메뉴 건너뛰기




Volumn 9, Issue 2, 2014, Pages 163-170

A novel system enhancing the endosomal escapes of peptides promotes Bak BH3 peptide inducing apoptosis in lung cancer A549 cells

Author keywords

Bak BH3; Cytosolic delivery; Inducing apoptosis; Tat INF7 ubiquitin (TIU) system

Indexed keywords

GLYCYLGLUTAMINYLVALYLGLYCYLARGINYLGLUTAMINYLLEUCYLALANYLISOLEUCYLISOLEUCYLGLYCYLASPARTYLASPARTYLISOLEUCYLASPARAGINYLARGININE; INF7 PEPTIDE; PEPTIDE; TRANSACTIVATOR PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; BAX PROTEIN (53-86); HYBRID PROTEIN; ONCOPROTEIN; PEPTIDE FRAGMENT;

EID: 84902548530     PISSN: 17762596     EISSN: 1776260X     Source Type: Journal    
DOI: 10.1007/s11523-013-0282-9     Document Type: Article
Times cited : (8)

References (27)
  • 1
    • 0032494119 scopus 로고    scopus 로고
    • Pharmacodynamic aspects of peptide administration biological response modifiers
    • Talmadge JE (1998) Pharmacodynamic aspects of peptide administration biological response modifiers. Adv Drug Deliv Rev 33(3):241-252
    • (1998) Adv Drug Deliv Rev , vol.33 , Issue.3 , pp. 241-252
    • Talmadge, J.E.1
  • 2
    • 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
    • DOI 10.1074/jbc.272.25.16010
    • Vives E, Brodin P, Lebleu B (1997) A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J Biol Chem 272(25):16010-16017 (Pubitemid 27265584)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 3
    • 33846591495 scopus 로고    scopus 로고
    • The taming of the cell penetrating domain of the HIV Tat: Myths and realities
    • DOI 10.1016/j.jconrel.2006.10.031, PII S0168365906006146
    • Chauhan A, Tikoo A, Kapur AK, Singh M (2007) The taming of the cell penetrating domain of the HIV Tat: myths and realities. J Control Release 117(2):148-162. doi:10.1016/j.jconrel.2006.10.031 (Pubitemid 46172502)
    • (2007) Journal of Controlled Release , vol.117 , Issue.2 , pp. 148-162
    • Chauhan, A.1    Tikoo, A.2    Kapur, A.K.3    Singh, M.4
  • 4
    • 79958714035 scopus 로고    scopus 로고
    • Potential of cell penetrating peptides for cell drug delivery
    • (Paris) doi:10.1051/medsci/2011275019
    • Poillot C, De Waard M (2011) Potential of cell penetrating peptides for cell drug delivery. Med Sci (Paris) 27(5):527-534. doi:10.1051/medsci/2011275019
    • (2011) Med Sci , vol.27 , Issue.5 , pp. 527-534
    • Poillot, C.1    De Waard, M.2
  • 7
    • 0042786952 scopus 로고    scopus 로고
    • 99mTc-antisense DNAs without entrapment
    • DOI 10.1016/S1536-1632(03)00106-9, PII S1536163203001069
    • Zhang YM, Liu CB, Liu N, Ferro Flores G, He J, Rusckowski M, Hnatowich DJ (2003) Electrostatic binding with tat and other cationic peptides increases cell accumulation of 99mTc-antisense DNAs without entrapment. Mol Imaging Biol: MIB: Off Publ Acad Mol Imaging 5(4):240-247 (Pubitemid 37074875)
    • (2003) Molecular Imaging and Biology , vol.5 , Issue.4 , pp. 240-247
    • Zhang, Y.-M.1    Liu, C.-B.2    Liu, N.3    Flores, G.F.4    He, J.5    Rusckowski, M.6    Hnatowich, D.J.7
  • 8
    • 79957460418 scopus 로고    scopus 로고
    • Endosomal escape pathways for delivery of biologicals
    • doi:10.1016/j.jconrel.2010.11.004
    • Varkouhi AK, Scholte M, Storm G, Haisma HJ (2011) Endosomal escape pathways for delivery of biologicals. J Control Release 151(3):220-228. doi:10.1016/j.jconrel.2010.11.004
    • (2011) J Control Release , vol.151 , Issue.3 , pp. 220-228
    • Varkouhi, A.K.1    Scholte, M.2    Storm, G.3    Haisma, H.J.4
  • 9
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • DOI 10.1038/nm996
    • Wadia JS, Stan RV, Dowdy SF (2004) Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med 10(3):310-315. doi:10.1038/nm996 (Pubitemid 38667624)
    • (2004) Nature Medicine , vol.10 , Issue.3 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 10
    • 35248880092 scopus 로고    scopus 로고
