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Volumn 368, Issue 2, 2015, Pages 179-184

The role of heat shock protein 70 (Hsp70) in radiation-induced immunomodulation

Author keywords

Heat shock proteins; Immunotherapy; Oncology; Radiation

Indexed keywords

HEAT SHOCK PROTEIN 70;

EID: 84941880491     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2015.02.013     Document Type: Review
Times cited : (95)

References (105)
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.U. Molecular chaperones in cellular protein folding. Nature 1996, 381:571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 3
    • 0034015880 scopus 로고    scopus 로고
    • Heat-induced alterations in the localization of HSP72 and HSP73 as measured by indirect immunohistochemistry and immunogold electron microscopy
    • Ellis S., Killender M., Anderson R.L. Heat-induced alterations in the localization of HSP72 and HSP73 as measured by indirect immunohistochemistry and immunogold electron microscopy. J. Histochem. Cytochem 2000, 48:321-332.
    • (2000) J. Histochem. Cytochem , vol.48 , pp. 321-332
    • Ellis, S.1    Killender, M.2    Anderson, R.L.3
  • 4
    • 0037316678 scopus 로고    scopus 로고
    • Alterations in inducible 72-kDa heat shock protein and the chaperone cofactor BAG-1 in human brain after head injury
    • Seidberg N.A., Clark R.S., Zhang X., Lai Y., Chen M., Graham S.H., et al. Alterations in inducible 72-kDa heat shock protein and the chaperone cofactor BAG-1 in human brain after head injury. J. Neurochem 2003, 84:514-521.
    • (2003) J. Neurochem , vol.84 , pp. 514-521
    • Seidberg, N.A.1    Clark, R.S.2    Zhang, X.3    Lai, Y.4    Chen, M.5    Graham, S.H.6
  • 5
    • 0031132876 scopus 로고    scopus 로고
    • Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells
    • Multhoff G., Botzler C., Jennen L., Schmidt J., Ellwart J., Issels R. Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells. J. Immunol 1997, 158:4341-4350.
    • (1997) J. Immunol , vol.158 , pp. 4341-4350
    • Multhoff, G.1    Botzler, C.2    Jennen, L.3    Schmidt, J.4    Ellwart, J.5    Issels, R.6
  • 6
    • 44849084963 scopus 로고    scopus 로고
    • Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages
    • Vega V.L., Rodriguez-Silva M., Frey T., Gehrmann M., Diaz J.C., Steinem C., et al. Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages. J. Immunol 2008, 180:4299-4307.
    • (2008) J. Immunol , vol.180 , pp. 4299-4307
    • Vega, V.L.1    Rodriguez-Silva, M.2    Frey, T.3    Gehrmann, M.4    Diaz, J.C.5    Steinem, C.6
  • 8
    • 0032608038 scopus 로고    scopus 로고
    • Heat shock proteins: facts, thoughts, and dreams
    • De Maio A. Heat shock proteins: facts, thoughts, and dreams. Shock 1999, 11:1-12.
    • (1999) Shock , vol.11 , pp. 1-12
    • De Maio, A.1
  • 9
    • 84905645522 scopus 로고    scopus 로고
    • Heat shock protein 70 serum levels differ significantly in patients with chronic hepatitis, liver cirrhosis, and hepatocellular carcinoma
    • Gehrmann M., Cervello M., Montalto G., Cappello F., Gulino A., Knape C., et al. Heat shock protein 70 serum levels differ significantly in patients with chronic hepatitis, liver cirrhosis, and hepatocellular carcinoma. Front. Immunol 2014, 5:307.
    • (2014) Front. Immunol , vol.5 , pp. 307
    • Gehrmann, M.1    Cervello, M.2    Montalto, G.3    Cappello, F.4    Gulino, A.5    Knape, C.6
  • 11
    • 58249110557 scopus 로고    scopus 로고
    • Heat shock protein Hsp72 controls oncogene-induced senescence pathways in cancer cells
    • Gabai V.L., Yaglom J.A., Waldman T., Sherman M.Y. Heat shock protein Hsp72 controls oncogene-induced senescence pathways in cancer cells. Mol. Cell. Biol 2009, 29:559-569.
    • (2009) Mol. Cell. Biol , vol.29 , pp. 559-569
    • Gabai, V.L.1    Yaglom, J.A.2    Waldman, T.3    Sherman, M.Y.4
  • 12
    • 33751203833 scopus 로고    scopus 로고
    • Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties
    • Garrido C., Brunet M., Didelot C., Zermati Y., Schmitt E., Kroemer G. Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties. Cell Cycle 2006, 5:2592-2601.
    • (2006) Cell Cycle , vol.5 , pp. 2592-2601
    • Garrido, C.1    Brunet, M.2    Didelot, C.3    Zermati, Y.4    Schmitt, E.5    Kroemer, G.6
  • 14
    • 84872358363 scopus 로고    scopus 로고
    • Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an update
    • Ciocca D.R., Arrigo A.P., Calderwood S.K. Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an update. Arch. Toxicol 2013, 87:19-48.
    • (2013) Arch. Toxicol , vol.87 , pp. 19-48
    • Ciocca, D.R.1    Arrigo, A.P.2    Calderwood, S.K.3
  • 15
    • 41149083495 scopus 로고    scopus 로고
    • Heat shock factor 1 represses estrogen-dependent transcription through association with MTA1
    • Khaleque M.A., Bharti A., Gong J., Gray P.J., Sachdev V., Ciocca D.R., et al. Heat shock factor 1 represses estrogen-dependent transcription through association with MTA1. Oncogene 2008, 27:1886-1893.
