References
- Hendrick JP, Hartl FU. Molecular chaperone functions of heat-shock proteins. Ann Rev Biochem 1993; 62: 349–384
- Lin HY, Masso-Welch P, Di YP, Cai JW, Shen JW, Subjeck JR. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Mol Biol Cell 1993; 4: 1109–1119
- Chen X, Easton D, Oh HJ, Lee-Yoon DS, Liu X, Subjeck J. The 170 kDa glucose regulated stress protein is a large hsp70-, hsp110-like protein of the endoplasmic reticulum. FEBS Lett 1996; 380: 68–72
- Easton DP, Kaneko Y, Subjeck JR. The hsp110 and Grp1 70 stress proteins: Newly recognized relatives of the hsp70s. Cell Stress Chaperones 2000; 5: 276–290
- Shen J, Hughes C, Chao C, Cai J, Bartels C, Gessner T, Subjeck J. Coinduction of glucose-regulated proteins and doxorubicin resistance in Chinese hamster cells. Proc Natl Acad Sci USA 1987; 84: 3278–3282
- Cai JW, Henderson BW, Shen JW, Subjeck JR. Induction of glucose regulated proteins during growth of a murine tumor. J Cell Physiol 1993; 154: 229–237
- Kuznetsov G, Chen LB, Nigam SK. Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J Biol Chem 1997; 272: 3057–3063
- Dierks T, Volkmer J, Schlenstedt G, Jung C, Sandholzer U, Zachmann K, Schlotterhose P, Neifer K, Schmidt B, Zimmermann R. A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum. Embo J 1996; 15: 6931–6942
- Spee P, Subjeck J, Neefjes J. Identification of novel peptide binding proteins in the endoplasmic reticulum: ERp72, calnexin, and grp170. Biochemistry 1999; 38: 10559–10566
- Calderwood SK, Ciocca DR. Heat shock proteins: Stress proteins with Janus-like properties in cancer. Int J Hyperthermia 2008; 24: 31–39
- Parmiani G, De Filippo A, Pilla L, Castelli C, Rivoltini L. Heat shock proteins gp96 as immunogens in cancer patients. Int J Hyperthermia 2006; 22: 223–227
- Tamura Y, Peng P, Liu K, Daou M, Srivastava PK. Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations. Science 1997; 278: 117–120
- Park JE, Facciponte J, Chen X, MacDonald I, Repasky EA, Manjili MH, Wang XY, Subjeck JR. Chaperoning function of stress protein grp170, a member of the hsp70 superfamily, is responsible for its immunoadjuvant activity. Cancer Research 2006; 66: 1161–1168
- Wang XY, Chen X, Manjili MH, Repasky E, Henderson R, Subjeck JR. Targeted immunotherapy using reconstituted chaperone complexes of heat shock protein 110 and melanoma-associated antigen gp100. Cancer Res 2003; 63: 2553–2560
- Basu S, Srivastava PK. Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity. J Exp Med 1999; 189: 797–802
- Udono H, Srivastava PK. Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70. J Immunol 1994; 152: 5398–5403
- Singh-Jasuja H, Scherer HU, Hilf N, Arnold-Schild D, Rammensee H-G, Toes REM, Schild H. The heat shock protein gp96 induces maturation of dendritic cells and down-regulation of its receptor. Eur J Immunol 2000; 30: 2211–2215
- Calderwood SK, Theriault JR, Gong J. How is the immune reponse affected by hyperthermia and heat shock proteins?. Int J Hyperthermia 2005; 21: 713–716
- Facciponte JG, Wang XY, Subjeck JR. Hsp110 and Grp170, members of the hsp70 superfamily, bind to scavenger receptor-A and scavenger receptor expressed by endothelial cells-I. Eur J Immunol 2007; 37: 2268–2279
- Binder RJ, Han DK, Srivastava PK. CD91: A receptor for heat shock protein gp96. Nat Immunol 2000; 1: 151–155
- Asea A, Kraeft SK, Kurt-Jones EA, Stevenson MA, Chen LB, Finberg RW, Koo GC, Calderwood SK. Hsp70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 2000; 6: 435–442
- Basu S, Binder RJ, Suto R, Anderson KM, Srivastava PK. 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
- Multhoff G. Activation of natural killer cells by heat shock protein 70. Int J Hyperthermia 2009; 25: 169–175
- Hilf N, Singh-Jasuja H, Schild H. The heat shock protein Gp96 links innate and specific immunity. Int J Hyperthermia 2002; 18: 521–533
- Manjili MH, Wang X-Y, Park J, MacDonald IJ, Li Y, Van Schie RCAA, Subjeck JR. Cancer immunotherapy: Stress proteins and hyperthermia. Int J Hyperthermia 2002; 18: 506–520