    • TAT transduction: The molecular mechanism and therapeutic prospects
    • DOI 10.1016/j.molmed.2007.08.002, PII S1471491407001645
    • Gump JM, Dowdy SF (2007) TAT transduction: the molecular mechanism and therapeutic prospects. Trends Mol Med 13(10):443-448. doi:10.1016/j.molmed.2007. 08.002 (Pubitemid 47562310)
    • (2007) Trends in Molecular Medicine , vol.13 , Issue.10 , pp. 443-448
    • Gump, J.M.1    Dowdy, S.F.2
  • 11
    • 65549133368 scopus 로고    scopus 로고
    • Delivery of macromolecules using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment
    • doi:10.1208/s12248-008-9071-2
    • El-Sayed A, Futaki S, Harashima H (2009) Delivery of macromolecules using arginine-rich cell-penetrating peptides: ways to overcome endosomal entrapment. AAPS J 11(1):13-22. doi:10.1208/s12248-008-9071-2
    • (2009) AAPS J , vol.11 , Issue.1 , pp. 13-22
    • El-Sayed, A.1    Futaki, S.2    Harashima, H.3
  • 12
    • 0038205763 scopus 로고    scopus 로고
    • Polycation gene delivery systems: Escape from endosomes to cytosol
    • DOI 10.1211/002235703765951311
    • Cho YW, Kim JD, Park K (2003) Polycation gene delivery systems: escape from endosomes to cytosol. J Pharm Pharmacol 55(6):721-734. doi:10.1211/ 002235703765951311 (Pubitemid 36752715)
    • (2003) Journal of Pharmacy and Pharmacology , vol.55 , Issue.6 , pp. 721-734
    • Cho, Y.W.1    Kim, J.-D.2    Park, K.3
  • 13
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • DOI 10.1038/371037a0
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC (1994) Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371(6492):37-43. doi:10.1038/371037a0 (Pubitemid 24277462)
    • (1994) Nature , vol.371 , Issue.6492 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 14
  • 15
    • 0028199067 scopus 로고
    • The influence of endosome-disruptive peptides on gene transfer using synthetic virus-like gene transfer systems
    • Plank C, Oberhauser B, Mechtler K, Koch C, Wagner E (1994) The influence of endosome-disruptive peptides on gene transfer using synthetic virus-like gene transfer systems. J Biol Chem 269(17):12918-12924 (Pubitemid 24202092)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.17 , pp. 12918-12924
    • Plank, C.1    Oberhauser, B.2    Mechtler, K.3    Koch, C.4    Wagner, E.5
  • 16
    • 21344450090 scopus 로고    scopus 로고
    • Strategies for cytosolic delivery of liposomal macromolecules
    • DOI 10.1016/j.ijpharm.2005.02.040, PII S0378517305002474, Selected Contribution from the 5th European Workshop on Particulate Systems
    • Fretz MM, Mastrobattista E, Koning GA, Jiskoot W, Storm G (2005) Strategies for cytosolic delivery of liposomal macromolecules. Int J Pharm 298(2):305-309. doi:10.1016/j.ijpharm.2005.02.040 (Pubitemid 40910733)
    • (2005) International Journal of Pharmaceutics , vol.298 , Issue.2 , pp. 305-309
    • Fretz, M.M.1    Mastrobattista, E.2    Koning, G.A.3    Jiskoot, W.4    Storm, G.5
  • 17
    • 36849070485 scopus 로고    scopus 로고
    • Degradable-brushed pHEMA-pDMAEMA synthesized via ATRP and click chemistry for gene delivery
    • DOI 10.1021/bc0701186
    • Jiang X, Lok MC, Hennink WE (2007) Degradable-brushed pHEMA-pDMAEMA synthesized via ATRP and click chemistry for gene delivery. Bioconjug Chem 18(6):2077-2084. doi:10.1021/bc0701186 (Pubitemid 350220011)
    • (2007) Bioconjugate Chemistry , vol.18 , Issue.6 , pp. 2077-2084
    • Jiang, X.1    Lok, M.C.2    Hennink, W.E.3
  • 18
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A, Finley D, Varshavsky A (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science 234(4773):179-186 (Pubitemid 17186094)
    • (1986) Science , vol.234 , Issue.4773 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 20
    • 0033531926 scopus 로고    scopus 로고
    • Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases
    • Holinger EP, Chittenden T, Lutz RJ (1999) Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases. J Biol Chem 274(19):13298-13304
