Small stress proteins and their therapeutic potential

Small Stress Proteins and Human Diseases

Volumn , Issue , 2011, Pages 417-438

  Houck, Scott A ^a   Ghosh, Joy G ^b   Clark, John I ^a,c  

^a UNIVERSITY OF WASHINGTON   (United States)

^b BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84875452252     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (102)

1. Head, M.W., Corbin, E., Goldman, J.E. (1993). Overexpression and abnormal modification of the stress proteins α B-crystallin and HSP27 in Alexander disease. Am J Pathol 143:1743-1753.
2. Vicart, P., Caron, A., Guicheney, P., Li, Z., Prevost, M.C., et al. (1998). A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 20:92-95.
3. Vleminckx, V., Van Damme, P., Goffin, K., Delye, H., Van Den Bosch, L., Robberecht, W. (2002). Upregulation of HSP27 in a transgenic model of ALS. J Neuropathol Exp Neurol 61:968-974.
4. Arrigo, A.P., Muller, W.E.G. (2002). Small Stress Proteins. New York, NY: Springer Verlag.
5. Crabb, J.W., Miyagi, M., Gu, X., Shadrach, K., West, K.A., et al. (2002). Drusen proteome analysis: an approach to the etiology of age-related macular degeneration. Proc Natl Acad Sci U S A 99:14682-14687.
6. Bloemendal, H., de Jong, W., Jaenicke, R., Lubsen, N.H., Slingsby, C., Tardieu A. (2004). Ageing and vision: structure, stability and function of lens crystallins. Prog Biophys Mol Biol.86:407-485.
7. Dabir, D.V., Trojanowski, J.Q., Richter-Landsberg, C., Lee, V.M., Forman, M.S. (2004). Expression of the small heat-shock protein αB-crystallin in tauopathies with glial pathology. Am J Pathol 164:155-166.
8. Nakata, K., Crabb, J.W., Hollyfield, J.G. (2005). Crystallin distribution in Bruch's membrane-choroid complex from AMD and age-matched donor eyes. Exp Eye Res 80:821-826.
9. Benjamin, I.J., Guo, Y., Srinivasan, S., Boudina, S., Taylor, R.P., et al. (2007). CRYAB and HSPB2 deficiency alters cardiac metabolism and paradoxically confers protection against myocardial ischemia in aging mice. Am J Physiol Heart Circ Physiol. 293:H3201-H3209.
10. Kampinga, H.H., Henning, R.H., van Gelder, I.C., Brundel, B.J. (2007). Beat shock proteins and atrial fibrillation. Cell Stress Chaperones12:97-100.
11. Quraishe, S., Asuni, A., Boelens, W.C., O'Connor, V., Wyttenbach, A. (2008). Expression of the small heat shock protein family in the mouse CNS: Differential anatomical and biochemical compartmentalization. Neuroscience 153:483-491.
12. Vos M.J., Hageman, J., Carra, S., Kampinga, H.H. (2008). Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 47:7001-7011.
13. He, H.W., Zhang, J., Zhou, H.M., Yan, Y.B. (2005). Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregation. Biophys J 89:2650-2658.
14. Muchowski, P.J., Wacker, J.L. (2005). Modulation of neurodegeneration by molecular Chaperones. Nat Rev Neurosci. 6:11-22.
15. Duennwald, M.L., Jagadish, S., Giorgini, F., Muchowski, P.J., Lindquist, S. (2006). A network of protein interactions determines polyglutamine toxicity. Proc Natl Acad Sci U S A. 103:11051-11056.
16. Roberson, E.D., Mucke, L. (2006). 100 years and counting: prospects for defeating Alzheimer's disease. Science 314:781-784.
17. Skovronsky, D.M., Lee, V.M., Trojanowski, J.Q. (2006). Neurodegenerative diseases: new concepts of pathogenesis and their Therapeutic implications. Annu Rev Pathol.1:151-170.
18. Teplow, D.B., Lazo, N.D., Bitan, G., Bernstein, S., Wyttenbach,T., et al. (2006). Elucidating amyloid β-protein folding and assembly: A multidisciplinary approach. Acc Chem Res 39:635-645.
19. Guo, Z., Eisenberg, D. (2007). The mechanism of the amyloidogenic conversion of T7 endonuclease I. J Biol Chem. 282:14968-14974.
