메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages

Direct translocation as major cellular uptake for CADY self-assembling peptide-based nanoparticles

Author keywords

[No Author keywords available]

Indexed keywords

GLYCYLLEUCYLTRYPTOPHYLARGINYLALANYLLEUCYLTRYPTOPHYLARGINYLLEUCYLLEUCYLARGINYLSERYLLEUCYLTRYPTOPHYLARGINYLLEUCYLLEUCYLTRYPTOPHYLLYSYLALANINE CYANURIC ACID; HEPARAN SULFATE; NANOCARRIER; NANOPARTICLE; PEPTIDE CADY; PHOSPHOLIPID; PROTEOHEPARAN SULFATE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; CALCIUM; CELL PENETRATING PEPTIDE; DRUG CARRIER;

EID: 80053609746     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025924     Document Type: Article
Times cited : (92)

References (49)
  • 1
    • 0032545933 scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire A, Xu S, Montgomery MK, Kostas SA, Driver SE, et al. (1988) Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 391: 806-811.
    • (1988) Nature , vol.391 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5
  • 2
    • 3242677639 scopus 로고    scopus 로고
    • siRNAs: applications in functional genomics and potential as therapeutics
    • Dorsett Y, Tuschl T, (2004) siRNAs: applications in functional genomics and potential as therapeutics. Nat Rev Drug Discovery 3: 318-329.
    • (2004) Nat Rev Drug Discovery , vol.3 , pp. 318-329
    • Dorsett, Y.1    Tuschl, T.2
  • 4
    • 58749104364 scopus 로고    scopus 로고
    • The promises and pitfalls of RNA-interference-based therapeutics
    • Castanotto D, Rossi JJ, (2009) The promises and pitfalls of RNA-interference-based therapeutics. Nature 457: 426-433.
    • (2009) Nature , vol.457 , pp. 426-433
    • Castanotto, D.1    Rossi, J.J.2
  • 6
    • 77649275761 scopus 로고    scopus 로고
    • Novel RNA-based strategies for therapeutic gene silencing
    • Sibley CR, Seow Y, Wood MJ, (2010) Novel RNA-based strategies for therapeutic gene silencing. Mol Ther 18: 466-476.
    • (2010) Mol Ther , vol.18 , pp. 466-476
    • Sibley, C.R.1    Seow, Y.2    Wood, M.J.3
  • 7
    • 47249138782 scopus 로고    scopus 로고
    • Mechanisms and strategies for effective delivery of antisense and siRNA oligonucleotides
    • Juliano R, Alam MR, Dixit V, Kang H, (2008) Mechanisms and strategies for effective delivery of antisense and siRNA oligonucleotides. Nucleic Acids Res 36: 4158-4171.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4158-4171
    • Juliano, R.1    Alam, M.R.2    Dixit, V.3    Kang, H.4
  • 8
    • 67649408951 scopus 로고    scopus 로고
    • siRNA delivery using peptide transduction domains
    • Eguchi A, Dowdy SF, (2009) siRNA delivery using peptide transduction domains. Trends Pharmacol Sci 30: 341-345.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 341-345
    • Eguchi, A.1    Dowdy, S.F.2
  • 9
    • 67249096677 scopus 로고    scopus 로고
    • Nonviral methods for siRNA delivery
    • Gao K, Huang G, (2009) Nonviral methods for siRNA delivery. Mol Pharm 6: 651-658.
    • (2009) Mol Pharm , vol.6 , pp. 651-658
    • Gao, K.1    Huang, G.2
  • 10
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: from molecular mechanism to therapeutics
    • Heitz F, Morris MC, Divita G, (2009) Twenty years of cell-penetrating peptides: from molecular mechanism to therapeutics. Br J Pharmacol 157: 195-206.
    • (2009) Br J Pharmacol , vol.157 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 11
    • 77958153239 scopus 로고    scopus 로고
    • In vivo biodistribution and efficacy of peptide mediated delivery
    • Järver P, Mäger I, Langel Ü, (2010) In vivo biodistribution and efficacy of peptide mediated delivery. Trends Pharmacol Sci 11: 528-535.
