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Volumn 288, Issue 4, 2013, Pages 2756-2766

Toll-like receptor agonists and febrile range hyperthermia synergize to induce heat shock protein 70 expression and extracellular release

Author keywords

[No Author keywords available]

Indexed keywords

CELL-FREE; CORE TEMPERATURE; EXTRACELLULAR; GENE MODIFICATION; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HISTONE H3; HSP70 EXPRESSION; INTRATRACHEAL; LUNG TISSUE; MAP KINASE; P38 MAPK; PATHWAY INHIBITORS; PRE-TREATMENT; RAW CELLS; TOLL-LIKE RECEPTOR 4; TOLL-LIKE RECEPTORS;

EID: 84873834308     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.427336     Document Type: Article
Times cited : (62)

References (75)
  • 1
    • 38549180598 scopus 로고    scopus 로고
    • The immunology of sepsis
    • Sriskandan, S., and Altmann, D. M. (2008) The immunology of sepsis. J. Pathol. 214, 211-223
    • (2008) J. Pathol. , vol.214 , pp. 211-223
    • Sriskandan, S.1    Altmann, D.M.2
  • 2
    • 33845951211 scopus 로고    scopus 로고
    • DAMPs, PAMPs and alarmins. All we need to know about danger
    • Bianchi, M. E. (2007) DAMPs, PAMPs and alarmins. All we need to know about danger. J. Leukocyte Biol. 81, 1-5
    • (2007) J. Leukocyte Biol. , vol.81 , pp. 1-5
    • Bianchi, M.E.1
  • 4
    • 0141998606 scopus 로고    scopus 로고
    • Molecular identification of a danger signal that alerts the immune system to dying cells
    • Shi, Y., Evans, J. E., and Rock, K. L. (2003) Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 425, 516-521
    • (2003) Nature , vol.425 , pp. 516-521
    • Shi, Y.1    Evans, J.E.2    Rock, K.L.3
  • 6
    • 0034650427 scopus 로고    scopus 로고
    • Cutting edge. Heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor- 4 complex
    • Ohashi, K., Burkart, V., Flohé, S., and Kolb, H. (2000) Cutting edge. Heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor- 4 complex. J. Immunol. 164, 558-561
    • (2000) J. Immunol. , vol.164 , pp. 558-561
    • Ohashi, K.1    Burkart, V.2    Flohé, S.3    Kolb, H.4
  • 7
    • 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., and Calderwood, S. K. (2002) Novel signal transduction pathway utilized by extracellular HSP70. Role of Toll-like receptor (TLR) 2 and TLR4. J. Biol. Chem. 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
  • 12
    • 33750819353 scopus 로고    scopus 로고
    • Extracellular heat shock protein-70 induces endotoxin tolerance in THP-1 cells
    • Aneja, R., Odoms, K., Dunsmore, K., Shanley, T. P., and Wong, H. R. (2006) Extracellular heat shock protein-70 induces endotoxin tolerance in THP-1 cells. J. Immunol. 177, 7184-7192
    • (2006) J. Immunol. , vol.177 , pp. 7184-7192
    • Aneja, R.1    Odoms, K.2    Dunsmore, K.3    Shanley, T.P.4    Wong, H.R.5
  • 18
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
    • Pirkkala, L., Nykänen, P., and Sistonen, L. (2001) Roles of the heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J. 15, 1118-1131
    • (2001) FASEB J. , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykänen, P.2    Sistonen, L.3
  • 19
    • 0027522356 scopus 로고
    • Cells in stress. Transcriptional activation of heat shock genes
    • Morimoto, R. I. (1993) Cells in stress. Transcriptional activation of heat shock genes. Science 259, 1409-1410
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, R.I.1
  • 20
    • 0036160052 scopus 로고    scopus 로고
