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Volumn 171, Issue 2, 2013, Pages 251-257

Dipeptide mimic oligomer transporter mediates intracellular delivery of Cathepsin D inhibitors: A potential target for cancer therapy

Author keywords

Apoptosis; Cancer; Cathepsin D inhibitors; Cell penetrating compounds; Pepstatin bioconjugate

Indexed keywords

BIOMOLECULES; CELL CULTURE; CELL DEATH; CELLS; CYTOLOGY; DISEASES; TUMORS;

EID: 84882788073     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2013.07.017     Document Type: Article
Times cited : (20)

References (31)
  • 2
    • 0034651918 scopus 로고    scopus 로고
    • Cathepsin D in breast cancer: Mechanisms and clinical applications, a 1999 overview
    • DOI 10.1016/S0009-8981(99)00226-0, PII S0009898199002260
    • H. Rochefort, M. Garcia, M. Glondu, V. Laurent, E. Liaudet, J.M. Rey, P. Roger, Cathepsin D in breast cancer: mechanisms and clinical applications, a 1999 overview, Clin. Chim. Acta 291 (2) (2000) 157-170. (Pubitemid 30089762)
    • (2000) Clinica Chimica Acta , vol.291 , Issue.2 , pp. 157-170
    • Rochefort, H.1    Garcia, M.2    Glondu, M.3    Laurent, V.4    Liaudet, E.5    Rey, J.-M.6    Roger, P.7
  • 3
    • 50649106648 scopus 로고    scopus 로고
    • Cathepsin D-many functions of one aspartic protease
    • P. Benes,V. Vetvicka, M. Fusek, Cathepsin D-many functions of one aspartic protease, Crit. Rev. Oncol. Hematol. 68 (1) (2008) 12-28.
    • (2008) Crit. Rev. Oncol. Hematol. , vol.68 , Issue.1 , pp. 12-28
    • Benes, P.1    Vetvicka, V.2    Fusek, M.3
  • 4
    • 77958546273 scopus 로고    scopus 로고
    • Pathophysiological functions of cathepsin D: Targeting its catalytic activity versus its protein binding activity?
    • O. Masson, A.S. Bach, D. Derocq, C. Prébois, V. Laurent-Matha, S. Pattingre, E. Liaudet-Coopman, Pathophysiological functions of cathepsin D: targeting its catalytic activity versus its protein binding activity? Biochimie 92 (11) (2010) 1635-1643.
    • (2010) Biochimie , vol.92 , Issue.11 , pp. 1635-1643
    • Masson, O.1    Bach, A.S.2    Derocq, D.3    Prébois, C.4    Laurent-Matha, V.5    Pattingre, S.6    Liaudet-Coopman, E.7
  • 5
    • 0030748777 scopus 로고    scopus 로고
    • Relationship between cathepsin-D content and disease-free survival in node-negative breast cancer patients: A meta-analysis
    • G. Ferrandina, G. Scambia, F. Bardelli, P. Benedetti Panici, S. Mancuso, A. Messori, Relationship between cathepsin-D content and disease-free survival in node-negative breast cancer patients: a meta-analysis, Br. J. Cancer 76 (5) (1997) 661-666. (Pubitemid 27354682)
    • (1997) British Journal of Cancer , vol.76 , Issue.5 , pp. 661-666
    • Ferrandina, G.1    Scambia, G.2    Bardelli, F.3    Benedetti Panici, P.4    Mancuso, S.5    Messori, A.6
  • 7
    • 2942711855 scopus 로고    scopus 로고
    • Cathepsin D expression levels in nongynecological solid tumors: Clinical and therapeutic implications
    • DOI 10.1023/B:CLIN.0000024740.44602.b7
    • G. Leto, F.M. Tumminello, M. Crescimanno, C. Flandina, N. Gebbia, Cathepsin D expression levels in nongynecological solid tumors: clinical and therapeutic implications, Clin. Exp. Metastasis 21 (2) (2004) 91-106. (Pubitemid 38988083)
    • (2004) Clinical and Experimental Metastasis , vol.21 , Issue.2 , pp. 91-106
    • Leto, G.1    Tumminello, F.M.2    Crescimanno, M.3    Flandina, C.4    Gebbia, N.5
  • 8
