Abstract
Heat shock proteins (HSP) are a group of proteins that have a molecular weight less than 100 kDa and whose production is induced by heat (42-46°C) shock. Infection, inflammation, some toxins such as ethanol, arsenic, trace metals and ultraviolet light, hunger, hypoxia, lack of nitrogen (in plants) and dehydration are the factors that could induce HSP production. HSPs are classified into four main groups according to their molecular weights; HSP 90 family, HSP 70 family, HSP 60 family and the small HSP family. They have functions mainly in cytoprotection, neurodegenerative pathologies, signal transduction pathways and cancer immunology.
Keywords:
Heat shock, prtoeins, cytoprotection
References
1
Aufricht C. Heat–shock protein 70: molecular supertool? Pediatr Nephrol 2005; 20: 707–713.
2
Morimoto RI, Santoro MG. Stress–inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection. Nat Biotechnol 1998; 16: 833–838.
3
Christians ES, Yan LJ, Benjamin IJ. Heat shock factor 1 and heat shock proteins: Critical partners in protection against acute cell injury. Crit Care Med 2002; 30: 43–50.
4
Sarge KD, Murphy SP, Morimoto RI. Activation of heat shock gene transcription by Heat Shock Factor 1 involves oligomerization, acquisition of DNA–binding activity, and nuclear localization and can occur in the absence of stress. Mol Cell Biol 2009; 13: 1392–1407.
5
Petrof EO, Ciancio M, Chang EB. Role and regulation of intestinal epithelial heat shock proteins in health and disease. Chin J Dig Dis 2004; 5: 45–50.
6
Otaka M, Odashima M, Watanabe S. Role of heat shock proteins (molecular chaperones) in intestinal mucosal protection. Biochem Biophys Res Commun 2006: 348: 1–5.
7
Pockley GA, Faire U, Kiessling R, Lemne C, Thulin T, Frosteg J. Circulating heat shock protein and heat shock protein antibody levels in established hypertension. J Hypertens 2002; 20: 1815–1820.
8
Ritossa FM. A new puffing pattern induced by a temperature shock and DNP in Drosophila. Experimenta 1962; 18: 571–573
9
Mayer MP, Bukau B. Hsp70 chaperones: Cellular functions and molecular mechanism. Review. Cell Mol Life Sci 2005; 62: 670–684.
10
Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell 2006; 125: 443–451.
11
Ellis RJ, van der Vies SM. Molecular chaperones. Annu Rev Biochem 1991; 60: 321–347.
12
Deocaris CC, Kaul SC, Wadhwa R. On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60. Cell Stress Chaperones. 2006; 11: 116–128.
13
Macario AJL, Macario EC. Sick chaperones, cellular stress, and disease. N Engl J Med. 2005; 353: 1489–1501.
14
Möbius J, Groos S, Meinhardt A, Seitz J. Differential distribution of the mitochondrial heat–shock protein 60 in rat gastrointestinal tract. Cell Tissue Res 1997; 287: 343–350.
15
Dobson CM. Protein folding and misfolding. Nature. 2005; 426: 884–90.
16
Muchowski PJ, Wacker JL. Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 2005; 6: 11–22.
17
Wacker JL, Zareie MH, Fong H, Sarikaya M, Muchowski PJ. Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partioning monomer. Nat Struct Mol Biol 2004; 11: 1215–2122.
18
Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004; 431: 805–810.
19
Selkoe DJ. Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat Cell Biol 2004; 6: 1054–61.
20
Forman MS, Trojanowski JQ, Lee VM–Y. Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nat Med 2004; 10: 1055– 1063.
21
Landles C, Bates GP. Huntingtin and the molecular pathogenesis of Huntington's disease. EMBO Report 2004; 5: 958–963.
22
Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med 2004; 10: 10–17.
23
Tanaka M, Kim YM, Lee G, Junn E, Iwatsubo T, Mouradian MM. Aggresomes formed by a–synuclein and synphilin–1 are cytoprotective. J Biol Chem 2004; 279: 4625–4631.
24
Sun Y, McRae TH. The small heat shock proteins and their role in human disease. FEBS J 2005; 272: 2613–2627.
25
Westerheide SD, Morimoto RI. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem 2005; 280: 33097–33100.
26
Pratt WB, Toft DO. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med 2003; 228: 111–133.
27
Jäättelä M. Escaping cell death: survival proteins in cancer. Exp Cell Res 1999; 248: 30–43.
28
Wang HH, Mao CY, Teng LS, Cao J. Recent advances in heat shock protein– based cancer vaccines. Hepatobiliary Pancreat Dis Int 2006; 5: 22–27.
29
Whitesell L, Bagatell R, Falsey R. The stress response: implications for the clinical development of hsp90 inhibitors. Curr Cancer Drug Targets 2003; 3: 349–358.
