메뉴 건너뛰기




Volumn 57, Issue 4 SPEC.ISS., 2005, Pages 547-558

Membrane-permeable arginine-rich peptides and the translocation mechanisms

Author keywords

Cell permeable peptide; Drug delivery; HIV 1 Tat; Oligoarginine; Penetratin; Protein transduction

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; VECTORS; VIRUSES;

EID: 13844272399     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.addr.2004.10.009     Document Type: Review
Times cited : (371)

References (61)
  • 1
    • 0141942114 scopus 로고    scopus 로고
    • Membrane permeability commonly shared among arginine-rich peptides
    • S. Futaki, S. Goto, and Y. Sugiura Membrane permeability commonly shared among arginine-rich peptides J. Mol. Recognit. 16 2003 260 264
    • (2003) J. Mol. Recognit. , vol.16 , pp. 260-264
    • Futaki, S.1    Goto, S.2    Sugiura, Y.3
  • 2
    • 0038048992 scopus 로고    scopus 로고
    • Modulation of cellular function by TAT mediated transduction of full length proteins
    • J.S. Wadia, and S.F. Dowdy Modulation of cellular function by TAT mediated transduction of full length proteins Curr. Prot. Pept. Sci. 4 2003 97 104
    • (2003) Curr. Prot. Pept. Sci. , vol.4 , pp. 97-104
    • Wadia, J.S.1    Dowdy, S.F.2
  • 4
    • 0033948268 scopus 로고    scopus 로고
    • Messenger proteins: Homeoproteins, TAT and others
    • A. Prochiantz Messenger proteins: homeoproteins, TAT and others Curr. Opin. Cell Biol. 12 2000 400 406
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 400-406
    • Prochiantz, A.1
  • 6
    • 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
    • E. Vivès, P. Brodin, and B. Lebleu A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus J. Biol. Chem. 272 1997 16010 16017
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vivès, E.1    Brodin, P.2    Lebleu, B.3
  • 7
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • D. Derossi, A.H. Joliot, G. Chassaing, and A. Prochiantz The third helix of the Antennapedia homeodomain translocates through biological membranes J. Biol. Chem. 269 1994 10444 10450
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 8
    • 0037169486 scopus 로고    scopus 로고
    • Possible existence of common internalization mechanisms among arginine-rich peptides
    • T. Suzuki, S. Futaki, M. Niwa, S. Tanaka, K. Ueda, and Y. Sugiura Possible existence of common internalization mechanisms among arginine-rich peptides J. Biol. Chem. 277 2002 2437 2443
    • (2002) J. Biol. Chem. , vol.277 , pp. 2437-2443
    • Suzuki, T.1    Futaki, S.2    Niwa, M.3    Tanaka, S.4    Ueda, K.5    Sugiura, Y.6
  • 9
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • S. Futaki, T. Suzuki, W. Ohashi, T. Yagami, S. Tanaka, K. Ueda, and Y. Sugiura Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery J. Biol. Chem. 276 2001 5836 5840
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 11
    • 0033802715 scopus 로고    scopus 로고
    • Evidence for an amphipathicity independent cellular uptake of amphipathic cell-penetrating peptides
    • A. Scheller, B. Wiesner, M. Melzig, M. Bienert, and J. Oehlke Evidence for an amphipathicity independent cellular uptake of amphipathic cell-penetrating peptides Eur. J. Biochem. 267 2000 6043 6050
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6043-6050
    • Scheller, A.1    Wiesner, B.2    Melzig, M.3    Bienert, M.4    Oehlke, J.5
  • 13
    • 0029006149 scopus 로고
    • Inhibition of nuclear translocation of transcription factor NF-kB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence
    • Y.Z. Lin, S.Y. Yao, R.A. Veach, T.R. Torgerson, and J. Hawiger Inhibition of nuclear translocation of transcription factor NF-kB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence J. Biol. Chem. 270 1995 14255 14258
    • (1995) J. Biol. Chem. , vol.270 , pp. 14255-14258
    • Lin, Y.Z.1    Yao, S.Y.2    Veach, R.A.3    Torgerson, T.R.4    Hawiger, J.5
  • 14
