메뉴 건너뛰기




Volumn 6, Issue 1, 2014, Pages 42-66

The complex function of Hsp70 in metastatic cancer

Author keywords

Hsp70; Invasion; Lysosome; Metastasis; Trafficking

Indexed keywords

CANCER VACCINE; HEAT SHOCK PROTEIN 70; HSP70 PC F VACCINE; UNCLASSIFIED DRUG;

EID: 84891330477     PISSN: None     EISSN: 20726694     Source Type: Journal    
DOI: 10.3390/cancers6010042     Document Type: Review
Times cited : (78)

References (197)
  • 2
    • 0027522356 scopus 로고
    • Cells in stress: Transcriptional activation of heat shock genes
    • Morimoto, R.I. Cells in stress: Transcriptional activation of heat shock genes. Science 1993, 259, 1409-1410.
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, R.I.1
  • 3
    • 0027159874 scopus 로고
    • MAP kinase activation during heat shock in quiescent and exponentially growing mammalian cells
    • Dubois, M.F.; Bensaude, O. MAP kinase activation during heat shock in quiescent and exponentially growing mammalian cells. FEBS Lett. 1993, 324, 191-195.
    • (1993) FEBS Lett. , vol.324 , pp. 191-195
    • Dubois, M.F.1    Bensaude, O.2
  • 4
    • 0028881770 scopus 로고
    • UV irradiation and heat shock mediate JNK activation via alternate pathways
    • Adler, V.; Schaffer, A.; Kim, J.; Dolan, L.; Ronai, Z. UV irradiation and heat shock mediate JNK activation via alternate pathways. J. Biol. Chem. 1995, 270, 26071-26077.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26071-26077
    • Adler, V.1    Schaffer, A.2    Kim, J.3    Dolan, L.4    Ronai, Z.5
  • 5
    • 15044351289 scopus 로고    scopus 로고
    • Molecular chaperones as regulatory elements of cellular networks
    • Soti, C.; Pál, C.; Papp, B.; Csermely, P. Molecular chaperones as regulatory elements of cellular networks. Curr. Opin. Cell Biol. 2005, 17, 210-215.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 210-215
    • Soti, C.1    Pál, C.2    Papp, B.3    Csermely, P.4
  • 6
    • 0037217892 scopus 로고    scopus 로고
    • Regulation of cancer metastasis by stress pathways
    • Xie, K.; Huang, S. Regulation of cancer metastasis by stress pathways. Clin. Exp. Metastasis 2003, 20, 31-43.
    • (2003) Clin. Exp. Metastasis , vol.20 , pp. 31-43
    • Xie, K.1    Huang, S.2
  • 7
    • 0030750217 scopus 로고    scopus 로고
    • Expression of heat shock protein 72 in renal cell carcinoma: Possible role and prognostic implications in cancer patients
    • Santarosa, M.; Favaro, D.; Quaia, M.; Galligioni, E. Expression of heat shock protein 72 in renal cell carcinoma: Possible role and prognostic implications in cancer patients. Eur. J. Cancer 1997, 33, 873-877.
    • (1997) Eur. J. Cancer , vol.33 , pp. 873-877
    • Santarosa, M.1    Favaro, D.2    Quaia, M.3    Galligioni, E.4
  • 9
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • Mosser, D.D.; Morimoto, R.I. Molecular chaperones and the stress of oncogenesis. Oncogene 2004, 23, 2907-2918.
    • (2004) Oncogene , vol.23 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 10
    • 67649217159 scopus 로고    scopus 로고
    • Inhibiting the transcription factor HSF1 as an anticancer strategy
    • Whitesell, L.; Lindquist, S. Inhibiting the transcription factor HSF1 as an anticancer strategy. Expert Opin. Ther. Targets 2009, 13, 469-478.
    • (2009) Expert Opin. Ther. Targets , vol.13 , pp. 469-478
    • Whitesell, L.1    Lindquist, S.2
  • 11
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: Biology and pharmacology
    • Powers, M.V.; Workman, P. Inhibitors of the heat shock response: Biology and pharmacology. FEBS Lett. 2007, 581, 3758-3769.
    • (2007) FEBS Lett. , vol.581 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 12
    • 33947530122 scopus 로고    scopus 로고
    • De-repression of heat shock transcription factor-1 in interleukin-6-treated hepatocytes is mediated by downregulation of glycogen synthase kinase 3beta and MAPK/ERK-1
    • Wigmore, S.J.; Sangster, K.; McNally, S.J.; Harrison, E.M.; Ross, J.A.; Fearon, K.C.H.; Garden, O.J. De-repression of heat shock transcription factor-1 in interleukin-6-treated hepatocytes is mediated by downregulation of glycogen synthase kinase 3beta and MAPK/ERK-1. Int. J. Mol. Med. 2007, 19, 413-420.
    • (2007) Int. J. Mol. Med. , vol.19 , pp. 413-420
    • Wigmore, S.J.1    Sangster, K.2    McNally, S.J.3    Harrison, E.M.4    Ross, J.A.5    Fearon, K.C.H.6    Garden, O.J.7
  • 13
    • 0034608892 scopus 로고    scopus 로고
    • Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
    • Nylandsted, J.; Rohde, M.; Brand, K.; Bastholm, L.; Elling, F.; Jäättelä, M. Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2. Proc. Natl. Acad. Sci. USA 2000, 97, 7871-7876.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3    Bastholm, L.4    Elling, F.5    Jäättelä, M.6
  • 14
    • 0028919063 scopus 로고
    • Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells
    • Wei, Y.Q.; Zhao, X.; Kariya, Y.; Teshigawara, K.; Uchida, A. Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells. Cancer Immunol. Immunother. 1995, 40, 73-78.
    • (1995) Cancer Immunol. Immunother. , vol.40 , pp. 73-78
    • Wei, Y.Q.1    Zhao, X.2    Kariya, Y.3    Teshigawara, K.4    Uchida, A.5
  • 15
    • 0033991539 scopus 로고    scopus 로고
    • Induction of apoptosis by abrogation of HSP70 expression in human oral cancer cells
    • Kaur, J.; Kaur, J.; Ralhan, R. Induction of apoptosis by abrogation of HSP70 expression in human oral cancer cells. Int. J. Cancer J. Int. Cancer 2000, 85, 1-5.
    • (2000) Int. J. Cancer J. Int. Cancer , vol.85 , pp. 1-5
    • Kaur, J.1    Kaur, J.2    Ralhan, R.3
  • 16
    • 0028961801 scopus 로고
    • Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells
    • Jäättelä, M. Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells. Int. J. Cancer 1995, 60, 689-693.
    • (1995) Int. J. Cancer , vol.60 , pp. 689-693
    • Jäättelä, M.1
  • 18
    • 0033578065 scopus 로고    scopus 로고
    • Oncogenic potential of Hsp72
    • Volloch, V.Z.; Sherman, M.Y. Oncogenic potential of Hsp72. Oncogene 1999, 18, 3648-3651.
    • (1999) Oncogene , vol.18 , pp. 3648-3651
    • Volloch, V.Z.1    Sherman, M.Y.2
  • 20
    • 0028970484 scopus 로고
    • Differential expression of Mr 70,000 heat shock protein in normal, premalignant, and malignant human uterine cervix
    • Ralhan, R.; Kaur, J. Differential expression of Mr 70,000 heat shock protein in normal, premalignant, and malignant human uterine cervix. Clin. Cancer Res. 1995, 1, 1217-1222.
    • (1995) Clin. Cancer Res. , vol.1 , pp. 1217-1222
    • Ralhan, R.1    Kaur, J.2
  • 21
    • 0029114617 scopus 로고
    • Immunohistochemical expression of C-myc oncogene, heat shock protein 70 and HLA-DR molecules in malignant cutaneous melanoma
    • Lazaris, A.C.; Theodoropoulos, G.E.; Aroni, K.; Saetta, A.; Davaris, P.S. Immunohistochemical expression of C-myc oncogene, heat shock protein 70 and HLA-DR molecules in malignant cutaneous melanoma. Virchows Arch. Int. J. Pathol. 1995, 426, 461-467.
    • (1995) Virchows Arch. Int. J. Pathol. , vol.426 , pp. 461-467
    • Lazaris, A.C.1    Theodoropoulos, G.E.2    Aroni, K.3    Saetta, A.4    Davaris, P.S.5
  • 22
    • 0031763046 scopus 로고    scopus 로고
    • Expression of 70-kDa heat shock protein in oral lesions: Marker of biological stress or pathogenicity
    • Kaur, J.; Srivastava, A.; Ralhan, R. Expression of 70-kDa heat shock protein in oral lesions: Marker of biological stress or pathogenicity. Oral Oncol. 1998, 34, 496-501.
    • (1998) Oral Oncol. , vol.34 , pp. 496-501
    • Kaur, J.1    Srivastava, A.2    Ralhan, R.3
  • 24
    • 3442878404 scopus 로고    scopus 로고
    • Plasma levels of heat shock protein 70 in patients with prostate cancer: A potential biomarker for prostate cancer
    • Abe, M.; Manola, J.B.; Oh, W.K.; Parslow, D.L.; George, D.J.; Austin, C.L.; Kantoff, P.W. Plasma levels of heat shock protein 70 in patients with prostate cancer: A potential biomarker for prostate cancer. Clin. Prostate Cancer 2004, 3, 49-53.
