Alpha-crystallins and tumorigenesis

Current Molecular Medicine

Volumn 12, Issue 9, 2012, Pages 1164-1173

  Chen, P ^a,b   Ji, W ^b   Liu, F Y ^a   Tang, H Z ^a   Fu, S ^a   Zhang, X ^b   Liu, M ^c   Gong, L ^b   Deng, M ^b   Hu, W F ^a,b   Hu, X H ^a,b   Chen, X W ^a   Li, Z L ^a   Li, X ^a   Liu, J ^a   Li, D W C ^a,b  

^a HUNAN NORMAL UNIVERSITY   (China)

^b UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^c HUAZHONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

A B crystallin; Apoptosis; Cancer; Lens; Metastasis; Pancreas; Tumor; Tumorigenesis

Indexed keywords

ALPHA CRYSTALLIN; CASPASE; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN BCL 2; PROTEIN P53; RAF PROTEIN; RAS PROTEIN; VINBLASTINE;

APOPTOSIS; BRAIN TUMOR; BREAST CANCER; CARCINOGENESIS; CELL PROLIFERATION; DOWN REGULATION; HEAD AND NECK CANCER; HUMAN; KIDNEY CANCER; METASTASIS; NONHUMAN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; REVIEW; UPREGULATION;

ALPHA-CRYSTALLIN A CHAIN; ALPHA-CRYSTALLIN B CHAIN; ALPHA-CRYSTALLINS; ANIMALS; APOPTOSIS; CELL TRANSFORMATION, NEOPLASTIC; HUMANS; MUTATION; NEOPLASM METASTASIS; NEOPLASMS;

EID: 84867795105     PISSN: 15665240     EISSN: 18755666     Source Type: Journal    
DOI: 10.2174/156652412803306747     Document Type: Review

References (172)

