Heat shock proteins – an important component of immune response


Authors: M. Remáková;  P. Novota
Authors‘ workplace: Revmatologický ústav Praha
Published in: Čes. Revmatol., 17, 2009, No. 4, p. 206-212.
Category: Overview Reports

Overview

Autoimmune diseases affect approximately 5–7% of the human population. They are characterized by the ability to distinguish and destroy self cells, tissues and organs. The genes of the major histocompatibility complex (MHC) belong to the most important genes which are associated with the development of autoimmune diseases. The function of MHC class I/II molecules in the development of autoimmune diseases has been well documented recently, whereas the impact of other MHC genes has not been sufficiently studied yet. An area of approximately 150 “non class I/II MHC genes” belongs to the group of MHC genes as well. These genes are predominantly involved in immune and inflammatory response of the organism, and thus represent an interesting subject in association with the development of autoimmune diseases. Three genes for heat shock proteins (HSP) of 70kDa in size are localized in this part of MHC, between the genes of class I and II. Experimental and clinical trials confirmed that HSP are involved in the regulation of some autoimmune diseases. Their high evolutionary conservation, significant role in intracellular processes, as well as inducibility of their expression during cellular stress highlight their significant role in homeostatic maintenance. This report describes the role of these molecules in etiopathogenesis of autoimmune diseases.

Key words:
autoimmunity, major histocompatibility complex (MHC), risk factor, heat shock protein (HSP)


Sources

1. Sargent CA, Dunham I, Trowsdale J, Campbell RD. Human major histocompatibility complex contains genes for the major heat shock HSP70. Proc Natl Acad Sci USA 1989; 86: 1968–72.

2. Lie BA, Thorsby E. Several genes in the extended human MHC contribute to predisposition to autoimmune diseases. Current Opinion in Immunology 2005; 17: 526–31.

3. Udono H, Ichiyanagi T, Mizukami S, Imai T. Heat shock protein in antigen trafficking – Implications on antigen presentation to T cells. International Journal of Hyperthermia 2009; 1-9.

4. Hickman-Miller H, Hildebrand WH. The immune response under stress: the role of Hsp-derived peptides. Trends in Immunology 2004; 25: 427–33.

5. Schmid D, Münz C. Immune surveillance of intracellular pathogens via autophagy. Cell Death and Differentiation 2005; 12: 1519–27.

6. Rock KL. Exiting the outside world for cross presentation. Immunity 2006; 25: 523-25.

7. Creswell P, Ackerman AL, Giodini A, Peaper DR, Wearsch PA. Mechanisms of MHC class I-restricted antigen processing and cross-presentation. Immunol Rev 2005, 207: 145–57.

8. Lindquist S, Craig EA. The heat-shock proteins. Annu Rev Genet 1988; 22: 631–37.

9. Weigl E, Kopeček P, Raška M, Hradilová Š. Heat shock proteins in immune reactions. Folia Microbiologica 1999; 44: 561–6.

10. Tavaria M, Gabriele T, Kola I, Anderson RL. A hitchhiker’s guide to the human Hsp70 family. Cell Stress Chaperones 1996; 1: 23–8.

11. Milner C, Campbell RD. Structure and expression of the three MHC-linked Hsp70 genes. Immunogenetics. 1990; 32: 242–51.

12. Prodromou C, Roe SM, O’Brien R, Ladbury JF, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 1997; 90: 65–75.

13. Gidalevitz T, Biswas C, Diag H, Schneidman-Duhovny D, Wolfson HJ, Stevens F, et al. Identification of the N-terminal peptide binding site of glukose-regulated protein 94. J Biol Chem 2004; 279: 16543–52.

14. Harris SF, Shiau AK, Agard DA. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 2004; 12: 1087–97.

15. Bertelsen EB, Zhou H, Lowry DF, Flynn GC, Dahlquist FW. Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution. Protein Sci 1999; 8: 343-54.

16. Jiang J, Prasad K, Lafer EM, Sousa R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol Cell 2005; 20: 513–24.

17. Zhu X, Zhao X, Burkholder WF, Gragerov A, Ogata CM, Gottesman ME. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 1996; 272: 1606–14.

18. Stevens SY, Cai S, Pellecchia M, Zuiderweg ER. The solution structure of the bacterial Hsp70 chaperone protein domain DnaK(393–507) in complex with the peptide NRLLLTG. Protein Sci 2003; 12: 2588–96.