    • (2004) Clin. Prostate Cancer , vol.3 , pp. 49-53
    • Abe, M.1    Manola, J.B.2    Oh, W.K.3    Parslow, D.L.4    George, D.J.5    Austin, C.L.6    Kantoff, P.W.7
  • 25
    • 0037223571 scopus 로고    scopus 로고
    • Expression profiling in multistage hepatocarcinogenesis: Identification of HSP70 as a molecular marker of early hepatocellular carcinoma
    • Chuma, M.; Sakamoto, M.; Yamazaki, K.; Ohta, T.; Ohki, M.; Asaka, M.; Hirohashi, S. Expression profiling in multistage hepatocarcinogenesis: Identification of HSP70 as a molecular marker of early hepatocellular carcinoma. Hepatology 2003, 37, 198-207.
    • (2003) Hepatology , vol.37 , pp. 198-207
    • Chuma, M.1    Sakamoto, M.2    Yamazaki, K.3    Ohta, T.4    Ohki, M.5    Asaka, M.6    Hirohashi, S.7
  • 26
    • 0027503365 scopus 로고
    • Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: Prognostic implications
    • Ciocca, D.R.; Clark, G.M.; Tandon, A.K.; Fuqua, S.A.; Welch, W.J.; McGuire, W.L. Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: Prognostic implications. J. Natl. Cancer Inst. 1993, 85, 570-574.
    • (1993) J. Natl. Cancer Inst. , vol.85 , pp. 570-574
    • Ciocca, D.R.1    Clark, G.M.2    Tandon, A.K.3    Fuqua, S.A.4    Welch, W.J.5    McGuire, W.L.6
  • 28
    • 22144458740 scopus 로고    scopus 로고
    • Expression of heat-shock proteins is associated with major adverse prognostic factors in acute myeloid leukemia
    • Thomas, X.; Campos, L.; Mounier, C.; Cornillon, J.; Flandrin, P.; Le, Q.-H.; Piselli, S.; Guyotat, D. Expression of heat-shock proteins is associated with major adverse prognostic factors in acute myeloid leukemia. Leuk. Res. 2005, 29, 1049-1058.
    • (2005) Leuk. Res. , vol.29 , pp. 1049-1058
    • Thomas, X.1    Campos, L.2    Mounier, C.3    Cornillon, J.4    Flandrin, P.5    Le, Q.-H.6    Piselli, S.7    Guyotat, D.8
  • 29
    • 0031472407 scopus 로고    scopus 로고
    • Heat shock protein 72/73 in relation to cytoplasmic p53 expression and prognosis in colorectal adenocarcinomas
    • Sun, X.F.; Zhang, H.; Carstensen, J.; Jansson, A.; Nordenskjöld, B. Heat shock protein 72/73 in relation to cytoplasmic p53 expression and prognosis in colorectal adenocarcinomas. Int. J. Cancer 1997, 74, 600-604.
    • (1997) Int. J. Cancer , vol.74 , pp. 600-604
    • Sun, X.F.1    Zhang, H.2    Carstensen, J.3    Jansson, A.4    Nordenskjöld, B.5
  • 30
    • 0033560745 scopus 로고    scopus 로고
    • Prognostic significance of heat shock proteins 27 and 70 in patients with squamous cell carcinoma of the esophagus
    • Kawanishi, K.; Shiozaki, H.; Doki, Y.; Sakita, I.; Inoue, M.; Yano, M.; Tsujinaka, T.; Shamma, A.; Monden, M. Prognostic significance of heat shock proteins 27 and 70 in patients with squamous cell carcinoma of the esophagus. Cancer 1999, 85, 1649-1657.
    • (1999) Cancer , vol.85 , pp. 1649-1657
    • Kawanishi, K.1    Shiozaki, H.2    Doki, Y.3    Sakita, I.4    Inoue, M.5    Yano, M.6    Tsujinaka, T.7    Shamma, A.8    Monden, M.9
  • 31
    • 0034058193 scopus 로고    scopus 로고
    • Clinical application of malignancy potential grading as a prognostic factor of human esophageal cancers
    • Shiozaki, H.; Doki, Y.; Kawanishi, K.; Shamma, A.; Yano, M.; Inoue, M.; Monden, M. Clinical application of malignancy potential grading as a prognostic factor of human esophageal cancers. Surgery 2000, 127, 552-561.
    • (2000) Surgery , vol.127 , pp. 552-561
    • Shiozaki, H.1    Doki, Y.2    Kawanishi, K.3    Shamma, A.4    Yano, M.5    Inoue, M.6    Monden, M.7
  • 32
    • 0033994048 scopus 로고    scopus 로고
    • Overexpression of the heat shock protein HSP70 family and p53 protein and prognosis for patients with gastric cancer
    • Maehara, Y.; Oki, E.; Abe, T.; Tokunaga, E.; Shibahara, K.; Kakeji, Y.; Sugimachi, K. Overexpression of the heat shock protein HSP70 family and p53 protein and prognosis for patients with gastric cancer. Oncology 2000, 58, 144-151.
    • (2000) Oncology , vol.58 , pp. 144-151
    • Maehara, Y.1    Oki, E.2    Abe, T.3    Tokunaga, E.4    Shibahara, K.5    Kakeji, Y.6    Sugimachi, K.7
  • 33
    • 67650021933 scopus 로고    scopus 로고
    • Tumor immune systems in esophageal cancer with special reference to heat-shock protein 70 and humoral immunity
    • Nakajima, M.; Kato, H.; Miyazaki, T.; Fukuchi, M.; Masuda, N.; Fukai, Y.; Sohda, M.; Ahmad, F.; Kuwano, H. Tumor immune systems in esophageal cancer with special reference to heat-shock protein 70 and humoral immunity. Anticancer Res. 2009, 29, 1595-1606.
    • (2009) Anticancer Res. , vol.29 , pp. 1595-1606
    • Nakajima, M.1    Kato, H.2    Miyazaki, T.3    Fukuchi, M.4    Masuda, N.5    Fukai, Y.6    Sohda, M.7    Ahmad, F.8    Kuwano, H.9
  • 34
    • 0031692853 scopus 로고    scopus 로고
    • Heat shock protein 72 expression in osteosarcomas correlates with good response to neoadjuvant chemotherapy
    • Trieb, K.; Lechleitner, T.; Lang, S.; Windhager, R.; Kotz, R.; Dirnhofer, S. Heat shock protein 72 expression in osteosarcomas correlates with good response to neoadjuvant chemotherapy. Hum. Pathol. 1998, 29, 1050-1055.
    • (1998) Hum. Pathol. , vol.29 , pp. 1050-1055
    • Trieb, K.1    Lechleitner, T.2    Lang, S.3    Windhager, R.4    Kotz, R.5    Dirnhofer, S.6
  • 35
    • 0028953056 scopus 로고
    • A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells
    • Multhoff, G.; Botzler, C.; Wiesnet, M.; Müller, E.; Meier, T.; Wilmanns, W.; Issels, R.D. A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells. Int. J. Cancer 1995, 61, 272-279.
    • (1995) Int. J. Cancer , vol.61 , pp. 272-279
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3    Müller, E.4    Meier, T.5    Wilmanns, W.6    Issels, R.D.7
  • 36
    • 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
  • 37
    • 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.; Multhoff, G. 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    Multhoff, G.7
  • 38
    • 13444271569 scopus 로고    scopus 로고
    • Photodynamic therapy-induced cell surface expression and release of heat shock proteins: Relevance for tumor response
    • Korbelik, M.; Sun, J.; Cecic, I. Photodynamic therapy-induced cell surface expression and release of heat shock proteins: Relevance for tumor response. Cancer Res. 2005, 65, 1018-1026.
    • (2005) Cancer Res. , vol.65 , pp. 1018-1026
    • Korbelik, M.1    Sun, J.2    Cecic, I.3
  • 39
    • 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.; Kraeft, S.K.; Kurt-Jones, E.A.; Stevenson, M.A.; Chen, L.B.; Finberg, R.W.; Koo, G.C.; Calderwood, S.K. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 2000, 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
  • 40
    • 77956825499 scopus 로고    scopus 로고
    • Germ cell-specific heat shock protein 70-2 is expressed in cervical carcinoma and is involved in the growth, migration, and invasion of cervical cells
    • Garg, M.; Kanojia, D.; Saini, S.; Suri, S.; Gupta, A.; Surolia, A.; Suri, A. Germ cell-specific heat shock protein 70-2 is expressed in cervical carcinoma and is involved in the growth, migration, and invasion of cervical cells. Cancer 2010, 116, 3785-3796.
    • (2010) Cancer , vol.116 , pp. 3785-3796
    • Garg, M.1    Kanojia, D.2    Saini, S.3    Suri, S.4    Gupta, A.5    Surolia, A.6    Suri, A.7
  • 41
    • 79960415006 scopus 로고    scopus 로고
    • Overexpression of HSP70 inhibits cofilin phosphorylation and promotes lymphocyte migration in heat-stressed cells
    • Simard, J.P.; Reynolds, D.N.; Kraguljac, A.P.; Smith, G.S.T.; Mosser, D.D. Overexpression of HSP70 inhibits cofilin phosphorylation and promotes lymphocyte migration in heat-stressed cells. J. Cell Sci. 2011, 124, 2367-2374.
