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Volumn 32, Issue 22, 2011, Pages 5262-5268

The cell penetrating ability of the proapoptotic peptide, KLAKLAKKLAKLAK fused to the N-terminal protein transduction domain of translationally controlled tumor protein, MIIYRDLISH

Author keywords

Apoptosis; Cancer; Molecular imaging; Protein transduction domain; TCTP

Indexed keywords

APOPTOSIS; CANCER; MOLECULAR IMAGING; PROTEIN TRANSDUCTION DOMAIN; TCTP;

EID: 79956076191     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2011.03.074     Document Type: Article
Times cited : (56)

References (31)
  • 1
    • 1542721107 scopus 로고    scopus 로고
    • Cell penetrating peptides in drug delivery
    • Snyder E.L., Dowdy S.F. Cell penetrating peptides in drug delivery. Pharm Res 2004, 21(3):389-393.
    • (2004) Pharm Res , vol.21 , Issue.3 , pp. 389-393
    • Snyder, E.L.1    Dowdy, S.F.2
  • 2
    • 0038325747 scopus 로고    scopus 로고
    • Protein transduction technology offers novel therapeutic approach for brain ischemia
    • Denicourt C., Dowdy S.F. Protein transduction technology offers novel therapeutic approach for brain ischemia. Trends Pharmacol Sci 2003, 24(5):216-218.
    • (2003) Trends Pharmacol Sci , vol.24 , Issue.5 , pp. 216-218
    • Denicourt, C.1    Dowdy, S.F.2
  • 3
    • 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. Break on through to the other side - biophysics and cell biology shed light on cell-penetrating peptides. Chembiochem 2005, 6(12):2126-2142.
    • (2005) Chembiochem , vol.6 , Issue.12 , pp. 2126-2142
    • Fischer, R.1    Fotin-Mleczek, M.2    Hufnagel, H.3    Brock, R.4
  • 4
    • 78349312521 scopus 로고    scopus 로고
    • A protein transduction domain located at the NH2-terminus of human translationally controlled tumor protein for delivery of active molecules to cells
    • Kim M., Kim M., Kim H.Y., Kim S., Jung J., Maeng J., et al. A protein transduction domain located at the NH2-terminus of human translationally controlled tumor protein for delivery of active molecules to cells. Biomaterials 2011, 32(1):222-230.
    • (2011) Biomaterials , vol.32 , Issue.1 , pp. 222-230
    • Kim, M.1    Kim, M.2    Kim, H.Y.3    Kim, S.4    Jung, J.5    Maeng, J.6
  • 5
    • 54349094566 scopus 로고    scopus 로고
    • Synthesis and biological characterisation of targeted pro-apoptotic peptide
    • Foillard S., Jin Z.H., Garanger E., Boturyn D., Favrot M.C., Coll J.L., et al. Synthesis and biological characterisation of targeted pro-apoptotic peptide. Chembiochem 2008, 9(14):2326-2332.
    • (2008) Chembiochem , vol.9 , Issue.14 , pp. 2326-2332
    • Foillard, S.1    Jin, Z.H.2    Garanger, E.3    Boturyn, D.4    Favrot, M.C.5    Coll, J.L.6
  • 8
    • 49849101354 scopus 로고    scopus 로고
    • Antitumor effect of a transducible fusogenic peptide releasing multiple proapoptotic peptides by caspase-3
    • Kwon M.K., Nam J.O., Park R.W., Lee B.H., Park J.Y., Byun Y.R., et al. Antitumor effect of a transducible fusogenic peptide releasing multiple proapoptotic peptides by caspase-3. Mol Cancer Ther 2008, 7(6):1514-1522.
    • (2008) Mol Cancer Ther , vol.7 , Issue.6 , pp. 1514-1522
    • Kwon, M.K.1    Nam, J.O.2    Park, R.W.3    Lee, B.H.4    Park, J.Y.5    Byun, Y.R.6
  • 9
    • 33748343425 scopus 로고    scopus 로고
    • A mitochondrial targeted fusion peptide exhibits remarkable cytotoxicity
    • Law B., Quinti L., Choi Y., Weissleder R., Tung C.H. A mitochondrial targeted fusion peptide exhibits remarkable cytotoxicity. Mol Cancer Ther 2006, 5(8):1944-1949.
    • (2006) Mol Cancer Ther , vol.5 , Issue.8 , pp. 1944-1949
    • Law, B.1    Quinti, L.2    Choi, Y.3    Weissleder, R.4    Tung, C.H.5
  • 10
    • 0035503496 scopus 로고    scopus 로고
    • A proapoptotic peptide for the treatment of solid tumors
    • Mai J.C., Mi Z., Kim S.H., Ng B., Robbins P.D. A proapoptotic peptide for the treatment of solid tumors. Cancer Res 2001, 61(21):7709-7712.
    • (2001) Cancer Res , vol.61 , Issue.21 , pp. 7709-7712
    • Mai, J.C.1    Mi, Z.2    Kim, S.H.3    Ng, B.4    Robbins, P.D.5
  • 11
    • 0034296675 scopus 로고    scopus 로고
    • Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo
    • Mi Z., Mai J., Lu X., Robbins P.D. Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo. Mol Ther 2000, 2(4):339-347.
    • (2000) Mol Ther , vol.2 , Issue.4 , pp. 339-347
    • Mi, Z.1    Mai, J.2    Lu, X.3    Robbins, P.D.4
  • 13
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: enemies within
    • Thornberry N.A., Lazebnik Y. Caspases: enemies within. Science 1998, 281(5381):1312-1316.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 14
    • 53549135472 scopus 로고    scopus 로고
    • Hunter-killer peptide (HKP) for targeted therapy
    • Ellerby H.M., Bredesen D.E., Fujimura S., John V. Hunter-killer peptide (HKP) for targeted therapy. J Med Chem 2008, 51(9):5887-5892.
    • (2008) J Med Chem , vol.51 , Issue.9 , pp. 5887-5892
    • Ellerby, H.M.1    Bredesen, D.E.2    Fujimura, S.3    John, V.4
  • 15
    • 20144387912 scopus 로고    scopus 로고
    • Selective apoptotic killing of malignant hemopoietic cells by antibody-targeted delivery of an amphipathic peptide
    • Marks A.J., Cooper M.S., Anderson R.J., Orchard K.H., Hale G., North J.M., et al. Selective apoptotic killing of malignant hemopoietic cells by antibody-targeted delivery of an amphipathic peptide. Cancer Res 2005, 65(6):2373-2377.
    • (2005) Cancer Res , vol.65 , Issue.6 , pp. 2373-2377
    • Marks, A.J.1    Cooper, M.S.2    Anderson, R.J.3    Orchard, K.H.4    Hale, G.5    North, J.M.6
  • 16
    • 67249139762 scopus 로고    scopus 로고
    • Cationic liposomes loaded with proapoptotic peptide D-(KLAKLAK)(2) and Bcl-2 antisense oligodeoxynucleotide G3139 for enhanced anticancer therapy
    • Ko Y.T., Falcao C., Torchilin V.P. Cationic liposomes loaded with proapoptotic peptide D-(KLAKLAK)(2) and Bcl-2 antisense oligodeoxynucleotide G3139 for enhanced anticancer therapy. Mol Pharmacol 2009, 6(3):971-977.
    • (2009) Mol Pharmacol , vol.6 , Issue.3 , pp. 971-977
    • Ko, Y.T.1    Falcao, C.2    Torchilin, V.P.3
  • 17
    • 0346460957 scopus 로고    scopus 로고
    • Cell-penetrating peptides - a reevaluation of the mechanism of cellular uptake
    • Richard J.P., Melikov K., Vives E., Ramos C., Verbeure B., Gait M.J., et al. Cell-penetrating peptides - a reevaluation of the mechanism of cellular uptake. J Biol Chem 2003, 278(1):585-590.
    • (2003) J Biol Chem , vol.278 , Issue.1 , pp. 585-590
    • Richard, J.P.1    Melikov, K.2    Vives, E.3    Ramos, C.4    Verbeure, B.5    Gait, M.J.6
  • 18
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters
    • Wender P.A., Mitchell D.J., Pattabiraman K., Pelkey E.T., Steinman L., Rothbard J.B. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc Natl Acad Sci U S A 2000, 97(24):13003-13008.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.24 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 19
    • 17844372767 scopus 로고    scopus 로고
    • Arginine-rich anti-vascular endothelial growth factor (anti-VEGF) hexapeptide inhibits collagen-induced arthritis and VEGF-stimulated productions of TNF-alpha and IL-6 by human monocytes
    • Yoo S.A., Bae D.G., Ryoo J.W., Kim H.R., Park G.S., Cho C.S., et al. Arginine-rich anti-vascular endothelial growth factor (anti-VEGF) hexapeptide inhibits collagen-induced arthritis and VEGF-stimulated productions of TNF-alpha and IL-6 by human monocytes. J Immunol 2005, 174(9):5846-5855.
    • (2005) J Immunol , vol.174 , Issue.9 , pp. 5846-5855
    • Yoo, S.A.1    Bae, D.G.2    Ryoo, J.W.3    Kim, H.R.4    Park, G.S.5    Cho, C.S.6
  • 21
    • 0041816277 scopus 로고    scopus 로고
    • Antennapedia and HIV transactivator of transcription (TAT) "protein transduction domains" promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans
    • Console S., Marty C., Garcia-Echeverria C., Schwendener R., Ballmer-Hofer K. Antennapedia and HIV transactivator of transcription (TAT) "protein transduction domains" promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans. J Biol Chem 2003, 278(37):35109-35114.
    • (2003) J Biol Chem , vol.278 , Issue.37 , pp. 35109-35114
