Білки теплового шоку: роль у формуванні імунної відповіді

У роботі здійснено аналіз результатів наукових досліджень біологічних властивостей білків теплового шоку про- й еукаріотів та ідентифікацію механізмів їх взаємодії з імунною системою людини. Білки теплового шоку знайдені у про- та еукаріотах, вони є консервативними молекулами, що виробляються клітиною у відповідь на стрес, а також містяться в клітинах і позаклітинному середовищі й у нормальних умовах. Найбільш важливою біологічною функ¬цією цих білків є шаперонна активність. Білки теплового шоку здатні модулювати реакції гуморального та клітинного імунітету. Висока консервативність будови цих білків різних організмів може зумовлювати розвиток аутоімунних захворювань у людини. При бактеріальній інфекції білки теплового шоку активують антиген-специфічний імунітет і стимулюють вироблення протизапальних цитокінів. Молекулярні комплекси цих білків і пухлинних/вірусних пептидів забезпечують активацію специфічних імунних реакцій, а також неспецифічне стимулювання імунокомпетентних клітин. Білки теплового шоку, природні аутоантитіла до них, інші ендогенні та екзогенні білки, що містяться в організмі людини, антигенпрезентувальні клітини та різні субпопуляції Т-лімфоцитів утворюють імунну саморегулювальну систему на кшталт ідіотипічної імунної мережі.

Рік видання: 
2014
Номер: 
3
УДК: 
571.27+577.112
С. 12–20., Іл. 2. Табл. 2. Бібліогр.: 44 назви.
Література: 

1. F.A. Ritossa, “A new puffing pattern induced by temperature shock and DNP in Drosophila”, Experientia, vol. 18, pp. 571—573, 1962.
2. A. Tissieres et al., “Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs”, J. Mol. Biol., vol. 84, pp. 389—398, 1974.
3. A.G. Pockley, “Heat shock proteins as regulators of the immune response”, Lancet, vol. 362 (9382), pp. 469—476, 2003.
4. L.E. Hightower, “Heat shock, stress proteins, chaperones and proteotoxicity”, Cell, vol. 66, pp. 191—197, 1991.
5. R.I. Morimoto, “Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators”, Genes Develop., vol. 12, pp. 3788—3796, 1998.
6. W.J. Welch, “How cells respond to stress”, Sci. American, vol. 268, pp. 56—64, 1993.
7. L. Pirkkala et al., “Roles of the heat shock transcription factors in regulation of the heat shock response and beyond”, FASEB J., vol. 15, pp. 1118—1131, 2001.
8. A. Mathew et al., “Stress-specific activation and repression of heat shock factors 1 and 2”, Mol. Cell. Biol., vol. 21, pp. 7163—7171, 2001.
9. S.H. Satyal et al., “Negative regulation of the heat shock transcriptional response by HSBP1”, Genes Develop., vol. 12, pp. 1962—1974, 1998.
10. M.J. Schlesinger, “Heat shock proteins”, J. Biol. Chem., vol. 265, no. 21, pp. 12111—12114, 1998.
11. A.G. Pockley, “Heat shock proteins in health and disease: therapeutic targets or therapeutic agents?”, Exp. Rev. Mol. Med., vol. 3, no. 23, pp. 1—21, 2001.
12. J.S. Giuliano et al., “Extracellular heat shock proteins: alarmins for the host immune system”, Open Inflammation J., vol. 4 (1-M6), pp. 49—60, 2011.
13. Z. Prohaszka, “Chaperones as part of immune networks,” in Molecular aspects of the stress response: chaperones, membranes and networks, P. Csermely and L. Vigh. Ed. New York: Springer Science+Business Media, 2007, pp. 159—166.
14. A.K. Randhawa and T.R. Hawn, “Toll-like receptors: their roles in bacterial recognition and respiratory infections”, Expert Rev. Anti Infect. Ther., vol. 6 (4), pp. 479—495, 2008.
15. D.B. Jones et al., “Sequence homologies between Hsp60 and autoantigens”, Immunol. Today., vol. 14, pp. 115— 118, 1993.
16. L.G. Delogu et al., “Infectious diseases and autoimmunity”, J. Infect. Dev. Ctries., vol. 5, no. 10, pp. 679—687, 2011.
17. I.R. Cohen and D.B. Young, “Autoimmunity, microbial immunity and the immunological homunculus”, Immunol. Today, vol. 12, no. 4, pp. 105—110, 1992.
18. A.B. Poletaev et al., “Integrating immunity: The immunculus and self-reactivity”, J. Autoimmunity, vol. 30, no. 1-2, pp. 68—73, 2008.