    • (2011) J. Cell Sci. , vol.124 , pp. 2367-2374
    • Simard, J.P.1    Reynolds, D.N.2    Kraguljac, A.P.3    Smith, G.S.T.4    Mosser, D.D.5
  • 43
    • 21344437943 scopus 로고    scopus 로고
    • Using a Xenograft Model of Human Breast Cancer Metastasis to Find Genes Associated with Clinically Aggressive Disease
    • Kluger, H.M.; Lev, D.C.; Kluger, Y.; McCarthy, M.M.; Kiriakova, G.; Camp, R.L.; Rimm, D.L.; Price, J.E. Using a Xenograft Model of Human Breast Cancer Metastasis to Find Genes Associated with Clinically Aggressive Disease. Cancer Res. 2005, 65, 5578-5587.
    • (2005) Cancer Res. , vol.65 , pp. 5578-5587
    • Kluger, H.M.1    Lev, D.C.2    Kluger, Y.3    McCarthy, M.M.4    Kiriakova, G.5    Camp, R.L.6    Rimm, D.L.7    Price, J.E.8
  • 45
    • 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
  • 47
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • Rohde, M.; Daugaard, M.; Jensen, M.H.; Helin, K.; Nylandsted, J.; Jäättelä, M. Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev. 2005, 19, 570-582.
    • (2005) Genes Dev. , vol.19 , pp. 570-582
    • Rohde, M.1    Daugaard, M.2    Jensen, M.H.3    Helin, K.4    Nylandsted, J.5    Jäättelä, M.6
  • 48
    • 18844378888 scopus 로고    scopus 로고
    • Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents
    • Gabai, V.L.; Budagova, K.R.; Sherman, M.Y. Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents. Oncogene 2005, 24, 3328-3338.
    • (2005) Oncogene , vol.24 , pp. 3328-3338
    • Gabai, V.L.1    Budagova, K.R.2    Sherman, M.Y.3
  • 49
    • 34248219927 scopus 로고    scopus 로고
    • Correlation between clinicopathology and expression of heat shock protein 72 and glycoprotein 96 in human gastric adenocarcinoma
    • Wang, X.-P.; Wang, Q.-X.; Ying, X.-P. Correlation between clinicopathology and expression of heat shock protein 72 and glycoprotein 96 in human gastric adenocarcinoma. Tohoku J. Exp. Med. 2007, 212, 35-41.
    • (2007) Tohoku J. Exp. Med. , vol.212 , pp. 35-41
    • Wang, X.-P.1    Wang, Q.-X.2    Ying, X.-P.3
  • 50
    • 84899668980 scopus 로고    scopus 로고
    • Molecular Cochaperones: Tumor Growth and Cancer Treatment
    • Calderwood, S.K. Molecular Cochaperones: Tumor Growth and Cancer Treatment. Scientifica 2013, 2013, 1-13.
    • (2013) Scientifica , vol.2013 , pp. 1-13
    • Calderwood, S.K.1
  • 51
    • 0037255754 scopus 로고    scopus 로고
    • CYP1a1, HSP70, P53, and c-fos expression in human liver carcinoma cells (HepG2) exposed to pentachlorophenol
    • Dorsey, W.C.; Tchounwou, P.B. CYP1a1, HSP70, P53, and c-fos expression in human liver carcinoma cells (HepG2) exposed to pentachlorophenol. Biomed. Sci. Instrum. 2003, 39, 389-396.
    • (2003) Biomed. Sci. Instrum. , vol.39 , pp. 389-396
    • Dorsey, W.C.1    Tchounwou, P.B.2
  • 53
    • 84055199464 scopus 로고    scopus 로고
    • Inducible Hsp70 in the regulation of cancer cell survival: Analysis of chaperone induction, expression and activity
    • Zorzi, E.; Bonvini, P. Inducible Hsp70 in the regulation of cancer cell survival: Analysis of chaperone induction, expression and activity. Cancers 2011, 3, 3921-3956.
    • (2011) Cancers , vol.3 , pp. 3921-3956
    • Zorzi, E.1    Bonvini, P.2
  • 54
    • 0017713229 scopus 로고
    • Fate of recirculating B16 melanoma metastatic variant cells in parabiotic syngeneic recipients
    • Fidler, I.J.; Nicolson, G.L. Fate of recirculating B16 melanoma metastatic variant cells in parabiotic syngeneic recipients. J. Natl. Cancer Inst. 1977, 58, 1867-1872.
    • (1977) J. Natl. Cancer Inst. , vol.58 , pp. 1867-1872
    • Fidler, I.J.1    Nicolson, G.L.2
  • 55
    • 0018143970 scopus 로고
    • In vivo monitoring of the death rate of artificial murine pulmonary micrometastases
    • Liotta, L.A.; Vembu, D.; Saini, R.K.; Boone, C. In vivo monitoring of the death rate of artificial murine pulmonary micrometastases. Cancer Res. 1978, 38, 1231-1236.
    • (1978) Cancer Res. , vol.38 , pp. 1231-1236
    • Liotta, L.A.1    Vembu, D.2    Saini, R.K.3    Boone, C.4
  • 56
    • 44449146369 scopus 로고    scopus 로고
    • Heat shock protein 72 associated with CD44v6 in human colonic adenocarcinoma
    • Wang, X.; Chen, W.; Li, X.; Lin, H.; Wang, Q. Heat shock protein 72 associated with CD44v6 in human colonic adenocarcinoma. Cell Biol. Int. 2008, 32, 860-864.
    • (2008) Cell Biol. Int. , vol.32 , pp. 860-864
    • Wang, X.1    Chen, W.2    Li, X.3    Lin, H.4    Wang, Q.5
  • 58
    • 0026703222 scopus 로고
    • Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity
    • Jäättelä, M.; Wissing, D.; Bauer, P.A.; Li, G.C. Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity. EMBO J. 1992, 11, 3507-3512.
    • (1992) EMBO J. , vol.11 , pp. 3507-3512
    • Jäättelä, M.1    Wissing, D.2    Bauer, P.A.3    Li, G.C.4
  • 59
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jäättelä, M.; Wissing, D.; Kokholm, K.; Kallunki, T.; Egeblad, M. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J. 1998, 17, 6124-6134.
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jäättelä, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 60
    • 0027469435 scopus 로고
    • Heat-shock proteins protect cells from monocyte cytotoxicity: Possible mechanism of self-protection
    • Jäättelä, M.; Wissing, D. Heat-shock proteins protect cells from monocyte cytotoxicity: Possible mechanism of self-protection. J. Exp. Med. 1993, 177, 231-236.
    • (1993) J. Exp. Med. , vol.177 , pp. 231-236
    • Jäättelä, M.1    Wissing, D.2
  • 61
    • 0028919555 scopus 로고
    • Heat shock protein 70 overexpression affects the response to ultraviolet light in murine fibroblasts. Evidence for increased cell viability and suppression of cytokine release
    • Simon, M.M.; Reikerstorfer, A.; Schwarz, A.; Krone, C.; Luger, T.A.; Jäättelä, M.; Schwarz, T. Heat shock protein 70 overexpression affects the response to ultraviolet light in murine fibroblasts. Evidence for increased cell viability and suppression of cytokine release. J. Clin. Invest. 1995, 95, 926-933.
    • (1995) J. Clin. Invest. , vol.95 , pp. 926-933
    • Simon, M.M.1    Reikerstorfer, A.2    Schwarz, A.3    Krone, C.4    Luger, T.A.5    Jäättelä, M.6    Schwarz, T.7
  • 62
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • Mosser, D.D.; Caron, A.W.; Bourget, L.; Denis-Larose, C.; Massie, B. Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol. Cell. Biol. 1997, 17, 5317-5327.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 63
    • 0032479150 scopus 로고    scopus 로고
    • Heat shock protein 72 modulates pathways of stress-induced apoptosis
    • Buzzard, K.A.; Giaccia, A.J.; Killender, M.; Anderson, R.L. Heat shock protein 72 modulates pathways of stress-induced apoptosis. J. Biol. Chem. 1998, 273, 17147-17153.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17147-17153
    • Buzzard, K.A.1    Giaccia, A.J.2    Killender, M.3    Anderson, R.L.4
  • 64
    • 0031722160 scopus 로고    scopus 로고
    • Tobacco smoke induces both apoptosis and necrosis in mammalian cells: Differential effects of HSP70
    • Vayssier, M.; Banzet, N.; François, D.; Bellmann, K.; Polla, B.S. Tobacco smoke induces both apoptosis and necrosis in mammalian cells: Differential effects of HSP70. Am. J. Physiol. 1998, 275, L771-L779.
    • (1998) Am. J. Physiol. , vol.275
    • Vayssier, M.1    Banzet, N.2    François, D.3    Bellmann, K.4    Polla, B.S.5
  • 69
    • 0035254227 scopus 로고    scopus 로고
    • Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase
    • Park, H.-S.; Lee, J.-S.; Huh, S.-H.; Seo, J.-S.; Choi, E.-J. Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase. EMBO J. 2001, 20, 446-456.