20. Ono, K., Condron, M.M., Ho, L., Wang, J., Zhao, W., et al.. (2008). Effects of grape seed-derived polyphenols on amyloid β-protein self-assembly and cytotoxicity. J Biol Chem. 283:32176-32187.
21. Saibil, H.R. (2008). Chaperone machines in action. Curr Opin Struct Biol. 18:35-42.
22. Cisse M., Mucke L. (2009). Alzheimer's disease: A prion protein connection. Nature 457:1090-1091.
23. Ecroyd, H., Carver, J.A. (2009). Crystallin proteins and amyloid fibrils. Cell Mol Life Sci. 66:62-81.
24. Aoyama, A., Steiger, R.H., Frohli, E., Schafer, R., von Deimling, A., et al. (1993). Expression of α B-crystallin in human brain tumors. Int J Cancer 55:760-764.
25. Takashi, M., Katsuno, S., Sakata, T., Ohshima, S., Kato, K. (1998). Different concentrations of two small stress proteins, αB crystallin and HSP27 in human urological tumor tissues. Urol Res 26:395-399.
26. Calderwood, S.K., Khaleque, M.A., Sawyer, D.B., Ciocca, D.R. (2006). Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci. 31:164-172.
27. Moyano, J.V., Evans, J.R., Chen, F., Lu, M., Werner, M.E., et al. (2006). ΑB-crystallin is a novel oncoprotein that predicts poor clinical outcome in breast cancer. J Clin Invest 116:261-270.
28. Pozsgai, E., Gomori, E., Szigeti, A., Boronkai, A., Gallyas, F. Jr, et al. (2007). Correlation between the progressive cytoplasmic expression of a novel small heatshock protein (Hsp16.2) and malignancy in brain tumors. BMC Cancer 7:233.
29. So, A., Hadaschik, B., Sowery, R., Gleave, M. (2007). The role of stress proteins in prostate cancer. Curr Genomics 8:252-261.
30. Ghosh, J.G., Houck, S.A., Clark, J.I. (2007a). Interactive domains in the molecular chaperone human αB crystallin modulate microtubule assembly and disassembly. PLoS ONE 2:e498.
31. Cherian, M. and Abraham, E.C. (1995). Decreased molecular chaperone property of α-crystallins due to posttranslational modifications. Biochem BiophysRes Commun 208: 675-679.
32. Liu, J.P., Schlosser, R., Ma, W.Y., Dong, Z., Feng, H., et al. (2004). Human αA-and αB-crystallins prevent UVA-induced apoptosis through regulation of PKCα, RAF/MEK/ERK and AKT signaling pathways. Exp Eye Res. 79:393-403.
33. Wyttenbach, A. (2004). Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis. J Mol Neurosci 23:69-96.
34. Gaestel, M. (2006). Molecular chaperones in signal transduction. Handb Exp Pharmacol 172:93-109.
35. Bellyei, S., Szigeti, A., Boronkai, A., Pozsgai, E., Gomori, E., et al. (2007a). Inhibition of cell death by a novel 16.2 kD heat shock protein predominantly via Hsp90 mediated lipid rafts stabilization and Akt activation pathway. Apoptosis 12:97-112.
36. Bellyei, S., Szigeti, A., Pozsgai, E., Boronkai, A., Gomori, E., et al. (2007b). Preventing apoptotic cell death by a novel small heat shock protein. Eur J Cell Biol. 86:161-171.
37. Lanneau, D., Brunet, M., Frisan, E., Solary, E., Fontenay, M., Garrido, C. (2008). Heat shock proteins: essential proteins for apoptosis regulation. J Cell Mol Med. 12:743-761.
38. Nicolaou, P., Knöll, R., Haghighi, K., Fan, G.C., Dorn, G.W. 2nd, et al. (2008). Human mutation in the anti-apoptotic heat shock protein 20 abrogates its cardioprotective effects. J Biol Chem 283:33465-33471.
39. Haslbeck, M., Franzmann, T., Weinfurtner, D., Buchner, J. (2005). Some like it hot: the structure and function of small heat-shock proteins. Nat Struct Mol Biol 12:842-846.