    • (2008) Oncogene , vol.27 , pp. 1886-1893
    • Khaleque, M.A.1    Bharti, A.2    Gong, J.3    Gray, P.J.4    Sachdev, V.5    Ciocca, D.R.6
  • 16
    • 0034713677 scopus 로고    scopus 로고
    • Stress proteins and the immune response
    • Moseley P. Stress proteins and the immune response. Immunopharmacology 2000, 48:299-302.
    • (2000) Immunopharmacology , vol.48 , pp. 299-302
    • Moseley, P.1
  • 17
    • 33845913216 scopus 로고    scopus 로고
    • Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy
    • Schmitt E., Gehrmann M., Brunet M., Multhoff G., Garrido C. Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy. J. Leukoc. Biol 2007, 81:15-27.
    • (2007) J. Leukoc. Biol , vol.81 , pp. 15-27
    • Schmitt, E.1    Gehrmann, M.2    Brunet, M.3    Multhoff, G.4    Garrido, C.5
  • 18
    • 0028000105 scopus 로고
    • Heat shock proteins in immune response to cancer: the Fourth Paradigm
    • Srivastava P.K. Heat shock proteins in immune response to cancer: the Fourth Paradigm. Experientia 1994, 50:1054-1060.
    • (1994) Experientia , vol.50 , pp. 1054-1060
    • Srivastava, P.K.1
  • 20
    • 84884589727 scopus 로고    scopus 로고
    • Hsp70 chaperone dynamics and molecular mechanism
    • Mayer M.P. Hsp70 chaperone dynamics and molecular mechanism. Trends Biochem. Sci 2013, 38:507-514.
    • (2013) Trends Biochem. Sci , vol.38 , pp. 507-514
    • Mayer, M.P.1
  • 22
    • 0032727033 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70) stimulates proliferation and cytolytic activity of natural killer cells
    • Multhoff G., Mizzen L., Winchester C.C., Milner C.M., Wenk S., Eissner G., et al. Heat shock protein 70 (Hsp70) stimulates proliferation and cytolytic activity of natural killer cells. Exp. Hematol 1999, 27:1627-1636.
    • (1999) Exp. Hematol , vol.27 , pp. 1627-1636
    • Multhoff, G.1    Mizzen, L.2    Winchester, C.C.3    Milner, C.M.4    Wenk, S.5    Eissner, G.6
  • 23
    • 77957153127 scopus 로고    scopus 로고
    • Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation
    • Henderson B., Pockley A.G. Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation. J. Leukoc. Biol 2010, 88:445-462.
    • (2010) J. Leukoc. Biol , vol.88 , pp. 445-462
    • Henderson, B.1    Pockley, A.G.2
  • 24
    • 84867829868 scopus 로고    scopus 로고
    • Dual role of heat shock proteins (HSPs) in anti-tumor immunity
    • Multhoff G., Pockley A.G., Streffer C., Gaipl U.S. Dual role of heat shock proteins (HSPs) in anti-tumor immunity. Curr. Mol. Med 2012, 12:1174-1182.
    • (2012) Curr. Mol. Med , vol.12 , pp. 1174-1182
    • Multhoff, G.1    Pockley, A.G.2    Streffer, C.3    Gaipl, U.S.4
  • 26
    • 84904347106 scopus 로고    scopus 로고
    • Extracellular Hsp70: export and function
    • De Maio A. Extracellular Hsp70: export and function. Curr. Protein Pept. Sci 2014, 15:225-231.
    • (2014) Curr. Protein Pept. Sci , vol.15 , pp. 225-231
    • De Maio, A.1
  • 27
    • 44849133308 scopus 로고    scopus 로고
    • Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3
    • Gehrmann M., Liebisch G., Schmitz G., Anderson R., Steinem C., De M.A., et al. Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3. PLoS ONE 2008, 3:e1925.
    • (2008) PLoS ONE , vol.3
    • Gehrmann, M.1    Liebisch, G.2    Schmitz, G.3    Anderson, R.4    Steinem, C.5    De, M.A.6
  • 28
    • 1642378564 scopus 로고    scopus 로고
    • Tracking down lipid flippases and their biological functions
    • Pomorski T., Holthuis J.C., Herrmann A., van Meer G. Tracking down lipid flippases and their biological functions. J. Cell Sci 2004, 117:805-813.
    • (2004) J. Cell Sci , vol.117 , pp. 805-813
    • Pomorski, T.1    Holthuis, J.C.2    Herrmann, A.3    van Meer, G.4
  • 30
    • 84898053295 scopus 로고    scopus 로고
    • Oxidatively modified phosphatidylserines on the surface of apoptotic cells are essential phagocytic "eat-me" signals: cleavage and inhibition of phagocytosis by Lp-PLA2
    • Tyurin V.A., Balasubramanian K., Winnica D., Tyurina Y.Y., Vikulina A.S., He R.R., et al. Oxidatively modified phosphatidylserines on the surface of apoptotic cells are essential phagocytic "eat-me" signals: cleavage and inhibition of phagocytosis by Lp-PLA2. Cell Death Differ 2014, 21:825-835.
    • (2014) Cell Death Differ , vol.21 , pp. 825-835
    • Tyurin, V.A.1    Balasubramanian, K.2    Winnica, D.3    Tyurina, Y.Y.4    Vikulina, A.S.5    He, R.R.6
  • 31
    • 82755163551 scopus 로고    scopus 로고
    • Constitutive exposure of phosphatidylserine on viable cells
    • Segawa K., Suzuki J., Nagata S. Constitutive exposure of phosphatidylserine on viable cells. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:19246-19251.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 19246-19251
    • Segawa, K.1    Suzuki, J.2    Nagata, S.3
  • 32
    • 68849112162 scopus 로고    scopus 로고
    • Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells
    • Schilling D., Gehrmann M., Steinem C., De M.A., Pockley A.G., Abend M., et al. Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells. FASEB J. 2009, 23:2467-2477.