    • (2001) EMBO J. , vol.20 , pp. 446-456
    • Park, H.-S.1    Lee, J.-S.2    Huh, S.-H.3    Seo, J.-S.4    Choi, E.-J.5
  • 70
    • 14844307612 scopus 로고    scopus 로고
    • HSP70 Deficiency Results in Activation of c-Jun N-terminal Kinase, Extracellular Signal-regulated Kinase, and Caspase-3 in Hyperosmolarity-induced Apoptosis
    • Lee, J.-S.; Lee, J.-J.; Seo, J.-S. HSP70 Deficiency Results in Activation of c-Jun N-terminal Kinase, Extracellular Signal-regulated Kinase, and Caspase-3 in Hyperosmolarity-induced Apoptosis. J. Biol. Chem. 2005, 280, 6634-6641.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6634-6641
    • Lee, J.-S.1    Lee, J.-J.2    Seo, J.-S.3
  • 71
    • 0037908648 scopus 로고    scopus 로고
    • Inactivation of dual-specificity phosphatases is involved in the regulation of extracellular signal-regulated kinases by heat shock and hsp72
    • Yaglom, J.; O'Callaghan-Sunol, C.; Gabai, V.; Sherman, M.Y. Inactivation of dual-specificity phosphatases is involved in the regulation of extracellular signal-regulated kinases by heat shock and hsp72. Mol. Cell. Biol. 2003, 23, 3813-3824.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3813-3824
    • Yaglom, J.1    O'Callaghan-Sunol, C.2    Gabai, V.3    Sherman, M.Y.4
  • 72
    • 0034745354 scopus 로고    scopus 로고
    • Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth
    • Song, J.; Takeda, M.; Morimoto, R.I. Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth. Nat. Cell Biol. 2001, 3, 276-282.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 276-282
    • Song, J.1    Takeda, M.2    Morimoto, R.I.3
  • 73
    • 33947267567 scopus 로고    scopus 로고
    • High levels of heat shock protein Hsp72 in cancer cells suppress default senescence pathways
    • Yaglom, J.A.; Gabai, V.L.; Sherman, M.Y. High levels of heat shock protein Hsp72 in cancer cells suppress default senescence pathways. Cancer Res. 2007, 67, 2373-2381.
    • (2007) Cancer Res. , vol.67 , pp. 2373-2381
    • Yaglom, J.A.1    Gabai, V.L.2    Sherman, M.Y.3
  • 77
    • 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
  • 78
    • 0037278885 scopus 로고    scopus 로고
    • Integrin adhesion receptors in tumor metastasis
    • Felding-Habermann, B. Integrin adhesion receptors in tumor metastasis. Clin. Exp. Metastasis 2003, 20, 203-213.
    • (2003) Clin. Exp. Metastasis , vol.20 , pp. 203-213
    • Felding-Habermann, B.1
  • 79
    • 33745684527 scopus 로고    scopus 로고
    • Metastasis: A question of life or death
    • Mehlen, P.; Puisieux, A. Metastasis: A question of life or death. Nat. Rev. Cancer 2006, 6, 449-458.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 449-458
    • Mehlen, P.1    Puisieux, A.2
  • 80
    • 17144394423 scopus 로고    scopus 로고
    • Heat shock protein 70 promotes cancer cell viability by safeguarding lysosomal integrity
    • Gyrd-Hansen, M.; Nylandsted, J.; Jäättelä, M. Heat shock protein 70 promotes cancer cell viability by safeguarding lysosomal integrity. Cell Cycle 2004, 3, 1484-1485.
    • (2004) Cell Cycle , vol.3 , pp. 1484-1485
    • Gyrd-Hansen, M.1    Nylandsted, J.2    Jäättelä, M.3
  • 82
    • 0038381506 scopus 로고    scopus 로고
    • Hsp72 inhibits focal adhesion kinase degradation in atp-depleted renal epithelial cells
    • Mao, H.; Li, F.; Ruchalski, K.; Mosser, D.D.; Schwartz, J.H.; Wang, Y.; Borkan, S.C. Hsp72 inhibits focal adhesion kinase degradation in atp-depleted renal epithelial cells. J. Biol. Chem. 2003, 278, 18214-18220.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18214-18220
    • Mao, H.1    Li, F.2    Ruchalski, K.3    Mosser, D.D.4    Schwartz, J.H.5    Wang, Y.6    Borkan, S.C.7
  • 83
    • 15244357105 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases in melanoma cell invasion
    • Hofmann, U.B.; Houben, R.; Bröcker, E.-B.; Becker, J.C. Role of matrix metalloproteinases in melanoma cell invasion. Biochimie 2005, 87, 307-314.
    • (2005) Biochimie , vol.87 , pp. 307-314
    • Hofmann, U.B.1    Houben, R.2    Bröcker, E.-B.3    Becker, J.C.4
  • 86
    • 79954994442 scopus 로고    scopus 로고
    • Extracellular heat shock protein (Hsp)70 and Hsp90α assist in matrix metalloproteinase-2 activation and breast cancer cell migration and invasion
    • Sims, J.D.; McCready, J.; Jay, D.G. Extracellular heat shock protein (Hsp)70 and Hsp90α assist in matrix metalloproteinase-2 activation and breast cancer cell migration and invasion. PLoS One 2011, 6, e18848.
    • (2011) PLoS One , vol.6
    • Sims, J.D.1    McCready, J.2    Jay, D.G.3
  • 87
    • 33748690535 scopus 로고    scopus 로고
    • Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matric metalloproteinase-9 expression in human monocytic U937 cells
    • Lee, K.-J.; Kim, Y.M.; Kim, D.Y.; Jeoung, D.; Han, K.; Lee, S.-T.; Lee, Y.-S.; Park, K.H.; Park, J.H.; Kim, D.J.; et al. Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matric metalloproteinase-9 expression in human monocytic U937 cells. Exp. Mol. Med. 2006, 38, 364-374.
    • (2006) Exp. Mol. Med. , vol.38 , pp. 364-374
    • Lee, K.-J.1    Kim, Y.M.2    Kim, D.Y.3    Jeoung, D.4    Han, K.5    Lee, S.-T.6    Lee, Y.-S.7    Park, K.H.8    Park, J.H.9    Kim, D.J.10
  • 90
    • 0037001673 scopus 로고    scopus 로고
    • General features of gastric carcinomas and comparison of HSP70 and NK cell immunoreactivity with prognostic factors
    • Canöz, O.; Belenli, O.; Patiroglu, T.E. General features of gastric carcinomas and comparison of HSP70 and NK cell immunoreactivity with prognostic factors. Pathol. Oncol. Res. 2002, 8, 262-269.
    • (2002) Pathol. Oncol. Res. , vol.8 , pp. 262-269
    • Canöz, O.1    Belenli, O.2    Patiroglu, T.E.3
  • 91
    • 84858967994 scopus 로고    scopus 로고
    • HSP90 and HSP70 proteins are essential for stabilization and activation of WASF3 metastasis-promoting protein
    • Teng, Y.; Ngoka, L.; Mei, Y.; Lesoon, L.; Cowell, J.K. HSP90 and HSP70 proteins are essential for stabilization and activation of WASF3 metastasis-promoting protein. J. Biol. Chem. 2012, 287, 10051-10059.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10051-10059
    • Teng, Y.1    Ngoka, L.2    Mei, Y.3    Lesoon, L.4    Cowell, J.K.5
  • 93
    • 79953708490 scopus 로고    scopus 로고
    • HSP70 decreases receptor-dependent phosphorylation of Smad2 and blocks TGF-β-induced epithelial-mesenchymal transition
    • Li, Y.; Kang, X.; Wang, Q. HSP70 decreases receptor-dependent phosphorylation of Smad2 and blocks TGF-β-induced epithelial-mesenchymal transition. J. Genet. Genomics 2011, 38, 111-116.
    • (2011) J. Genet. Genomics , vol.38 , pp. 111-116
    • Li, Y.1    Kang, X.2    Wang, Q.3
  • 94
    • 2442427558 scopus 로고    scopus 로고
    • Hsp72 interacts with paxillin and facilitates the reassembly of focal adhesions during recovery from ATP depletion
    • Mao, H.; Wang, Y.; Li, Z.; Ruchalski, K.L.; Yu, X.; Schwartz, J.H.; Borkan, S.C. Hsp72 interacts with paxillin and facilitates the reassembly of focal adhesions during recovery from ATP depletion. J. Biol. Chem. 2004, 279, 15472-15480.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15472-15480
    • Mao, H.1    Wang, Y.2    Li, Z.3    Ruchalski, K.L.4    Yu, X.5    Schwartz, J.H.6    Borkan, S.C.7
  • 95
    • 84870325964 scopus 로고    scopus 로고
    • Knockdown of Hop downregulates RhoC expression, and decreases pseudopodia formation and migration in cancer cell lines
    • Willmer, T.; Contu, L.; Blatch, G.L.; Edkins, A.L. Knockdown of Hop downregulates RhoC expression, and decreases pseudopodia formation and migration in cancer cell lines. Cancer Lett. 2013, 328, 252-260.