- Wang X-Y, Li Y, Yang G, Subjeck JR. Current ideas about applications of heat shock proteins in vaccine design and immunotherapy. Int J Hyperthermia 2005; 21: 717–722
- Yamazaki K, Nguyen T, Podack ER. Cutting edge: Tumor secreted heat shock-fusion protein elicits CD8 cells for rejection. J Immunol 1999; 163: 5178–5182
- Baker-LePain JC, Sarzotti M, Fields TA, Li CY, Nicchitta CV. GRP94 (gp96) and GRP94 N-terminal geldanamycin binding domain elicit tissue nonrestricted tumor suppression. J Exp Med 2002; 196: 1447–1459
- Massa C, Guiducci C, Arioli I, Parenza M, Colombo MP, Melani C. Enhanced efficacy of tumor cell vaccines transfected with secretable hsp70. Cancer Res 2004; 64: 1502–1508
- Lewis MJ, Pelham HR. Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell 1992; 68: 353–364
- Munro S, Pelham HR. A C-terminal signal prevents secretion of luminal ER proteins. Cell 1987; 48: 899–907
- Southern PJ, Berg P. Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter. J Mol Appl Genet 1982; 1: 327–341
- Schumacher RJ, Hansen WJ, Freeman BC, Alnemri E, Litwack G, Toft DO. Cooperative action of hsp70, hsp90, and DnaJ proteins in protein renaturation. Biochemistry 1996; 35: 14889–14898
- Miyahira Y, Murata K, Rodriguez D, Rodriguez JR, Esteban M, Rodrigues MM, Zavala F. Quantification of antigen specific CD8+ T cells using an ELISPOT assay. J Immunol Methods 1995; 181: 45–54
- Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
- Wang X-Y, Arnouk H, Chen X, Kazim L, Repasky EA, Subjeck JR. Extracellular targeting of endoplasmic reticulum chaperone glucose-regulated protein 170 enhances tumor immunity to a poorly immunogenic melanoma. J Immunol, 2006; 177: 1543–1551
- Huang AY, Gulden PH, Woods AS, Thomas MC, Tong CD, Wang W, Engelhard VH, Pasternack G, Cotter R, Hunt D, et al. The immunodominant major histocompatibility complex class I-restricted antigen of a murine colon tumor derives from an endogenous retroviral gene product. Proc Natl Acad Sci USA 1996; 93: 9730–9735
- Park J, Easton DP, Chen X, MacDonald IJ, Wang XY, Subjeck JR. The chaperoning properties of mouse grp170, a member of the third family of hsp70 related proteins. Biochemistry 2003; 42: 14893–14902
- Golgher D, Korangy F, Gao B, Gorski K, Jaffee E, Edidin M, Pardoll DM, Elliott T. An immunodominant MHC class II-restricted tumor antigen is conformation dependent and binds to the endoplasmic reticulum chaperone, calreticulin. J Immunol 2001; 167: 147–155
- Arnold D, Faath S, Rammensee H, Schild H. Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96. J Exp Med 1995; 182: 885–889
- Beachy SH, Kisailus AJ, Repasky EA, Subjeck JR, Wang XY, Kazim AL. Engineering secretable forms of chaperones for immune modulation and vaccine Development. Methods 2007; 4: 184–193
- Nieland TJ, Tan MC, Monne-van Muijen M, Koning F, Kruisbeek AM, van Bleek GM. Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein GP96/GRP94. Proc Natl Acad Sci USA 1996; 93: 6135–6139
- Meng SD, Gao T, Gao GF, Tien P. HBV-specific peptide associated with heat-shock protein gp96. Lancet 2001; 357: 528–529
- Breloer M, Marti T, Fleischer B, von Bonin A. Isolation of processed, H–2Kb-binding ovalbumin-derived peptides associated with the stress proteins hsp70 and gp96. Eur J Immunol 1998; 28: 1016–1021
- Ishii T, Udono H, Yamano T, Ohta H, Uenaka A, Ono T, Hizuta A, Tanaka N, Srivastava PK, Nakayama E. Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96. J Immunol 1999; 162: 1303–1309
- Binder RJ, Kelly JB, III, Vatner RE, Srivastava PK. Specific immunogenicity of heat shock protein gp96 derives from chaperoned antigenic peptides and not from contaminating proteins. J Immunol 2007; 179: 7254–7261
- Kunisawa J, Shastri N. Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway. Immunity 2006; 24: 523–534
- Callahan MK, Garg M, Srivastava PK. Heat-shock protein 90 associates with N-terminal extended peptides and is required for direct and indirect antigen presentation. Proc Natl Acad Sci USA 2008; 105: 1662–1667