    • Console, S.1    Marty, C.2    Garcia-Echeverria, C.3    Schwendener, R.4    Ballmer-Hofer, K.5
  • 22
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans
    • Tyagi M., Rusnati M., Presta M., Giacca M. Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans. J Biol Chem 2001, 276(5):3254-3261.
    • (2001) J Biol Chem , vol.276 , Issue.5 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 23
    • 68949099606 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane permeabilization and remodelling in apoptosis
    • Jourdain A., Martinou J.C. Mitochondrial outer-membrane permeabilization and remodelling in apoptosis. Int J Biochem Cell Biol 2009, 41(10):1884-1889.
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.10 , pp. 1884-1889
    • Jourdain, A.1    Martinou, J.C.2
  • 24
    • 38149011240 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphological dynamics during apoptosis by Bcl-2 family proteins: a key in Bak?
    • Brooks C., Dong Z. Regulation of mitochondrial morphological dynamics during apoptosis by Bcl-2 family proteins: a key in Bak?. Cell Cycle 2007, 6(24):3043-3047.
    • (2007) Cell Cycle , vol.6 , Issue.24 , pp. 3043-3047
    • Brooks, C.1    Dong, Z.2
  • 25
    • 70450205079 scopus 로고    scopus 로고
    • Apoptosis and human diseases: mitochondrion damage and lethal role of released cytochrome C as proapoptotic protein
    • Caroppi P., Sinibaldi F., Fiorucci L., Santucci R. Apoptosis and human diseases: mitochondrion damage and lethal role of released cytochrome C as proapoptotic protein. Curr Med Chem 2009, 16(31):4058-4065.
    • (2009) Curr Med Chem , vol.16 , Issue.31 , pp. 4058-4065
    • Caroppi, P.1    Sinibaldi, F.2    Fiorucci, L.3    Santucci, R.4
  • 26
    • 0035283038 scopus 로고    scopus 로고
    • Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes
    • Bratton S.B., Walker G., Srinivasula S.M., Sun X.M., Butterworth M., Alnemri E.S., et al. Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes. EMBO J 2001, 20(5):998-1009.
    • (2001) EMBO J , vol.20 , Issue.5 , pp. 998-1009
    • Bratton, S.B.1    Walker, G.2    Srinivasula, S.M.3    Sun, X.M.4    Butterworth, M.5    Alnemri, E.S.6
  • 27
    • 35248880092 scopus 로고    scopus 로고
    • TAT transduction: the molecular mechanism and therapeutic prospects
    • Gump J.M., Dowdy S.F. TAT transduction: the molecular mechanism and therapeutic prospects. Trends Mol Med 2007, 13(10):443-448.
    • (2007) Trends Mol Med , vol.13 , Issue.10 , pp. 443-448
    • Gump, J.M.1    Dowdy, S.F.2
  • 28
    • 0034802647 scopus 로고    scopus 로고
    • Heparin binding by the HIV-1 tat protein transduction domain
    • Hakansson S., Jacobs A., Caffrey M. Heparin binding by the HIV-1 tat protein transduction domain. Protein Sci 2001, 10(10):2138-2139.
    • (2001) Protein Sci , vol.10 , Issue.10 , pp. 2138-2139
    • Hakansson, S.1    Jacobs, A.2    Caffrey, M.3
  • 29
    • 0030966373 scopus 로고    scopus 로고
    • Interaction of HIV-1 Tat protein with heparin. Role of the backbone structure, sulfation, and size
    • Rusnati M., Coltrini D., Oreste P., Zoppetti G., Albini A., Noonan D., et al. Interaction of HIV-1 Tat protein with heparin. Role of the backbone structure, sulfation, and size. J Biol Chem 1997, 272(17):11313-11320.
    • (1997) J Biol Chem , vol.272 , Issue.17 , pp. 11313-11320
    • Rusnati, M.1    Coltrini, D.2    Oreste, P.3    Zoppetti, G.4    Albini, A.5    Noonan, D.6
  • 30
    • 34250867475 scopus 로고    scopus 로고
    • The emerging role of serine proteases in apoptosis
    • Moffitt K.L., Martin S.L., Walker B. The emerging role of serine proteases in apoptosis. Biochem Soc Trans 2007, 35(Pt 3):559-560.
    • (2007) Biochem Soc Trans , vol.35 , Issue.PT 3 , pp. 559-560
    • Moffitt, K.L.1    Martin, S.L.2    Walker, B.3
  • 31
    • 0036088471 scopus 로고    scopus 로고
    • IAP proteins: blocking the road to death's door
    • Salvesen G.S., Duckett C.S. IAP proteins: blocking the road to death's door. Nat Rev Mol Cell Biol 2002, 3(6):401-410.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , Issue.6 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.