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Volumn 34, Issue 30, 2013, Pages

Heat shock protein-mediated cell penetration and cytosolic delivery of macromolecules by a telomerase-derived peptide vaccine

Author keywords

Cell penetrating peptide; Heat shock protein 70; Heat shock protein 90; Telomerase

Indexed keywords

AMINO ACIDS; CELL CULTURE; DISEASES; GENE EXPRESSION; GENE THERAPY; MACROMOLECULES; VACCINES;

EID: 84880507288     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2013.06.015     Document Type: Article
Times cited : (33)

References (41)
  • 1
    • 0033493173 scopus 로고    scopus 로고
    • Telomerase activity in human solid tumors. Diagnostic utility and clinical applications
    • Vasef M.A., Ross J.S., Cohen M.B. Telomerase activity in human solid tumors. Diagnostic utility and clinical applications. Am J Clin Pathol 1999, 112:S68-S75.
    • (1999) Am J Clin Pathol , vol.112
    • Vasef, M.A.1    Ross, J.S.2    Cohen, M.B.3
  • 2
    • 0032745120 scopus 로고    scopus 로고
    • Differential gene expression of human telomerase-associated protein hTERT and TEP1 in human hematopoietic cells
    • Uchida N., Otsuka T., Shigematsu H., Maeda M., Sugio Y., Itoh Y., et al. Differential gene expression of human telomerase-associated protein hTERT and TEP1 in human hematopoietic cells. Leuk Res 1999, 23:1127-1132.
    • (1999) Leuk Res , vol.23 , pp. 1127-1132
    • Uchida, N.1    Otsuka, T.2    Shigematsu, H.3    Maeda, M.4    Sugio, Y.5    Itoh, Y.6
  • 3
    • 67649598300 scopus 로고    scopus 로고
    • Cancer vaccination with telomerase peptide GV1001
    • Kyte J.A. Cancer vaccination with telomerase peptide GV1001. Expert Opin Investig Drugs 2009, 18:687-694.
    • (2009) Expert Opin Investig Drugs , vol.18 , pp. 687-694
    • Kyte, J.A.1
  • 4
    • 33845247353 scopus 로고    scopus 로고
    • Telomerase peptide vaccination of patients with non-resectable pancreatic cancer: a dose escalating phase I/II study
    • Bernhardt S.L., Gjertsen M.K., Trachsel S., Moller M., Eriksen J.A., Meo M., et al. Telomerase peptide vaccination of patients with non-resectable pancreatic cancer: a dose escalating phase I/II study. Br J Cancer 2006, 95:1474-1482.
    • (2006) Br J Cancer , vol.95 , pp. 1474-1482
    • Bernhardt, S.L.1    Gjertsen, M.K.2    Trachsel, S.3    Moller, M.4    Eriksen, J.A.5    Meo, M.6
  • 6
    • 79960329487 scopus 로고    scopus 로고
    • Telomerase peptide vaccination combined with temozolomide: a clinical trial in stage IV melanoma patients
    • Kyte J.A., Gaudernack G., Dueland S., Trachsel S., Julsrud L., Aamdal S. Telomerase peptide vaccination combined with temozolomide: a clinical trial in stage IV melanoma patients. Clin Cancer Res 2011, 17:4568-4580.
    • (2011) Clin Cancer Res , vol.17 , pp. 4568-4580
    • Kyte, J.A.1    Gaudernack, G.2    Dueland, S.3    Trachsel, S.4    Julsrud, L.5    Aamdal, S.6
  • 7
    • 80455140226 scopus 로고    scopus 로고
    • Telomerase peptide vaccination in NSCLC: a phase II trial in stage III patients vaccinated after chemoradiotherapy and an 8-year update on a phase I/II trial
    • Brunsvig P.F., Kyte J.A., Kersten C., Sundstrom S., Moller M., Nyakas M., et al. Telomerase peptide vaccination in NSCLC: a phase II trial in stage III patients vaccinated after chemoradiotherapy and an 8-year update on a phase I/II trial. Clin Cancer Res 2011, 17:6847-6857.
    • (2011) Clin Cancer Res , vol.17 , pp. 6847-6857
    • Brunsvig, P.F.1    Kyte, J.A.2    Kersten, C.3    Sundstrom, S.4    Moller, M.5    Nyakas, M.6
  • 8
    • 77953963578 scopus 로고    scopus 로고
    • Aphase II open label trial evaluating safety and efficacy of a telomerase peptide vaccination in patients with advanced hepatocellular carcinoma
    • Greten T.F., Forner A., Korangy F., N'Kontchou G., Barget N., Ayuso C., et al. Aphase II open label trial evaluating safety and efficacy of a telomerase peptide vaccination in patients with advanced hepatocellular carcinoma. BMC Cancer 2010, 10:209.
    • (2010) BMC Cancer , vol.10 , pp. 209