    • (2010) Trends Pharmacol Sci , vol.11 , pp. 528-535
    • Järver, P.1    Mäger, I.2    Langel, Ü.3
  • 12
    • 77949890248 scopus 로고    scopus 로고
    • Cell penetrating peptides: overview and applications to the delivery of oligonucleotides
    • Said Hassane F, Saleh AF, Abes R, Gait MJ, Lebleu B, (2010) Cell penetrating peptides: overview and applications to the delivery of oligonucleotides. Cell Mol Life Sci 67: 715-726.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 715-726
    • Said Hassane, F.1    Saleh, A.F.2    Abes, R.3    Gait, M.J.4    Lebleu, B.5
  • 13
    • 77958150472 scopus 로고    scopus 로고
    • Happy birthday cell penetrating peptides: already 20 years
    • Brasseur R, Divita G, (2010) Happy birthday cell penetrating peptides: already 20 years. Biochim Biophys Acta 1798: 2177-2181.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 2177-2181
    • Brasseur, R.1    Divita, G.2
  • 14
    • 77958150359 scopus 로고    scopus 로고
    • Peptide-mediated protein delivery-Which pathways are penetrable?
    • Räägel H, Säälik P, Pooga M, (2010) Peptide-mediated protein delivery-Which pathways are penetrable? Biochim Biophys Acta 1798: 2240-2248.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 2240-2248
    • Räägel, H.1    Säälik, P.2    Pooga, M.3
  • 15
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: from molecular mechanisms to therapeutics
    • Morris MC, Deshayes S, Heitz F, Divita G, (2008) Cell-penetrating peptides: from molecular mechanisms to therapeutics. Biol Cell 100: 201-217.
    • (2008) Biol Cell , vol.100 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 16
    • 33846223900 scopus 로고    scopus 로고
    • Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis
    • Nakase I, Tadokoro A, Kawabata N, Takeuchi T, Katoh H, et al. (2007) Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis. Biochemistry 246: 492-450.
    • (2007) Biochemistry , vol.246 , pp. 450-492
    • Nakase, I.1    Tadokoro, A.2    Kawabata, N.3    Takeuchi, T.4    Katoh, H.5
  • 17
    • 34147103472 scopus 로고    scopus 로고
    • First step of the cell-penetrating peptide mechanism involves Rac1 GTPase-dependent actin-network Remodelling
    • Gerbal-Chaloin S, Gondeau C, Aldrian-Herrada G, Heitz F, Gauthier-Rouvière C, et al. (2007) First step of the cell-penetrating peptide mechanism involves Rac1 GTPase-dependent actin-network Remodelling. Biol Cell 99: 223-238.
    • (2007) Biol Cell , vol.99 , pp. 223-238
    • Gerbal-Chaloin, S.1    Gondeau, C.2    Aldrian-Herrada, G.3    Heitz, F.4    Gauthier-Rouvière, C.5
  • 18
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia JJ, Stan RV, Dowdy S, (2004) Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med 10: 310-315.
    • (2004) Nat Med , vol.10 , pp. 310-315
    • Wadia, J.J.1    Stan, R.V.2    Dowdy, S.3
  • 19
    • 0346460957 scopus 로고    scopus 로고
    • Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake
    • Richard JP, Melikov K, Vives E, Ramos C, Verbeure B, et al. (2003) Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake. J Biol Chem 278: 585-590.
    • (2003) J Biol Chem , vol.278 , pp. 585-590
    • Richard, J.P.1    Melikov, K.2    Vives, E.3    Ramos, C.4    Verbeure, B.5
  • 20
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • Duchardt F, Fotin-Mleczek M, Schwarz H, Fischer, Brock R, (2007) A comprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic 8: 848-66.
