1. L.E. Hightower, Cultured animal cells exposed to amino acid analogues or puro-mycin rapidly synthesize several polypeptides, J. Cell Physiol. 102:401 (1980).
2. J. Anathan, A.L. Goldberg, and R. Voellmy, Abnormal proteins serve as eukary-otic stress signals and trigger the activation of heat shock genes, Science 232:252 (1986).
3. J. Lis, and C. Wu, Protein traffic on the heat shock promoter: parking, stalling, and trucking along, Cell. 74:1 (1993).
4. L. Sistonen, K.D. Sarge, B. Phillips, K. Abravaya, and R.I. Morimoto, Activation of heat shock factor 2 during hemin-induced differentiation of human erythroleuk-emia cells, Mol. Cell. Biol. 72:4104 (1992).
5. S.C. Lindquist, The heat shock response, Ann. Rev. Biochem. 55:1151 (1986).
6. W.J. Welch, Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease, Physiol. Rev. 72:1063 (1992).
7. W.B. Pratt, The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid recepto, J. Biol. Chem. 268:21455 (1993).
8. A.W. Yem, A G. Tomasselli, R. L. Heinrikson, H. Zurcher-Neely, V.A. Ruff, R.A. Johnson, and M.R. Deibel, Jr., The hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13, J. Biol. Chem. 267:2868 (1992).
9. E.R. Sanchez, Hsp56: A novel heat shock protein associated with untransformed steroid receptor complexes, J. Biol. Chem. 265:22067 (1990).
10. F.U. Hartl, J. Martin, and W. Neupert, Protein folding in the cell: the role of chap-erones hsp70 and hsp 60. Ann. Rev. Biophys. Biomol. Struct. 293 (1992).
11. C. Georgopoulos, and W.J. Welch, Role of the major heat shock proteins as molecular chaperones, Ann. Rev. Cell. Biol. 601 (1993).
12. T. Langer, G. Pfeifer, J. Martin, W. Baumeistere, and F.U. Hartl, Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accomodates the protein within its central cavity, EMBO J. 11:4757 (1992).
13. H. Kubota, G. Hynes, A. Canne, A. Ashworth, and K. Willison, Identification of six TCP-1 related genes encoding divergent subunits of the TCP-1 containing chaperonin, Curr. Biol. 4:89 (1994).
14. C.B. Anfinsen, Principles that govern the folding of protein chains, Science 8:223 (1973).
15. R.J. Ellis, and S.M. van der Vies, Molecular chaperones, Ann. Rev. Biochem. 321 (1991).
16. J.S. Brugge, Interaction of the Rous sarcoma Virus protein, pp60src, with the cellular proteins pp50 and pp90, Curr. Topics Microbiol. Immunol. 123:1 (1986).
17. D.F. Smith, and D.O. Toft, Steroid receptors and their associated proteins, Mol. Endocrinol. 7:4 (1993).
18. U. Jakob, M. Gaestel, K. Engel, and J. Buchner, Small heat shock proteins are molecular chaperones, J. Biol. Chem. 268:1517 (1993).
19. T. Miron, K. Vancompernnolle, J. Vandkerckhove, M. Wilchek, and B.A. Geiger, 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein, J. Cell Biol. 114:255 (1991).
20. J.N. Lavoie, G. Gingras-Breton, R.M. Tanguay, and J. Landry, Induction of Chinese hamster hsp27 gene expression in mouse cells confers resistance to heat shock; hsp 27 stabilization of the microfilament organization, J. Biol. Chem. 268:3420 (1993).
21. J.N. Lavoie, E. Hickey, L.A. Weber, and J. Landry, Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27, J. Biol. Chem. 268:24210 (1993).
22. K. Vass, M.L. Berger, T.S.J. Nowak, W.J. Welch, and H. Lassmann, Induction of stress protein Hsp 70 in nerve cells after status epilepticus in the rat, Neurosci. Lett. 100:259 (1989).
23. R.S. Sloviter, and D.H. Lowenstein, Heat shock protein expression in vulnerable cells of the rat hippocampus as an indicator of excitation-induced neuronal stress, J. Neurosci. 12:3004 (1992).
24. C.J. Delcayre, L. Samuel, F. Marotte, F. Best-Belpomme, J.J. Mercadier, and L. Rappaport, Synthesis of stress proteins in rat cardiac mycocytes 2-4 days after the imposition of hemodynamic overload, J. Clin. Invest. 85:460 (1988).
