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Volumn 177, Issue 11, 2006, Pages 7849-7857

Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; EGTAZIC ACID; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; HEAT SHOCK PROTEIN 70; IONOMYCIN;

EID: 33750570923     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.177.11.7849     Document Type: Article
Times cited : (276)

References (54)
  • 2
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea, A., S. K. Kraeft, E. A. Kurt-Jones, M. A. Stevenson, L. B. Chen, R. W. Finberg, G. C. Koo, and S. K. Calderwood. 2000. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 6: 435-442.
    • (2000) Nat. Med. , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 3
    • 0036214288 scopus 로고    scopus 로고
    • Interaction of heat shock proteins with peptides and antigen presenting cells: Chaperoning of the innate and adaptive immune responses
    • Srivastava, P. 2002. Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu. Rev. Immunol. 20: 395-425.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 4
    • 15544373100 scopus 로고    scopus 로고
    • Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells
    • Theriault, J. R., S. S. Mambula, T. Sawamura, M. A. Stevenson, and S. K. Calderwood. 2005. Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells. FEBS Lett. 579: 1951-1960.
    • (2005) FEBS Lett. , vol.579 , pp. 1951-1960
    • Theriault, J.R.1    Mambula, S.S.2    Sawamura, T.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 5
    • 29144450008 scopus 로고    scopus 로고
    • How is the immune response affected by hyperthermia and heat shock proteins?
    • Calderwood, S. K., J. R. Theriault, and J. Gong. 2005. How is the immune response affected by hyperthermia and heat shock proteins? Int. J. Hyperthermia 21: 713-716.
    • (2005) Int. J. Hyperthermia , vol.21 , pp. 713-716
    • Calderwood, S.K.1    Theriault, J.R.2    Gong, J.3
  • 6
    • 0036830232 scopus 로고    scopus 로고
    • Tumor cell membrane-bound heat shock protein 70 elicits antitumor immunity
    • Chen, X., Q. Tao, H. Yu, L. Zhang, and X. Cao. 2002. Tumor cell membrane-bound heat shock protein 70 elicits antitumor immunity. Immunol. Lett. 84: 81-87.
    • (2002) Immunol. Lett. , vol.84 , pp. 81-87
    • Chen, X.1    Tao, Q.2    Yu, H.3    Zhang, L.4    Cao, X.5
  • 9
    • 0037290769 scopus 로고    scopus 로고
    • ISO: A critical evaluation of the role of peptides in heat shock/chaperone protein-mediated tumor rejection
    • Baker-LePain, J. C., R. C. Reed, and C. V. Nicchitta. 2003. ISO: a critical evaluation of the role of peptides in heat shock/chaperone protein-mediated tumor rejection. Curr. Opin. Immunol. 15: 89-94.
    • (2003) Curr. Opin. Immunol. , vol.15 , pp. 89-94
    • Baker-LePain, J.C.1    Reed, R.C.2    Nicchitta, C.V.3
  • 10
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway
    • Basu, S., R. J. Binder, R. Suto, K. M. Anderson, and P. K. Srivastava. 2000. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway. Int. Immunol. 12: 1539-1546.
    • (2000) Int. Immunol. , vol.12 , pp. 1539-1546
    • Basu, S.1    Binder, R.J.2    Suto, R.3    Anderson, K.M.4    Srivastava, P.K.5
  • 11
    • 12344292277 scopus 로고    scopus 로고
    • Chaperones and slow death: A recipe for tumor immunotherapy
    • Calderwood, S. K. 2005. Chaperones and slow death: a recipe for tumor immunotherapy. Trends Biotechnol. 23: 57-59.