40. Nakamoto, H., Vigh, L. (2007). The small heat shock proteins and their clients. Cell Mol Life Sci 64:294-306.
41. Arrigo, A.P., Simon, S., Gibert, B., Kretz-Remy, C., Nivon, M., et al. (2007). Hsp27 (HspB1) and αB-crystallin (HspB5) as therapeutic targets. FEBS Lett 581:3665-3674.
42. Arai, H., Atomi, Y. (1997). Chaperone activity of α B-crystallin suppresses tubulin aggregation through complex formation. Cell Struct Funct 22:539-544.
43. Liang, J.J. (2000). Interaction between β-amyloid and lens αB-crystallin. FEBS Lett 484:98-101.
44. Perng, M.D., Cairns, L., van den, IJessel.P., Prescott, A., Hutcheson, A.M., Quinlan, R.A. (1999). Intermediate filament interactions can be altered by HSP27 and αB-crystallin. J Cell Sci 112:2099-2112.
45. Xi, J.H., Bai, F., McGaha, R., Andley, U.P. (2006). Α-crystallin expression affects microtubule assembly and prevents their aggregation. Faseb J 20:846-857.
46. Devi, R.R., Yao, W., Vijayalakshmi, P., Sergeev, Y.V., Sundaresan, P., Hejtmancik, J.F. (2008). Crystallin gene mutations in Indian families with inherited pediatric cataract. Mol Vis 14:1157-1170.
47. Litt, M., Kramer, P., LaMorticella, D.M., Murphey, W., Lovrien, E.W., Weleber, R.G. (1998). Autosomal dominant congenital cataract associated with a missense mutation in the human α crystallin gene CRYAA. Hum Mol Genet 7:471-474.
48. Perng, M.D., Zhang, Q., Quinlan, R.A. (2007). Insights into the beaded filament of the eye lens. Exp Cell Res 313:2180-2188.
49. Santhiya, S.T., Soker, T., Klopp, N., Illig, T., Prakash, M.V., et al. (2006). Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family. Mol Vis 12:768-773.
50. Simon, S., Michiel, M., Skouri-Panet, F., Lechaire, J.P., Vicart, P., Tardieu, A. (2007). Residue R120 is essential for the quaternary structure and functional integrity of human αB-crystallin. Biochemistry 46:9605-9614.
51. De, S., Rabin, D.M., Salero, E., Lederman, P.L., Temple, S., Stern, J.H. (2007). Human retinal pigment epithelium cell changes and expression of αB-crystallin: a biomarker for retinal pigment epithelium cell change in age-related macular degeneration. Arch Ophthalmol 125:641-645.
52. Johnson, P.T., Brown, M.N., Pulliam, B.C., Anderson, D.H., Johnson, L.V. (2005). Synaptic pathology, altered gene expression, and degeneration in photoreceptors impacted by drusen. Invest Ophthalmol Vis Sci 46:4788-4795.
53. Renkawek, K., Bosman, G.J., de Jong, W.W. (1994). Expression of small heat-shock protein hsp 27 in reactive gliosis in Alzheimer disease and other types of dementia. Acta Neuropathol 87:511-519.
54. Renkawek, K., de Jong, W.W., Merck, K.B., Frenken, C.W., van Workum, F.P., Bosman G.J. (1992). α B-crystallin is present in reactive glia in Creutzfeldt-Jakob disease. Acta Neuropathol 83:324-327.
55. Renkawek, K, Stege, G.J., Bosman, G.J. (1999). Dementia, gliosis and expression of the small heat shock proteins hsp27 and α B-crystallin in Parkinson's disease. Neuroreport 10:2273-2276.
56. Wang, J., Martin, E., Gonzales, V., Borchelt, D.R., Lee, M.K. (2008). Differential regulation of small heat shock proteins in transgenic mouse models of neurodegenerative diseases. Neurobiol Aging 29:586-597.
57. Wilhelmus, M.M., Boelens, W.C., Otte-Holler, I., Kamps, B., Kusters, B., et al. (2006). Small heat shock protein HspB8: its distribution in Alzheimer's disease brains and its inhibition of amyloid-β protein aggregation and cerebrovascular amyloid-β toxicity. Acta Neuropathol 111:139-149.
58. Evgrafov, O.V., Mersiyanova, I., Irobi, J., Van Den Bosch, L., Dierick, I., et al. (2004). Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. Nat Genet 36:602-606.