T.J. Donnelly, R.E. Sievers, F.L.J. Vissern, W.J. Welch, and C.L. Wolfe, Heat shock protein induction in rat hearts: a role for improved myocardial salvage after ischemia and reperfusion?, Circulation 85:769 (1992).
R.W. Currie, R.M. Tanguay, and J.G. Kingma, Heat shock response and limitation of tissue necrosis during occlusion/reperfusion in rabbit hearts, Circulation 87:963 (1993).
D. Yellon, M.E. Iliodromitis, D.S. Latchman, D.M. Van Winkle, J.M. Downey,
F.M. Williams, and T.J. Williams, Whole body heat stress fails to limit infarct size in the reperfused rabbit heart, Cardiovasc. Res. 26:342 (1992).
M.F. Barbe, M. Tytell, D.J. Gower, and W.J. Welch, Hyperthermia protects against light damage in the rat retina, Science 247:1817 (1988). J. Villar, J.D. Edelson, M. Post, B. Mullen, and A. Slutsky. Induction of heat stress proteins is associated with decreased mortality in an animal model of acute long injury, Am. Rev. Respir. Dis. 147:111 (1993).
W.J. Koenig, R.A. Lohner, G.A. Perdrizet, M.E. Lohner, R.T. Schweitzer, and V.L. Lewis, Jr, Improving acute skin-flap survival through stress conditioning using heat shock and recovery, Plast. Reconstuct. Surg. 90:659 (1992).
G.M. Hahn, and G.C. Li, Thermotolerance, thermoresistance, and thermosens-itization, Stress Proteins in Biology and Medicine (R.I. Morimoto, A. Tissieres, and
C. Georgopoulos, eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 79-100.
M.M. Gottesman, and I. Pastan, The multidrug transporter, a double-edged sword, J. Biol. Chem. 265:12163 (1988).
N. Hosokawa, K. Hirayoshi, A. Nakai, Y. Hosokawa, N. Marui, M. Yoshida, T. Sakai, H. Nishino, A. Aoike, K. Kawai, and K. Nagata, Flavonoids inhibit the expression of heat shock proteins, Cell Struct. Funct. 75:393 (1990). M.J. Blake, R. Udelsman, G.J. Feulner, D.D. Norton, and N.J. Holbrook, Stress induced heat shock protein 70 expression in adrenal cortex: an adrenocorticotropic hormone-sensitive, age-dependent response, Proc. Natl. Acad. Sci. USA. 88:9873 (1991).
R. Udelsman, M.J. Blake, and N.J. Holbrook, Molecular response to surgical stress: Specific and simultaneous heat shock protein induction in the adrenal cortex, aorta, and vena cava, Surgery 770:1125 (1991).
R. Udelsman, M.J. Blake, C.A. Stagg, D-G. Li, D.J. Putney, and N.J. Holbrook, Vascular heat shock protein expression in response to stress. Endocrine and autonomic regulation of this age-dependent response, J. Clin. Invest. 97:465 (1993). M.J. Blake, D.J. Buckley, and A.R. Buckley, Dopaminergic regulation of heat shock protein-70 expression in adrenal gland and aorta, Endocrinology 132:1063 (1993).
D.C. DeNagel, and S.K. Pierce, Heat shock proteins in immune responses, Crit. Rev. Immunol. 75:71 (1993).
S.G. Nadler, M.A. Tepper, B. Schacter, and C.E. Mazzucco, Interaction of the immunosuppressant Deoxyspergualin with a member of the hsp70 family of heat shock proteins, Science 258:484 (1992).
R.A. Young, and T.J. Elliot, Stress proteins, infection, and immune surveillance, Cell 59:5 (1989).
41. D.B. Young, Heat-shock proteins: immunity and autoimmunity, Curr. Opin. Immunol. 4:396 (1992).
42. W.M. Born, P. Happ, A. Dallas, C. Reardon, R. Kubo, T. Shinnick, P. Brennan, and R. O'Brien, Recognition of heat shock proteins and gamma/delta function, Immunol. Today 11 (1990).
43. G. Zhong, and R.C. Brunham, Antigenic analysis of the chlamydial 75-kilodaIton protein, Infect. Immun. 60:323 (1992).
44. S J. Blander, and M.A. Horwitz, Major cytoplasmic membrane protein of Legionella pneumophila, a genus common antigen and member of the hsp60 family of heat shock proteins, induces protective immunity in a guinea pig model of Legionnaire's disease, J. Clin. Invest. 91:111 (1993).