    • (2005) Trends Biotechnol. , vol.23 , pp. 57-59
    • Calderwood, S.K.1
  • 12
    • 0032923377 scopus 로고    scopus 로고
    • The secretory route of the leaderless protein interleukin 1β involves exocytosis of endolysosome-related vesicles
    • Andrei, C., C. Dazzi, L. Lotti, M. R. Torrisi, G. Chimini, and A. Rubartelli. 1999. The secretory route of the leaderless protein interleukin 1β involves exocytosis of endolysosome-related vesicles. Mol. Biol. Cell 10: 1463-1475.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1463-1475
    • Andrei, C.1    Dazzi, C.2    Lotti, L.3    Torrisi, M.R.4    Chimini, G.5    Rubartelli, A.6
  • 13
    • 0033783352 scopus 로고    scopus 로고
    • Fibroblast growth factors, their receptors and signaling
    • Powers, C. J., S. W. McLeskey, and A. Wellstein. 2000. Fibroblast growth factors, their receptors and signaling. Endocr. Relat. Cancer 7: 165-197.
    • (2000) Endocr. Relat. Cancer , vol.7 , pp. 165-197
    • Powers, C.J.1    McLeskey, S.W.2    Wellstein, A.3
  • 16
    • 0024541931 scopus 로고
    • Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins
    • Hightower, L. E., and P. T. Guidon, Jr. 1989. Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins. J. Cell Physiol. 138: 257-266.
    • (1989) J. Cell Physiol. , vol.138 , pp. 257-266
    • Hightower, L.E.1    Guidon Jr., P.T.2
  • 17
    • 0030612880 scopus 로고    scopus 로고
    • Interleukin-1β secretion is impaired by inhibitors of the Atp binding cassette transporter, ABC1
    • Hamon, Y., M. F. Luciani, F. Becq, B. Verrier, A. Rubartelli, and G. Chimini. 1997. Interleukin-1β secretion is impaired by inhibitors of the Atp binding cassette transporter, ABC1. Blood 90: 2911-2915.
    • (1997) Blood , vol.90 , pp. 2911-2915
    • Hamon, Y.1    Luciani, M.F.2    Becq, F.3    Verrier, B.4    Rubartelli, A.5    Chimini, G.6
  • 20
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. 1992. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8: 67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 21
    • 14844354847 scopus 로고    scopus 로고
    • ATP binding cassette transporter ABC1 is required for the release of interleukin-1β by P2X7-stimulated and lipopolysaccharide-primed mouse Schwann cells
    • Marty, V., C. Medina, C. Combe, P. Parnet, and T. Amedee. 2005. ATP binding cassette transporter ABC1 is required for the release of interleukin-1β by P2X7-stimulated and lipopolysaccharide-primed mouse Schwann cells. Glia 49: 511-519.
    • (2005) Glia , vol.49 , pp. 511-519
    • Marty, V.1    Medina, C.2    Combe, C.3    Parnet, P.4    Amedee, T.5
  • 23
    • 0037131427 scopus 로고    scopus 로고
    • Toll-like receptor (TLR) signaling in response to Aspergillus fumigatus
    • Mambula, S. S., K. Sau, P. Henneke, D. T. Golenbock, and S. M. Levitz. 2002. Toll-like receptor (TLR) signaling in response to Aspergillus fumigatus. J. Biol. Chem. 277: 39320-39326.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39320-39326
    • Mambula, S.S.1    Sau, K.2    Henneke, P.3    Golenbock, D.T.4    Levitz, S.M.5
  • 24
    • 15944373162 scopus 로고    scopus 로고
    • Expression of heat shock proteins and heat shock protein messenger ribonucleic acid in human prostate carcinoma in vitro and in tumors in vivo
    • Tang, D., M. A. Khaleque, E. L. Jones, J. R. Theriault, C. Li, W. H. Wong, M. A. Stevenson, and S. K. Calderwood. 2005. Expression of heat shock proteins and heat shock protein messenger ribonucleic acid in human prostate carcinoma in vitro and in tumors in vivo. Cell Stress Chaperones 10: 46-58.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 46-58
    • Tang, D.1    Khaleque, M.A.2    Jones, E.L.3    Theriault, J.R.4    Li, C.5    Wong, W.H.6    Stevenson, M.A.7    Calderwood, S.K.8
  • 26
    • 0031684172 scopus 로고    scopus 로고
    • Tumor cell apoptosis, lymphocyte recruitment and tumor vascular changes are induced by low temperature, long duration (fever-like) whole body hyperthermia
    • Burd, R., T. S. Dziedzic, Y. Xu, M. A. Caligiuri, J. R. Subjeck, and E. A. Repasky. 1998. Tumor cell apoptosis, lymphocyte recruitment and tumor vascular changes are induced by low temperature, long duration (fever-like) whole body hyperthermia. J. Cell. Physiol. 177: 137-147.