19. Pinhasi-Kimhi O, Michalovitz D, Ben-Zeev A, Oren M. Specific interaction between the p53 cellular tumour antigen and major heat shock proteins. Nature. 1986; 320: 182–4.

20. Becker J, Craig EA. Heat-shock proteins as molecular chaperones. Eur J Biochem 1994; 219: 11–23.

21. Javid B, MacAry PA, Lehner PJ. Structure and function: heat shock proteins and adaptive immunity. The Journal of Immunology. 2007; 179: 2035–40.

22. Blond-Elguindi S, Cwirla SE, Dower WJ, Lipshutz RJ, Sprang SR, Sambrook JF. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 1993; 75: 717–28.

23. Moseley P. Stress proteins and the immune response. Immunopharmacology 2000; 48: 299–302.

24. Basu S, Binder RJ, Ramalingam T, Srivastava PK. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70 and calreticulin. Immunity 2001; 14: 303–13.

25. van Eden W, van der Zee R, Prakken B. Heat shock proteins induce T-cell regulation of chronic inflammation. Nat Rev Immunol 2005; 5: 318–30.

26. Granja C, Moliterno RA, Ferreira MS, Fonseca JA, Kalil J, Coelho V. T-cell autoreactivity to Hsp in human transplantation may involve both proinflammatory and regulatory functions. Hum Immunol 2004; 65: 124–34.

27. Flohe SB, Bruggemann J, Lendemans S, Nikulina M, Meierhoff G, Flohe S, et al. Human heat shock protein 60 induces maturation of dendritic cells versus a Th1-promoting phenotype. J Immunol 2003; 170: 2340–8.

28. Moudgil KD, Durai M. Regulation of autoimmune arthritis by self-heatshock proteins. Trends Immunol 2008; 29: 412–18.

29. Perschinka H, Mayr M, Millonig G, Mayerl C, van der Zee R, Morrison SG, et al. Cross-reactive B-cell epitopes of microbial and human heat shock protein 60/65 in atherosclerosis. Arterioscler Thromb Vasc Biol 2003; 23: 1060–5.

30. Alard JE, Dueymes M, Youinou P, Jamin C. Modulation of endothelial cell damages by anti-Hsp60 autoantibodies in systemic autoimmune diseases. Autoimmun Rev 2007; 6: 438–43.

31. Cohen IR. The cognitive paradigm and the imunological homunculus. Immunol Today. 1992; 13: 490-4.

32. Horváth L, Czirják L, Fekete B, Jakab L, Prohászka Z, Cervenak L, et al. Levels of antibodies against C1q and 60 kDa family of heat shock proteins in the sera of patients with various autoimmune diseases. Immunology Letters 2001; 75: 103–9.

33. Hirata D, Hirai I, Iwamoto M, Yoshio T, Takeda A, Masuyama JI, et al. Preferential binding with Escherichia coli hsp60 of antibodies prelevant in sera from patients with rheumatoid arthritis. Clin Immunol Immunopathol 1997; 82: 141–8.

34. Ozawa Y, Kasuga A, Nomaguchi H, Maruyama T, Kasatani T, Shimada A, et al. Detection of autoantibodies to the pancreatic islet heat shock protein 60 in insulin-dependent diabetes mellitus. J Autoimmunol 1996; 9: 517–24.

35. Panchapakesan J, Daglis M, Gatenby P. Antibodies to 65 kDa and 70 kDa heat shock proteins an rheumatoid arthritis and systemic lupus erythematosus. Immunol Cell Biol 1992; 70: 295–300.

36. Vilagut L, Parés A, ViĖas O, Vila J, Jiménez de Anta MT, Rodés J. Antibodies to mycobacterial 65-kD heat shock protein cross-react with the main mitochondrial antigens in patients with primary biliary cirrhosis. Eur J Clin Invest 1997; 27: 667–72.

37. Stevens TR, Winrow VR, Blake DR, Rampton DS. Circulating antibodies to heat-shock protein 60 in Crohn’s disease and ulcerative colitis. Clin Exp Immunol 1992; 90: 271–4.