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • M.C. Morris, J. Depollier, J. Mery, F. Heitz, and G. Divita A peptide carrier for the delivery of biologically active proteins into mammalian cells Nat. Biotechnol. 19 2001 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
  • 15
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • G. Elliott, and P. O'Hare Intercellular trafficking and protein delivery by a herpesvirus structural protein Cell 88 1997 223 233
    • (1997) Cell , vol.88 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 18
    • 0344824453 scopus 로고    scopus 로고
    • Arginine-based molecular transporters: The synthesis and chemical evaluation of releasable taxol-transporter conjugates
    • T.A. Kirschberg, C.L. VanDeusen, J.B. Rothbard, M. Yang, and P.A. Wender Arginine-based molecular transporters: the synthesis and chemical evaluation of releasable taxol-transporter conjugates Org. Lett. 5 2003 3459 3462
    • (2003) Org. Lett. , vol.5 , pp. 3459-3462
    • Kirschberg, T.A.1    Vandeusen, C.L.2    Rothbard, J.B.3    Yang, M.4    Wender, P.A.5
  • 20
  • 21
    • 0034006169 scopus 로고    scopus 로고
    • Tat peptide-derivatized magnetic nanoparticles allow in vivo tracking and recovery of progenitor cells
    • M. Lewin, N. Carlesso, C.H. Tung, X.W. Tang, D. Cory, D.T. Scadden, and R. Weissleder Tat peptide-derivatized magnetic nanoparticles allow in vivo tracking and recovery of progenitor cells Nat. Biotechnol. 18 2000 410 414
    • (2000) Nat. Biotechnol. , vol.18 , pp. 410-414
    • Lewin, M.1    Carlesso, N.2    Tung, C.H.3    Tang, X.W.4    Cory, D.5    Scadden, D.T.6    Weissleder, R.7
  • 22
    • 0035902477 scopus 로고    scopus 로고
    • TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors
    • V.P. Torchilin, R. Rammohan, V. Weissig, and T.S. Levchenko TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors Proc. Natl. Acad. Sci. U. S. A. 98 2001 8786 8791
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8786-8791
    • Torchilin, V.P.1    Rammohan, R.2    Weissig, V.3    Levchenko, T.S.4
  • 25
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • A.D. Frankel, and C.O. Pabo Cellular uptake of the tat protein from human immunodeficiency virus Cell 55 1988 1189 1193
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 26
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • M. Green, and P.M. Loewenstein Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein Cell 55 1988 1179 1188
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 30
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • S.R. Schwarze, A. Ho, A. Vocero-Akbani, and S.F. Dowdy In vivo protein transduction: delivery of a biologically active protein into the mouse Science 285 1999 1569 1572
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 31
    • 0029048796 scopus 로고
    • Structural variety of arginine-rich RNA-binding peptides
    • R. Tan, and A.D. Frankel Structural variety of arginine-rich RNA-binding peptides Proc. Natl. Acad. Sci. U. S. A. 92 1995 5282 5286
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 5282-5286
    • Tan, R.1    Frankel, A.D.2
  • 33
    • 0141891450 scopus 로고    scopus 로고
    • Can transcription factors function as cell-cell signalling molecules?
    • A. Prochiantz, and A. Joliot Can transcription factors function as cell-cell signalling molecules? Nat. Rev., Mol. Cell Biol. 4 2003 814 819
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 814-819
    • Prochiantz, A.1    Joliot, A.2
  • 34
    • 0037172801 scopus 로고    scopus 로고
    • Translocation of branched-chain arginine peptides through cell membranes: Flexibility in the spatial disposition of positive charges in membrane-permeable peptides
    • S. Futaki, I. Nakase, T. Suzuki, Y. Zhang, and Y. Sugiura Translocation of branched-chain arginine peptides through cell membranes: flexibility in the spatial disposition of positive charges in membrane-permeable peptides Biochemistry 41 2002 7925 7930