1. Bloemendal H. Lens proteins. CRC Crit Rev Biochem 1982; 12: 1-38.
2. Piatigorsky J. Lens crystallins and their gene families. Cell 1984; 38(3): 620-1.
3. Piatigorsky J. Gene expression and genetic engineering in the lens. Friedenwald lecture. Invest Ophthalmol Vis Sci 1987; 28(1): 9-28.
4. Groenen PJ, Merck KB, de Jong WW, Bloemendal H. Structure and modifications of the junior chaperone -crystallin. From lens transparency to molecular pathology. Eur J Biochem 1994; 225(1): 1-19.
5. Pras E, Frydman M, Levy-Nissenbaum E, et al. A nonsense mutation (W9X) in CRYAA causes autosomal recessive cataract in an inbred Jewish Persian family. Invest Ophthalmol Vis Sci 2000; 41: 3511-5.
6. Mackay DS, Andley UP, Shiels A. Cell death triggered by a novel mutation in the αA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q. Eur J Hum Genet 2003; 11: 784-93.
7. Litt M, Kramer P, LaMorticella DM, Murphey W, Lovrien EW, Weleber RG. Autosomal dominant congenital cataract associated with a missense mutation in the human -crystallin gene CRYAA. Hum Mol Genet 1998; 7: 471-4.
8. Gu F, Luo W, Li X, et al. A novel mutation in αA-crystallin (CRYAA) caused autosomal dominant congenital cataract in a large Chinese family. Hum Mutat 2008; 29: 769.
9. Santhiya ST, Soker T, Klopp N, et al. Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family. Mol Vis 2006; 12: 768-73.
10. Vicart P, Caron A, Guicheney P, Li Z, et al. A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 1998; 20: 92-5.
11. Berry V, Francis P, Reddy MA, et al. B crystallin gene (CRY aB) mutation causes dominant congenital posterior polar cataract in humans. Am J Hum Genet 2001; 69: 1141-5.
12. Hui Li, Chang Li, Qiulun Lu, et al. Cataract mutation P20S of αB-crystalline impairs chaperone activity of αA-crystalline and induces apoptosis of human lens epithelial cells. Biophy. Biochem. Acta. 2008; 1782:303-309.
13. Liu M, Ke T, Wang Z, et al. Identification of a CRY aB mutation associated with autosomal dominant posterior polar cataract in a Chinese family. Invest Ophthalmol Vis Sci 2006a; 47: 3461-6.
14. Liu Y, Zhang X, Luo L, et al. A novel B-crystallin mutation associated with autosomal dominant congenital lamellar cataract. Invest Ophthalmol Vis Sci 2006b; 47: 1069-75.
15. Kato K, Shinohara H, Kurobe N, Goto S, Inaguma Y, Ohshima K. Immunoreactive aA crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method. Biochim Biophys Acta 1991; 1080: 173-180.
16. Deng M, Chen PC, Xie S, et al. The small heat shock protein αA-crystallin is expressed in pancreas and acts as a negative regulator of carcinogenesis. Biochim Biophys Acta 2010; 1802(7-8): 621-31.
17. Bhat SP, Nagineni CN. B subunit of lens specific protein - crystallin is present in other ocular and non-ocular tissues. Biochem Biophys Res Commun 1989; 158; 319-25.
18. Iwaki T, Kume-Iwaki A, Liem RKH, Goldman JE. B-crystallin is expressed in non lenticular tissues and accumulates in Alexander's disease brain. Cell 1989; 57, 71-8.
19. Dubin RA, Wawrousek EF, Piatigorsky J. Expression of the murine B-crystallin gene is not restricted to lens. Mol Cell Biol 1989; 9: 1083-91.
20. Sax CM, Piatigorsky J. Expression of the α-crystallin/small heat shock protein/molecular chaperone genes in the lens and other tissues. Adv Enzymol Relat Areas Mol Biol 1994; 69: 155-201.
21. Horwitz J. The function of α-crystallin in vision. Semin Cell Dev Biol 2000; 11: 53-60.
22. Horwitz J. acrystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992; 89: 10449-1045.
23. Rao PV, Horwitz J, Zigler JS Jr. α-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation. Biochem Biophys Res Commun 1993; 190: 786-93.
24. Kelley MJ, David LL, Iwasaki N, Wright J, Shearer TR. a-Crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract. J Biol Chem 1993; 268: 18844-9.
25. Boyle D, Takemoto L. Characterization of the α-γ and α-β complex: evidence for an in vivo functional role of α-crystallin as a molecular chaperone. Exp Eye Res 1994; 58: 9-15.
26. Nicholl ID, Quinlan RA. Chaperone activity of -crystallins modulates intermediate filament assembly. EMBO J 1994; 13: 945-53.
27. Wang K, Spector A. α-crystallin stabilizes actin filaments and prevents cytochalasin-induced depolymerization in a phosphorylation-dependent manner. Eur J Biochem 1996; 242: 56-66.