    • (2009) FASEB J. , vol.23 , pp. 2467-2477
    • Schilling, D.1    Gehrmann, M.2    Steinem, C.3    De, M.A.4    Pockley, A.G.5    Abend, M.6
  • 33
    • 33845512042 scopus 로고    scopus 로고
    • Antigen recognition induces phosphatidylserine exposure on the cell surface of human CD8+ T cells
    • Fischer K., Voelkl S., Berger J., Andreesen R., Pomorski T., Mackensen A. Antigen recognition induces phosphatidylserine exposure on the cell surface of human CD8+ T cells. Blood 2006, 108:4094-4101.
    • (2006) Blood , vol.108 , pp. 4094-4101
    • Fischer, K.1    Voelkl, S.2    Berger, J.3    Andreesen, R.4    Pomorski, T.5    Mackensen, A.6
  • 34
    • 49249118310 scopus 로고    scopus 로고
    • New jobs for ancient chaperones
    • Srivastava P.K. New jobs for ancient chaperones. Sci. Am 2008, 299:50-55.
    • (2008) Sci. Am , vol.299 , pp. 50-55
    • Srivastava, P.K.1
  • 35
    • 79955046674 scopus 로고    scopus 로고
    • Intracellular proteins displayed on the surface of tumor cells as targets for therapeutic intervention with antibody-related agents
    • Weidle U.H., Maisel D., Klostermann S., Schiller C., Weiss E.H. Intracellular proteins displayed on the surface of tumor cells as targets for therapeutic intervention with antibody-related agents. Cancer Genomics Proteomics 2011, 8:49-63.
    • (2011) Cancer Genomics Proteomics , vol.8 , pp. 49-63
    • Weidle, U.H.1    Maisel, D.2    Klostermann, S.3    Schiller, C.4    Weiss, E.H.5
  • 36
    • 0242330183 scopus 로고    scopus 로고
    • Overexpression of HSP70 is induced by ionizing radiation in C3H 10T1/2 cells and protects from DNA damage
    • Calini V., Urani C., Camatini M. Overexpression of HSP70 is induced by ionizing radiation in C3H 10T1/2 cells and protects from DNA damage. Toxicol. In Vitro 2003, 17:561-566.
    • (2003) Toxicol. In Vitro , vol.17 , pp. 561-566
    • Calini, V.1    Urani, C.2    Camatini, M.3
  • 37
    • 2542462084 scopus 로고    scopus 로고
    • Differential up-regulation of cytosolic and membrane-bound heat shock protein 70 in tumor cells by anti-inflammatory drugs
    • Gehrmann M., Brunner M., Pfister K., Reichle A., Kremmer E., Multhoff G. Differential up-regulation of cytosolic and membrane-bound heat shock protein 70 in tumor cells by anti-inflammatory drugs. Clin. Cancer Res 2004, 10:3354-3364.
    • (2004) Clin. Cancer Res , vol.10 , pp. 3354-3364
    • Gehrmann, M.1    Brunner, M.2    Pfister, K.3    Reichle, A.4    Kremmer, E.5    Multhoff, G.6
  • 39
    • 0024297490 scopus 로고
    • Effect of radiation on the expression of carcinoembryonic antigen on the membranes of human gastric adenocarcinoma cells - immunological study using monoclonal antibodies
    • Hareyama M., Imai K., Ban T., Koshiba H., Kubo K., Shidou M., et al. Effect of radiation on the expression of carcinoembryonic antigen on the membranes of human gastric adenocarcinoma cells - immunological study using monoclonal antibodies. Nippon Igaku Hoshasen Gakkai Zasshi 1988, 48:1572-1574.
    • (1988) Nippon Igaku Hoshasen Gakkai Zasshi , vol.48 , pp. 1572-1574
    • Hareyama, M.1    Imai, K.2    Ban, T.3    Koshiba, H.4    Kubo, K.5    Shidou, M.6
  • 40
    • 0030877151 scopus 로고    scopus 로고
    • Late and persistent up-regulation of intercellular adhesion molecule-1 (ICAM-1) expression by ionizing radiation in human endothelial cells in vitro
    • Gaugler M.H., Squiban C., Van Der M.A., Bertho J.M., Vandamme M., Mouthon M.A. Late and persistent up-regulation of intercellular adhesion molecule-1 (ICAM-1) expression by ionizing radiation in human endothelial cells in vitro. Int. J. Radiat. Biol 1997, 72:201-209.
    • (1997) Int. J. Radiat. Biol , vol.72 , pp. 201-209
    • Gaugler, M.H.1    Squiban, C.2    Van Der, M.A.3    Bertho, J.M.4    Vandamme, M.5    Mouthon, M.A.6
  • 41
    • 84905739456 scopus 로고    scopus 로고
    • Radiation as immunomodulator: implications for dendritic cell-based immunotherapy
    • Roses R.E., Datta J., Czerniecki B.J. Radiation as immunomodulator: implications for dendritic cell-based immunotherapy. Radiat. Res 2014, 182:211-218.
    • (2014) Radiat. Res , vol.182 , pp. 211-218
    • Roses, R.E.1    Datta, J.2    Czerniecki, B.J.3
  • 42
    • 84905741842 scopus 로고    scopus 로고
    • Unlocking the combination: potentiation of radiation-induced antitumor responses with immunotherapy
    • Wattenberg M.M., Fahim A., Ahmed M.M., Hodge J.W. Unlocking the combination: potentiation of radiation-induced antitumor responses with immunotherapy. Radiat. Res 2014, 10.1667/RR13374.1.