    • Greten, T.F.1    Forner, A.2    Korangy, F.3    N'Kontchou, G.4    Barget, N.5    Ayuso, C.6
  • 9
    • 68549083643 scopus 로고    scopus 로고
    • Unconventional cytokine profiles and development of T cell memory in long-term survivors after cancer vaccination
    • Kyte J.A., Trachsel S., Risberg B., Thor Straten P., Lislerud K., Gaudernack G. Unconventional cytokine profiles and development of T cell memory in long-term survivors after cancer vaccination. Cancer Immunol Immunother 2009, 58:1609-1626.
    • (2009) Cancer Immunol Immunother , vol.58 , pp. 1609-1626
    • Kyte, J.A.1    Trachsel, S.2    Risberg, B.3    Thor Straten, P.4    Lislerud, K.5    Gaudernack, G.6
  • 10
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel A.D., Pabo C.O. Cellular uptake of the tat protein from human immunodeficiency virus. Cell 1988, 55:1189-1193.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 11
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • Green M., Loewenstein P.M. Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell 1988, 55:1179-1188.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 12
    • 84863099046 scopus 로고    scopus 로고
    • Cell-penetrating peptides: breaking through to the other side
    • Koren E., Torchilin V.P. Cell-penetrating peptides: breaking through to the other side. Trends Mol Med 2012, 18:385-393.
    • (2012) Trends Mol Med , vol.18 , pp. 385-393
    • Koren, E.1    Torchilin, V.P.2
  • 13
    • 11844268027 scopus 로고    scopus 로고
    • Cationic TAT peptide transduction domain enters cells by macropinocytosis
    • Kaplan I.M., Wadia J.S., Dowdy S.F. Cationic TAT peptide transduction domain enters cells by macropinocytosis. JControl Release 2005, 102:247-253.
    • (2005) JControl Release , vol.102 , pp. 247-253
    • Kaplan, I.M.1    Wadia, J.S.2    Dowdy, S.F.3
  • 14
    • 34250835903 scopus 로고    scopus 로고
    • Acomprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • Duchardt F., Fotin-Mleczek M., Schwarz H., Fischer R., Brock R. Acomprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic 2007, 8:848-866.
    • (2007) Traffic , vol.8 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 15
    • 84934438837 scopus 로고    scopus 로고
    • Protein misassembly: macromolecular crowding and molecular chaperones
    • Ellis R.J. Protein misassembly: macromolecular crowding and molecular chaperones. Adv Exp Med Biol 2007, 594:1-13.
    • (2007) Adv Exp Med Biol , vol.594 , pp. 1-13
    • Ellis, R.J.1
  • 16
    • 0345035504 scopus 로고    scopus 로고
    • Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved
    • Robert J., Menoret A., Cohen N. Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved. JImmunol 1999, 163:4133-4139.
    • (1999) JImmunol , vol.163 , pp. 4133-4139
    • Robert, J.1    Menoret, A.2    Cohen, N.3
  • 17
    • 11344280957 scopus 로고    scopus 로고
    • Extracellular roles for the molecular chaperone, hsp90
    • Eustace B.K., Jay D.G. Extracellular roles for the molecular chaperone, hsp90. Cell Cycle 2004, 3:1098-1100.
    • (2004) Cell Cycle , vol.3 , pp. 1098-1100
    • Eustace, B.K.1    Jay, D.G.2
  • 18
    • 34548189523 scopus 로고    scopus 로고
    • Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis
    • Tsutsumi S., Neckers L. Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis. Cancer Sci 2007, 98:1536-1539.
    • (2007) Cancer Sci , vol.98 , pp. 1536-1539
    • Tsutsumi, S.1    Neckers, L.2
  • 20
    • 35548948037 scopus 로고    scopus 로고
    • New tricks for an old dog: the evolving world of Hsp70
    • Morano K.A. New tricks for an old dog: the evolving world of Hsp70. Ann N Y Acad Sci 2007, 1113:1-14.
    • (2007) Ann N Y Acad Sci , vol.1113 , pp. 1-14
    • Morano, K.A.1
  • 22
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini M., Heltai S., Zocchi M.R., Rugarli C. Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer 1992, 51:613-619.
    • (1992) Int J Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 23
    • 0024392717 scopus 로고
    • Apeptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family
    • Vanbuskirk A., Crump B.L., Margoliash E., Pierce S.K. Apeptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family. JExp Med 1989, 170:1799-1809.
    • (1989) JExp Med , vol.170 , pp. 1799-1809
    • Vanbuskirk, A.1    Crump, B.L.2    Margoliash, E.3    Pierce, S.K.4
  • 24
    • 0028979675 scopus 로고
    • Amechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto R., Srivastava P.K. Amechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 1995, 269:1585-1588.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.K.2
  • 25
    • 2942716692 scopus 로고    scopus 로고
    • Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness
    • Eustace B.K., Sakurai T., Stewart J.K., Yimlamai D., Unger C., Zehetmeier C., et al. Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nat Cell Biol 2004, 6:507-514.
    • (2004) Nat Cell Biol , vol.6 , pp. 507-514
    • Eustace, B.K.1    Sakurai, T.2    Stewart, J.K.3    Yimlamai, D.4    Unger, C.5    Zehetmeier, C.6
  • 26
    • 38349132541 scopus 로고    scopus 로고
    • Acritical role for HSP90 in cancer cell invasion involves interaction with the extracellular domain of HER-2
    • Sidera K., Gaitanou M., Stellas D., Matsas R., Patsavoudi E. Acritical role for HSP90 in cancer cell invasion involves interaction with the extracellular domain of HER-2. JBiol Chem 2008, 283:2031-2041.
    • (2008) JBiol Chem , vol.283 , pp. 2031-2041
    • Sidera, K.1    Gaitanou, M.2    Stellas, D.3    Matsas, R.4    Patsavoudi, E.5
  • 27
    • 0037177825 scopus 로고    scopus 로고
    • Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4
    • Asea A., Rehli M., Kabingu E., Boch J.A., Bare O., Auron P.E., et al. Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4. JBiol Chem 2002, 277:15028-15034.
    • (2002) JBiol Chem , vol.277 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3    Boch, J.A.4    Bare, O.5    Auron, P.E.6
  • 28
    • 0037144808 scopus 로고    scopus 로고
    • CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes
    • Becker T., Hartl F.U., Wieland F. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. JCell Biol 2002, 158:1277-1285.
    • (2002) JCell Biol , vol.158 , pp. 1277-1285
    • Becker, T.1    Hartl, F.U.2    Wieland, F.3
  • 29
    • 18644364531 scopus 로고    scopus 로고
    • Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation
    • Delneste Y., Magistrelli G., Gauchat J., Haeuw J., Aubry J., Nakamura K., et al. Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation. Immunity 2002, 17:353-362.
    • (2002) Immunity , vol.17 , pp. 353-362
    • Delneste, Y.1    Magistrelli, G.2    Gauchat, J.3    Haeuw, J.4    Aubry, J.5    Nakamura, K.6
  • 30
    • 0345305789 scopus 로고    scopus 로고
    • Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells
    • Berwin B., Hart J.P., Rice S., Gass C., Pizzo S.V., Post S.R., et al. Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. EMBO J 2003, 22:6127-6136.
    • (2003) EMBO J , vol.22 , pp. 6127-6136
    • Berwin, B.1    Hart, J.P.2    Rice, S.3    Gass, C.4    Pizzo, S.V.5    Post, S.R.6
  • 31
    • 83755195729 scopus 로고    scopus 로고
    • Association of heat-shock protein 70 with lipid rafts is required for Japanese encephalitis virus infection in Huh7 cells
    • Zhu Y.Z., Cao M.M., Wang W.B., Wang W., Ren H., Zhao P., et al. Association of heat-shock protein 70 with lipid rafts is required for Japanese encephalitis virus infection in Huh7 cells. JGen Virol 2012, 93:61-71.
    • (2012) JGen Virol , vol.93 , pp. 61-71
    • Zhu, Y.Z.1    Cao, M.M.2    Wang, W.B.3    Wang, W.4    Ren, H.5    Zhao, P.6
  • 32
    • 60349109590 scopus 로고    scopus 로고
    • Heat shock protein 70 on Neuro2a cells is a putative receptor for Japanese encephalitis virus
    • Das S., Laxminarayana S.V., Chandra N., Ravi V., Desai A. Heat shock protein 70 on Neuro2a cells is a putative receptor for Japanese encephalitis virus. Virology 2009, 385:47-57.
    • (2009) Virology , vol.385 , pp. 47-57
    • Das, S.1    Laxminarayana, S.V.2    Chandra, N.3    Ravi, V.4    Desai, A.5