28. Clark JI, Huang QL. Modulation of the chaperone-like activity of bovine -crystallin. Proc Natl Acad Sci U S A 1996; 93: 15185-9.
29. Sun TX, Das BK, Liang JJ. Conformational and functional differences between recombinant human lens αA- and αB- crystallin. J Biol Chem 1997; 272: 6220-5.
30. Reddy GB, Das KP, Petrash JM, Surewicz WK. Temperatur dependent chaperone activity and structural properties of human αA- and αB-crystallins. J Biol Chem 2000; 275: 4565-70.
31. Cobb BA, Petrash JM. Structural and functional changes in the A-crystallin R116C mutant in hereditary cataracts. Biochemistry 2000; 39: 15791-8.
32. Bova MP, Yaron O, Huang Q, et al. Mutation R120G in αB- crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc Natl Acad Sci U S A 1999; 96: 6137-42.
33. Derham BK, van Boekel MA, Muchowski PJ, et al. Chaperone function of mutant versions of aA- and αB-crystallin prepared to pinpoint chaperone binding sites. Eur J Biochem 2001; 268: 713-21.
34. Takemoto L. Release of aA sequence 158-173 correlates with a decrease in the molecular chaperone properties of native - crystallin. Exp Eye Res 1994; 59: 239-42.
35. Arrigo AP, Simon S. Expression and functions of heat shock proteins in the normal and pathological mammalian eye. Curr Mol Med 2010; 10(9): 776-93.
36. Basha E, O'Neil H, Vierling E. Small heat shock proteins and - crystallins: dynamic proteins with flexible functions. Trends Biochem Sci 2012; 37(3): 106-17.
37. Andley UP. Effects of -crystallin on lens cell function and cataract pathology. Curr Mol Med. 2009; 9:887-92.
38. Klemenz R, Frohli E, Steiger RH, Schafer R, Aoyama A. B-crystallin is a small heat shock protein. Proc Natl Acad Sci U S A 1991; 88(9): 3652-6.
39. Golenhofen N, Perng MD, Quinlan RA, Drenckhahn D. Comparison of the small heat shock proteins αB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochem Cell Biol 2004; 122(5): 415-25.
40. Kappe G, Franck E, Verschuure P, Boelens WC, Leunissen JA, de Jong WW. The human genome encodes 10 -crystallin-related small heat shock proteins: HspB1-10. Cell Stress Chaperones 2003 Spring; 8(1): 53-61.
41. Gusev NB, Bogatcheva NV, Marston SB. Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins. Biochemistry (Mosc) 2002; 67(5): 511-9.
42. Webster KA. Serine phosphorylation and suppression of apoptosis by the small heat shock protein B-crystallin. Circ Res 2003; 92(2): 130-2.
43. Parcellier A, Schmitt E, Brunet M, Hammann A, Solary E, Garrido C. Small heat shock proteins HSP27 and αB-crystallin: cytoprotective and oncogenic functions. Antioxid Redox Signal 2005; 7(3-4): 404-13.
44. Reddy GB, Kumar PA, Kumar MS. Chaperone-like activity and hydrophobicity of -crystallin. IUBMB Life 2006; 58(11): 632-41.
45. Chang NW, Pei RJ, Tseng HC, et al. Co-treating with arecoline and 4-nitroquinoline 1-oxide to establish a mouse model mimicking oral tumorigenesis. Chem Biol Interact 2010; 183(1): 231-7.
46. Benndorf R, Welsh MJ. Shocking degeneration. Nat Genet 2004; 36(6): 547-8.
47. Sun Y, MacRae TH. The small heat shock proteins and their role in human disease. FEBS J 2005; 272(11): 2613-27.
48. Mehlen P, Schulze-Osthoff K, Arrigo AP. Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J Biol Chem 1996; 271: 16510-4.
49. Mehlen P, Kretz-Remy C, Preville X, Arrigo A-P. Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNF -induced cell death. EMBO J 1996; 15: 2695-706.
50. Martin JL, Mestril R, Hilal-Dandan R, Brunton LL, Dillmann WH. Small heat shock proteins and protection against ischemic injury in cardiac myocytes. Circulation 1997; 96(12): 4343.
51. Andley UP, Song Z, Wwrousek EF, Bassnett S. The molecular chaperone A-crystallin enhances lens epithelial cell growth and resistance to UVA stress. J Biol Chem 1998; 273: 31252-61.
52. Andley UP, Song Z, Wawrousek EF, Fleming TP, Bassnett S. Differential protective activity of αA- and αB-crystallin in lens epithelial cells. J Biol Chem 2000; 275: 36823-31.
53. Hoover HE, Thuerauf DJ, Martindale JJ, Glembotski CC. αB-crystallin gene induction and phosphorylation by MKK6-activated p38. A potential role for αB-crystallin as a target of the p38 branch of the cardiac stress response. J Biol Chem 2000; 275: 23825-33.