    • (2014) Radiat. Res
    • Wattenberg, M.M.1    Fahim, A.2    Ahmed, M.M.3    Hodge, J.W.4
  • 43
    • 7444258053 scopus 로고    scopus 로고
    • Sublethal irradiation of human tumor cells modulates phenotype resulting in enhanced killing by cytotoxic T lymphocytes
    • Garnett C.T., Palena C., Chakraborty M., Tsang K.Y., Schlom J., Hodge J.W. Sublethal irradiation of human tumor cells modulates phenotype resulting in enhanced killing by cytotoxic T lymphocytes. Cancer Res 2004, 64:7985-7994.
    • (2004) Cancer Res , vol.64 , pp. 7985-7994
    • Garnett, C.T.1    Palena, C.2    Chakraborty, M.3    Tsang, K.Y.4    Schlom, J.5    Hodge, J.W.6
  • 44
    • 0035377009 scopus 로고    scopus 로고
    • Antigen decoding by T lymphocytes: from synapses to fate determination
    • Lanzavecchia A., Sallusto F. Antigen decoding by T lymphocytes: from synapses to fate determination. Nat. Immunol 2001, 2:487-492.
    • (2001) Nat. Immunol , vol.2 , pp. 487-492
    • Lanzavecchia, A.1    Sallusto, F.2
  • 45
    • 84878392088 scopus 로고    scopus 로고
    • Essentials of Th17 cell commitment and plasticity
    • Muranski P., Restifo N.P. Essentials of Th17 cell commitment and plasticity. Blood 2013, 121:2402-2414.
    • (2013) Blood , vol.121 , pp. 2402-2414
    • Muranski, P.1    Restifo, N.P.2
  • 46
    • 30744458573 scopus 로고    scopus 로고
    • Lymphopenia and interleukin-2 therapy alter homeostasis of CD4+CD25+ regulatory T cells
    • Zhang H., Chua K.S., Guimond M., Kapoor V., Brown M.V., Fleisher T.A., et al. Lymphopenia and interleukin-2 therapy alter homeostasis of CD4+CD25+ regulatory T cells. Nat. Med 2005, 11:1238-1243.
    • (2005) Nat. Med , vol.11 , pp. 1238-1243
    • Zhang, H.1    Chua, K.S.2    Guimond, M.3    Kapoor, V.4    Brown, M.V.5    Fleisher, T.A.6
  • 47
    • 84858766182 scopus 로고    scopus 로고
    • The blockade of immune checkpoints in cancer immunotherapy
    • Pardoll D.M. The blockade of immune checkpoints in cancer immunotherapy. Nat. Rev. Cancer 2012, 12:252-264.
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 252-264
    • Pardoll, D.M.1
  • 48
    • 84921448324 scopus 로고    scopus 로고
    • The evolution of checkpoint blockade as a cancer therapy: what's here, what's next?
    • Shin D.S., Ribas A. The evolution of checkpoint blockade as a cancer therapy: what's here, what's next?. Curr. Opin. Immunol 2015, 33C:23-35.
    • (2015) Curr. Opin. Immunol , vol.33C , pp. 23-35
    • Shin, D.S.1    Ribas, A.2
  • 50
    • 85006217674 scopus 로고    scopus 로고
    • CTLA-4 blockade with ipilimumab: biology, safety, efficacy, and future considerations
    • Camacho L.H. CTLA-4 blockade with ipilimumab: biology, safety, efficacy, and future considerations. Cancer Med 2015, 10.1002/cam4.371.
    • (2015) Cancer Med
    • Camacho, L.H.1
  • 51
    • 84871483917 scopus 로고    scopus 로고
    • Breast cancer immunobiology driving immunotherapy: vaccines and immune checkpoint blockade
    • Emens L.A. Breast cancer immunobiology driving immunotherapy: vaccines and immune checkpoint blockade. Expert Rev. Anticancer Ther 2012, 12:1597-1611.
    • (2012) Expert Rev. Anticancer Ther , vol.12 , pp. 1597-1611
    • Emens, L.A.1
  • 52
    • 84926419753 scopus 로고    scopus 로고
    • Myeloid cells in cancer-related inflammation
    • Caronni N., Savino B., Bonecchi R. Myeloid cells in cancer-related inflammation. Immunobiology 2015, 220:249-253.
    • (2015) Immunobiology , vol.220 , pp. 249-253
    • Caronni, N.1    Savino, B.2    Bonecchi, R.3
  • 53
    • 17144374753 scopus 로고    scopus 로고
    • Toward an understanding of NKT cell biology: progress and paradoxes
    • Kronenberg M. Toward an understanding of NKT cell biology: progress and paradoxes. Annu. Rev. Immunol 2005, 23:877-900.
    • (2005) Annu. Rev. Immunol , vol.23 , pp. 877-900
    • Kronenberg, M.1
  • 54
    • 0035911242 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) contributes to interferon gamma-dependent natural killer cell protection from tumor metastasis
    • Smyth M.J., Cretney E., Takeda K., Wiltrout R.H., Sedger L.M., Kayagaki N., et al. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) contributes to interferon gamma-dependent natural killer cell protection from tumor metastasis. J. Exp. Med 2001, 193:661-670.
    • (2001) J. Exp. Med , vol.193 , pp. 661-670
    • Smyth, M.J.1    Cretney, E.2    Takeda, K.3    Wiltrout, R.H.4    Sedger, L.M.5    Kayagaki, N.6
  • 57
    • 24344505476 scopus 로고    scopus 로고
    • Human natural killer cells: molecular mechanisms controlling NK cell activation and tumor cell lysis
    • Moretta L., Bottino C., Pende D., Vitale M., Mingari M.C., Moretta A. Human natural killer cells: molecular mechanisms controlling NK cell activation and tumor cell lysis. Immunol. Lett 2005, 100:7-13.