59. Irobi, J., Van Impe, K., Seeman, P., Jordanova, A., Dierick, I., et al. (2004). Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy. Nat Genet 36:597-601.
60. Tang, B.S., Zhao, G.H., Luo, W., Xia, K., Cai, F., et al. (2005). Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L. Hum Genet 116:222-224.
61. Ghosh, J.G. & Clark, J.I. (2005). Insights into the domains required for dimerization and assembly of human αB-crystallin. Protein Sci 14:684-695.
62. Ghosh, J.G., Estrada, M.R., Clark, J.I. (2005). Interactive domains for chaperone activity in the small heat shock protein, human αB crystallin. Biochemistry 44:14854-14869.
63. Ghosh, J.G., Estrada, M.R., Clark, J.I. (2006a). Structure-based analysis of the β8 interactive sequence of human αB crystallin. Biochemistry 45:9878-9886.
64. Ghosh, J.G., Estrada, M.R., Houck, S.A., Clark, J.I. (2006b). The function of the β3 interactive domain in the small heat shock protein and molecular chaperone, human αB crystallin. Cell Stress Chaperones 11:187-197.
65. Ghosh, J.G., Houck, S.A., Doneanu, C.E., Clark, J.I. (2006c). The β4-β8 groove is an ATP-interactive site in the α crystallin core domain of the small heat shock protein, human αB crystallin. J Mol Biol 364:364-375.
66. Ghosh, J.G., Houck, S.A., Clark, J.I. (2007b). Interactive sequences in the stress protein and molecular chaperone human αB crystallin recognize and modulate the assembly of filaments. Int J Biochem Cell Biol 39:1804-1815.
67. Ghosh, J.G., Shenoy, A.K., Jr., Clark, J.I. (2007c). Interactions between important regulatory proteins and human αB crystallin. Biochemistry 46:6308-6317.
68. Ghosh, J.G., Houck, S.A., Clark, J.I. (2008). Interactive sequences in the molecular chaperone, human αB crystallin modulate the fibrillation of amyloidogenic proteins. Int J Biochem Cell Biol 40:954-967.
69. Kappé, G., Franck, E., Verschuure, P., Boelens, W.C., Leunissen, J.A., de Jong, W.W. (2003). The human genome encodes 10 α-crystallin-related small heat shock proteins: HspB1-10. Cell Stress Chaperones 8:53-61.
70. Kim, K.K., Kim, R., Kim, S.H. (1998). Crystal structure of a small heat-shock protein. Nature 394:595-599.
71. van Montfort,R.L., Basha, E., Friedrich, K.L., Slingsby, C., Vierling. E. (2001a). Crystal structure and assembly of a eukaryotic small heat shock protein. Nat Struct Biol 8:1025-1030.
72. Van Montfort, R., Slingsby, C., Vierling, E. (2001b). Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones. Adv Protein Chem. 59:105-156.
73. Stamler, R., Kappé, G., Boelens, W., Slingsby, C. (2005). Wrapping the α-crystallin domain fold in a chaperone assembly. J Mol Biol. 353:68-79.
74. Pasta, S.Y., Raman, B., Ramakrishna, T., Rao., Ch. M. (2004). The IXI/V motif in the C-terminal extension of α-crystallins: alternative interactions and oligomeric assemblies. Mol Vis 10:655-662.
75. Haley, D.A., Horwitz, J., Stewart, P.L. (1998). The small heat-shock protein, αB-crystallin, has a variable quaternary structure. J Mol Biol 277:27-35.
76. Haley, D.A., Bova, M.P., Huang, Q.L., McHaourab, H.S., Stewart, P.L. (2000). Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies. J Mol Biol 298:261-272.
77. Salerno, J.C., Eifert, C.L., Salerno, K.M., Koretz, J.F. (2003). Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region. Protein Eng. 16:847-851.
78. Horwitz, J. (2009). Α crystallin: the quest for a homogeneous quaternary structure. Exp Eye Res. 88:190-194.
79. Levitt, M. (1992). Accurate modeling of protein conformation by automatic segment matching. J Mol Biol 226:507-533.
80. Fechteler, T., Dengler, U., Schomburg, D. (1995). Prediction of protein three-dimensional structures in insertion and deletion regions: a procedure for searching data bases of representative protein fragments using geometric scoring criteria. J Mol Biol 253:114-131.