19. J. Milland and M.S. Sandrin, “ABO blood group and related antigens, natural antibodies and transplantation”, Tissue Antigens, vol. 68, no. 6, pp. 459—466, 2006.
20. S. Lacroix-Desmazes et al., “Self-reactive antibodies (natural autoantibodies) in healthy individuals”, J. Immunol. Meth., vol. 216, pp. 117—137, 1998.
21. N.K. Jerne, “Towards a network theory of the immune system”, Ann. Immunol. (Paris), vol. 125C, no. 1-2, pp. 373—389, 1974.
22. S. Lacroix-Desmazes et al., “Immunoglobulins and the regulation of autoimmunity through the immune network”, Clin. Exp. Rheumatol., vol. 14, pp. S9—S15, 1996.
23. A. Menoret et al., “Natural autoantibodies against heatshock proteins hsp70 and gp96: implications for immunotherapy using heat-shock proteins”, Immunol., vol. 101, pp. 364—370, 2000.
24. C. Habich et al., “Heat shock protein 60: identification of specific epitopes for binding to primary macrophages”, FEBS Lett., vol. 580, pp. 115—120, 2006.
25. S.H.E. Kaufmann, “Heat shock proteins and the immune response”, Immunol. Today, vol. 11, pp. 129—136, 1996.
26. J.M. Ramage et al., “T cell responses to heat shock protein 60: differential responses by CD4+ T cell subsets according to their expression of CD45 isotypes”, J. Immunol., vol. 162, pp. 704—710, 1999.
27. S.M. Anderton et al., “Activation of T cells recognizing self 60-kD heat shock protein can protect against experimental arthritis”, J. Exp. Med., vol. 181, pp. 943—952, 1995.
28. J. van Roon et al., “Reactivity of T cells from patients with rheumatoid arthritis towards human and mycobacterial hsp60”, FASEB J., vol. 10, pp. A1312, 1996.
29. W. van Eden et al., “Cloning of the mycobacterial epitope recognized by T lymphocytes in adjuvant arthritis”, Nature, vol. 331, pp. 171—173, 1988.
30. O.S. Birk et al., “The 60-kDa heat shock protein modulates allograft rejection”, Proc. Natl. Acad. Sci. USA, vol. 96, pp. 5159—5163, 1999.
31. K.V.V. Abhijnya and A.S. Sreedhar, “Heat shock proteins in the cancer immunity: comprehensive review on potential chemotherapeutic interventions”, J. Clin. Cell. Immunol., vol. S5, pp. 1—8, 2012.
32. P.K. Srivastava et al., “Tumor rejection antigens of chemically induced sarcomas of inbred mice”, Proc. Natl. Acad. Sci. USA, vol. 83, pp. 3407—3411, 1986.
33. A.M. Ciupitu et al., “Immunization with heat shock protein 70 from methylcholanthreneinduced sarcomas induces tumor protection correlating with in vitro T cell responses”, Canc. Immunol. Immunother., vol. 51, pp. 163— 170, 2002.
34. X.-Y. Wang et al., “Characterization of heat shock protein 110 and glucose-regulated protein 170 as cancer vaccines and the effect of fever-range hyperthermia on vaccine activity”, J. Immunol., vol. 165, pp. 490—497, 2001.
35. J. Robert et al., “Phylogenetic conservation of the molecular and immunological properties of the chaperone gp96 and hsp70”, Eur. J. Immunol., vol. 31, pp. 186— 195, 2001.
36. H. Udono and P.K. Srivastava, “Comparison of tumorspecific immunogenicities of stress-induced proteins gp96, hsp90 and hsp70”, J. Immunol., vol. 152, pp. 5398—5403, 1994.
37. S. Janetzki et al., “Immunization of cancer patients with autologous cancer-derived heat shock protein gp96 preparations: a pilot study”, Int. J. Cancer, vol. 88, pp. 232— 238, 2000.
38. B. Berwin et al., “CD91-independent cross-presentation of grp94(gp96)-associated peptides”, J. Immunol., vol. 168, pp. 4282—4286, 2002.
39. R.J. Peach et al., “Both extracellular immunoglobin-like domains of CD80 contain residues critical for binding T cell surface receptors CTLA-4 and CD28”, J. Biol. Chem., vol. 270, no. 36, pp. 21181—21187, 1995. 4
0. S. Basu et al., “CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70 and calreticulin”, Immunity, vol. 14, pp. 303—313, 2001.