    • (1998) J. Cell. Physiol. , vol.177 , pp. 137-147
    • Burd, R.1    Dziedzic, T.S.2    Xu, Y.3    Caligiuri, M.A.4    Subjeck, J.R.5    Repasky, E.A.6
  • 27
    • 0034522082 scopus 로고    scopus 로고
    • Regulation of immune activity by mild (fever-range) whole body hyperthermia: Effects on epidermal Langerhans cells
    • Ostberg, J. R., R. Patel, and E. A. Repasky. 2000. Regulation of immune activity by mild (fever-range) whole body hyperthermia: effects on epidermal Langerhans cells. Cell Stress Chaperones 5: 458-461.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 458-461
    • Ostberg, J.R.1    Patel, R.2    Repasky, E.A.3
  • 28
    • 0020451771 scopus 로고
    • Thermotolerance and heat shock proteins in mammalian cells
    • Hahn, G. M., and G. C. Li. 1982. Thermotolerance and heat shock proteins in mammalian cells. Radiat. Res. 92: 452-457.
    • (1982) Radiat. Res. , vol.92 , pp. 452-457
    • Hahn, G.M.1    Li, G.C.2
  • 29
    • 9744260942 scopus 로고    scopus 로고
    • The 70 kilodalton heat shock protein is an inhibitor of apoptosis in prostate cancer
    • Jones, E. L., M. J. Zhao, M. A. Stevenson, and S. K. Calderwood. 2004. The 70 kilodalton heat shock protein is an inhibitor of apoptosis in prostate cancer. Int. J. Hyperthermia 20: 835-849.
    • (2004) Int. J. Hyperthermia , vol.20 , pp. 835-849
    • Jones, E.L.1    Zhao, M.J.2    Stevenson, M.A.3    Calderwood, S.K.4
  • 30
    • 33750567138 scopus 로고    scopus 로고
    • Heat induced HSP70 release from prostate carcinoma cells involves both active secretion and passive release from necrotic cells
    • In press
    • Mambula, S. S. a. S. K. C. 2006. Heat induced HSP70 release from prostate carcinoma cells involves both active secretion and passive release from necrotic cells. Int. J. Hyperthermia. In press.
    • (2006) Int. J. Hyperthermia
    • Mambula, S.S.1
  • 31
    • 0031470026 scopus 로고    scopus 로고
    • Heat shock and proinflammatory stressors induce differential localization of heat shock proteins in human monocytes
    • Mariethoz, E., M. R. Jacquier-Sarlin, G. Multhoff, A. M. Healy, F. Tacchini-Cottier, and B. S. Polla. 1997. Heat shock and proinflammatory stressors induce differential localization of heat shock proteins in human monocytes. Inflammation 21: 629-642.
    • (1997) Inflammation , vol.21 , pp. 629-642
    • Mariethoz, E.1    Jacquier-Sarlin, M.R.2    Multhoff, G.3    Healy, A.M.4    Tacchini-Cottier, F.5    Polla, B.S.6
  • 33
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • Arai, M., and K. Kuwajima. 2000. Role of the molten globule state in protein folding. Adv. Protein Chem. 53: 209-282.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 209-282
    • Arai, M.1    Kuwajima, K.2
  • 34
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. 1995. Molten globule and protein folding. Adv. Protein Chem. 47: 83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 35
    • 3042800587 scopus 로고    scopus 로고
    • Phospholipases C and A2 control lysosome-mediated IL-1β secretion: Implications for inflammatory processes
    • Andrei, C., P. Margiocco, A. Poggi, L. V. Lotti, M. R. Torrisi, and A. Rubartelli. 2004. Phospholipases C and A2 control lysosome-mediated IL-1β secretion: implications for inflammatory processes. Proc. Natl. Acad. Sci. USA 101: 9745-9750.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9745-9750
    • Andrei, C.1    Margiocco, P.2    Poggi, A.3    Lotti, L.V.4    Torrisi, M.R.5    Rubartelli, A.6
  • 36
    • 0036775236 scopus 로고    scopus 로고
    • The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway
    • Gardella, S., C. Andrei, D. Ferrera, L. V. Lotti, M. R. Torrisi, M. E. Bianchi, and A. Rubartelli. 2002. The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway. EMBO Rep. 3: 995-1001.