    • (2013) Cancer Lett. , vol.328 , pp. 252-260
    • Willmer, T.1    Contu, L.2    Blatch, G.L.3    Edkins, A.L.4
  • 96
    • 80054805091 scopus 로고    scopus 로고
    • A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration
    • Boroughs, L.K.; Antonyak, M.A.; Johnson, J.L.; Cerione, R.A. A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration. J. Biol. Chem. 2011, 286, 37094-37107.
    • (2011) J. Biol. Chem. , vol.286 , pp. 37094-37107
    • Boroughs, L.K.1    Antonyak, M.A.2    Johnson, J.L.3    Cerione, R.A.4
  • 97
    • 34447326992 scopus 로고    scopus 로고
    • Down-regulation of WAVE3, a metastasis promoter gene, inhibits invasion and metastasis of breast cancer cells
    • Sossey-Alaoui, K.; Safina, A.; Li, X.; Vaughan, M.M.; Hicks, D.G.; Bakin, A.V.; Cowell, J.K. Down-regulation of WAVE3, a metastasis promoter gene, inhibits invasion and metastasis of breast cancer cells. Am. J. Pathol. 2007, 170, 2112-2121.
    • (2007) Am. J. Pathol. , vol.170 , pp. 2112-2121
    • Sossey-Alaoui, K.1    Safina, A.2    Li, X.3    Vaughan, M.M.4    Hicks, D.G.5    Bakin, A.V.6    Cowell, J.K.7
  • 98
    • 20444435118 scopus 로고    scopus 로고
    • WAVE3-mediated cell migration and lamellipodia formation are regulated downstream of phosphatidylinositol 3-Kinase
    • Sossey-Alaoui, K.; Li, X.; Ranalli, T.A.; Cowell, J.K. WAVE3-mediated cell migration and lamellipodia formation are regulated downstream of phosphatidylinositol 3-Kinase. J. Biol. Chem. 2005, 280, 21748-21755.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21748-21755
    • Sossey-Alaoui, K.1    Li, X.2    Ranalli, T.A.3    Cowell, J.K.4
  • 99
    • 77957239866 scopus 로고    scopus 로고
    • Inactivation of the WASF3 gene in prostate cancer cells leads to suppression of tumorigenicity and metastases
    • Teng, Y.; Ren, M.Q.; Cheney, R.; Sharma, S.; Cowell, J.K. Inactivation of the WASF3 gene in prostate cancer cells leads to suppression of tumorigenicity and metastases. Br. J. Cancer 2010, 103, 1066-1075.
    • (2010) Br. J. Cancer , vol.103 , pp. 1066-1075
    • Teng, Y.1    Ren, M.Q.2    Cheney, R.3    Sharma, S.4    Cowell, J.K.5
  • 101
    • 79951857812 scopus 로고    scopus 로고
    • BAG3 (BCL2-associated athanogene 3) interacts with MMP-2 to positively regulate invasion by ovarian carcinoma cells
    • Suzuki, M.; Iwasaki, M.; Sugio, A.; Hishiya, A.; Tanaka, R.; Endo, T.; Takayama, S.; Saito, T. BAG3 (BCL2-associated athanogene 3) interacts with MMP-2 to positively regulate invasion by ovarian carcinoma cells. Cancer Lett. 2011, 303, 65-71.
    • (2011) Cancer Lett. , vol.303 , pp. 65-71
    • Suzuki, M.1    Iwasaki, M.2    Sugio, A.3    Hishiya, A.4    Tanaka, R.5    Endo, T.6    Takayama, S.7    Saito, T.8
  • 102
    • 78650048935 scopus 로고    scopus 로고
    • The Regulatory mechanism of extracellular Hsp90α on matrix metalloproteinase-2 processing and tumor angiogenesis
    • Song, X.; Wang, X.; Zhuo, W.; Shi, H.; Feng, D.; Sun, Y.; Liang, Y.; Fu, Y.; Zhou, D.; Luo, Y. The Regulatory mechanism of extracellular Hsp90α on matrix metalloproteinase-2 processing and tumor angiogenesis. J. Biol. Chem. 2010, 285, 40039-40049.
    • (2010) J. Biol. Chem. , vol.285 , pp. 40039-40049
    • Song, X.1    Wang, X.2    Zhuo, W.3    Shi, H.4    Feng, D.5    Sun, Y.6    Liang, Y.7    Fu, Y.8    Zhou, D.9    Luo, Y.10
  • 103
    • 79955478704 scopus 로고    scopus 로고
    • RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation
    • Walsh, N.; Larkin, A.; Swan, N.; Conlon, K.; Dowling, P.; McDermott, R.; Clynes, M. RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation. Cancer Lett. 2011, 306, 180-189.
    • (2011) Cancer Lett. , vol.306 , pp. 180-189
    • Walsh, N.1    Larkin, A.2    Swan, N.3    Conlon, K.4    Dowling, P.5    McDermott, R.6    Clynes, M.7
  • 104
    • 33646576169 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tumor metastasis
    • Deryugina, E.I.; Quigley, J.P. Matrix metalloproteinases and tumor metastasis. Cancer Metastasis Rev. 2006, 25, 9-34.
    • (2006) Cancer Metastasis Rev. , vol.25 , pp. 9-34
    • Deryugina, E.I.1    Quigley, J.P.2
  • 105
    • 67649421096 scopus 로고    scopus 로고
    • Molecular principles of cancer invasion and metastasis
    • Leber, M.F.; Efferth, T. Molecular principles of cancer invasion and metastasis. Int. J. Oncol. 2009, 34, 881-895.
    • (2009) Int. J. Oncol. , vol.34 , pp. 881-895
    • Leber, M.F.1    Efferth, T.2
  • 106
    • 83555165986 scopus 로고    scopus 로고
    • MMP-9 induces CD44 cleavage and CD44 mediated cell migration in glioblastoma xenograft cells
    • Chetty, C.; Vanamala, S.K.; Gondi, C.S.; Dinh, D.H.; Gujrati, M.; Rao, J.S. MMP-9 induces CD44 cleavage and CD44 mediated cell migration in glioblastoma xenograft cells. Cell. Signal. 2012, 24, 549-559.
    • (2012) Cell. Signal. , vol.24 , pp. 549-559
    • Chetty, C.1    Vanamala, S.K.2    Gondi, C.S.3    Dinh, D.H.4    Gujrati, M.5    Rao, J.S.6
  • 107
    • 35548970287 scopus 로고    scopus 로고
    • Heat shock proteins in cancer
    • Sherman, M.; Multhoff, G. Heat shock proteins in cancer. Ann. NY Acad. Sci. 2007, 1113, 192-201.
    • (2007) Ann. NY Acad. Sci. , vol.1113 , pp. 192-201
    • Sherman, M.1    Multhoff, G.2
  • 108
    • 7744222195 scopus 로고    scopus 로고
    • Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability
    • Arispe, N.; Doh, M.; Simakova, O.; Kurganov, B.; de Maio, A. Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability. FASEB J. 2004, 18, 1636-1645.
    • (2004) FASEB J. , vol.18 , pp. 1636-1645
    • Arispe, N.1    Doh, M.2    Simakova, O.3    Kurganov, B.4    de Maio, A.5
  • 109
    • 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
  • 110
    • 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
  • 111
    • 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
  • 113
    • 20744436655 scopus 로고    scopus 로고
    • Exosome-dependent trafficking of HSP70: A novel secretory pathway for cellular stress proteins
    • Lancaster, G.I.; Febbraio, M.A. Exosome-dependent trafficking of HSP70: A novel secretory pathway for cellular stress proteins. J. Biol. Chem. 2005, 280, 23349-23355.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23349-23355
    • Lancaster, G.I.1    Febbraio, M.A.2
  • 114
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes
    • Mambula, S.S.; Calderwood, S.K. Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes. J. Immunol. 2006, 177, 7849-7857.
    • (2006) J. Immunol. , vol.177 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 115
    • 84860849807 scopus 로고    scopus 로고
    • Anticancer drugs cause release of exosomes with heat shock proteins from human hepatocellular carcinoma cells that elicit effective natural killer cell antitumor responses in vitro
    • Lv, L.-H.; Wan, Y.-L.; Lin, Y.; Zhang, W.; Yang, M.; Li, G.-L.; Lin, H.-M.; Shang, C.-Z.; Chen, Y.-J.; Min, J. Anticancer drugs cause release of exosomes with heat shock proteins from human hepatocellular carcinoma cells that elicit effective natural killer cell antitumor responses in vitro. J. Biol. Chem. 2012, 287, 15874-15885.
    • (2012) J. Biol. Chem. , vol.287 , pp. 15874-15885
    • Lv, L.-H.1    Wan, Y.-L.2    Lin, Y.3    Zhang, W.4    Yang, M.5    Li, G.-L.6    Lin, H.-M.7    Shang, C.-Z.8    Chen, Y.-J.9    Min, J.10
  • 116
    • 33646369952 scopus 로고    scopus 로고
    • Immunostimulatory functions of membrane-bound and exported heat shock protein 70
    • Radons, J.; Multhoff, G. Immunostimulatory functions of membrane-bound and exported heat shock protein 70. Exerc. Immunol. Rev. 2005, 11, 17-33.
