108-115
    • Takenaka, Y.1    Yanagi, A.2    Masuda, H.3    Mitsui, Y.4    Mizuno, H.5    Haga, N.6
  • 41
    • 67349116815 scopus 로고    scopus 로고
    • Fusion of a cell penetrating peptide from HIV-1 TAT to the Theileria parva antigen Tp2 enhances the stimulation of bovine CD8+ T cell responses
    • Tineg A.N., et al. Fusion of a cell penetrating peptide from HIV-1 TAT to the Theileria parva antigen Tp2 enhances the stimulation of bovine CD8+ T cell responses. Vet. Immunol. Immunopathol. 2009, 130:107-113.
    • (2009) Vet. Immunol. Immunopathol. , vol.130 , pp. 107-113
    • Tineg, A.N.1
  • 42
    • 77952369001 scopus 로고    scopus 로고
    • Helper-independent piggyBac plasmids for gene delivery approaches: strategies for avoiding potential genotoxic effects
    • Urshitz J., et al. Helper-independent piggyBac plasmids for gene delivery approaches: strategies for avoiding potential genotoxic effects. Proc. Natl. Acad. Sci. USA 2010, 107:8117-8122.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8117-8122
    • Urshitz, J.1
  • 43
    • 79551710488 scopus 로고    scopus 로고
    • 1001 model organisms to study cilia and flagella
    • Vincensini L., Blisnick T., Bastin P. 1001 model organisms to study cilia and flagella. Biol. Cell 2011, 103:109-130.
    • (2011) Biol. Cell , vol.103 , pp. 109-130
    • Vincensini, L.1    Blisnick, T.2    Bastin, P.3
  • 44
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vives E., Brodin P., Lebleu B. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 1997, 272:16010-16017.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 45
    • 33745187338 scopus 로고    scopus 로고
    • Arginine-rich intracellular delivery peptides noncovalently transport protein into living cells
    • Wang Y.H., et al. Arginine-rich intracellular delivery peptides noncovalently transport protein into living cells. Biochem. Biophys. Res. Commun. 2006, 346:758-767.
    • (2006) Biochem. Biophys. Res. Commun. , vol.346 , pp. 758-767
    • Wang, Y.H.1
  • 46
    • 34247605933 scopus 로고    scopus 로고
    • An intracellular delivery method for siRNA by an arginine-rich peptide
    • Wang Y.H., Hou Y.W., Lee H.J. An intracellular delivery method for siRNA by an arginine-rich peptide. J. Biochem. Biophys. Methods 2007, 70:579-586.
    • (2007) J. Biochem. Biophys. Methods , vol.70 , pp. 579-586
    • Wang, Y.H.1    Hou, Y.W.2    Lee, H.J.3
  • 47
    • 78650721545 scopus 로고    scopus 로고
    • Nona-arginine facilitates delivery of quantum dots into cells via multiple pathways
    • Xu Y., et al. Nona-arginine facilitates delivery of quantum dots into cells via multiple pathways. J. Biomed. Biotechnol. 2010, 2010:948543.
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 948543
    • Xu, Y.1


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