    • (2002) EMBO Rep. , vol.3 , pp. 995-1001
    • Gardella, S.1    Andrei, C.2    Ferrera, D.3    Lotti, L.V.4    Torrisi, M.R.5    Bianchi, M.E.6    Rubartelli, A.7
  • 37
    • 0032813156 scopus 로고    scopus 로고
    • A short region of its homeodomain is necessary for engrailed nuclear export and secretion
    • Maizel, A., O. Bensaude, A. Prochiantz, and A. Joliot. 1999. A short region of its homeodomain is necessary for engrailed nuclear export and secretion. Development 126: 3183-3190.
    • (1999) Development , vol.126 , pp. 3183-3190
    • Maizel, A.1    Bensaude, O.2    Prochiantz, A.3    Joliot, A.4
  • 38
    • 0037821650 scopus 로고    scopus 로고
    • Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2
    • Peterson, E. A., M. R. Sutherland, M. E. Nesheim, and E. L. Pryzdial. 2003. Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2. J. Cell Sci. 116: 2399-2408.
    • (2003) J. Cell Sci. , vol.116 , pp. 2399-2408
    • Peterson, E.A.1    Sutherland, M.R.2    Nesheim, M.E.3    Pryzdial, E.L.4
  • 39
    • 0036819191 scopus 로고    scopus 로고
    • Lipid interaction differentiates the constitutive and stress-induced heat shock proteins Hsc70 and Hsp70
    • Arispe, N., M. Doh, and A. De Maio. 2002. Lipid interaction differentiates the constitutive and stress-induced heat shock proteins Hsc70 and Hsp70. Cell Stress Chaperones 7: 330-338.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 330-338
    • Arispe, N.1    Doh, M.2    De Maio, A.3
  • 40
    • 0029912569 scopus 로고    scopus 로고
    • Lysosomal exocytosis induced by hyperthermia: A new model of cancer death III: Effect on liver metastasis
    • Barni, S., V. Bertone, M. G. Silvotti, I. Freitas, G. Mathe, and P. Pontiggia. 1996. Lysosomal exocytosis induced by hyperthermia: a new model of cancer death III: effect on liver metastasis. Biomed. Pharmacother. 50: 79-84.
    • (1996) Biomed. Pharmacother. , vol.50 , pp. 79-84
    • Barni, S.1    Bertone, V.2    Silvotti, M.G.3    Freitas, I.4    Mathe, G.5    Pontiggia, P.6
  • 41
    • 0028860524 scopus 로고
    • Lysosomal exocytosis induced by hyperthermia: A new model of cancer cell death II: Effect on peritoneal macrophages
    • Pontiggia, P., S. Bami, G. Mathe, V. Bertone, and E. Pontiggia. 1995. Lysosomal exocytosis induced by hyperthermia: a new model of cancer cell death II: effect on peritoneal macrophages. Biomed. Pharmacother. 49: 429-430.
    • (1995) Biomed. Pharmacother. , vol.49 , pp. 429-430
    • Pontiggia, P.1    Bami, S.2    Mathe, G.3    Bertone, V.4    Pontiggia, E.5
  • 42
    • 2942551229 scopus 로고    scopus 로고
    • Phospholipse c inhibitor, u73122, stimulates release of hsp-70 stress protein from A431 human carcinoma cells
    • Evdonin, A. L., I. V. Guzhova, B. A. Margulis, and N. D. Medvedeva. 2004. Phospholipse c inhibitor, u73122, stimulates release of hsp-70 stress protein from A431 human carcinoma cells. Cancer Cell Int. 4: 2.