    • (2005) Immunol. Lett , vol.100 , pp. 7-13
    • Moretta, L.1    Bottino, C.2    Pende, D.3    Vitale, M.4    Mingari, M.C.5    Moretta, A.6
  • 59
    • 84906047226 scopus 로고    scopus 로고
    • The chemokine system, and its CCR5 and CXCR4 receptors, as potential targets for personalized therapy in cancer
    • Weitzenfeld P., Ben-Baruch A. The chemokine system, and its CCR5 and CXCR4 receptors, as potential targets for personalized therapy in cancer. Cancer Lett 2014, 352:36-53.
    • (2014) Cancer Lett , vol.352 , pp. 36-53
    • Weitzenfeld, P.1    Ben-Baruch, A.2
  • 60
    • 84865760928 scopus 로고    scopus 로고
    • Regulating the suppressors: apoptosis and inflammation govern the survival of tumor-induced myeloid-derived suppressor cells (MDSC)
    • Ostrand-Rosenberg S., Sinha P., Chornoguz O., Ecker C. Regulating the suppressors: apoptosis and inflammation govern the survival of tumor-induced myeloid-derived suppressor cells (MDSC). Cancer Immunol. Immunother 2012, 61:1319-1325.
    • (2012) Cancer Immunol. Immunother , vol.61 , pp. 1319-1325
    • Ostrand-Rosenberg, S.1    Sinha, P.2    Chornoguz, O.3    Ecker, C.4
  • 61
    • 84907486438 scopus 로고    scopus 로고
    • The programmed death-1 immune-suppressive pathway: barrier to antitumor immunity
    • Ostrand-Rosenberg S., Horn L.A., Haile S.T. The programmed death-1 immune-suppressive pathway: barrier to antitumor immunity. J. Immunol 2014, 193:3835-3841.
    • (2014) J. Immunol , vol.193 , pp. 3835-3841
    • Ostrand-Rosenberg, S.1    Horn, L.A.2    Haile, S.T.3
  • 62
    • 0035059950 scopus 로고    scopus 로고
    • Activating receptors and coreceptors involved in human natural killer cell-mediated cytolysis
    • Moretta A., Bottino C., Vitale M., Pende D., Cantoni C., Mingari M.C., et al. Activating receptors and coreceptors involved in human natural killer cell-mediated cytolysis. Annu. Rev. Immunol 2001, 19:197-223.
    • (2001) Annu. Rev. Immunol , vol.19 , pp. 197-223
    • Moretta, A.1    Bottino, C.2    Vitale, M.3    Pende, D.4    Cantoni, C.5    Mingari, M.C.6
  • 63
    • 1242314233 scopus 로고    scopus 로고
    • Heat shock protein 70-reactivity is associated with increased cell surface density of CD94/CD56 on primary natural killer cells
    • Gross C., Schmidt-Wolf I.G., Nagaraj S., Gastpar R., Ellwart J., Kunz-Schughart L.A., et al. Heat shock protein 70-reactivity is associated with increased cell surface density of CD94/CD56 on primary natural killer cells. Cell Stress Chaperones 2003, 8:348-360.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 348-360
    • Gross, C.1    Schmidt-Wolf, I.G.2    Nagaraj, S.3    Gastpar, R.4    Ellwart, J.5    Kunz-Schughart, L.A.6
  • 64
    • 0031925152 scopus 로고    scopus 로고
    • The role of heat shock proteins in the stimulation of an immune response
    • Multhoff G., Botzler C., Issels R. The role of heat shock proteins in the stimulation of an immune response. Biol. Chem 1998, 379:295-300.
    • (1998) Biol. Chem , vol.379 , pp. 295-300
    • Multhoff, G.1    Botzler, C.2    Issels, R.3
  • 66
    • 20444431560 scopus 로고    scopus 로고
    • Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells
    • Gastpar R., Gehrmann M., Bausero M.A., Asea A., Gross C., Schroeder J.A., et al. Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells. Cancer Res 2005, 65:5238-5247.
    • (2005) Cancer Res , vol.65 , pp. 5238-5247
    • Gastpar, R.1    Gehrmann, M.2    Bausero, M.A.3    Asea, A.4    Gross, C.5    Schroeder, J.A.6
  • 67
    • 0142103373 scopus 로고    scopus 로고
    • Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B
    • Gross C., Koelch W., DeMaio A., Arispe N., Multhoff G. Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B. J. Biol. Chem 2003, 278:41173-41181.
    • (2003) J. Biol. Chem , vol.278 , pp. 41173-41181
    • Gross, C.1    Koelch, W.2    DeMaio, A.3    Arispe, N.4    Multhoff, G.5
  • 68
    • 84864075586 scopus 로고    scopus 로고
    • Immunotherapeutic targeting of membrane hsp70-expressing tumors using recombinant human granzyme B
    • Gehrmann M., Stangl S., Kirschner A., Foulds G.A., Sievert W., Doss B.T., et al. Immunotherapeutic targeting of membrane hsp70-expressing tumors using recombinant human granzyme B. PLoS ONE 2012, 7:e41341.
    • (2012) PLoS ONE , vol.7
    • Gehrmann, M.1    Stangl, S.2    Kirschner, A.3    Foulds, G.A.4    Sievert, W.5    Doss, B.T.6
  • 69
    • 79960964063 scopus 로고    scopus 로고
    • A novel expression and purification system for the production of enzymatic and biologically active human granzyme B
    • Gehrmann M., Doss B.T., Wagner M., Zettlitz K.A., Kontermann R.E., Foulds G., et al. A novel expression and purification system for the production of enzymatic and biologically active human granzyme B. J. Immunol. Methods 2011, 371:8-17.