    • Heat shock factor 1 and heat shock proteins. Critical partners in protection against acute cell injury
    • Christians, E. S., Yan, L. J., and Benjamin, I. J. (2002) Heat shock factor 1 and heat shock proteins. Critical partners in protection against acute cell injury. Crit. Care Med 30, S43-50
    • (2002) Crit. Care Med , vol.30
    • Christians, E.S.1    Yan, L.J.2    Benjamin, I.J.3
  • 22
    • 0033555548 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription-1 and heat shock factor-1 interact and activate the transcription of the Hsp-70 and Hsp-90β gene promoters
    • Stephanou, A., Isenberg, D. A., Nakajima, K., and Latchman, D. S. (1999) Signal transducer and activator of transcription-1 and heat shock factor-1 interact and activate the transcription of the Hsp-70 and Hsp-90β gene promoters. J. Biol. Chem. 274, 1723-1728
    • (1999) J. Biol. Chem. , vol.274 , pp. 1723-1728
    • Stephanou, A.1    Isenberg, D.A.2    Nakajima, K.3    Latchman, D.S.4
  • 23
    • 0032519758 scopus 로고    scopus 로고
    • The nuclear factor interleukin-6 (NF-IL6) and signal transducer and activator of transcription-3 (STAT-3) signalling pathways cooperate to mediate the activation of the hsp90β gene by interleukin-6 but have opposite effects on its inducibility by heat shock
    • Stephanou, A., Isenberg, D. A., Akira, S., Kishimoto, T., and Latchman, D. S. (1998) The nuclear factor interleukin-6 (NF-IL6) and signal transducer and activator of transcription-3 (STAT-3) signalling pathways cooperate to mediate the activation of the hsp90β gene by interleukin-6 but have opposite effects on its inducibility by heat shock. Biochem. J. 330, 189-195
    • (1998) Biochem. J. , vol.330 , pp. 189-195
    • Stephanou, A.1    Isenberg, D.A.2    Akira, S.3    Kishimoto, T.4    Latchman, D.S.5
  • 25
    • 84859926202 scopus 로고    scopus 로고
    • Tonicity enhancer binding protein (TonEBP) and hypoxia-inducible factor (HIF) coordinate heat shock protein 70 (Hsp70) expression in hypoxic nucleus pulposus cells Role of Hsp70 in HIF-1α degradation
    • Gogate, S. S., Fujita, N., Skubutyte, R., Shapiro, I. M., and Risbud, M. V. (2012) Tonicity enhancer binding protein (TonEBP) and hypoxia-inducible factor (HIF) coordinate heat shock protein 70 (Hsp70) expression in hypoxic nucleus pulposus cells. Role of Hsp70 in HIF-1α degradation. J. Bone Miner Res. 27, 1106-1117
    • (2012) J Bone Miner Res , vol.27 , pp. 1106-1117
    • Gogate, S.S.1    Fujita, N.2    Skubutyte, R.3    Shapiro, I.M.4    Risbud, M.V.5
  • 26
    • 79956295821 scopus 로고    scopus 로고
    • Identification of a NF-κB cardioprotective gene program. NF-κB regulation of Hsp70.1 contributes to cardioprotection after permanent coronary occlusion
    • Wilhide, M. E., Tranter, M., Ren, X., Chen, J., Sartor, M. A., Medvedovic, M., and Jones, W. K. (2011) Identification of a NF-κB cardioprotective gene program. NF-κB regulation of Hsp70.1 contributes to cardioprotection after permanent coronary occlusion. J. Mol. Cell Cardiol. 51, 82-89
    • (2011) J. Mol. Cell Cardiol. , vol.51 , pp. 82-89
    • Wilhide, M.E.1    Tranter, M.2    Ren, X.3    Chen, J.4    Sartor, M.A.5    Medvedovic, M.6    Jones, W.K.7
  • 27
    • 77950863008 scopus 로고    scopus 로고
    • Hyperthermia in the febrile range induces HSP72 expression proportional to exposure temperature but not to HSF-1 DNA-binding activity in human lung epithelial A549 cells