    • (2007) Traffic , vol.8 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer4    Brock, R.5
  • 21
    • 31544438701 scopus 로고    scopus 로고
    • Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides
    • Fischer R, Fotin-Mleczek M, Hufnagel H, Brock R, (2005) Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides. Chembiochem 6: 2126-2142.
    • (2005) Chembiochem , vol.6 , pp. 2126-2142
    • Fischer, R.1    Fotin-Mleczek, M.2    Hufnagel, H.3    Brock, R.4
  • 22
    • 1042288299 scopus 로고    scopus 로고
    • Insight into the mechanism of internalization of the cell-penetrating carrier peptide Pep-1 through conformational analysis
    • Deshayes S, Heitz A, Morris MC, Charnet P, Divita G, et al. (2004) Insight into the mechanism of internalization of the cell-penetrating carrier peptide Pep-1 through conformational analysis. Biochemistry 43: 1449-1457.
    • (2004) Biochemistry , vol.43 , pp. 1449-1457
    • Deshayes, S.1    Heitz, A.2    Morris, M.C.3    Charnet, P.4    Divita, G.5
  • 23
    • 0037592877 scopus 로고    scopus 로고
    • Insight into the mechanism of the peptide-based gene delivery system MPG: implications for delivery of siRNA into mammalian cells
    • Simeoni F, Morris MC, Heitz F, Divita G, (2003) Insight into the mechanism of the peptide-based gene delivery system MPG: implications for delivery of siRNA into mammalian cells. Nucleic Acids Res 31: 2717-2724.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2717-2724
    • Simeoni, F.1    Morris, M.C.2    Heitz, F.3    Divita, G.4
  • 24
    • 58149217884 scopus 로고    scopus 로고
    • A new potent secondary amphipathic cell-penetrating peptide for siRNA delivery into mammalian cells
    • Crombez L, Aldrian-Herrada G, Konate K, Nguyen QN, McMaster GK, et al. (2009) A new potent secondary amphipathic cell-penetrating peptide for siRNA delivery into mammalian cells. Mol Ther 17: 95-103.
    • (2009) Mol Ther , vol.17 , pp. 95-103
    • Crombez, L.1    Aldrian-Herrada, G.2    Konate, K.3    Nguyen, Q.N.4    McMaster, G.K.5
  • 25
    • 67149093390 scopus 로고    scopus 로고
    • Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein
    • Eguchi A, Meade BR, Chang YC, Fredrickson CT, Willert K, et al. (2009) Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein. Nat Biotechnol 27: 567-571.
    • (2009) Nat Biotechnol , vol.27 , pp. 567-571
    • Eguchi, A.1    Meade, B.R.2    Chang, Y.C.3    Fredrickson, C.T.4    Willert, K.5
  • 26
    • 79956015439 scopus 로고    scopus 로고
    • Design of a peptide-based vector, PepFect6, for efficient delivery of siRNA in cell culture and systemically in vivo
    • El Andaloussi S, Lehto T, Mäger I, Rosenthal-Aizman K, Oprea II, et al. (2011) Design of a peptide-based vector, PepFect6, for efficient delivery of siRNA in cell culture and systemically in vivo. Nucleic Acids Res 39: 3972-3987.
    • (2011) Nucleic Acids Res , vol.39 , pp. 3972-3987
    • El Andaloussi, S.1    Lehto, T.2    Mäger, I.3    Rosenthal-Aizman, K.4    Oprea, I.I.5
  • 27
    • 68149125757 scopus 로고    scopus 로고
    • Targeting cyclin B1 through peptide-based delivery of siRNA prevents tumour growth
    • Crombez L, Morris MC, Dufort S, Aldrian-Herrada G, Nguyen Q, et al. (2009) Targeting cyclin B1 through peptide-based delivery of siRNA prevents tumour growth. Nucleic Acids Res 37: 4559-4569.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4559-4569
    • Crombez, L.1    Morris, M.C.2    Dufort, S.3    Aldrian-Herrada, G.4    Nguyen, Q.5
  • 28
    • 77951225648 scopus 로고    scopus 로고
    • Insight into the cellular uptake mechanism of a secondary amphipathic cell penetrating peptide for siRNA delivery
    • Konate K, Crombez L, Deshayes S, Thomas A, Brasseur R, et al. (2010) Insight into the cellular uptake mechanism of a secondary amphipathic cell penetrating peptide for siRNA delivery. Biochemistry 49: 3393-3402.