    • (2011) J. Immunol. Methods , vol.371 , pp. 8-17
    • Gehrmann, M.1    Doss, B.T.2    Wagner, M.3    Zettlitz, K.A.4    Kontermann, R.E.5    Foulds, G.6
  • 70
    • 0036819181 scopus 로고    scopus 로고
    • Inhibition of tumor growth in mice with severe combined immunodeficiency is mediated by heat shock protein 70 (Hsp70)-peptide-activated, CD94 positive natural killer cells
    • Moser C., Schmidbauer C., Gurtler U., Gross C., Gehrmann M., Thonigs G., et al. Inhibition of tumor growth in mice with severe combined immunodeficiency is mediated by heat shock protein 70 (Hsp70)-peptide-activated, CD94 positive natural killer cells. Cell Stress Chaperones 2002, 7:365-373.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 365-373
    • Moser, C.1    Schmidbauer, C.2    Gurtler, U.3    Gross, C.4    Gehrmann, M.5    Thonigs, G.6
  • 71
    • 2542558307 scopus 로고    scopus 로고
    • Treatment of colon and lung cancer patients with ex vivo heat shock protein 70-peptide-activated, autologous natural killer cells: a clinical phase I trial
    • Krause S.W., Gastpar R., Andreesen R., Gross C., Ullrich H., Thonigs G., et al. Treatment of colon and lung cancer patients with ex vivo heat shock protein 70-peptide-activated, autologous natural killer cells: a clinical phase I trial. Clin. Cancer Res 2004, 10:3699-3707.
    • (2004) Clin. Cancer Res , vol.10 , pp. 3699-3707
    • Krause, S.W.1    Gastpar, R.2    Andreesen, R.3    Gross, C.4    Ullrich, H.5    Thonigs, G.6
  • 72
    • 79960369894 scopus 로고    scopus 로고
    • Detection of irradiation-induced, membrane heat shock protein 70 (Hsp70) in mouse tumors using Hsp70 Fab fragment
    • Stangl S., Themelis G., Friedrich L., Ntziachristos V., Sarantopoulos A., Molls M., et al. Detection of irradiation-induced, membrane heat shock protein 70 (Hsp70) in mouse tumors using Hsp70 Fab fragment. Radiother. Oncol 2011, 99:313-316.
    • (2011) Radiother. Oncol , vol.99 , pp. 313-316
    • Stangl, S.1    Themelis, G.2    Friedrich, L.3    Ntziachristos, V.4    Sarantopoulos, A.5    Molls, M.6
  • 73
    • 33646484351 scopus 로고    scopus 로고
    • Control of metastasized pancreatic carcinomas in SCID/beige mice with human IL-2/TKD-activated NK cells
    • Stangl S., Wortmann A., Guertler U., Multhoff G. Control of metastasized pancreatic carcinomas in SCID/beige mice with human IL-2/TKD-activated NK cells. J. Immunol 2006, 176:6270-6276.
    • (2006) J. Immunol , vol.176 , pp. 6270-6276
    • Stangl, S.1    Wortmann, A.2    Guertler, U.3    Multhoff, G.4
  • 74
    • 84893862822 scopus 로고    scopus 로고
    • Validation of heat shock protein 70 as a tumor-specific biomarker for monitoring the outcome of radiation therapy in tumor mouse models
    • Bayer C., Liebhardt M.E., Schmid T.E., Trajkovic-Arsic M., Hube K., Specht H.M., et al. Validation of heat shock protein 70 as a tumor-specific biomarker for monitoring the outcome of radiation therapy in tumor mouse models. Int. J. Radiat. Oncol. Biol. Phys 2014, 88:694-700.
    • (2014) Int. J. Radiat. Oncol. Biol. Phys , vol.88 , pp. 694-700
    • Bayer, C.1    Liebhardt, M.E.2    Schmid, T.E.3    Trajkovic-Arsic, M.4    Hube, K.5    Specht, H.M.6
  • 75
    • 0032101221 scopus 로고    scopus 로고
    • Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world
    • Srivastava P.K., Menoret A., Basu S., Binder R.J., McQuade K.L. Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world. Immunity 1998, 8:657-665.
    • (1998) Immunity , vol.8 , pp. 657-665
    • Srivastava, P.K.1    Menoret, A.2    Basu, S.3    Binder, R.J.4    McQuade, K.L.5
  • 76
    • 0034541171 scopus 로고    scopus 로고
    • Cutting edge: heat shock protein gp96 induces maturation and migration of CD11c+ cells in vivo
    • Binder R.J., Anderson K.M., Basu S., Srivastava P.K. Cutting edge: heat shock protein gp96 induces maturation and migration of CD11c+ cells in vivo. J. Immunol 2000, 165:6029-6035.
    • (2000) J. Immunol , vol.165 , pp. 6029-6035
    • Binder, R.J.1    Anderson, K.M.2    Basu, S.3    Srivastava, P.K.4
  • 77
    • 42049087381 scopus 로고    scopus 로고
    • Heat-shock protein-based vaccines for cancer and infectious disease
    • Binder R.J. Heat-shock protein-based vaccines for cancer and infectious disease. Expert Rev. Vaccines 2008, 7:383-393.
    • (2008) Expert Rev. Vaccines , vol.7 , pp. 383-393
    • Binder, R.J.1
  • 78
    • 84902194486 scopus 로고    scopus 로고
    • Heat-shock proteins-based immunotherapy for advanced melanoma in the era of target therapies and immunomodulating agents
    • Tosti G., Cocorocchio E., Pennacchioli E., Ferrucci P.F., Testori A., Martinoli C. Heat-shock proteins-based immunotherapy for advanced melanoma in the era of target therapies and immunomodulating agents. Expert Opin. Biol. Ther 2014, 14:955-967.