    • Tulapurkar, M. E., Asiegbu, B. E., Singh, I. S., and Hasday, J. D. (2009) Hyperthermia in the febrile range induces HSP72 expression proportional to exposure temperature but not to HSF-1 DNA-binding activity in human lung epithelial A549 cells. Cell Stress Chaperones 14, 499-508
    • (2009) Cell Stress Chaperones , vol.14 , pp. 499-508
    • Tulapurkar, M.E.1    Asiegbu, B.E.2    Singh, I.S.3    Hasday, J.D.4
  • 28
    • 0025095784 scopus 로고
    • Structure and expression of the three MHC-linked HSP70 genes
    • Milner, C. M., and Campbell, R. D. (1990) Structure and expression of the three MHC-linked HSP70 genes. Immunogenetics 32, 242-251
    • (1990) Immunogenetics , vol.32 , pp. 242-251
    • Milner, C.M.1    Campbell, R.D.2
  • 29
    • 0026033354 scopus 로고
    • Expression of a heat-inducible gene of the HSP70 family in human myelomonocytic cells. Regulation by bacterial products and cytokines
    • Fincato, G., Polentarutti, N., Sica, A., Mantovani, A., and Colotta, F. (1991) Expression of a heat-inducible gene of the HSP70 family in human myelomonocytic cells. Regulation by bacterial products and cytokines. Blood 77, 579-586
    • (1991) Blood , vol.77 , pp. 579-586
    • Fincato, G.1    Polentarutti, N.2    Sica, A.3    Mantovani, A.4    Colotta, F.5
  • 30
    • 0027953899 scopus 로고
    • In vivo production of heat shock protein in mouse peritoneal macrophages by administration of lipopolysaccharide
    • Zhang, Y. H., Takahashi, K., Jiang, G. Z., Zhang, X. M., Kawai, M., Fukada, M., and Yokochi, T. (1994) In vivo production of heat shock protein in mouse peritoneal macrophages by administration of lipopolysaccharide. Infect. Immun. 62, 4140-4144
    • (1994) Infect. Immun. , vol.62 , pp. 4140-4144
    • Zhang, Y.H.1    Takahashi, K.2    Jiang, G.Z.3    Zhang, X.M.4    Kawai, M.5    Fukada, M.6    Yokochi, T.7
  • 31
    • 0032766562 scopus 로고    scopus 로고
    • Fever in the intensive care unit
    • Cunha, B. A. (1999) Fever in the intensive care unit. Intensive Care Med. 25, 648-651
    • (1999) Intensive Care Med. , vol.25 , pp. 648-651
    • Cunha, B.A.1
  • 32
    • 0028031497 scopus 로고
    • Endotoxemia and bacteremia in patients with sepsis syndrome in the intensive care unit
    • Guidet, B., Barakett, V., Vassal, T., Petit, J. C., and Offenstadt, G. (1994) Endotoxemia and bacteremia in patients with sepsis syndrome in the intensive care unit. Chest 106, 1194-1201
    • (1994) Chest , vol.106 , pp. 1194-1201
    • Guidet, B.1    Barakett, V.2    Vassal, T.3    Petit, J.C.4    Offenstadt, G.5
  • 33
    • 80054086275 scopus 로고    scopus 로고
    • Prolonged exposure to hyperthermic stress augments neutrophil recruitment to lung during the post-exposure recovery period
    • Tulapurkar, M. E., Hasday, J. D., and Singh, I. S. (2011) Prolonged exposure to hyperthermic stress augments neutrophil recruitment to lung during the post-exposure recovery period. Int. J. Hyperthermia 27, 717-725
    • (2011) Int. J. Hyperthermia , vol.27 , pp. 717-725
    • Tulapurkar, M.E.1    Hasday, J.D.2    Singh, I.S.3
  • 34
    • 79958717888 scopus 로고    scopus 로고
    • Response of mice to continuous 5-day passive hyperthermia resembles human heat acclimation
    • Sareh, H., Tulapurkar, M. E., Shah, N. G., Singh, I. S., and Hasday, J. D. (2011) Response of mice to continuous 5-day passive hyperthermia resembles human heat acclimation. Cell Stress Chaperones 16, 297-307
