메뉴 건너뛰기




Volumn 201, Issue , 2015, Pages 14-21

Cell penetrating peptides improve tumor delivery of cargos through neuropilin-1-dependent extravasation

Author keywords

Cell penetrating peptide; Drug delivery; Extravasation; Neuropilin 1; Protein transduction domain

Indexed keywords

BACTERIOPHAGES; CELL ENGINEERING; CELLS; CYTOLOGY; DRUG DELIVERY; ENDOTHELIAL CELLS; OLIGONUCLEOTIDES; PEPTIDES; POLYPEPTIDES; TUMORS;

EID: 84921038666     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2015.01.011     Document Type: Article
Times cited : (55)

References (32)
  • 2
    • 79953054576 scopus 로고    scopus 로고
    • The EPR effect: Unique features of tumor blood vessels for drug delivery, factors involved, and limitations and augmentation of the effect
    • J. Fang, H. Nakamura, and H. Maeda The EPR effect: unique features of tumor blood vessels for drug delivery, factors involved, and limitations and augmentation of the effect Adv. Drug Deliv. Rev. 63 2011 136 151
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , pp. 136-151
    • Fang, J.1    Nakamura, H.2    Maeda, H.3
  • 3
    • 79953048071 scopus 로고    scopus 로고
    • Tumor delivery of macromolecular drugs based on the EPR effect
    • V. Torchilin Tumor delivery of macromolecular drugs based on the EPR effect Adv. Drug Deliv. Rev. 63 2011 131 135
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , pp. 131-135
    • Torchilin, V.1
  • 4
    • 0036139515 scopus 로고    scopus 로고
    • The neuropilins: Multifunctional semaphorin and VEGF receptors that modulate axon guidance and angiogenesis
    • G. Neufeld, T. Cohen, N. Shraga, T. Lange, O. Kessler, and Y. Herzog The neuropilins: multifunctional semaphorin and VEGF receptors that modulate axon guidance and angiogenesis Trends Cardiovasc. Med. 12 2002 13 19
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 13-19
    • Neufeld, G.1    Cohen, T.2    Shraga, N.3    Lange, T.4    Kessler, O.5    Herzog, Y.6
  • 6
    • 70349482671 scopus 로고    scopus 로고
    • C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration
    • T. Teesalu, K.N. Sugahara, V.R. Kotamraju, and E. Ruoslahti C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration Proc. Natl. Acad. Sci. U. S. A. 106 2009 16157 16162
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16157-16162
    • Teesalu, T.1    Sugahara, K.N.2    Kotamraju, V.R.3    Ruoslahti, E.4
  • 9
    • 41949129114 scopus 로고    scopus 로고
    • Semaphorin 3A suppresses VEGF-mediated angiogenesis yet acts as a vascular permeability factor
    • L.M. Acevedo, S. Barillas, S.M. Weis, J.R. Gothert, and D.A. Cheresh Semaphorin 3A suppresses VEGF-mediated angiogenesis yet acts as a vascular permeability factor Blood 111 2008 2674 2680
    • (2008) Blood , vol.111 , pp. 2674-2680
    • Acevedo, L.M.1    Barillas, S.2    Weis, S.M.3    Gothert, J.R.4    Cheresh, D.A.5
  • 11
    • 84859488831 scopus 로고    scopus 로고
    • Structural basis for selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1
    • M.W. Parker, P. Xu, X. Li, and C.W. Vander Kooi Structural basis for selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1 J. Biol. Chem. 287 2012 11082 11089
    • (2012) J. Biol. Chem. , vol.287 , pp. 11082-11089
    • Parker, M.W.1    Xu, P.2    Li, X.3    Vander Kooi, C.W.4
  • 12
    • 77952341533 scopus 로고    scopus 로고
    • Furin processing of semaphorin 3 F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin
    • M.W. Parker, L.M. Hellman, P. Xu, M.G. Fried, and C.W. Vander Kooi Furin processing of semaphorin 3 F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin Biochemistry 49 2010 4068 4075
    • (2010) Biochemistry , vol.49 , pp. 4068-4075
    • Parker, M.W.1    Hellman, L.M.2    Xu, P.3    Fried, M.G.4    Vander Kooi, C.W.5
  • 15
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From molecular mechanisms to therapeutics
    • M.C. Morris, S. Deshayes, F. Heitz, and G. Divita Cell-penetrating peptides: from molecular mechanisms to therapeutics Biol. Cell. 100 2008 201 217
    • (2008) Biol. Cell. , vol.100 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 16
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics
    • F. Heitz, M.C. Morris, and G. Divita Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics Br. J. Pharmacol. 157 2009 195 206
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 17
    • 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
  • 18
    • 77952990022 scopus 로고    scopus 로고
    • Fast membrane association is a crucial factor in the peptide pep-1 translocation mechanism: A kinetic study followed by surface plasmon resonance
    • S.T. Henriques, M.A. Castanho, L.K. Pattenden, and M.I. Aguilar Fast membrane association is a crucial factor in the peptide pep-1 translocation mechanism: a kinetic study followed by surface plasmon resonance Biopolymers 94 2010 314 322