    • 0025596963 scopus 로고
    • Overexpression of transfected cathepsin D in transformed cells increases their malignant phenotype and metastatic potency
    • M. Garcia, D. Derocq, P. Pujol, H. Rochefort, Overexpression of transfected cathepsin D in transformed cells increases their malignant phenotype and metastatic potency, Oncogene 5 (12) (1990) 1809-1814. (Pubitemid 120034707)
    • (1990) Oncogene , vol.5 , Issue.12 , pp. 1809-1814
    • Garcia, M.1    Derocq, D.2    Pujol, P.3    Rochefort, H.4
  • 9
    • 0036676298 scopus 로고    scopus 로고
    • Down-regulation of cathepsin-D expression by antisense gene transfer inhibits tumor growth and experimental lung metastasis of human breast cancer cells
    • M. Glondu, E. Liaudet-Coopman, D. Derocq, N. Platet, H. Rochefort, M. Garcia, Down-regulation of cathepsin-D expression by antisense gene transfer inhibits tumor growth and experimental lung metastasis of human breast cancer cells, Oncogene 21 (33) (2002) 5127-5134.
    • (2002) Oncogene , vol.21 , Issue.33 , pp. 5127-5134
    • Glondu, M.1    Liaudet-Coopman, E.2    Derocq, D.3    Platet, N.4    Rochefort, H.5    Garcia, M.6
  • 10
    • 0041912315 scopus 로고    scopus 로고
    • Stress-induced apoptosis is impaired in cells with a lysosomal targeting defect but is not affected in cells synthesizing a catalytically inactive cathepsin D
    • DOI 10.1038/sj.cdd.4401272
    • C. Tardy, J. Tyynela, A. Hasilik, T. Levade, N. Andrieu-Abadie, Stress-induced apopto-sis is impaired in cells with a lysosomal targeting defect but is not affected in cells synthesizing a catalytically inactive cathepsin D, Cell Death Differ. 10 (9) (2003) 1090-1100. (Pubitemid 37069486)
    • (2003) Cell Death and Differentiation , vol.10 , Issue.9 , pp. 1090-1100
    • Tardy, C.1    Tyynela, J.2    Hasilik, A.3    Levade, T.4    Andrieu-Abadie, N.5
  • 11
    • 53349091482 scopus 로고    scopus 로고
    • Cathepsin D protects human neuroblastoma cells from doxorubicin-induced cell death
    • V. Sagulenko, D. Muth, E. Sagulenko, T. Paffhausen, M. Schwab, F. Westermann, Cathepsin D protects human neuroblastoma cells from doxorubicin-induced cell death, Carcinogenesis 29 (10) (2008) 1869-1877.
    • (2008) Carcinogenesis , vol.29 , Issue.10 , pp. 1869-1877
    • Sagulenko, V.1    Muth, D.2    Sagulenko, E.3    Paffhausen, T.4    Schwab, M.5    Westermann, F.6
  • 13
    • 0017255236 scopus 로고
    • Interaction of human cathepsin-D with inhibitor pepstatin
    • C.G. Knight, A.J. Barrett, Interaction of human cathepsin-D with inhibitor pepstatin, Biochem. J. 155 (1) (1976) 117-125.
    • (1976) Biochem. J. , vol.155 , Issue.1 , pp. 117-125
    • Knight, C.G.1    Barrett, A.J.2
  • 14
  • 15
    • 0027507716 scopus 로고
    • Inhibition of aspartyl proteinases
    • S.S. Abdel-Meguid, Inhibition of aspartyl proteinases, Med. Res. Rev. 13 (1993) 731-778.
    • (1993) Med. Res. Rev. , vol.13 , pp. 731-778
    • Abdel-Meguid, S.S.1
  • 17
    • 1542609485 scopus 로고    scopus 로고
    • Transduction peptides: From technology to physiology
    • DOI 10.1038/ncb0304-189
    • A. Joliot, A. Prochiantz, Transduction peptides: from technology to physiology, Nat. Cell Biol. 6 (3) (2004) 189-196. (Pubitemid 38344356)
    • (2004) Nature Cell Biology , vol.6 , Issue.3 , pp. 189-196
    • Joliot, A.1    Prochiantz, A.2
  • 18
    • 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