    • (2011) Cell Stress Chaperones , vol.16 , pp. 297-307
    • Sareh, H.1    Tulapurkar, M.E.2    Shah, N.G.3    Singh, I.S.4    Hasday, J.D.5
  • 36
    • 73549123428 scopus 로고    scopus 로고
    • Febrile-range temperature modifies cytokine gene expression in LPS-stimulated macrophages by differentially modifying NF-κB recruitment to cytokine gene promoters
    • Cooper, Z. A., Ghosh, A., Gupta, A., Maity, T., Benjamin, I. J., Vogel, S. N., Hasday, J. D., and Singh, I. S. (2010) Febrile-range temperature modifies cytokine gene expression in LPS-stimulated macrophages by differentially modifying NF-κB recruitment to cytokine gene promoters. Am. J. Physiol. Cell Physiol. 298, C171-C181
    • (2010) Am. J. Physiol. Cell Physiol. , Issue.298
    • Cooper, Z.A.1    Ghosh, A.2    Gupta, A.3    Maity, T.4    Benjamin, I.J.5    Vogel, S.N.6    Hasday, J.D.7    Singh, I.S.8
  • 38
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts,' prepared from a small number of cells
    • Schreiber, E., Matthias, P., Müller, M. M., and Schaffner, W. (1989) Rapid detection of octamer binding proteins with 'mini-extracts,' prepared from a small number of cells. Nucleic Acids Res. 17, 6419
    • (1989) Nucleic Acids Res , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Müller, M.M.3    Schaffner, W.4
  • 39
    • 0037085476 scopus 로고    scopus 로고
    • A high affinity HSF-1 binding site in the 5'-untranslated region of the murine tumor necrosis factor-α gene is a transcriptional repressor
    • Singh, I. S., He, J. R., Calderwood, S., and Hasday, J. D. (2002) A high affinity HSF-1 binding site in the 5'-untranslated region of the murine tumor necrosis factor-α gene is a transcriptional repressor. J. Biol. Chem. 277, 4981-4988
    • (2002) J. Biol. Chem. , vol.277 , pp. 4981-4988
    • Singh, I.S.1    He, J.R.2    Calderwood, S.3    Hasday, J.D.4
  • 40
    • 0034737461 scopus 로고    scopus 로고
    • Inhibition of tumor necrosis factor-α transcription in macrophages exposed to febrile range temperature. A possible role for heat shock factor-1 as a negative transcriptional regulator
    • Singh, I. S., Viscardi, R. M., Kalvakolanu, I., Calderwood, S., and Hasday, J. D. (2000) Inhibition of tumor necrosis factor-α transcription in macrophages exposed to febrile range temperature. A possible role for heat shock factor-1 as a negative transcriptional regulator. J. Biol. Chem. 275, 9841-9848
    • (2000) J. Biol. Chem. , vol.275 , pp. 9841-9848
    • Singh, I.S.1    Viscardi, R.M.2    Kalvakolanu, I.3    Calderwood, S.4    Hasday, J.D.5
  • 41
    • 79952070673 scopus 로고    scopus 로고
    • Distinct, gene-specific effect of heat shock on heat shock factor-1 recruitment and gene expression ofCXCchemokine genes
    • Maity, T. K., Henry, M. M., Tulapurkar, M. E., Shah, N. G., Hasday, J. D., and Singh, I. S. (2011) Distinct, gene-specific effect of heat shock on heat shock factor-1 recruitment and gene expression ofCXCchemokine genes. Cytokine 54, 61-67
    • (2011) Cytokine , vol.54 , pp. 61-67
    • Maity, T.K.1    Henry, M.M.2    Tulapurkar, M.E.3    Shah, N.G.4    Hasday, J.D.5    Singh, I.S.6
  • 42
    • 4344592639 scopus 로고    scopus 로고
    • Distinct stimulus-specific histone modifications at Hsp70 chromatin targeted by the transcription factor heat shock factor-1
    • Thomson, S., Hollis, A., Hazzalin, C. A., and Mahadevan, L. C. (2004) Distinct stimulus-specific histone modifications at Hsp70 chromatin targeted by the transcription factor heat shock factor-1. Mol. Cell 15, 585-594