    • (2005) Exerc. Immunol. Rev. , vol.11 , pp. 17-33
    • Radons, J.1    Multhoff, G.2
  • 117
    • 37849185221 scopus 로고    scopus 로고
    • Extracellular heat shock protein 70 mediates heat stress-induced epidermal growth factor receptor transactivation in A431 carcinoma cells
    • Evdonin, A.L.; Guzhova, I.V.; Margulis, B.A.; Medvedeva, N.D. Extracellular heat shock protein 70 mediates heat stress-induced epidermal growth factor receptor transactivation in A431 carcinoma cells. FEBS Lett. 2006, 580, 6674-6678.
    • (2006) FEBS Lett. , vol.580 , pp. 6674-6678
    • Evdonin, A.L.1    Guzhova, I.V.2    Margulis, B.A.3    Medvedeva, N.D.4
  • 119
    • 77954164469 scopus 로고    scopus 로고
    • Connecting Hsp70, sphingolipid metabolism and lysosomal stability
    • Petersen, N.H.T.; Kirkegaard, T.; Olsen, O.D.; Jäättelä, M. Connecting Hsp70, sphingolipid metabolism and lysosomal stability. Cell Cycle 2010, 9, 2305-2309.
    • (2010) Cell Cycle , vol.9 , pp. 2305-2309
    • Petersen, N.H.T.1    Kirkegaard, T.2    Olsen, O.D.3    Jäättelä, M.4
  • 120
    • 58149398237 scopus 로고    scopus 로고
    • Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form
    • Kurz, T.; Brunk, U.T. Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form. Autophagy 2009, 5, 93-95.
    • (2009) Autophagy , vol.5 , pp. 93-95
    • Kurz, T.1    Brunk, U.T.2
  • 121
    • 49649108912 scopus 로고    scopus 로고
    • Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion
    • Yang, Y.; Rao, R.; Shen, J.; Tang, Y.; Fiskus, W.; Nechtman, J.; Atadja, P.; Bhalla, K. Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion. Cancer Res. 2008, 68, 4833-4842.
    • (2008) Cancer Res. , vol.68 , pp. 4833-4842
    • Yang, Y.1    Rao, R.2    Shen, J.3    Tang, Y.4    Fiskus, W.5    Nechtman, J.6    Atadja, P.7    Bhalla, K.8
  • 123
    • 17144361820 scopus 로고    scopus 로고
    • Lysosomes as targets for cancer therapy
    • Fehrenbacher, N.; Jäättelä, M. Lysosomes as targets for cancer therapy. Cancer Res. 2005, 65, 2993-2995.
    • (2005) Cancer Res. , vol.65 , pp. 2993-2995
    • Fehrenbacher, N.1    Jäättelä, M.2
  • 124
    • 33846164404 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • Vasiljeva, O.; Reinheckel, T.; Peters, C.; Turk, D.; Turk, V.; Turk, B. Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des. 2007, 13, 387-403.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 387-403
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 126
    • 56449113201 scopus 로고    scopus 로고
    • Lysosomal cathepsin B participates in the podosome-mediated extracellular matrix degradation and invasion via secreted lysosomes in v-Src fibroblasts
    • Tu, C.; Ortega-Cava, C.F.; Chen, G.; Fernandes, N.D.; Cavallo-Medved, D.; Sloane, B.F.; Band, V.; Band, H. Lysosomal cathepsin B participates in the podosome-mediated extracellular matrix degradation and invasion via secreted lysosomes in v-Src fibroblasts. Cancer Res. 2008, 68, 9147-9156.
    • (2008) Cancer Res. , vol.68 , pp. 9147-9156
    • Tu, C.1    Ortega-Cava, C.F.2    Chen, G.3    Fernandes, N.D.4    Cavallo-Medved, D.5    Sloane, B.F.6    Band, V.7    Band, H.8
  • 129
    • 77955713312 scopus 로고    scopus 로고
    • A new feature of the stress response: Increase in endocytosis mediated by Hsp70
    • Vega, V.L.; Charles, W.; de Maio, A. A new feature of the stress response: Increase in endocytosis mediated by Hsp70. Cell Stress Chaperones 2010, 15, 517-527.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 517-527
    • Vega, V.L.1    Charles, W.2    de Maio, A.3
  • 130
    • 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.; Multhoff, G.; Arispe, N.; de Maio, A. 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    Multhoff, G.7    Arispe, N.8    de Maio, A.9
  • 132
    • 15544373100 scopus 로고    scopus 로고
    • Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells
    • Thériault, J.R.; Mambula, S.S.; Sawamura, T.; Stevenson, M.A.; Calderwood, S.K. Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells. FEBS Lett. 2005, 579, 1951-1960.
    • (2005) FEBS Lett. , vol.579 , pp. 1951-1960
    • Thériault, J.R.1    Mambula, S.S.2    Sawamura, T.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 133
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu, S.; Binder, R.J.; Ramalingam, T.; Srivastava, P.K. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 2001, 14, 303-313.
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 134
    • 33845446813 scopus 로고    scopus 로고
    • Role of scavenger receptors in the binding and internalization of heat shock protein 70
    • Thériault, J.R.; Adachi, H.; Calderwood, S.K. Role of scavenger receptors in the binding and internalization of heat shock protein 70. J. Immunol. 2006, 177, 8604-8611.
    • (2006) J. Immunol. , vol.177 , pp. 8604-8611
    • Thériault, J.R.1    Adachi, H.2    Calderwood, S.K.3
  • 135
    • 35748934798 scopus 로고    scopus 로고
    • Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling
    • Bendz, H.; Ruhland, S.C.; Pandya, M.J.; Hainzl, O.; Riegelsberger, S.; Brauchle, C.; Mayer, M.P.; Buchner, J.; Issels, R.D.; Noessner, E. Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling. J. Biol. Chem. 2007, 282, 31688-31702.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31688-31702
    • Bendz, H.1    Ruhland, S.C.2    Pandya, M.J.3    Hainzl, O.4    Riegelsberger, S.5    Brauchle, C.6    Mayer, M.P.7    Buchner, J.8    Issels, R.D.9    Noessner, E.10
  • 137
    • 84865175386 scopus 로고    scopus 로고
    • The role of heat shock proteins in antigen cross presentation
    • Murshid, A.; Gong, J.; Calderwood, S.K. The role of heat shock proteins in antigen cross presentation. Front. Immunol. 2012, 3, 63.
    • (2012) Front. Immunol. , vol.3 , pp. 63
    • Murshid, A.1    Gong, J.2    Calderwood, S.K.3
  • 138
    • 0033120990 scopus 로고    scopus 로고
    • Cutting edge: Receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells
    • Arnold-Schild, D.; Hanau, D.; Spehner, D.; Schmid, C.; Rammensee, H.G.; de la Salle, H.; Schild, H. Cutting edge: Receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells. J. Immunol. 1999, 162, 3757-3760.
    • (1999) J. Immunol. , vol.162 , pp. 3757-3760
    • Arnold-Schild, D.1    Hanau, D.2    Spehner, D.3    Schmid, C.4    Rammensee, H.G.5    de la Salle, H.6    Schild, H.7
  • 144
    • 1642536402 scopus 로고    scopus 로고
    • The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells
    • Gastpar, R.; Gross, C.; Rossbacher, L.; Ellwart, J.; Riegger, J.; Multhoff, G. The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells. J. Immunol. 2004, 172, 972-980.
    • (2004) J. Immunol. , vol.172 , pp. 972-980
    • Gastpar, R.1    Gross, C.2    Rossbacher, L.3    Ellwart, J.4    Riegger, J.5    Multhoff, G.6
  • 146
  • 147
    • 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.; Stevenson, M.A.; Calderwood, S.K. Novel signal transduction pathway utilized by extracellular HSP70: Role of toll-like receptor (TLR) 2 and TLR4. J. Biol. Chem. 2002, 277, 15028-15034.
    • (2002) J. Biol. 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    Stevenson, M.A.7    Calderwood, S.K.8
  • 149
    • 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-kappa B pathway
    • Basu, S.; Binder, R.J.; Suto, R.; Anderson, K.M.; Srivastava, P.K. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int. Immunol. 2000, 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
  • 150
    • 0037087398 scopus 로고    scopus 로고
    • Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs
    • Panjwani, N.N.; Popova, L.; Srivastava, P.K. Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs. J. Immunol. 2002, 168, 2997-3003.
    • (2002) J. Immunol. , vol.168 , pp. 2997-3003
    • Panjwani, N.N.1    Popova, L.2    Srivastava, P.K.3
  • 151
    • 33748513676 scopus 로고    scopus 로고
    • Killing of normal melanocytes, combined with heat shock protein 70 and CD40L expression, cures large established melanomas
    • Sanchez-Perez, L.; Kottke, T.; Daniels, G.A.; Diaz, R.M.; Thompson, J.; Pulido, J.; Melcher, A.; Vile, R.G. Killing of normal melanocytes, combined with heat shock protein 70 and CD40L expression, cures large established melanomas. J. Immunol. 2006, 177, 4168-4177.