54. Ray PS, Martin JL, Swanson EA, Otani H, Dillmann WH, Das DK. Transgene overexpression of B crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion. FASEB J 2001; 15: 393-402.
55. Kamradt MC, Chen F, Cryns VL. The small heat shock protein αB-crystallin negatively regulates cytochrome c- and caspase-8- dependent activation of caspase-3 by inhibiting its autoproteolytic maturation. J Biol Chem 2001; 276: 16059-63.
56. Kamradt MC, Chen F, Sam S, Cryns VL. The small heat shock protein αB-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation. J Biol Chem. 2002; 277: 38731-6.
57. Li DW-C, Xiang H, Mao Y-W, et al. Caspase-3 is actively involved in okadaic acid-induced lens epithelial cell apoptosis. Exp Cell Res 2001; 266: 279-91.
58. 2-induced apoptosis through downregulation the αB crystallin gene. J Biol Chem 2001; 276: 43435-45.
59. Andley UP, Patel HC, Xi JH. The R116C mutation in A- crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis. J Biol Chem 2002; 277: 10178-86.
60. Mao Y-W, Liu J-P, Xiang H, Li DW-C. Human αA- and αB- crystallins bind to Bax and Bcl-XS to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ 2004; 11: 512-26.
61. Liu J-P, Schlosser R, Ma W-Y, et al. Human αA- and αB-crystallins prevent UVA-induced apoptosis through regulation of PKC, RAF/MEK/ERK and AKT signaling pathways. Exp. Eye Res 2004; 79: 393-403.
62. Li DW, Liu JP, Mao YW, et al. Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by B-crystallin through inhibition of RAS activation. Mol Biol Cell 2005; 16: 4437-53.
63. Bennardini F, Wrzosek A, Chiesi M. B-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ Res 1992; 71(2): 288-94.
64. Zhang L, Yan Q, Liu J-P, et al. Apoptosis: its functions and control in the ocular lens. Curr. Mol. Med. 2010; 10:864-875.
65. Li DW-C, Deng LGM, Liu JP, Liu M, Mao YW. Small Stress Proteins and Human Diseases. The two lens structural proteins, αA- and αB-crystallins, prevent stress-induced apoptosis through regulation of multiple signaling transduction pathways, Arrigo S, Ed 2009; NY, USA: Nova Science Publisher.
66. Trepel J, Mollapour M, Giaccone G, Neckers L. Targeting the dynamic HSP90 complex in cancer. Nat Rev Cancer 2010; 10: 537-49.
67. Evans CG, Chang L, Gestwicki JE. Gestwicki Heat shock protein 70 (Hasp70) as an emerging drug target. J Med Chem 2010; 53: 4585-602.
68. Khalil AA, Kabapy NF, Deraz SF, Smith C. Heat shock proteins in oncology: Diagnostic biomarkers or therapeutic targets. Biochim Biophys Acta 2011; 1816(2): 89-104.
69. Arrigo AP, Simon S, Gibert B, et al. Hsp27 (HspB1) and B-crystallin (HspB5) as therapeutic targets. FEBS Lett 2007; 581(19): 3665-74.
70. Kase S, Parikh JG, Rao NA. Expression of -crystallin in retinoblastoma. Arch Ophthalmol 2009; 127(2): 187-92.
71. Moyano JV, Evans JR, Chen F, et al. B-crystallin is a novel oncoprotein that predicts poor clinical outcome in breast cancer. J Clin Invest 2006; 116(1): 261-70.
72. Sherman M, Multhoff G. Heat shock proteins in cancer. Ann N Y Acad Sci, 2007. 1113: p. 192-201.
73. Didelot C, Lanneau D, Brunet M, et al. Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins. Curr Med Chem 2007; 14(27): 2839-47.
74. Ciocca DR, Calderwood SK. Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 2005; 10(2): 86-103.
75. Ferlay J, Shin HR, Bray F, Forman D, Mathers C, Parkin DM. Estimates of worldwide burden of cancer in 2008: GLOBOCAN 2008. Int J Cancer 2010; 127(12): 2893-917.
76. National Cancer Institute - Breast Cancer Study. Available at: http://www.cancer.gov/cancertopics/types/breast. [Accessed January 30, 2012].
77. Chelouche-Lev D, Kluger HM, Berger AJ, Rimm DL, Price JE. B-crystallin as a marker of lymph node involvement in breast carcinoma. Cancer 2004; 100(12): 2543-8.
78. Kim HS, Lee Y, Lim YA, Kang HJ, Kim LS. B-crystallin is a novel oncoprotein associated with poor prognosis in breast cancer. J Breast Cancer 2011; 14(1): 14-9.
79. Livasy CA, Karaca G, Nanda R, et al. Phenotypic evaluation of the basal-like subtype of invasive breast carcinoma. Mod Pathol 2006; 19(2): 264-71.
80. Sitterding SM, Wiseman WR, Schiller CL, et al. B-crystallin: a novel marker of invasive basal-like and metaplastic breast carcinomas. Ann Diagn Pathol 2008; 12(1): 33-40.