    • (2004) Mol. Cell , vol.15 , pp. 585-594
    • Thomson, S.1    Hollis, A.2    Hazzalin, C.A.3    Mahadevan, L.C.4
  • 44
    • 0036735155 scopus 로고    scopus 로고
    • Variable expression of Toll-like receptor in murine innate and adaptive immune cell lines
    • Applequist, S. E., Wallin, R. P., and Ljunggren, H. G. (2002) Variable expression of Toll-like receptor in murine innate and adaptive immune cell lines. Int. Immunol. 14, 1065-1074
    • (2002) Int. Immunol. , vol.14 , pp. 1065-1074
    • Applequist, S.E.1    Wallin, R.P.2    Ljunggren, H.G.3
  • 45
    • 0028817029 scopus 로고
    • Warming macrophages to febrile range destabilizes tumor necrosis factor-α mRNA without inducing heat shock
    • Ensor, J. E., Crawford, E. K., and Hasday, J. D. (1995) Warming macrophages to febrile range destabilizes tumor necrosis factor-α mRNA without inducing heat shock. Am. J. Physiol. 269, C1140-C1146
    • (1995) Am. J. Physiol. , vol.269
    • Ensor, J.E.1    Crawford, E.K.2    Hasday, J.D.3
  • 46
    • 2142762520 scopus 로고    scopus 로고
    • TLRs. Differential adapter utilization by Toll-like receptors mediates TLR-specific patterns of gene expression
    • Vogel, S. N., Fitzgerald, K. A., and Fenton, M. J. (2003) TLRs. Differential adapter utilization by Toll-like receptors mediates TLR-specific patterns of gene expression. Mol. Interv. 3, 466-477
    • (2003) Mol. Interv. , vol.3 , pp. 466-477
    • Vogel, S.N.1    Fitzgerald, K.A.2    Fenton, M.J.3
  • 48
    • 18244384703 scopus 로고    scopus 로고
    • Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress
    • Guettouche, T., Boellmann, F., Lane, W. S., and Voellmy, R. (2005) Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress. BMC Biochem. 6, 4
    • (2005) BMC Biochem , vol.6 , pp. 4
    • Guettouche, T.1    Boellmann, F.2    Lane, W.S.3    Voellmy, R.4
  • 50
    • 3042855318 scopus 로고    scopus 로고
    • Bacterial endotoxin modifies heat shock factor-1 activity in RAW 264.7 cells. Implications for TNF-α regulation during exposure to febrile range temperatures
    • Singh, I. S., He, J. R., Hester, L., Fenton, M. J., and Hasday, J. D. (2004) Bacterial endotoxin modifies heat shock factor-1 activity in RAW 264.7 cells. Implications for TNF-α regulation during exposure to febrile range temperatures. J. Endotoxin Res. 10, 175-184
    • (2004) J. Endotoxin Res. , vol.10 , pp. 175-184
    • Singh, I.S.1    He, J.R.2    Hester, L.3    Fenton, M.J.4    Hasday, J.D.5
  • 51
    • 0028822276 scopus 로고
    • HSF access to heat shock elements in vivo depends critically on promoter architecture defined by GAGA factor, TFIID, and RNA polymerase II binding sites
    • Shopland, L. S., Hirayoshi, K., Fernandes, M., and Lis, J. T. (1995) HSF access to heat shock elements in vivo depends critically on promoter architecture defined by GAGA factor, TFIID, and RNA polymerase II binding sites. Genes Dev. 9, 2756-2769
    • (1995) Genes Dev. , vol.9 , pp. 2756-2769
    • Shopland, L.S.1    Hirayoshi, K.2    Fernandes, M.3    Lis, J.T.4
  • 52
    • 35948954744 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 at Ser10 facilitates RNA polymerase II release from promoterproximal pausing in Drosophila
    • Ivaldi, M. S., Karam, C. S., and Corces, V. G. (2007) Phosphorylation of histone H3 at Ser10 facilitates RNA polymerase II release from promoterproximal pausing in Drosophila. Genes Dev. 21, 2818-2831