  • 33
    • 16244364801 scopus 로고    scopus 로고
    • Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells
    • Reyes-Del Valle J., Chavez-Salinas S., Medina F., Del Angel R.M. Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells. JVirol 2005, 79:4557-4567.
    • (2005) JVirol , vol.79 , pp. 4557-4567
    • Reyes-Del Valle, J.1    Chavez-Salinas, S.2    Medina, F.3    Del Angel, R.M.4
  • 34
    • 84862950352 scopus 로고    scopus 로고
    • Heat-shock protein 70 is associated with the entry of Marek's disease virus into fibroblast
    • Wang X.J. Heat-shock protein 70 is associated with the entry of Marek's disease virus into fibroblast. Acta Virol 2011, 55:189-194.
    • (2011) Acta Virol , vol.55 , pp. 189-194
    • Wang, X.J.1
  • 35
    • 0037343539 scopus 로고    scopus 로고
    • JlpA of Campylobacter jejuni interacts with surface-exposed heat shock protein 90alpha and triggers signalling pathways leading to the activation of NF-kappaB and p38 MAP kinase in epithelial cells
    • Jin S., Song Y.C., Emili A., Sherman P.M., Chan V.L. JlpA of Campylobacter jejuni interacts with surface-exposed heat shock protein 90alpha and triggers signalling pathways leading to the activation of NF-kappaB and p38 MAP kinase in epithelial cells. Cell Microbiol 2003, 5:165-174.
    • (2003) Cell Microbiol , vol.5 , pp. 165-174
    • Jin, S.1    Song, Y.C.2    Emili, A.3    Sherman, P.M.4    Chan, V.L.5
  • 36
    • 84871694842 scopus 로고    scopus 로고
    • Heat shock proteins: conditional mediators of inflammation in tumor immunity
    • Calderwood S.K., Murshid A., Gong J. Heat shock proteins: conditional mediators of inflammation in tumor immunity. Front Immunol 2012, 3:75.
    • (2012) Front Immunol , vol.3 , pp. 75
    • Calderwood, S.K.1    Murshid, A.2    Gong, J.3
  • 37
    • 0141446039 scopus 로고    scopus 로고
    • Cell membrane lipid rafts mediate caveolar endocytosis of HIV-1 Tat fusion proteins
    • Fittipaldi A., Ferrari A., Zoppe M., Arcangeli C., Pellegrini V., Beltram F., et al. Cell membrane lipid rafts mediate caveolar endocytosis of HIV-1 Tat fusion proteins. JBiol Chem 2003, 278:34141-34149.
    • (2003) JBiol Chem , vol.278 , pp. 34141-34149
    • Fittipaldi, A.1    Ferrari, A.2    Zoppe, M.3    Arcangeli, C.4    Pellegrini, V.5    Beltram, F.6
  • 38
    • 0030904245 scopus 로고    scopus 로고
    • Atruncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vives E., Brodin P., Lebleu B. Atruncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. JBiol Chem 1997, 272:16010-16017.
    • (1997) JBiol Chem , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 39
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster L.J., De Hoog C.L., Mann M. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc Natl Acad Sci U S A 2003, 100:5813-5818.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 40
    • 5644297038 scopus 로고    scopus 로고
    • Lipid raft proteomics: analysis of in-solution digest of sodium dodecyl sulfate-solubilized lipid raft proteins by liquid chromatography-matrix-assisted laser desorption/ionization tandem mass spectrometry
    • Li N., Shaw A.R., Zhang N., Mak A., Li L. Lipid raft proteomics: analysis of in-solution digest of sodium dodecyl sulfate-solubilized lipid raft proteins by liquid chromatography-matrix-assisted laser desorption/ionization tandem mass spectrometry. Proteomics 2004, 4:3156-3166.
    • (2004) Proteomics , vol.4 , pp. 3156-3166
    • Li, N.1    Shaw, A.R.2    Zhang, N.3    Mak, A.4    Li, L.5
  • 41
    • 0036819191 scopus 로고    scopus 로고
    • Lipid interaction differentiates the constitutive and stress-induced heat shock proteins Hsc70 and Hsp70
    • Arispe N., Doh M., De Maio A. Lipid interaction differentiates the constitutive and stress-induced heat shock proteins Hsc70 and Hsp70. Cell Stress Chaperones 2002, 7:330-338.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 330-338
    • Arispe, N.1    Doh, M.2    De Maio, A.3


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