41. C. Habich et al., “The receptor for heat shock protein 60 on macrophages is saturable, specific, and distinct from receptors for other heat shock proteins”, J. Immunol., vol. 168, pp. 569—576, 2002.
42. N.E. Blachere et al., “Heat shock proteinpeptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity”, J. Exp. Med., vol. 186, pp. 1315—1322, 1997.
43. K. Suzue and R.A. Young, “Adjuvant-free hsp70 fusion protein system elicits humoral and cellular immune responses to HIV-1 p24”, J. Immunol., vol. 156, pp. 873— 879, 1996.
44. K.M. Anderson and P.K. Srivastava, “Heat, heat shock, heat shock proteins and death: a central link in innate and adaptive immune responses”, Immunol. Lett., vol. 74, pp. 35—39, 2000.

Список літератури у транслітерації: 

1. F.A. Ritossa, “A new puffing pattern induced by temperature shock and DNP in Drosophila”, Experientia, vol. 18, pp. 571–573, 1962.
2. A. Tissieres et al., “Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs”, J. Mol. Biol., vol. 84, pp. 389–398, 1974.
3. A.G. Pockley, “Heat shock proteins as regulators of the immune response”, Lancet, vol. 362 (9382), pp. 469–476, 2003.
4. L.E. Hightower, “Heat shock, stress proteins, chaperones and proteotoxicity”, Cell, vol. 66, pp. 191–197, 1991.
5. R.I. Morimoto, “Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators”, Genes Develop., vol. 12, pp. 3788–3796, 1998.
6. W.J. Welch, “How cells respond to stress”, Sci. American, vol. 268, pp. 56–64, 1993.
7. L. Pirkkala et al., “Roles of the heat shock transcription factors in regulation of the heat shock response and beyond”, FASEB J., vol. 15, pp. 1118–1131, 2001.
8. A. Mathew et al., “Stress-specific activation and repression of heat shock factors 1 and 2”, Mol. Cell. Biol., vol. 21, pp. 7163–7171, 2001.
9. S.H. Satyal et al., “Negative regulation of the heat shock transcriptional response by HSBP1”, Genes Develop., vol. 12, pp. 1962–1974, 1998.
10. M.J. Schlesinger, “Heat shock proteins”, J. Biol. Chem., vol. 265, no. 21, pp. 12111–12114, 1998.
11. A.G. Pockley, “Heat shock proteins in health and disease: therapeutic targets or therapeutic agents?”, Exp. Rev. Mol. Med., vol. 3, no. 23, pp. 1–21, 2001.
12. J.S. Giuliano et al., “Extracellular heat shock proteins: alarmins for the host immune system”, Open Inflammation J., vol. 4 (1-M6), pp. 49–60, 2011.
13. Z. Prohaszka, “Chaperones as part of immune networks,” in Molecular aspects of the stress response: chaperones, membranes and networks, P. Csermely and L. Vigh. Ed. New York: Springer Science+Business Media, 2007, pp. 159–166.
14. A.K. Randhawa and T.R. Hawn, “Toll-like receptors: their roles in bacterial recognition and respiratory infections”, Expert Rev. Anti Infect. Ther., vol. 6 (4), pp. 479–495, 2008.
15. D.B. Jones et al., “Sequence homologies between Hsp60 and autoantigens”, Immunol. Today., vol. 14, pp. 115–118, 1993.
16. L.G. Delogu et al., “Infectious diseases and autoimmunity”, J. Infect. Dev. Ctries., vol. 5, no. 10, pp. 679–687, 2011.
17. I.R. Cohen and D.B. Young, “Autoimmunity, microbial immunity and the immunological homunculus”, Immunol. Today, vol. 12, no. 4, pp. 105–110, 1992.
18. A.B. Poletaev et al., “Integrating immunity: The immunculus and self-reactivity”, J. Autoimmunity, vol. 30, no. 1-2, pp. 68–73, 2008.
19. J. Milland and M.S. Sandrin, “ABO blood group and related antigens, natural antibodies and transplantation”, Tissue Antigens, vol. 68, no. 6, pp. 459–466, 2006.
20. S. Lacroix-Desmazes et al., “Self-reactive antibodies (natural autoantibodies) in healthy individuals”, J. Immunol. Meth., vol. 216, pp. 117–137, 1998.
21. N.K. Jerne, “Towards a network theory of the immune system”, Ann. Immunol. (Paris), vol. 125C, no. 1-2, pp. 373–389, 1974.
22. S. Lacroix-Desmazes et al., “Immunoglobulins and the regulation of autoimmunity through the immune network”, Clin. Exp. Rheumatol., vol. 14, pp. S9–S15, 1996.