81. Jehle, S., van Rossum, B., Stout, J.R., Noguchi, S.M., Falber, K., et al. (2009). ΑB-crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer. J Mol Biol 385:1481-1497.
82. Koteiche, H.A., McHaourab, H.S. (1999). Folding pattern of the α-crystallin domain in αA-crystallin determined by site-directed spin labeling. J Mol Biol 294:561-577.
83. Liang, J.J., Liu, B.F. (2006). Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants. Protein Sci 15:1619-1627.
84. Sharma, K.K., Kumar, R.S., Kumar. G.S., Quinn. P.T. (2000). Synthesis and characterization of a peptide identified as a functional element in αA-crystallin. J Biol Chem 275:3767-3771.
85. Bhattacharyya, J., Sharma, K.K. (2001). Conformational specificity of mini-αA-crystallin as a molecular chaperone. J Pept Res 57:428-434.
86. Geysen, H.M. (1990). Molecular technology: peptide epitope mapping and the pin technology. Southeast Asian J Trop Med Public Health 21:523-533.
87. Derham, B.K., van Boekel, M.A., Muchowski, P.J., Clark, J.I., Horwitz, J., et al. (2001). Chaperone function of mutant versions of α A-and α B-crystallin prepared to pinpoint chaperone binding sites. Eur J Biochem 268:713-721.
88. Muchowski, P.J., Wu, G.J., Liang, J.J., Adman, E.T., Clark, J.I. (1999). Site-directed mutations within the core "α-crystallin" domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions. J Mol Biol 289:397-411.
89. Pasta, S.Y., Raman, B., Ramakrishna, T., Rao, Ch. M. (2003). Role of the conserved SRLFDQFFG region of α-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity. J Biol Chem 278:51159-51166.
90. Saha, S., Das, K.P. (2004). Relationship between chaperone activity and oligomeric size of recombinant human αA-and αB-crystallin: a tryptic digestion study. Proteins 57:610-617.
91. Sharma, K.K., Kaur, H., Kester, K. (1997). Functional elements in molecular chaperone α-crystallin: identification of binding sites in α B-crystallin. Biochem Biophys Res Commun 239:217-222.
92. Shroff, N.P., Bera, S., Cherian-Shaw, M., Abraham, E.C. (2001). Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of αB-crystallin. Mol Cell Biochem 220:127-133.
93. Ghosh, J.G., Shenoy, A.K., Jr., Clark, J.I. (2006d). N-and C-Terminal motifs in human αB crystallin play an important role in the recognition, selection, and solubilization of substrates. Biochemistry 45:13847-13854.
94. Klabunde, T., Petrassi, H.M., Oza, V.B., Raman, P., Kelly, J.W., Sacchettini, J.C. (2000). Rational design of potent human transthyretin amyloid disease inhibitors. Nat Struct Biol 7:312-321.
95. Trinh, C.H., Smith, D.P., Kalverda, A.P., Phillips, S.E., Radford, S.E. (2002). Crystal structure of monomeric human β-2-microglobulin reveals clues to its amyloidogenic properties. Proc Natl Acad Sci U S A 99:9771-9776.
96. Comeau, S.R., Gatchell, D.W., Vajda, S., Camacho, C.J. (2004a). ClusPro: a fully automated algorithm for protein-protein docking. Nucleic Acids Res 32:W96-W99.
97. Comeau, S.R., Gatchell, D.W., Vajda, S., Camacho, C.J. (2004b). ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20:45-50.
98. McParland, V.J., Kad, N.M., Kalverda, A.P., Brown, A., Kirwin-Jones, P., et al. (2000). Partially unfolded states of β(2)-microglobulin and amyloid formation in vitro. Biochemistry 39:8735-8746.
99. Nelson, R., Eisenberg, D. (2006). Recent atomic models of amyloid fibril structure. Curr Opin Struct Biol 16:260-265.
100. Schormann, N., Murrell, J.R., Benson, M.D. (1998). Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation. Amyloid 5:175-187.
101. Friedrich, K.L., Giese, K.C., Buan, N.R., Vierling, E. (2004). Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes. J Biol Chem 279:1080-1089.
102. Lee, G.J., Roseman, A.M., Saibil, H.R., Vierling, E. (1997). A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. Embo J 16:659-671.