    • (2002) Biochemistry , vol.41 , pp. 7925-7930
    • Futaki, S.1    Nakase, I.2    Suzuki, T.3    Zhang, Y.4    Sugiura, Y.5
  • 37
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • D.J. Mitchell, D.T. Kim, L. Steinman, C.G. Fathman, and J.B. Rothbard Polyarginine enters cells more efficiently than other polycationic homopolymers J. Pept. Res. 56 2000 318 325
    • (2000) J. Pept. Res. , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Steinman, L.3    Fathman, C.G.4    Rothbard, J.B.5
  • 38
    • 0037103242 scopus 로고    scopus 로고
    • Arginine-rich molecular transporters for drug delivery: Role of backbone spacing in cellular uptake
    • J.B. Rothbard, E. Kreider, C.L. VanDeusen, L. Wright, B.L. Wylie, and P.A. Wender Arginine-rich molecular transporters for drug delivery: role of backbone spacing in cellular uptake J. Med. Chem. 45 2002 3612 3618
    • (2002) J. Med. Chem. , vol.45 , pp. 3612-3618
    • Rothbard, J.B.1    Kreider, E.2    Vandeusen, C.L.3    Wright, L.4    Wylie, B.L.5    Wender, P.A.6
  • 39
    • 0037073171 scopus 로고    scopus 로고
    • Oligocarbamate molecular transporters: Design, synthesis, and biological evaluation of a new class of transporters for drug delivery
    • P.A. Wender, J.B. Rothbard, T.C. Jessop, E.L. Kreider, and B.L. Wylie Oligocarbamate molecular transporters: design, synthesis, and biological evaluation of a new class of transporters for drug delivery J. Am. Chem. Soc. 124 2002 13382 13383
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 13382-13383
    • Wender, P.A.1    Rothbard, J.B.2    Jessop, T.C.3    Kreider, E.L.4    Wylie, B.L.5
  • 42
    • 0038615916 scopus 로고    scopus 로고
    • Novel binding and efficient cellular uptake of guanidine-based peptide nucleic acids (GPNA)
    • P. Zhou, M. Wang, L. Du, G.W. Fisher, A. Waggoner, and D.H. Ly Novel binding and efficient cellular uptake of guanidine-based peptide nucleic acids (GPNA) J. Am. Chem. Soc. 125 2003 6878 6879
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6878-6879
    • Zhou, P.1    Wang, M.2    Du, L.3    Fisher, G.W.4    Waggoner, A.5    Ly, D.H.6
  • 43
    • 0035951091 scopus 로고    scopus 로고
    • Neomycin B-arginine conjugate, a novel HIV-1 Tat antagonist: Synthesis and anti-HIV activities
    • A. Litovchick, A. Lapidot, M. Eisenstein, A. Kalinkovich, and G. Borkow Neomycin B-arginine conjugate, a novel HIV-1 Tat antagonist: synthesis and anti-HIV activities Biochemistry 40 2001 15612 15623
    • (2001) Biochemistry , vol.40 , pp. 15612-15623
    • Litovchick, A.1    Lapidot, A.2    Eisenstein, M.3    Kalinkovich, A.4    Borkow, G.5
  • 44
    • 0141954275 scopus 로고    scopus 로고
    • Cellular uptake of aminoglycosides, guanidinoglycosides, and poly-arginine
    • N.W. Luedtke, P. Carmichael, and Y. Tor Cellular uptake of aminoglycosides, guanidinoglycosides, and poly-arginine J. Am. Chem. Soc. 125 2003 12374 12375
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12374-12375
    • Luedtke, N.W.1    Carmichael, P.2    Tor, Y.3
  • 47
    • 1642578411 scopus 로고    scopus 로고
    • Mechanism of improved gene transfer by the N-terminal stearylation of octaarginine: Enhanced cellular association by hydrophobic core formation
    • I.A. Khalil, S. Futaki, M. Niwa, Y. Baba, N. Kaji, H. Kamiya, and H. Harashima Mechanism of improved gene transfer by the N-terminal stearylation of octaarginine: enhanced cellular association by hydrophobic core formation Gene Ther. 11 2004 636 644
    • (2004) Gene Ther. , vol.11 , pp. 636-644
    • Khalil, I.A.1    Futaki, S.2    Niwa, M.3    Baba, Y.4    Kaji, N.5    Kamiya, H.6    Harashima, H.7
  • 48
    • 0038176513 scopus 로고    scopus 로고
    • Oligomers of the arginine-rich motif of the HIV-1 TAT protein are capable of transferring plasmid DNA into cells
    • C. Rudolph, C. Plank, J. Lausier, U. Schillinger, R.H. Muller, and J. Rosenecker Oligomers of the arginine-rich motif of the HIV-1 TAT protein are capable of transferring plasmid DNA into cells J. Biol. Chem. 278 2003 11411 11418