    • (2006) J. Immunol. , vol.177 , pp. 4168-4177
    • Sanchez-Perez, L.1    Kottke, T.2    Daniels, G.A.3    Diaz, R.M.4    Thompson, J.5    Pulido, J.6    Melcher, A.7    Vile, R.G.8
  • 152
    • 14844355875 scopus 로고    scopus 로고
    • Identification of stimulating and inhibitory epitopes within the heat shock protein 70 molecule that modulate cytokine production and maturation of dendritic cells
    • Wang, Y.; Whittall, T.; McGowan, E.; Younson, J.; Kelly, C.; Bergmeier, L.A.; Singh, M.; Lehner, T. Identification of stimulating and inhibitory epitopes within the heat shock protein 70 molecule that modulate cytokine production and maturation of dendritic cells. J. Immunol. 2005, 174, 3306-3316.
    • (2005) J. Immunol. , vol.174 , pp. 3306-3316
    • Wang, Y.1    Whittall, T.2    McGowan, E.3    Younson, J.4    Kelly, C.5    Bergmeier, L.A.6    Singh, M.7    Lehner, T.8
  • 153
    • 0035007710 scopus 로고    scopus 로고
    • The role of heat shock protein (hsp70) in dendritic cell maturation: Hsp70 induces the maturation of immature dendritic cells but reduces DC differentiation from monocyte precursors
    • Kuppner, M.C.; Gastpar, R.; Gelwer, S.; Nössner, E.; Ochmann, O.; Scharner, A.; Issels, R.D. The role of heat shock protein (hsp70) in dendritic cell maturation: Hsp70 induces the maturation of immature dendritic cells but reduces DC differentiation from monocyte precursors. Eur. J. Immunol. 2001, 31, 1602-1609.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1602-1609
    • Kuppner, M.C.1    Gastpar, R.2    Gelwer, S.3    Nössner, E.4    Ochmann, O.5    Scharner, A.6    Issels, R.D.7
  • 154
    • 63149158731 scopus 로고    scopus 로고
    • Heat shock protein 70, released from heat-stressed tumor cells, initiates antitumor immunity by inducing tumor cell chemokine production and activating dendritic cells via TLR4 pathway
    • Chen, T.; Guo, J.; Han, C.; Yang, M.; Cao, X. Heat shock protein 70, released from heat-stressed tumor cells, initiates antitumor immunity by inducing tumor cell chemokine production and activating dendritic cells via TLR4 pathway. J. Immunol. 2009, 182, 1449-1459.
    • (2009) J. Immunol. , vol.182 , pp. 1449-1459
    • Chen, T.1    Guo, J.2    Han, C.3    Yang, M.4    Cao, X.5
  • 155
    • 84872142174 scopus 로고    scopus 로고
    • The immunosuppressive activity of heat shock protein 70
    • Stocki, P.; Dickinson, A.M. The immunosuppressive activity of heat shock protein 70. Autoimmune Dis. 2012, 2012, 617213.
    • (2012) Autoimmune Dis. , vol.2012 , pp. 617213
    • Stocki, P.1    Dickinson, A.M.2
  • 157
    • 77950349873 scopus 로고    scopus 로고
    • Caught with their PAMPs down? The extracellular signalling actions of molecular chaperones are not due to microbial contaminants
    • Henderson, B.; Calderwood, S.K.; Coates, A.R.M.; Cohen, I.; van Eden, W.; Lehner, T.; Pockley, A.G. Caught with their PAMPs down? The extracellular signalling actions of molecular chaperones are not due to microbial contaminants. Cell Stress Chaperones 2010, 15, 123-141.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 123-141
    • Henderson, B.1    Calderwood, S.K.2    Coates, A.R.M.3    Cohen, I.4    van Eden, W.5    Lehner, T.6    Pockley, A.G.7
  • 158
    • 67149133632 scopus 로고    scopus 로고
    • Heat shock proteins and immune system
    • Tsan, M.-F.; Gao, B. Heat shock proteins and immune system. J. Leukoc. Biol. 2009, 85, 905-910.
    • (2009) J. Leukoc. Biol. , vol.85 , pp. 905-910
    • Tsan, M.-F.1    Gao, B.2
  • 159
    • 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
  • 160
    • 84863601838 scopus 로고    scopus 로고
    • Chronic inflammation in cancer development
    • Multhoff, G.; Molls, M.; Radons, J. Chronic inflammation in cancer development. Front. Immunol. 2011, 2, 98.
    • (2011) Front. Immunol. , vol.2 , pp. 98
    • Multhoff, G.1    Molls, M.2    Radons, J.3
  • 161
    • 84871548554 scopus 로고    scopus 로고
    • HSP70 enhances immunosuppressive function of CD4(+)CD25(+)FoxP3(+) T regulatory cells and cytotoxicity in CD4(+)CD25(-) T cells
    • Wachstein, J.; Tischer, S.; Figueiredo, C.; Limbourg, A.; Falk, C.; Immenschuh, S.; Blasczyk, R.; Eiz-Vesper, B. HSP70 enhances immunosuppressive function of CD4(+)CD25(+)FoxP3(+) T regulatory cells and cytotoxicity in CD4(+)CD25(-) T cells. PLoS One 2012, 7, e51747.
    • (2012) PLoS One , vol.7
    • Wachstein, J.1    Tischer, S.2    Figueiredo, C.3    Limbourg, A.4    Falk, C.5    Immenschuh, S.6    Blasczyk, R.7    Eiz-Vesper, B.8
  • 162
    • 76649097628 scopus 로고    scopus 로고
    • Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells
    • Chalmin, F.; Ladoire, S.; Mignot, G.; Vincent, J.; Bruchard, M.; Remy-Martin, J.-P.; Boireau, W.; Rouleau, A.; Simon, B.; Lanneau, D.; et al. Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells. J. Clin. Invest. 2010, 120, 457-471.
    • (2010) J. Clin. Invest. , vol.120 , pp. 457-471
    • Chalmin, F.1    Ladoire, S.2    Mignot, G.3    Vincent, J.4    Bruchard, M.5    Remy-Martin, J.-P.6    Boireau, W.7    Rouleau, A.8    Simon, B.9    Lanneau, D.10
  • 163
    • 17144417382 scopus 로고    scopus 로고
    • Heat-shock proteins induce T-cell regulation of chronic inflammation
    • Van Eden, W.; van der Zee, R.; Prakken, B. Heat-shock proteins induce T-cell regulation of chronic inflammation. Nat. Rev. Immunol. 2005, 5, 318-330.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 318-330
    • Van Eden, W.1    van der Zee, R.2    Prakken, B.3
  • 165
    • 84859489665 scopus 로고    scopus 로고
    • Inducible heat shock protein 70 reduces T cell responses and stimulatory capacity of monocyte-derived dendritic cells
    • Stocki, P.; Wang, X.N.; Dickinson, A.M. Inducible heat shock protein 70 reduces T cell responses and stimulatory capacity of monocyte-derived dendritic cells. J. Biol. Chem. 2012, 287, 12387-12394.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12387-12394
    • Stocki, P.1    Wang, X.N.2    Dickinson, A.M.3
  • 167
    • 0032578691 scopus 로고    scopus 로고
    • Proteinase requirements of epidermal growth factor-induced ovarian cancer cell invasion
    • Ellerbroek, S.M.; Hudson, L.G.; Stack, M.S. Proteinase requirements of epidermal growth factor-induced ovarian cancer cell invasion. Int. J. Cancer 1998, 78, 331-337.
    • (1998) Int. J. Cancer , vol.78 , pp. 331-337
    • Ellerbroek, S.M.1    Hudson, L.G.2    Stack, M.S.3
  • 168
    • 84867804151 scopus 로고    scopus 로고
    • The EGF receptor and HER2 participate in TNF-α-dependent MAPK activation and IL-8 secretion in intestinal epithelial cells
    • Jijon, H.B.; Buret, A.; Hirota, C.L.; Hollenberg, M.D.; Beck, P.L. The EGF receptor and HER2 participate in TNF-α-dependent MAPK activation and IL-8 secretion in intestinal epithelial cells. Mediators Inflamm. 2012, 2012, 207398.
    • (2012) Mediators Inflamm. , vol.2012 , pp. 207398
    • Jijon, H.B.1    Buret, A.2    Hirota, C.L.3    Hollenberg, M.D.4    Beck, P.L.5
  • 169
    • 0032731892 scopus 로고    scopus 로고
    • Tumor invasion: Role of growth factor-induced cell motility
    • Wells, A. Tumor invasion: Role of growth factor-induced cell motility. Adv. Cancer Res. 2000, 78, 31-101.
    • (2000) Adv. Cancer Res. , vol.78 , pp. 31-101
    • Wells, A.1
  • 170
    • 84856603638 scopus 로고    scopus 로고
    • Extracellular HSPA1A promotes the growth of hepatocarcinoma by augmenting tumor cell proliferation and apoptosis-resistance
    • Wu, F.-H.; Yuan, Y.; Li, D.; Liao, S.-J.; Yan, B.; Wei, J.-J.; Zhou, Y.-H.; Zhu, J.-H.; Zhang, G.-M.; Feng, Z.-H. Extracellular HSPA1A promotes the growth of hepatocarcinoma by augmenting tumor cell proliferation and apoptosis-resistance. Cancer Lett. 2012, 317, 157-164.