30
Yokota S, Kitahara M, Nagata K. Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells. Cancer Res 2000; 60: 2942–2948.
31
Koyasu S, Nishida E, Miyata Y, Sakai H, Yahara I. HSP100, a 100–kDa heat shock protein, is a Ca2+–calmodulin–regulated actin–binding protein. J Biol Chem 1989; 264: 15083–15087.
32
Atalay M, Oksala NK, Laaksonen DE, Khanna S, Nakao C, Lappalainen J, Roy S, Hänninen O, Sen CK. Exercise training modulates heat shock protein response in diabetic rats. J Appl Physiol 2004; 97: 605–611.
33
Neckers L, Percy SI. Heat shock protein 90. Curr Opin Oncol 2003; 15: 419–424.
34
Pearl LH, Prodromou C. Structure and in vivo function of Hsp90. Curr Opin Struct Biol 2000; 10: 46–51.
35
Garrido C, Gurbuxani S, Ravagnan L, Kroemer G. Heat shock proteins: endogenous modulators of apoptotic cell death. Biochem Biophys Res Commun 2001; 286: 433–442.
36
Schmitt E, Gehrmann M, Brunet M, Multhoff G, Garrido C. Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy. J Leukoc Biol 2007; 81: 1–13.
37
Poulaki V, Iliaki E, Mitsiades N, Mitsiades CS, Paulus YN, Bula DV, Gragoudas ES, Miller JW. Inhibition of Hsp90 attenuates inflammation in endotoxin–induced uveitis. FASEB J 2007; 21: 2113–23.
38
Pockley AG, Bulmer J, Hanks BM, Wright BH. Identification of human heat shock protein 60 (Hsp60) and anti–Hsp60 antibodies in the peripheral circulation of normal individuals. Cell Stress Chaperones 1999; 4: 29–35.
39
Kregel K. C. Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. J Appl Physiol 2002; 92: 2177–2186.
40
Hartl FU, Hayer–Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2000; 295: 1852–1858.
41
Sakamoto N, Kokura S, Okuda T, et al. Heme oxygenase–1 (Hsp32) is involved in the protection of small intestine by whole body mild hyperthermia from ischemia/reperfusion injury in rat. Int J Hyperthermia 2005; 21: 603–614.
42
Vicencio A, Bidmon B, Ryu J, Reidy K, Thulin G, Mann A, Gaudio KM, Kashgarian M, Siegel NJ. Developmental expression of HSP–72 and ischemic tolerance of the immature kidney. Pediatr Nephrol 2003; 18: 85–91.
43
Parcellier A, Gurbuxani S, Schmitt E, Solary E, Garrido C. Heat shock proteins, cellular chaperones that modulate mitochondrial cell death pathways. Biochem Biophys Res Commun 2003; 304: 505– 512.
44
Horwich AL, Farr GW, Fenton WA. GroEL–GroES–mediated protein folding. Chem Rev 2006; 106: 1917–1930.
45
Zhao Q, Wang J, Levichkin IV, Stasinopoulos S, Ryan MT, Hoogenraad NJ. A mitochondrial specific stress response in mammalian cells. EMBO J 2002; 21: 4411– 4419.
46
Brudzynski K, Martinez V, Gupta RS. Immunocytochemical localization of heat–shock protein 60–related protein in beta–cell secretory granules and its altered distribution in non–obese diabetic mice. Diabetologia 1992; 35: 316–324.
47
Shin BK, Wang H, Yim AM, et al. Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. J Biol Chem 2003; 278: 7607–7616.
48
Lebret T, Watson RW, Molinie V, O'Neill A, Gabriel C, Fitzpatrick JM, Botto H. Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma. Cancer 2003; 98: 970–977.
49
Cappello F. HSP60 and HSP10 as diagnostic and prognostic tools in the management of exocervical carcinoma. Gynecol Oncol 2003; 91: 661.
50
Sun Y, McRae TH. Small heat shock proteins: molecular structure and chaperone function Cell Mol Life Sci 2005; 62: 2460– 2476.
51
MacRae TH. Structure and function of small heat shock/a–crystallin proteins: stablished concepts and emerging ideas. Cell Mol Life Sci 2000; 57: 899–913.
52
Mounier N, Arrigo AP. Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones 2002; 7: 167–176.
53
Zhang H, Fu X, Jiao W, Zhang X, Liu C, Chang Z. The association of small heat shock protein 16. 3 with the plasma membrane of Mycobacterium tuberculosis: Dissociation of oligomers is a prerequisite. Biochem Biophys Res Commun 2005; 330: 1055–1061.
54
Horwitz J. The function of alpha–crystallin in vision. Sem Cell Dev Biol 2000; 11, 53–60.
55
Oesterreich S, Weng CN, Qiu M, Hilsenbeck SG, Osborne CK, Fuqua SA. The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines. Can Res 1993; 53: 4443–4448.