    • (1999) J Biol Chem , vol.274 , Issue.19 , pp. 13298-13304
    • Holinger, E.P.1    Chittenden, T.2    Lutz, R.J.3
  • 21
    • 9544221644 scopus 로고    scopus 로고
    • Sequence and helicity requirements for the proapoptotic activity of Bax BH3 peptides
    • Shangary S, Oliver CL, Tillman TS, Cascio M, Johnson DE (2004) Sequence and helicity requirements for the proapoptotic activity of Bax BH3 peptides. Mol Cancer Ther 3(11):1343-1354
    • (2004) Mol Cancer Ther , vol.3 , Issue.11 , pp. 1343-1354
    • Shangary, S.1    Oliver, C.L.2    Tillman, T.S.3    Cascio, M.4    Johnson, D.E.5
  • 22
    • 12744262142 scopus 로고    scopus 로고
    • A ubiquitin-based assay for the cytosolic uptake of protein transduction domains
    • doi:10.1016/j.ymthe.2004.10.010
    • Loison F, Nizard P, Sourisseau T, Le Goff P, Debure L, Le Drean Y, Michel D (2005) A ubiquitin-based assay for the cytosolic uptake of protein transduction domains. Mol Ther 11(2):205-214. doi:10.1016/j.ymthe.2004.10.010
    • (2005) Mol Ther , vol.11 , Issue.2 , pp. 205-214
    • Loison, F.1    Nizard, P.2    Sourisseau, T.3    Le Goff, P.4    Debure, L.5    Le Drean, Y.6    Michel, D.7
  • 23
    • 0025797055 scopus 로고
    • Endocytosis and targeting of exogenous HIV-1 Tat protein
    • Mann DA, Frankel AD (1991) Endocytosis and targeting of exogenous HIV-1 Tat protein. EMBO J 10(7):1733-1739 (Pubitemid 21905640)
    • (1991) EMBO Journal , vol.10 , Issue.7 , pp. 1733-1739
    • Mann, D.A.1    Frankel, A.D.2
  • 24
    • 67651211690 scopus 로고    scopus 로고
    • Enhanced gene expression by a novel stearylated INF7 peptide derivative through fusion independent endosomal escape
    • doi:10.1016/j.jconrel.2009.05.018
    • El-Sayed A, Masuda T, Khalil I, Akita H, Harashima H (2009) Enhanced gene expression by a novel stearylated INF7 peptide derivative through fusion independent endosomal escape. J Control Release 138(2):160-167. doi:10.1016/j.jconrel.2009.05.018
    • (2009) J Control Release , vol.138 , Issue.2 , pp. 160-167
    • El-Sayed, A.1    Masuda, T.2    Khalil, I.3    Akita, H.4    Harashima, H.5
  • 25
    • 36749015570 scopus 로고    scopus 로고
    • Membrane binding of pH-sensitive influenza fusion peptides. Positioning, configuration, and induced leakage in a lipid vesicle model
    • DOI 10.1021/bi701075y
    • Esbjorner EK, Oglecka K, Lincoln P, Graslund A, Norden B (2007) Membrane binding of pH-sensitive influenza fusion peptides. Positioning, configuration, and induced leakage in a lipid vesicle model. Biochemistry 46(47):13490-13504. doi:10.1021/bi701075y (Pubitemid 350209946)
    • (2007) Biochemistry , vol.46 , Issue.47 , pp. 13490-13504
    • Esbjorner, E.K.1    Oglecka, K.2    Lincoln, P.3    Graslund, A.4    Norden, B.5
  • 26
    • 58149189434 scopus 로고    scopus 로고
    • The effect of endosomal escape peptides on in vitro gene delivery of polyethylene glycol-based vehicles
    • doi:10.1002/jgm.1234
    • Moore NM, Sheppard CL, Barbour TR, Sakiyama-Elbert SE (2008) The effect of endosomal escape peptides on in vitro gene delivery of polyethylene glycol-based vehicles. J Gene Med 10(10):1134-1149. doi:10.1002/jgm.1234
    • (2008) J Gene Med , vol.10 , Issue.10 , pp. 1134-1149
    • Moore, N.M.1    Sheppard, C.L.2    Barbour, T.R.3    Sakiyama-Elbert, S.E.4
  • 27
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • DOI 10.1093/emboj/20.18.5187
    • Borodovsky A, Kessler BM, Casagrande R, Overkleeft HS, Wilkinson KD, Ploegh HL (2001) A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO J 20(18):5187-5196. doi:10.1093/emboj/20.18.5187 (Pubitemid 32910913)
    • (2001) EMBO Journal , vol.20 , Issue.18 , pp. 5187-5196
    • Borodovsky, A.1    Kessler, B.M.2    Casagrande, R.3    Overkleeft, H.S.4    Wilkinson, K.D.5    Ploegh, H.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.