    • (2004) Cancer Cell Int. , vol.4 , pp. 2
    • Evdonin, A.L.1    Guzhova, I.V.2    Margulis, B.A.3    Medvedeva, N.D.4
  • 43
    • 3042626249 scopus 로고    scopus 로고
    • Selective tyrosine hyperphosphorylation of cytoskeletal and stress proteins in primary human breast cancers: Implications for adjuvant use of kinase-inhibitory drugs
    • Lim, Y. P., C. Y. Wong, L. L. Ooi, B. J. Druker, and R. J. Epstein. 2004. Selective tyrosine hyperphosphorylation of cytoskeletal and stress proteins in primary human breast cancers: implications for adjuvant use of kinase-inhibitory drugs. Clin. Cancer Res. 10: 3980-3987.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 3980-3987
    • Lim, Y.P.1    Wong, C.Y.2    Ooi, L.L.3    Druker, B.J.4    Epstein, R.J.5
  • 45
    • 0040597130 scopus 로고    scopus 로고
    • Constitutive phosphorylation of the acidic tails of the high mobility group 1 proteins by casein kinase II alters their conformation, stability, and DNA binding specificity
    • Wisniewski, J. R., Z. Szewczuk, I. Petry, R. Schwanbeck, and U. Renner. 1999. Constitutive phosphorylation of the acidic tails of the high mobility group 1 proteins by casein kinase II alters their conformation, stability, and DNA binding specificity. J. Biol. Chem. 274: 20116-20122.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20116-20122
    • Wisniewski, J.R.1    Szewczuk, Z.2    Petry, I.3    Schwanbeck, R.4    Renner, U.5
  • 46
    • 23344453615 scopus 로고    scopus 로고
    • Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues
    • Tytell, M. 2005. Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues. Int. J. Hyperthermia 21: 445-455.
    • (2005) Int. J. Hyperthermia , vol.21 , pp. 445-455
    • Tytell, M.1
  • 47
    • 20744436655 scopus 로고    scopus 로고
    • Exosome-dependent trafficking of HSP70: A novel secretory pathway for cellular stress proteins
    • Lancaster, G. I., and M. A. Febbraio. 2005. Exosome-dependent trafficking of HSP70: a novel secretory pathway for cellular stress proteins. J. Biol. Chem. 280: 23349-23355.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23349-23355
    • Lancaster, G.I.1    Febbraio, M.A.2
  • 48
    • 20444431560 scopus 로고    scopus 로고
    • Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells
    • Gastpar, R., M. Gehrmann, M. A. Bausero, A. Asea, C. Gross, J. A. Schroeder, and G. Multhoff. 2005. Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells. Cancer Res. 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    Multhoff, G.7
  • 51
    • 26044433779 scopus 로고    scopus 로고
    • Message in a bottle: Role of the 70-kDa heat shock protein family in anti-tumor immunity
    • Calderwood, S. K., J. R. Theriault, and J. Gong. 2005. Message in a bottle: role of the 70-kDa heat shock protein family in anti-tumor immunity. Eur. J. Immunol. 35: 2518-2527.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 2518-2527
    • Calderwood, S.K.1    Theriault, J.R.2    Gong, J.3
  • 52
    • 0036865303 scopus 로고    scopus 로고
    • Activation of natural killer cells by heat shock protein 70
    • Multhoff, G. 2002. Activation of natural killer cells by heat shock protein 70. Int. J. Hyperthermia 18: 576-585.
    • (2002) Int. J. Hyperthermia , vol.18 , pp. 576-585
    • Multhoff, G.1
  • 54
    • 0033968608 scopus 로고    scopus 로고
    • Comparison of the effects of two different whole body hyperthermia protocols on the distribution of murine leukocyte populations
    • Ostberg, J. R., and E. A. Repasky. 2000. Comparison of the effects of two different whole body hyperthermia protocols on the distribution of murine leukocyte populations. Int. J. Hyperthermia 16: 29-43.
    • (2000) Int. J. Hyperthermia , vol.16 , pp. 29-43
    • Ostberg, J.R.1    Repasky, E.A.2


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