45. F.J. Gomez, A.M. Gomez, and G.S. Deepe, Jr., An 80-kilodalton antigen from Histoplasmia capsulatum that has homology to heat shock prtoein 70 induces cell-mediated immune responses and protection in mice. Infect. Immun. 60:2565 (1992).
46. P. Dubois, J.P. Dedet, T. Fandeur, C. Roussilhon, M. Jendoubi, S. Pauillac, O. Mercereau-Puijalon, and L. Pereira da Silva, Protective immunization of the squirrel monkey against asexual blood-stages of Plasmodium falciparum by use of parasite protein fractions, Proc. Natl. Acad. Sci. USA 81:229 (1984).
47. L. Renia, D. Mattei, J. Goma, S. Pied, P. Dubois, F. Miltgen, A. Nussler, H. Matile, F. Menegaux, M. Gentilini, and D. Mazier, A malaria heat-shock-like determinant expressed on the infected hepatocyte surface is the target of antibody dependent cell-mediated cytotoxic mechanisms by non-parenchymal liver cells, Eur. J. Immunol. 20:1445 (1990).
48. N.A. Buchmeier, and F. Heffron, Induction of Salmonella stress proteins upon infection of macrophages, Science 248:130 (1990).
49. M. Ensgraber, and M. Loos, A 66-kiIodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus, Infect. Immun. 60:3072 (1992).
50. R.P. Morrison, R.J. Belland, K. Lyng, and H.D. Caldwell, Chlamydial disease pathogenesis: the 57-kD chlamydial hypersensitivity antigen is a stress response protein, J. Exp. Med. 770:1271 (1989).
51. M-C. Shanafelt, P. Hindersson, C. Soderberg, N. Mensi, C.W. Turck, D. Webb, H. Yssel, and G. Peltz, T cell and antibody reactivity with the Borrelia burgdorferi 60 kDa heat shock protein in Lyme arthritis, J. Immunol. 146:3985 (1991).
52. S.H.E. Kaufmann, Heat shock proteins and autoimmunity: fact or fiction?, Curr. Biol. 1:359 (1991).
53. I.R. Cohen, Autoimmunity to chaperonins in the pathogenesis of arthritis and diabetes, Ann. Rev. Immunol. 567 (1991).
54. D.L. Kaufman, M. Clare-Salzer, J. Tian, T. Forsthuber, G.S.P. Ting, P. Robinson, M.A. Atkinson, E.E. Sercarz, A.J. Tobin, and P.V. Lehmann, Spontaneous loss of T-cell tolerance to glutamic acid decarboxylase in murine insulin-dependent diabetes, Nature 365:69 (1993).
55. R. Tisch, X-D. Yang, S.M. Singer, R.S. Liblau, L. Fugger, and H.O. McDevitt, Immune response to glutamic acid decarboxylase correlates with insulitis in non-obese diabetic mice, Nature 365:12 (1993).
56. E.R. De Graeff-Meeder, R. Van Der Zee, G.T. Rijkes, H-J. Schuurman, W. Kuis,
J.M.J. Bijlsma, B.J. M. Zegers, and W. Van Eden, Recognition of human 60 kD heat shock protein by mononuclear cells from patients with juvenile chronic arthritis, Lancet 337:1368 (1991).
57. Z. Li, and P.K. Srivastava, Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation. EMBOJ. 12:3143 (1993).
58. H. Udono, and P.K. Srivastava, Heat shock protein 70-associated peptides elicit specific cancer immunity, J. Exp. Med. 178:1391 (1993).
59. A.R. Lüssow, C. Barrios, J. van Embden, R. Van der Zee, A.S. Verdini, A. Pessi, J. A. Louis, P-H. Lambert, and G. Del Guidice, Mycobacterial heat-shock proteins as carrier molecules, Eur. J. Immunol. 21:2291 (1991).
60. C.A. Barrios, R. Lüssow, J. Van Embden, R. Van der Zee, R. Rappuoli, P. Constantino, J.A. Louis, P-H. Lambert, and G. Del Guidice, Mycobacterial heat shock proteins as carrier molecules. II: The use of the 70 kDa mycobacterial heat shock proteins as carrier for conjugated vaccines can circumvent the need for adjuvants and Bacillus Calmette Guerin priming, Eur. J. Immunol. 22:1365 (1992).
61. W.J. Welch, How cells respond to stress, Sei. Am. 268:56 (1993).
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