    • E. Vives, P. Brodin, 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 (25) (1997) 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
  • 19
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
    • P.A. Wender, D.J. Mitchell, K. Pattabiraman, E.T. Pelkey, L. Steinman, J.B. Rothbard, The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters, Proc. Natl. Acad. Sci. U. S. A. 97 (24) (2000) 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
  • 20
    • 35448940482 scopus 로고    scopus 로고
    • A novel cell penetrating aspartic protease inhibitor blocks processing and presentation of tetanus toxoid more efficiently than pepstatin A
    • DOI 10.1016/j.bbrc.2007.09.114, PII S0006291X07021134
    • N. Zaidi, T. Burster, V. Sommandas, T. Herrmann, B.O. Boehm, C. Driessen, W. Voelter, H. Kalbacher, A novel cell penetrating aspartic protease inhibitor blocks processing and presentation of tetanus toxoid more efficiently than pepstatin A, Biochem. Biophys. Res. Commun. 364 (2) (2007) 243-249. (Pubitemid 47633408)
    • (2007) Biochemical and Biophysical Research Communications , vol.364 , Issue.2 , pp. 243-249
    • Zaidi, N.1    Burster, T.2    Sommandas, V.3    Herrmann, T.4    Boehm, B.O.5    Driessen, C.6    Voelter, W.7    Kalbacher, H.8
  • 24
    • 0027400775 scopus 로고
    • Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling
    • P.E. Scarborough, K. Guruprasad, C. Topham, G.R. Richo, G.E. Conner, T.L. Blundell, B.M. Dunn, Exploration of subsite binding-specificity of human cathepsin-D through kinetics and rule-based molecular modeling, Protein Sci. 2 (2) (1993) 264-276. (Pubitemid 23045479)
    • (1993) Protein Science , vol.2 , Issue.2 , pp. 264-276
    • Scarborough, P.E.1    Guruprasad, K.2    Topham, C.3    Richo, G.R.4    Conner, G.E.5    Blundell, T.L.6    Dunn, B.M.7
  • 25
    • 0027104001 scopus 로고
    • Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy
    • E.M. Manders, J. Stap, G.J. Brakenhoff, R. van Driel, J.A. Aten, Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy, J. Cell Sci. 103 (Pt 3) (1992) 857-862. (Pubitemid 23023255)
    • (1992) Journal of Cell Science , vol.103 , Issue.3 , pp. 857-862
    • Manders, E.M.M.1    Stap, J.2    Brakenhoff, G.J.3    Van Driel, R.4    Aten, J.A.5
  • 28
    • 33748369114 scopus 로고    scopus 로고
    • Methods and protocols of modern solid phase peptide synthesis
    • DOI 10.1385/MB:33:3:239, PII MB333239
    • M. Amblard, J.A. Fehrentz, J. Martinez, G. Subra, Methods and protocols of modern solid phase peptide synthesis, Mol. Biotechnol. 33 (3) (2006) 239-254. (Pubitemid 44337228)
    • (2006) Molecular Biotechnology , vol.33 , Issue.3 , pp. 239-254
    • Amblard, M.1    Fehrentz, J.-A.2    Martinez, J.3    Subra, G.4
  • 29
    • 0033955920 scopus 로고    scopus 로고
    • Probing the cathepsin D using a BODIPY FL-pepstatin A: Applications in fluorescence polarization and microscopy
    • DOI 10.1016/S0165-022X(00)00048-8, PII S0165022X00000488
    • C.S. Chen, W.N.U. Chen, M.J. Zhou, S. Arttamangkul, R.P. Haugland, Probing the cathepsin D using a BODIPY FL-pepstatin A: applications in fluorescence polarization and microscopy, J. Biochem. Biophys. Methods 42 (3) (2000) 137-151. (Pubitemid 30100551)
    • (2000) Journal of Biochemical and Biophysical Methods , vol.42 , Issue.3 , pp. 137-151
    • Chen, C.-S.1    Chen, W.-N.U.2    Zhou, M.3    Arttamangkul, S.4    Haugland, R.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.