    • (2014) Expert Opin. Biol. Ther , vol.14 , pp. 955-967
    • Tosti, G.1    Cocorocchio, E.2    Pennacchioli, E.3    Ferrucci, P.F.4    Testori, A.5    Martinoli, C.6
  • 79
    • 33646348754 scopus 로고    scopus 로고
    • A phase II trial of vaccination with autologous, tumor-derived heat-shock protein peptide complexes Gp96, in combination with GM-CSF and interferon-alpha in metastatic melanoma patients
    • Pilla L., Patuzzo R., Rivoltini L., Maio M., Pennacchioli E., Lamaj E., et al. A phase II trial of vaccination with autologous, tumor-derived heat-shock protein peptide complexes Gp96, in combination with GM-CSF and interferon-alpha in metastatic melanoma patients. Cancer Immunol. Immunother 2006, 55:958-968.
    • (2006) Cancer Immunol. Immunother , vol.55 , pp. 958-968
    • Pilla, L.1    Patuzzo, R.2    Rivoltini, L.3    Maio, M.4    Pennacchioli, E.5    Lamaj, E.6
  • 80
    • 10744233222 scopus 로고    scopus 로고
    • Vaccination with autologous tumor-derived heat-shock protein gp96 after liver resection for metastatic colorectal cancer
    • Mazzaferro V., Coppa J., Carrabba M.G., Rivoltini L., Schiavo M., Regalia E., et al. Vaccination with autologous tumor-derived heat-shock protein gp96 after liver resection for metastatic colorectal cancer. Clin. Cancer Res 2003, 9:3235-3245.
    • (2003) Clin. Cancer Res , vol.9 , pp. 3235-3245
    • Mazzaferro, V.1    Coppa, J.2    Carrabba, M.G.3    Rivoltini, L.4    Schiavo, M.5    Regalia, E.6
  • 81
    • 33644636996 scopus 로고    scopus 로고
    • Therapeutic cancer vaccines
    • Srivastava P.K. Therapeutic cancer vaccines. Curr. Opin. Immunol 2006, 18:201-205.
    • (2006) Curr. Opin. Immunol , vol.18 , pp. 201-205
    • Srivastava, P.K.1
  • 82
    • 33846332800 scopus 로고    scopus 로고
    • Experience with heat shock protein-peptide complex 96 vaccine therapy in patients with indolent non-Hodgkin lymphoma
    • Oki Y., McLaughlin P., Fayad L.E., Pro B., Mansfield P.F., Clayman G.L., et al. Experience with heat shock protein-peptide complex 96 vaccine therapy in patients with indolent non-Hodgkin lymphoma. Cancer 2007, 109:77-83.
    • (2007) Cancer , vol.109 , pp. 77-83
    • Oki, Y.1    McLaughlin, P.2    Fayad, L.E.3    Pro, B.4    Mansfield, P.F.5    Clayman, G.L.6
  • 83
    • 84865618692 scopus 로고    scopus 로고
    • Inhibition of HSP70: a challenging anti-cancer strategy
    • Goloudina A.R., Demidov O.N., Garrido C. Inhibition of HSP70: a challenging anti-cancer strategy. Cancer Lett 2012, 325:117-124.
    • (2012) Cancer Lett , vol.325 , pp. 117-124
    • Goloudina, A.R.1    Demidov, O.N.2    Garrido, C.3
  • 85
    • 84892185056 scopus 로고    scopus 로고
    • Pifithrin-mu, an inhibitor of heat-shock protein 70, can increase the antitumor effects of hyperthermia against human prostate cancer cells
    • Sekihara K., Harashima N., Tongu M., Tamaki Y., Uchida N., Inomata T., et al. Pifithrin-mu, an inhibitor of heat-shock protein 70, can increase the antitumor effects of hyperthermia against human prostate cancer cells. PLoS ONE 2013, 8:e78772.
    • (2013) PLoS ONE , vol.8
    • Sekihara, K.1    Harashima, N.2    Tongu, M.3    Tamaki, Y.4    Uchida, N.5    Inomata, T.6
  • 87
    • 84906274976 scopus 로고    scopus 로고
    • Effective immunotherapy of rat glioblastoma with prolonged intratumoral delivery of exogenous heat shock protein Hsp70
    • Shevtsov M.A., Pozdnyakov A.V., Mikhrina A.L., Yakovleva L.Y., Nikolaev B.P., Dobrodumov A.V., et al. Effective immunotherapy of rat glioblastoma with prolonged intratumoral delivery of exogenous heat shock protein Hsp70. Int. J. Cancer 2014, 135:2118-2128.
    • (2014) Int. J. Cancer , vol.135 , pp. 2118-2128
    • Shevtsov, M.A.1    Pozdnyakov, A.V.2    Mikhrina, A.L.3    Yakovleva, L.Y.4    Nikolaev, B.P.5    Dobrodumov, A.V.6
  • 88
    • 84902985997 scopus 로고    scopus 로고
    • Pilot study of intratumoral injection of recombinant heat shock protein 70 in the treatment of malignant brain tumors in children
    • Shevtsov M.A., Kim A.V., Samochernych K.A., Romanova I.V., Margulis B.A., Guzhova I.V., et al. Pilot study of intratumoral injection of recombinant heat shock protein 70 in the treatment of malignant brain tumors in children. Onco Targets Ther 2014, 7:1071-1081.
    • (2014) Onco Targets Ther , vol.7 , pp. 1071-1081
    • Shevtsov, M.A.1    Kim, A.V.2    Samochernych, K.A.3    Romanova, I.V.4    Margulis, B.A.5    Guzhova, I.V.6
  • 90
    • 84960987950 scopus 로고
    • The concentration of oxygen dissolved in tissues at the time of irradiation as a factor in radiotherapy
    • Gray L.H., Conger A.D., Ebert M., Hornsey S., Scott O.C. The concentration of oxygen dissolved in tissues at the time of irradiation as a factor in radiotherapy. Br. J. Radiol 1953, 26:638-648.