38. Millar DG, Ohashi PS. Hsp70 family members, danger signals and autoimunity. In: Asea AAA, De Maio A (eds). Heat shock proteins: potent mediators of inflammation and imunity. Springer Netherlands 2007; 189–211.

39. Martin CA, Carson SE, Kowalewski R, Bernstein D, Valentino M, Santiago-Schwarz F. Abberant extracellular and dendritic cell (DC) surface expression of the heat shock protein (hsp)70 in the rheumatoid joint: possible mechanism of hsp/DC-mediated cross-priming. J Immunol 2003; 171: 5736–42.

40. Santiago-Schwarz F, Anand P, Liu S, Carsons SE. Dendritic cells (DCs) in rheumatoid arthritis (RA): progenitor cells and soluble factors contained in RA synovial fluid yield a subset of myeloid DCs that preferentially activate Th1 inflammatory-type responses. J Immunol 2001; 167: 1758–68.

41. Jahromi MM, Eisenbarth GS. Cellular and molecular pathogenesis of type 1A diabetes. Cell Mol Life Sci 2007; 64: 865–72.

42. Bellmann K, Wenz A, Radons J, Burkart V, Kleemann R, Kolb H. Heat shock induces resistance in rat pancreatic islet cells against nitric oxide, oxygen radicals and streptozotocin toxicity in vitro. J Clin Invest 1995; 95: 2840–5.

43. Kutlu B, Cardozo AK, Darville MI, Kruhoffer M, Magnusson N, Orntoft T. Discovery of gene networks regulating cytokine-induced dysfunction and apoptosis in insulin-producing INS-1 cells. Diabetes 2003; 52: 2701–19.

44. Burkart V, Germaschewski L, Schloot NC, Bellmann K, Kolb H. Deficient heat shock protein 70 response to stress in leukocytes at onset of type 1 diabetes. Biochemical and Biophysical Research Communications 2008; 369: 421–5.

45. Rossmann A, Henderson B, Heidecker B, Seiler R, Fraedrich G, Singh M, et al. T-cells from advanced atherosclerotic lesions recognize hHsp60 and have a restricted T-cell receptor repertoire. Exp Gerontol 2008; 43: 229–37.

46. van Roon JA, van EdenW, van Roy JL, Lafeber FJ, Bijlsma JW. Stimulation of suppressive T cell responses by human but not bacterial 60-kD heatshock protein in synovial fluid of patients with rheumatoid arthritis. J Clin Invest 1997; 100: 459–63.

47. Harats D, Yacov N, Gilburd B, Shoenfeld Y, George J. Oral tolerance with heat shock protein 65 attenuates Mycobacterium tuberculosis-induced and high-fat-diet-driven atherosclerotic lesions. J Am Coll Cardiol 2002; 40: 1333–8.

48. Prakken BJ, Roord S, Ronaghy A,Wauben M, Albani S, van Eden W. Heat shock protein 60 and adjuvant arthritis: a model for T cell regulation in human arthritis. Springer Semin Immunopathol 2003; 25: 47–63.

49. Quintana FJ, Carmi P, Mor F, Cohen IR. Inhibition of adjuvant arthritis by a DNA vaccine encoding human heat shock protein 60. J Immunol 2002; 169: 3422–8.

50. Multhoff G. Heat shock proteins in imunity. Handb Exp Pharmacol. 2006; 172: 279–304.

51. Radons J, Multhoff G. Immunostimulatory functions of membranebound and exported heat shock protein 70. Exerc Immunol Rev 2005; 11: 17–33.

52. Galazka G, Jurewicz A, Orlowski W, Stasiolek M, Brosnan CF, Raine CS, et al. EAE tolerance induction with Hsp70-peptide complexes depends on H60 and NKG2D aktivity. J Immunol 2007; 179: 4503–12.

53. Millar DG, Garza KM, Odermatt B, Elford AR, Ono N, Li Z, et al. Hsp70 promotes antigen-presenting cell function and converts T-cell tolerance to autoimmunity in vivo. Nat Med 2003; 9: 1469–76.

54. Gruber R, Lederer S, Bechtel U, Lob S, Riethmüller G, Feucht HE. Increased antibody titers against mycobacterial heat-shock protein 65 in patients with vasculitis and arteriosclerosis. Int Arch Allergy Immunol 1996; 110: 95–8.

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Dermatology & STDs Paediatric rheumatology Rheumatology
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