    • (2007) Genes Dev. , vol.21 , pp. 2818-2831
    • Ivaldi, M.S.1    Karam, C.S.2    Corces, V.G.3
  • 53
    • 78049440475 scopus 로고    scopus 로고
    • Chromatin landscape dictates HSF binding to target DNA elements
    • Guertin, M. J., and Lis, J. T. (2010) Chromatin landscape dictates HSF binding to target DNA elements. PLoS Genet 6, 1001114
    • (2010) PLoS Genet , vol.6 , pp. 1001114
    • Guertin, M.J.1    Lis, J.T.2
  • 54
    • 21044446502 scopus 로고    scopus 로고
    • Heat shock, histone H3 phosphorylation and the cell cycle
    • Dyson, M. H., Thomson, S., and Mahadevan, L. C. (2005) Heat shock, histone H3 phosphorylation and the cell cycle. Cell Cycle 4, 13-17
    • (2005) Cell Cycle , vol.4 , pp. 13-17
    • Dyson, M.H.1    Thomson, S.2    Mahadevan, L.C.3
  • 55
    • 84873816845 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 56
    • 1842714965 scopus 로고    scopus 로고
    • Suppression of cadmium-induced JNK/p38 activation and HSP70 family gene expression by LL-Z1640-2 in NIH3T3 cells
    • Sugisawa, N., Matsuoka, M., Okuno, T., and Igisu, H. (2004) Suppression of cadmium-induced JNK/p38 activation and HSP70 family gene expression by LL-Z1640-2 in NIH3T3 cells. Toxicol. Appl. Pharmacol. 196, 206-214
    • (2004) Toxicol. Appl. Pharmacol. , vol.196 , pp. 206-214
    • Sugisawa, N.1    Matsuoka, M.2    Okuno, T.3    Igisu, H.4
  • 57
    • 33646401110 scopus 로고    scopus 로고
    • Extracellular pH changes activate the p38-MAPK signalling pathway in the amphibian heart
    • Stathopoulou, K., Gaitanaki, C., and Beis, I. (2006) Extracellular pH changes activate the p38-MAPK signalling pathway in the amphibian heart. J. Exp. Biol. 209, 1344-1354
    • (2006) J. Exp. Biol. , vol.209 , pp. 1344-1354
    • Stathopoulou, K.1    Gaitanaki, C.2    Beis, I.3
  • 58
    • 0032479983 scopus 로고    scopus 로고
    • Mitogenand stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • Deak, M., Clifton, A. D., Lucocq, L. M., and Alessi, D. R. (1998) Mitogenand stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 17, 4426-4441
    • (1998) EMBO J. , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, L.M.3    Alessi, D.R.4
  • 59
    • 0041975981 scopus 로고    scopus 로고
    • MSK1 and MSK2 mediate mitogen- and stress-induced phosphorylation of histone H3. A controversy resolved
    • Davie, J. R. (2003) MSK1 and MSK2 mediate mitogen- and stress-induced phosphorylation of histone H3. A controversy resolved. Sci. STKE 2003, PE33
    • (2003) Sci. STKE , vol.2003
    • Davie, J.R.1
  • 64
    • 78549289516 scopus 로고    scopus 로고
    • Posttranslational modifications in histones underlie heat acclimation-mediated cytoprotective memory
    • Tetievsky, A., and Horowitz, M. (2010) Posttranslational modifications in histones underlie heat acclimation-mediated cytoprotective memory. J. Appl. Physiol. 109, 1552-1561
    • (2010) J. Appl. Physiol. , vol.109 , pp. 1552-1561
    • Tetievsky, A.1    Horowitz, M.2
  • 66
    • 15444381172 scopus 로고    scopus 로고
    • A central role for the Hsp90.Cdc37 molecular chaperone module in interleukin-1 receptor-associated- kinase-dependent signaling by Toll-like receptors
    • De Nardo, D., Masendycz, P., Ho, S., Cross, M., Fleetwood, A. J., Reynolds, E. C., Hamilton, J. A., and Scholz, G. M. (2005) A central role for the Hsp90.Cdc37 molecular chaperone module in interleukin-1 receptor-associated- kinase-dependent signaling by Toll-like receptors. J. Biol. Chem. 280, 9813-9822