    • (1953) Br. J. Radiol , vol.26 , pp. 638-648
    • Gray, L.H.1    Conger, A.D.2    Ebert, M.3    Hornsey, S.4    Scott, O.C.5
  • 91
    • 0034743861 scopus 로고    scopus 로고
    • Oxygen status of malignant tumors: pathogenesis of hypoxia and significance for tumor therapy
    • Vaupel P., Kelleher D.K., Hockel M. Oxygen status of malignant tumors: pathogenesis of hypoxia and significance for tumor therapy. Semin. Oncol 2001, 28:29-35.
    • (2001) Semin. Oncol , vol.28 , pp. 29-35
    • Vaupel, P.1    Kelleher, D.K.2    Hockel, M.3
  • 93
    • 0036891466 scopus 로고    scopus 로고
    • Phosphatidylserine is a marker of tumor vasculature and a potential target for cancer imaging and therapy
    • Ran S., Thorpe P.E. Phosphatidylserine is a marker of tumor vasculature and a potential target for cancer imaging and therapy. Int. J. Radiat. Oncol. Biol. Phys 2002, 54:1479-1484.
    • (2002) Int. J. Radiat. Oncol. Biol. Phys , vol.54 , pp. 1479-1484
    • Ran, S.1    Thorpe, P.E.2
  • 95
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl F.U., Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002, 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 96
    • 84880298293 scopus 로고    scopus 로고
    • The role of heat shock proteins in bladder cancer
    • Ischia J., So A.I. The role of heat shock proteins in bladder cancer. Nat. Rev. Urol 2013, 10:386-395.
    • (2013) Nat. Rev. Urol , vol.10 , pp. 386-395
    • Ischia, J.1    So, A.I.2
  • 98
    • 84899138473 scopus 로고    scopus 로고
    • Fractionated radiotherapy is the main stimulus for the induction of cell death and of Hsp70 release of p53 mutated glioblastoma cell lines
    • Rubner Y., Muth C., Strnad A., Derer A., Sieber R., Buslei R., et al. Fractionated radiotherapy is the main stimulus for the induction of cell death and of Hsp70 release of p53 mutated glioblastoma cell lines. Radiat. Oncol 2014, 9:89.
    • (2014) Radiat. Oncol , vol.9 , pp. 89
    • Rubner, Y.1    Muth, C.2    Strnad, A.3    Derer, A.4    Sieber, R.5    Buslei, R.6
  • 99
    • 84941874515 scopus 로고    scopus 로고
    • Recombinant heat shock protein 70 in combination with radiotherapy as a source of tumor antigens to improve dendritic cell immunotherapy
    • Wang Y.S., Liu S.J., Huang S.C., Chang C.C., Huang Y.C., Fong W.L., et al. Recombinant heat shock protein 70 in combination with radiotherapy as a source of tumor antigens to improve dendritic cell immunotherapy. Front. Oncol 2012, 2:149.
    • (2012) Front. Oncol , vol.2 , pp. 149
    • Wang, Y.S.1    Liu, S.J.2    Huang, S.C.3    Chang, C.C.4    Huang, Y.C.5    Fong, W.L.6
  • 100
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release
    • Broquet A.H., Thomas G., Masliah J., Trugnan G., Bachelet M. Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release. J. Biol. Chem 2003, 278:21601-21606.
    • (2003) J. Biol. Chem , vol.278 , pp. 21601-21606
    • Broquet, A.H.1    Thomas, G.2    Masliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 101
    • 0035964907 scopus 로고    scopus 로고
    • In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance
    • Guzhova I., Kislyakova K., Moskaliova O., Fridlanskaya I., Tytell M., Cheetham M., et al. In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance. Brain Res 2001, 914:66-73.
    • (2001) Brain Res , vol.914 , pp. 66-73
    • Guzhova, I.1    Kislyakova, K.2    Moskaliova, O.3    Fridlanskaya, I.4    Tytell, M.5    Cheetham, M.6
  • 102
    • 0042235547 scopus 로고    scopus 로고
    • Heat shock proteins as regulators of the immune response
    • Pockley A.G. Heat shock proteins as regulators of the immune response. Lancet 2003, 362:469-476.
    • (2003) Lancet , vol.362 , pp. 469-476
    • Pockley, A.G.1
  • 103
    • 0034937685 scopus 로고    scopus 로고
    • Effects of the flavonoid drug quercetin on the response of human prostate tumours to hyperthermia in vitro and in vivo
    • Asea A., Ara G., Teicher B.A., Stevenson M.A., Calderwood S.K. Effects of the flavonoid drug quercetin on the response of human prostate tumours to hyperthermia in vitro and in vivo. Int. J. Hyperthermia 2001, 17:347-356.
    • (2001) Int. J. Hyperthermia , vol.17 , pp. 347-356
    • Asea, A.1    Ara, G.2    Teicher, B.A.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 104
    • 23844544016 scopus 로고    scopus 로고
    • Alternative mechanism by which IFN-gamma enhances tumor recognition: active release of heat shock protein 72
    • Bausero M.A., Gastpar R., Multhoff G., Asea A. Alternative mechanism by which IFN-gamma enhances tumor recognition: active release of heat shock protein 72. J. Immunol 2005, 175:2900-2912.
    • (2005) J. Immunol , vol.175 , pp. 2900-2912
    • Bausero, M.A.1    Gastpar, R.2    Multhoff, G.3    Asea, A.4
  • 105
    • 0025876649 scopus 로고
    • Static and dynamic lipid asymmetry in cell membranes
    • Devaux P.F. Static and dynamic lipid asymmetry in cell membranes. Biochemistry 1991, 30:1163-1173.
    • (1991) Biochemistry , vol.30 , pp. 1163-1173
    • Devaux, P.F.1


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