    • (2012) Cancer Lett. , vol.317 , pp. 157-164
    • Wu, F.-H.1    Yuan, Y.2    Li, D.3    Liao, S.-J.4    Yan, B.5    Wei, J.-J.6    Zhou, Y.-H.7    Zhu, J.-H.8    Zhang, G.-M.9    Feng, Z.-H.10
  • 171
    • 84880610121 scopus 로고    scopus 로고
    • Invasion potential of H22 hepatocarcinoma cells is increased by HMGB1-induced tumor NF-κB signaling via initiation of HSP70
    • doi:10.3892/or.2013.2595
    • Gong, W.; Wang, Z.-Y.; Chen, G.-X.; Liu, Y.-Q.; Gu, X.-Y.; Liu, W.-W. Invasion potential of H22 hepatocarcinoma cells is increased by HMGB1-induced tumor NF-κB signaling via initiation of HSP70. Oncol. Rep. 2013, doi:10.3892/or.2013.2595.
    • (2013) Oncol. Rep.
    • Gong, W.1    Wang, Z.-Y.2    Chen, G.-X.3    Liu, Y.-Q.4    Gu, X.-Y.5    Liu, W.-W.6
  • 173
  • 174
    • 5544237716 scopus 로고    scopus 로고
    • Reactive oxygen species as mediators of angiogenesis signaling: Role of NAD(P)H oxidase
    • Ushio-Fukai, M.; Alexander, R.W. Reactive oxygen species as mediators of angiogenesis signaling: Role of NAD(P)H oxidase. Mol. Cell. Biochem. 2004, 264, 85-97.
    • (2004) Mol. Cell. Biochem. , vol.264 , pp. 85-97
    • Ushio-Fukai, M.1    Alexander, R.W.2
  • 175
    • 4143050218 scopus 로고    scopus 로고
    • The potential role of neutrophils in promoting the metastatic phenotype of tumors releasing interleukin-8
    • De Larco, J.E.; Wuertz, B.R.K.; Furcht, L.T. The potential role of neutrophils in promoting the metastatic phenotype of tumors releasing interleukin-8. Clin. Cancer Res. 2004, 10, 4895-4900.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 4895-4900
    • De Larco, J.E.1    Wuertz, B.R.K.2    Furcht, L.T.3
  • 176
    • 66649102550 scopus 로고    scopus 로고
    • Extracellular Hsp72, an endogenous DAMP, is released by virally infected airway epithelial cells and activates neutrophils via Toll-like receptor (TLR)-4
    • Wheeler, D.S.; Chase, M.A.; Senft, A.P.; Poynter, S.E.; Wong, H.R.; Page, K. Extracellular Hsp72, an endogenous DAMP, is released by virally infected airway epithelial cells and activates neutrophils via Toll-like receptor (TLR)-4. Respir. Res. 2009, 10, 31.
    • (2009) Respir. Res. , vol.10 , pp. 31
    • Wheeler, D.S.1    Chase, M.A.2    Senft, A.P.3    Poynter, S.E.4    Wong, H.R.5    Page, K.6
  • 177
    • 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. J. Cell Biol. 2002, 158, 1277-1285.
    • (2002) J. Cell Biol. , vol.158 , pp. 1277-1285
    • Becker, T.1    Hartl, F.-U.2    Wieland, F.3
  • 183
    • 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
  • 184
    • 80455158315 scopus 로고    scopus 로고
    • Heat shock proteins and cancer vaccines: Developments in the past decade and chaperoning in the decade to come
    • Murshid, A.; Gong, J.; Stevenson, M.A.; Calderwood, S.K. Heat shock proteins and cancer vaccines: Developments in the past decade and chaperoning in the decade to come. Expert Rev. Vaccines 2011, 10, 1553-1568.
    • (2011) Expert Rev. Vaccines , vol.10 , pp. 1553-1568
    • Murshid, A.1    Gong, J.2    Stevenson, M.A.3    Calderwood, S.K.4
  • 186
    • 71049173726 scopus 로고    scopus 로고
    • Heat-shock protein 70-2 (HSP70-2) expression in bladder urothelial carcinoma is associated with tumour progression and promotes migration and invasion
    • Garg, M.; Kanojia, D.; Seth, A.; Kumar, R.; Gupta, A.; Surolia, A.; Suri, A. Heat-shock protein 70-2 (HSP70-2) expression in bladder urothelial carcinoma is associated with tumour progression and promotes migration and invasion. Eur. J. Cancer 2010, 46, 207-215.
    • (2010) Eur. J. Cancer , vol.46 , pp. 207-215
    • Garg, M.1    Kanojia, D.2    Seth, A.3    Kumar, R.4    Gupta, A.5    Surolia, A.6    Suri, A.7
  • 187
    • 67651033526 scopus 로고    scopus 로고
    • Silencing of heat shock protein 70 expression enhances radiotherapy efficacy and inhibits cell invasion in endometrial cancer cell line
    • Du, X.L.; Jiang, T.; Wen, Z.Q.; Gao, R.; Cui, M.; Wang, F. Silencing of heat shock protein 70 expression enhances radiotherapy efficacy and inhibits cell invasion in endometrial cancer cell line. Croat. Med. J. 2009, 50, 143-150.
    • (2009) Croat. Med. J. , vol.50 , pp. 143-150
    • Du, X.L.1    Jiang, T.2    Wen, Z.Q.3    Gao, R.4    Cui, M.5    Wang, F.6
  • 188
    • 84870365240 scopus 로고    scopus 로고
    • Why does cancer therapy lack effective anti-metastasis drugs?
    • Weber, G.F. Why does cancer therapy lack effective anti-metastasis drugs? Cancer Lett. 2013, 328, 207-211.
    • (2013) Cancer Lett. , vol.328 , pp. 207-211
    • Weber, G.F.1
  • 189
    • 84856088031 scopus 로고    scopus 로고
    • Metastasis is an early event in mouse mammary carcinomas and is associated with cells bearing stem cell markers
    • Weng, D.; Penzner, J.H.; Song, B.; Koido, S.; Calderwood, S.K.; Gong, J. Metastasis is an early event in mouse mammary carcinomas and is associated with cells bearing stem cell markers. Breast Cancer Res. 2012, 14, R18.
    • (2012) Breast Cancer Res. , vol.14
    • Weng, D.1    Penzner, J.H.2    Song, B.3    Koido, S.4    Calderwood, S.K.5    Gong, J.6
  • 190
    • 0030454056 scopus 로고    scopus 로고
    • Heat-shock protein 72 cell-surface expression on human lung carcinoma cells in associated with an increased sensitivity to lysis mediated by adherent natural killer cells
    • Botzler, C.; Issels, R.; Multhoff, G. Heat-shock protein 72 cell-surface expression on human lung carcinoma cells in associated with an increased sensitivity to lysis mediated by adherent natural killer cells. Cancer Immunol. Immunother. 1996, 43, 226-230.
    • (1996) Cancer Immunol. Immunother. , vol.43 , pp. 226-230
    • Botzler, C.1    Issels, R.2    Multhoff, G.3
  • 191
    • 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
  • 192
    • 0031869555 scopus 로고    scopus 로고
    • Differential Hsp70 plasma-membrane expression on primary human tumors and metastases in mice with severe combined immunodeficiency
    • Botzler, C.; Schmidt, J.; Luz, A.; Jennen, L.; Issels, R.; Multhoff, G. Differential Hsp70 plasma-membrane expression on primary human tumors and metastases in mice with severe combined immunodeficiency. Int. J. Cancer 1998, 77, 942-948.
    • (1998) Int. J. Cancer , vol.77 , pp. 942-948
    • Botzler, C.1    Schmidt, J.2    Luz, A.3    Jennen, L.4    Issels, R.5    Multhoff, G.6
  • 193
    • 0034569491 scopus 로고    scopus 로고
    • Adoptive transfer of human natural killer cells in mice with severe combined immunodeficiency inhibits growth of Hsp70-expressing tumors
    • Multhoff, G.; Pfister, K.; Botzler, C.; Jordan, A.; Scholz, R.; Schmetzer, H.; Burgstahler, R.; Hiddemann, W. Adoptive transfer of human natural killer cells in mice with severe combined immunodeficiency inhibits growth of Hsp70-expressing tumors. Int. J. Cancer 2000, 88, 791-797.
    • (2000) Int. J. Cancer , vol.88 , pp. 791-797
    • Multhoff, G.1    Pfister, K.2    Botzler, C.3    Jordan, A.4    Scholz, R.5    Schmetzer, H.6    Burgstahler, R.7    Hiddemann, W.8
  • 194
    • 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.; Gürtler, U.; Gross, C.; Gehrmann, M.; Thonigs, G.; Pfister, K.; Multhoff, G. 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    Gürtler, U.3    Gross, C.4    Gehrmann, M.5    Thonigs, G.6    Pfister, K.7    Multhoff, G.8
  • 195
    • 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.; Pfister, K.; Multhoff, G. 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    Pfister, K.7    Multhoff, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.