    • (2005) J. Biol. Chem. , vol.280 , pp. 9813-9822
    • De Nardo, D.1    Masendycz, P.2    Ho, S.3    Cross, M.4    Fleetwood, A.J.5    Reynolds, E.C.6    Hamilton, J.A.7    Scholz, G.M.8
  • 67
    • 0037414787 scopus 로고    scopus 로고
    • Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor α release by murine macrophages
    • Gao, B., and Tsan, M. F. (2003) Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor α release by murine macrophages. J. Biol. Chem. 278, 174-179
    • (2003) J. Biol. Chem. , vol.278 , pp. 174-179
    • Gao, B.1    Tsan, M.F.2
  • 68
    • 67149133632 scopus 로고    scopus 로고
    • Heat shock proteins and immune system
    • Tsan, M. F., and Gao, B. (2009) Heat shock proteins and immune system. J. Leukocyte Biol. 85, 905-910
    • (2009) J. Leukocyte Biol. , vol.85 , pp. 905-910
    • Tsan, M.F.1    Gao, B.2
  • 69
    • 39349110899 scopus 로고    scopus 로고
    • Heat shock proteins and Toll-like receptors
    • Asea, A. (2008) Heat shock proteins and Toll-like receptors. Handb. Exp. Pharmacol. 183, 111-127
    • (2008) Handb. Exp. Pharmacol. , vol.183 , pp. 111-127
    • Asea, A.1
  • 70
    • 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., and Srivastava, P. K. (2001) CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 14, 303-313
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 71
    • 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., Rodríguez-Silva, M., Frey, T., Gehrmann, M., Diaz, J. C., Steinem, C., Multhoff, G., Arispe, N., and De Maio, A. (2008) 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. 180, 4299-4307
    • (2008) J. Immunol. , vol.180 , pp. 4299-4307
    • Vega, V.L.1    Rodríguez-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
  • 72
    • 32644441610 scopus 로고    scopus 로고
    • Exogenous heat shock protein 70 binds macrophage lipid raft microdomain and stimulates phagocytosis, processing, and MHC-II presentation of antigens
    • Wang, R., Kovalchin, J. T., Muhlenkamp, P., and Chandawarkar, R. Y. (2006) Exogenous heat shock protein 70 binds macrophage lipid raft microdomain and stimulates phagocytosis, processing, and MHC-II presentation of antigens. Blood 107, 1636-1642
    • (2006) Blood , vol.107 , pp. 1636-1642
    • Wang, R.1    Kovalchin, J.T.2    Muhlenkamp, P.3    Chandawarkar, R.Y.4
  • 73
    • 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., and Multhoff, G. (2004) The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells. J. Immunol. 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
  • 74
    • 73649084415 scopus 로고    scopus 로고
    • Chaperokine function of recombinant Hsp72 produced in insect cells using a baculovirus expression system is retained
    • Zheng, H., Nagaraja, G. M., Kaur, P., Asea, E. E., and Asea, A. (2010) Chaperokine function of recombinant Hsp72 produced in insect cells using a baculovirus expression system is retained. J. Biol. Chem. 285, 349-356
    • (2010) J. Biol. Chem. , vol.285 , pp. 349-356
    • Zheng, H.1    Nagaraja, G.M.2    Kaur, P.3    Asea, E.E.4    Asea, A.5
  • 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., and McQuade, K. L. (1998) Heat shock proteins come of age. Primitive functions acquire new roles in an adaptive world. Immunity 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.