    • (2010) Biochemistry , vol.49 , pp. 3393-3402
    • Konate, K.1    Crombez, L.2    Deshayes, S.3    Thomas, A.4    Brasseur, R.5
  • 29
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner SD, Schmid SL, (2003) Regulated portals of entry into the cell. Nature 422: 37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 30
    • 77649272916 scopus 로고    scopus 로고
    • The use of inhibitors to study endocytic pathways of gene carriers: optimization and pitfalls
    • Vercauteren D, Vandenbroucke RE, Jones AT, Rejman J, Demeester J, et al. (2010) The use of inhibitors to study endocytic pathways of gene carriers: optimization and pitfalls. Mol Ther 18: 561-569.
    • (2010) Mol Ther , vol.18 , pp. 561-569
    • Vercauteren, D.1    Vandenbroucke, R.E.2    Jones, A.T.3    Rejman, J.4    Demeester, J.5
  • 31
    • 0345306592 scopus 로고    scopus 로고
    • The GTP/GDP cycling of Rho GTPase TCL is an essential regulator of the early endocytic pathway
    • de Toledo M, Senic-Matuglia F, Salamero J, Uze G, Comunale F, et al. (2003) The GTP/GDP cycling of Rho GTPase TCL is an essential regulator of the early endocytic pathway. Mol Biol Cell 14: 4846-4856.
    • (2003) Mol Biol Cell , vol.14 , pp. 4846-4856
    • de Toledo, M.1    Senic-Matuglia, F.2    Salamero, J.3    Uze, G.4    Comunale, F.5
  • 34
    • 0034762332 scopus 로고    scopus 로고
    • Internalization of cholera toxin by different endocytic mechanisms
    • Torgersen ML, Skretting G, van Deurs B, Sandvig K, (2001) Internalization of cholera toxin by different endocytic mechanisms. J Cell Sci 114: 3737-3747.
    • (2001) J Cell Sci , vol.114 , pp. 3737-3747
    • Torgersen, M.L.1    Skretting, G.2    van Deurs, B.3    Sandvig, K.4
  • 35
    • 38149080449 scopus 로고    scopus 로고
    • Distinct role of clathrin-mediated endocytosis in the functional uptake of cholera toxin
    • Broeck DV, Lagrou AR, De Wolf MJS, (2007) Distinct role of clathrin-mediated endocytosis in the functional uptake of cholera toxin. Acta Biochim 54: 757-767.
    • (2007) Acta Biochim , vol.54 , pp. 757-767
    • Broeck, D.V.1    Lagrou, A.R.2    De Wolf, M.J.S.3
  • 36
    • 0023449563 scopus 로고
    • Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway
    • Tran D, Carpentier J-L, Sawano F, Gorden P, Orci L, (1987) Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway. Proc Natl Acad Sci 84: 7957-7961.
    • (1987) Proc Natl Acad Sci , vol.84 , pp. 7957-7961
    • Tran, D.1    Carpentier, J.-L.2    Sawano, F.3    Gorden, P.4    Orci, L.5
  • 38
    • 3543051871 scopus 로고    scopus 로고
    • Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells
    • Rothbard JB, Jessop TC, Lewis RS, Murray BA, Wender PA, (2004) Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells. J Am Chem Soc 126: 9506-9507.