23. A. Menoret et al., “Natural autoantibodies against heat-shock proteins hsp70 and gp96: implications for immunotherapy using heat-shock proteins”, Immunol., vol. 101, pp. 364–370, 2000.
24. C. Habich et al., “Heat shock protein 60: identification of specific epitopes for binding to primary macrophages”, FEBS Lett., vol. 580, pp. 115–120, 2006.
25. S.H.E. Kaufmann, “Heat shock proteins and the immune response”, Immunol. Today, vol. 11, pp. 129–136, 1996.
26. J.M. Ramage et al., “T cell responses to heat shock protein 60: differential responses by CD4+ T cell subsets according to their expression of CD45 isotypes”, J. Immunol., vol. 162, pp. 704–710, 1999.
27. S.M. Anderton et al., “Activation of T cells recognizing self 60-kD heat shock protein can protect against experimental arthritis”, J. Exp. Med., vol. 181, pp. 943–952, 1995.
28. J. van Roon et al., “Reactivity of T cells from patients with rheumatoid arthritis towards human and mycobacterial hsp60”, FASEB J., vol. 10, pp. A1312, 1996.
29. W. van Eden et al., “Cloning of the mycobacterial epitope recognized by T lymphocytes in adjuvant arthritis”, Nature, vol. 331, pp. 171–173, 1988.
30. O.S. Birk et al., “The 60-kDa heat shock protein modulates allograft rejection”, Proc. Natl. Acad. Sci. USA, vol. 96, pp. 5159–5163, 1999.
31. K.V.V. Abhijnya and A.S. Sreedhar, “Heat shock proteins in the cancer immunity: comprehensive review on potential chemotherapeutic interventions”, J. Clin. Cell. Immunol., vol. S5, pp. 1–8, 2012.
32. P.K. Srivastava et al., “Tumor rejection antigens of chemically induced sarcomas of inbred mice”, Proc. Natl. Acad. Sci. USA, vol. 83, pp. 3407–3411, 1986.
33. A.M. Ciupitu et al., “Immunization with heat shock protein 70 from methylcholanthreneinduced sarcomas induces tumor protection correlating with in vitro T cell responses”, Canc. Immunol. Immunother., vol. 51, pp. 163–170, 2002.
34. X.-Y. Wang et al., “Characterization of heat shock protein 110 and glucose-regulated protein 170 as cancer vaccines and the effect of fever-range hyperthermia on vaccine activity”, J. Immunol., vol. 165, pp. 490–497, 2001.
35. J. Robert et al., “Phylogenetic conservation of the molecular and immunological properties of the chaperone gp96 and hsp70”, Eur. J. Immunol., vol. 31, pp. 186–195, 2001.
36. H. Udono and P.K. Srivastava, “Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90 and hsp70”, J. Immunol., vol. 152, pp. 5398–5403, 1994.
37. S. Janetzki et al., “Immunization of cancer patients with autologous cancer-derived heat shock protein gp96 preparations: a pilot study”, Int. J. Cancer, vol. 88, pp. 232–238, 2000.
38. B. Berwin et al., “CD91-independent cross-presentation of grp94(gp96)-associated peptides”, J. Immunol., vol. 168, pp. 4282–4286, 2002.
39. R.J. Peach et al., “Both extracellular immunoglobin-like domains of CD80 contain residues critical for binding T cell surface receptors CTLA-4 and CD28”, J. Biol. Chem., vol. 270, no. 36, pp. 21181–21187, 1995.
40. S. Basu et al., “CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70 and calreticulin”, Immunity, vol. 14, pp. 303–313, 2001.
41. C. Habich et al., “The receptor for heat shock protein 60 on macrophages is saturable, specific, and distinct from receptors for other heat shock proteins”, J. Immunol., vol. 168, pp. 569–576, 2002.
42. N.E. Blachere et al., “Heat shock proteinpeptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity”, J. Exp. Med., vol. 186, pp. 1315–1322, 1997.
43. K. Suzue and R.A. Young, “Adjuvant-free hsp70 fusion protein system elicits humoral and cellular immune responses to HIV-1 p24”, J. Immunol., vol. 156, pp. 873–879, 1996.
44. K.M. Anderson and P.K. Srivastava, “Heat, heat shock, heat shock proteins and death: a central link in innate and adaptive immune responses”, Immunol. Lett., vol. 74, pp. 35–39, 2000.

Текст статтіРозмір
2014-3-2.pdf408.53 КБ