    • (2003) J. Biol. Chem. , vol.278 , pp. 11411-11418
    • Rudolph, C.1    Plank, C.2    Lausier, J.3    Schillinger, U.4    Muller, R.H.5    Rosenecker, J.6
  • 49
    • 0036836978 scopus 로고    scopus 로고
    • Novel branching membrane translocational peptide as gene delivery vector
    • C.H. Tung, S. Mueller, and R. Weissleder Novel branching membrane translocational peptide as gene delivery vector Bioorg. Med. Chem. 10 2002 3609 3614
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3609-3614
    • Tung, C.H.1    Mueller, S.2    Weissleder, R.3
  • 50
    • 0042383244 scopus 로고    scopus 로고
    • Gene transfer via reversible plasmid condensation with cysteine-flanked, internally spaced arginine-rich peptides
    • Z. Siprashvili, F.A. Scholl, S.F. Oliver, A. Adams, C.H. Contag, P.A. Wender, and P.A. Khavari Gene transfer via reversible plasmid condensation with cysteine-flanked, internally spaced arginine-rich peptides Hum. Gene Ther. 14 2003 1225 1233
    • (2003) Hum. Gene Ther. , vol.14 , pp. 1225-1233
    • Siprashvili, Z.1    Scholl, F.A.2    Oliver, S.F.3    Adams, A.4    Contag, C.H.5    Wender, P.A.6    Khavari, P.A.7
  • 53
    • 0038725603 scopus 로고    scopus 로고
    • TAT-liposomes: A novel intracellular drug carrier
    • V.P. Torchilin, and T.S. Levchenko TAT-liposomes: a novel intracellular drug carrier Curr. Prot. Pept. Sci. 4 2003 133 140
    • (2003) Curr. Prot. Pept. Sci. , vol.4 , pp. 133-140
    • Torchilin, V.P.1    Levchenko, T.S.2
  • 55
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • S.D. Conner, and S.L. Schmid Regulated portals of entry into the cell Nature 422 2003 37 44
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 56
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • J.S. Wadia, R.V. Stan, and S.F. Dowdy Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis Nat. Med. 10 2004 310 315
    • (2004) Nat. Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 58
    • 1842529513 scopus 로고    scopus 로고
    • A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides
    • R. Fischer, K. Kohler, M. Fotin-Mleczek, and R. Brock A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides J. Biol. Chem. 279 2004 12625 12635
    • (2004) J. Biol. Chem. , vol.279 , pp. 12625-12635
    • Fischer, R.1    Kohler, K.2    Fotin-Mleczek, M.3    Brock, R.4
  • 59
    • 0348010364 scopus 로고    scopus 로고
    • Cytoplasmic and nuclear delivery of a TAT-derived peptide and a β-peptide after endocytic uptake into HeLa cells
    • T.B. Potocky, A.K. Menon, and S.H. Gellman Cytoplasmic and nuclear delivery of a TAT-derived peptide and a β-peptide after endocytic uptake into HeLa cells J. Biol. Chem. 278 2003 50188 50194
    • (2003) J. Biol. Chem. , vol.278 , pp. 50188-50194
    • Potocky, T.B.1    Menon, A.K.2    Gellman, S.H.3
  • 60
    • 0041816277 scopus 로고    scopus 로고
    • Antennapedia and HIV transactivator of transcription (TAT) gprotein transduction domainsh promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans
    • S. Console, C. Marty, C. Garcia-Echeverria, R. Schwendener, and K. Ballmer-Hofer Antennapedia and HIV transactivator of transcription (TAT) gprotein transduction domainsh promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans J. Biol. Chem. 278 2003 35109 35114
    • (2003) J. Biol. Chem. , vol.278 , pp. 35109-35114
    • Console, S.1    Marty, C.2    Garcia-Echeverria, C.3    Schwendener, R.4    Ballmer-Hofer, K.5
  • 61
    • 0038352064 scopus 로고    scopus 로고
    • Quantitative comparison of membrane transduction and endocytosis of oligopeptides
    • J.L. Zaro, and W. Shen Quantitative comparison of membrane transduction and endocytosis of oligopeptides Biochem. Biophys. Res. Comm. 307 2003 241 247
    • (2003) Biochem. Biophys. Res. Comm. , vol.307 , pp. 241-247
    • Zaro, J.L.1    Shen, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.