    • (2010) Biopolymers , vol.94 , pp. 314-322
    • Henriques, S.T.1    Castanho, M.A.2    Pattenden, L.K.3    Aguilar, M.I.4
  • 20
    • 84878668366 scopus 로고    scopus 로고
    • Arginine-rich peptides: Methods of translocation through biological membranes
    • S. Futaki, H. Hirose, and I. Nakase Arginine-rich peptides: methods of translocation through biological membranes Curr. Pharm. Des. 19 2013 2863 2868
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 2863-2868
    • Futaki, S.1    Hirose, H.2    Nakase, I.3
  • 21
    • 82755194760 scopus 로고    scopus 로고
    • Protein transduction domain delivery of therapeutic macromolecules
    • A. van den Berg, and S.F. Dowdy Protein transduction domain delivery of therapeutic macromolecules Curr. Opin. Biotechnol. 22 2011 888 893
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 888-893
    • Van Den Berg, A.1    Dowdy, S.F.2
  • 22
    • 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
  • 23
    • 78650824227 scopus 로고    scopus 로고
    • In vivo imaging of HIF-active tumors by an oxygen-dependent degradation protein probe with an interchangeable labeling system
    • T. Kuchimaru, T. Kadonosono, S. Tanaka, T. Ushiki, M. Hiraoka, and S. Kizaka-Kondoh In vivo imaging of HIF-active tumors by an oxygen-dependent degradation protein probe with an interchangeable labeling system PLoS One 5 2010 e15736
    • (2010) PLoS One , vol.5 , pp. e15736
    • Kuchimaru, T.1    Kadonosono, T.2    Tanaka, S.3    Ushiki, T.4    Hiraoka, M.5    Kizaka-Kondoh, S.6
  • 25
    • 0034805390 scopus 로고    scopus 로고
    • Cysteine-rich and basic domain HIV-1 Tat peptides inhibit angiogenesis and induce endothelial cell apoptosis
    • H. Jia, M. Lohr, S. Jezequel, D. Davis, S. Shaikh, D. Selwood, and I. Zachary Cysteine-rich and basic domain HIV-1 Tat peptides inhibit angiogenesis and induce endothelial cell apoptosis Biochem. Biophys. Res. Commun. 283 2001 469 479
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 469-479
    • Jia, H.1    Lohr, M.2    Jezequel, S.3    Davis, D.4    Shaikh, S.5    Selwood, D.6    Zachary, I.7
  • 27
    • 0037124068 scopus 로고    scopus 로고
    • Characterization of neuropilin-1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165
    • C. Gu, B.J. Limberg, G.B. Whitaker, B. Perman, D.J. Leahy, J.S. Rosenbaum, D.D. Ginty, and A.L. Kolodkin Characterization of neuropilin-1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165 J. Biol. Chem. 277 2002 18069 18076
    • (2002) J. Biol. Chem. , vol.277 , pp. 18069-18076
    • Gu, C.1    Limberg, B.J.2    Whitaker, G.B.3    Perman, B.4    Leahy, D.J.5    Rosenbaum, J.S.6    Ginty, D.D.7    Kolodkin, A.L.8
  • 28
    • 57749189130 scopus 로고    scopus 로고
    • Caveolae and transcytosis in endothelial cells: Role in atherosclerosis
    • P.G. Frank, S. Pavlides, and M.P. Lisanti Caveolae and transcytosis in endothelial cells: role in atherosclerosis Cell Tissue Res. 335 2009 41 47
    • (2009) Cell Tissue Res. , vol.335 , pp. 41-47
    • Frank, P.G.1    Pavlides, S.2    Lisanti, M.P.3
  • 29
    • 0036663014 scopus 로고    scopus 로고
    • In vivo delivery of a Bcl-xL fusion protein containing the TAT protein transduction domain protects against ischemic brain injury and neuronal apoptosis
    • G. Cao, W. Pei, H. Ge, Q. Liang, Y. Luo, F.R. Sharp, A. Lu, R. Ran, S.H. Graham, and J. Chen In vivo delivery of a Bcl-xL fusion protein containing the TAT protein transduction domain protects against ischemic brain injury and neuronal apoptosis J. Neurosci. 22 2002 5423 5431
    • (2002) J. Neurosci. , vol.22 , pp. 5423-5431
    • Cao, G.1    Pei, W.2    Ge, H.3    Liang, Q.4    Luo, Y.5    Sharp, F.R.6    Lu, A.7    Ran, R.8    Graham, S.H.9    Chen, J.10
  • 30
    • 23944512155 scopus 로고    scopus 로고
    • Insulin-cell penetrating peptide hybrids with improved intestinal absorption efficiency
    • J.F. Liang, and V.C. Yang Insulin-cell penetrating peptide hybrids with improved intestinal absorption efficiency Biochem. Biophys. Res. Commun. 335 2005 734 738
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 734-738
    • Liang, J.F.1    Yang, V.C.2
  • 31
    • 64649092671 scopus 로고    scopus 로고
    • Conjugation with cationic cell-penetrating peptide increases pulmonary absorption of insulin
    • L.N. Patel, J. Wang, K.J. Kim, Z. Borok, E.D. Crandall, and W.C. Shen Conjugation with cationic cell-penetrating peptide increases pulmonary absorption of insulin Mol. Pharm. 6 2009 492 503
    • (2009) Mol. Pharm. , vol.6 , pp. 492-503
    • Patel, L.N.1    Wang, J.2    Kim, K.J.3    Borok, Z.4    Crandall, E.D.5    Shen, W.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.