    • (2004) J Am Chem Soc , vol.126 , pp. 9506-9507
    • Rothbard, J.B.1    Jessop, T.C.2    Lewis, R.S.3    Murray, B.A.4    Wender, P.A.5
  • 39
    • 77958154973 scopus 로고    scopus 로고
    • Cell biology meets biophysics to unveil the different mechanisms of penetratin internalization in cells
    • Alves ID, Jiao CY, Aubry S, Aussedat B, Burlina F, et al. (2010) Cell biology meets biophysics to unveil the different mechanisms of penetratin internalization in cells. Biochim Biophys Acta 1798: 2231-2239.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 2231-2239
    • Alves, I.D.1    Jiao, C.Y.2    Aubry, S.3    Aussedat, B.4    Burlina, F.5
  • 40
    • 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, et al. (2010) Structural polymorphism of non-covalent peptide-based delivery systems: highway to cellular uptake. Biochim Biophys Acta 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
  • 41
    • 33749385780 scopus 로고    scopus 로고
    • Cell-penetrating peptides and antimicrobial peptides: how different are they?
    • Henriques ST, Melo MN, Castanho MA, (2006) Cell-penetrating peptides and antimicrobial peptides: how different are they? Biochem J 399: 1-7.
    • (2006) Biochem J , vol.399 , pp. 1-7
    • Henriques, S.T.1    Melo, M.N.2    Castanho, M.A.3
  • 42
    • 0344824647 scopus 로고    scopus 로고
    • Plasma membrane disruption: repair, prevention, adaptation
    • McNeil PL, Steinhardt RA, (2003) Plasma membrane disruption: repair, prevention, adaptation. Annu Rev Cell Dev Biol 19: 697-731.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 697-731
    • McNeil, P.L.1    Steinhardt, R.A.2
  • 43
    • 74049160383 scopus 로고    scopus 로고
    • Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction
    • Gump JM, June RK, Dowdy SF, (2010) Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction. J Biol Chem 285: 1500-1507.
    • (2010) J Biol Chem , vol.285 , pp. 1500-1507
    • Gump, J.M.1    June, R.K.2    Dowdy, S.F.3
  • 44
    • 66549123169 scopus 로고    scopus 로고
    • Low concentration thresholds of plasma membranes for rapid energy-independent translocation of a cell-penetrating peptide
    • Watkins CL, Schmaljohann D, Futaki S, Jones AT, (2009) Low concentration thresholds of plasma membranes for rapid energy-independent translocation of a cell-penetrating peptide. Biochem J 420: 179-89.
    • (2009) Biochem J , vol.420 , pp. 179-189
    • Watkins, C.L.1    Schmaljohann, D.2    Futaki, S.3    Jones, A.T.4
  • 45
    • 0030804766 scopus 로고    scopus 로고
    • A new peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • Morris MC, Vidal P, Chaloin L, Heitz F, Divita G, (1997) A new peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Res 25: 2730-2736.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2730-2736
    • Morris, M.C.1    Vidal, P.2    Chaloin, L.3    Heitz, F.4    Divita, G.5
  • 46
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris MC, Depollier J, Mery J, Heitz F, Divita G, (2001) A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nat Biotechnol 19: 1173-1176.
    • (2001) Nat Biotechnol , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 47
    • 77952580991 scopus 로고    scopus 로고
    • Secondary structure of cell-penetrating peptides controls membrane interaction and insertion
    • Eiríksdóttir E, Konate K, Langel U, Divita G, Deshayes S, (2010) Secondary structure of cell-penetrating peptides controls membrane interaction and insertion. Biochim Biophys Acta 1798: 1119-1128.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1119-1128
    • Eiríksdóttir, E.1    Konate, K.2    Langel, U.3    Divita, G.4    Deshayes, S.5
  • 48
    • 58249095956 scopus 로고    scopus 로고
    • The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake
    • Palm-Apergi C, Lorents A, Padari K, Pooga M, Hällbrink M, (2009) The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake. FASEB J 23: 214-223.
    • (2009) FASEB J , vol.23 , pp. 214-223
    • Palm-Apergi, C.1    Lorents, A.2    Padari, K.3    Pooga, M.4    Hällbrink, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.