81. Ivanov O, Chen F, Wiley EL, et al. B-crystallin is a novel predictor of resistance to neoadjuvant chemotherapy in breast cancer. BreastCancer Res Treat 2008; 111(3): 411-7.
82. Ou K, Yu K, Kesuma D, et al. Novel breast cancer biomarkers identified by integrative proteomic and gene expression mapping. J Proteome Res 2008; 7(4): 1518-28.
83. Klemenz R, Scheier B, Muller A, Steiger R, Aoyama A. B crystallin expression in response to hormone, oncogenes and stress. Verh Dtsch Ges Pathol 1994; 78: 34-5.
84. Shao ZM, Li DQ, Wang L, et al. Identification of breast cancer metastasis-associated proteins in an isogenic tumor metastasis model using two-dimensional gel electrophoresis and liquid chromatography-ion trap-mass spectrometry. Proteomics 2006; 6(11): 3352-68.
85. Gruvberger-Saal SK, Parsons R. Is the small heat shock protein αB-crystallin an oncogene? J Clin Invest 2006; 116(1): 30-2.
86. Cicek M, Samant RS, Kinter M, Welch DR, Casey G. Identification of metastasis-associated proteins through protein analysis of metastatic MDA-MB-435 and metastasis-suppressed BRMS1 transfected-MDA-MB-435 cells. Clin Exp Metastasis 2004; 21(2): 149-57.
87. Kabbage M, Chahed K, Hamrita B, et al. Protein alterations in infiltrating ductal carcinomas of the breast as detected by nonequilibrium pH gradient electrophoresis and mass spectrometry. J Biomed Biotechnol 2008; 2008: 564127.
88. Wang ZC, E D, Batu DL, Saixi YL, Zhang B, Ren LQ. 2D-DIGE proteomic analysis of changes in estrogen/progesterone-induced rat breast hyperplasia upon treatment with the Mongolian remedy RuXian-I. Molecules 2011; 16(4): 3048-65.
89. Bosman JD, Yehiely F, Evans JR, Cryns VL. Regulation of αB-crystallin gene expression by the transcription factor Ets1 in breast cancer. Breast Cancer Res Treat 2010; 119(1): 63-70.
90. Hoadley KA, Weigman VJ, Fan C, et al. EGFR associated expression profiles vary with breast tumor subtype. Bmc Genomics 2007; 31: 8.
91. Schulte TW, Blagosklonny MV, Romanova L, et al. Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway. Mol Cell Biol 1996; 16(10): 5839-45.
92. Sato S, Fujita N, Tsuruo T. Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci U S A 2000; 97(20): 10832-7.
93. Gaestel M. sHsp-phosphorylation: enzymes, signaling pathways and functional implications. Prog Mol Subcell Biol 2002; 28: 151-69.
94. Rogalla T, Ehrnsperger M, Preville X, et al. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem 1999; 74(27): 18947-56.
95. Morrison LE, Hoover HE, Thuerauf DJ, Glembotski CC. Mimicking phosphorylation of αB-crystallin on serine-59 is necessary and sufficient to provide maximal protection of cardiac myocytes from apoptosis. Circ Res 2003; 92(2): 203-11.
96. Launay N, Tarze A, Vicart P, Lilienbaum A. Serine 59 phosphorylation of αB-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells. J Biol Chem 2010; 285(48): 37324-32.
97. Stark AM, Nabavi A, Mehdorn HM, Blomer U. Glioblastoma multiforme-report of 267 cases treated at a single institution. Surg Neurol 2005; 63(2): 162-9; discussion 9.
98. Kato S, Hirano A, Kato M, Herz F, Ohama E. Comparative study on the expression of stress-response protein (srp) 72, srp 27, αB-crystallin and ubiquitin in brain tumours. An immunohistochemical investigation. Neuropathol Appl Neurobiol 1993; 19(5): 436-42.
99. Iwaki T, Iwaki A, Miyazono M, Goldman JE. Preferential expression of αB-crystallin in astrocytic elements of neuroectodermal tumors. Cancer 1991; 68(10): 2230-40.
100. Aoyama A, Steiger RH, Frohli E, et al. Expression of B-crystallin in human brain tumors. Int J Cancer 1993; 55(5): 760-4.
101. Odreman F, Vindigni M, Gonzales ML, et al. Proteomic studies on low- and high-grade human brain astrocytomas. J Proteome Res 2005; 4(3): 698-708.
102. Khalil AA. Biomarker discovery: a proteomic approach for brain cancer profiling. Cancer Sci 2007; 98(2): 201-13.
103. Shin JH, Kim SW, Lim CM, Jeong JY, Piao CS, Lee JK. B-crystallin suppresses oxidative stress-induced astrocyte apoptosis by inhibiting caspase-3 activation. Neurosci Res 2009; 64(4): 355-61.
104. Stegh AH, Kesari S, Mahoney JE, et al. Bcl2L12-mediated inhibition of effector caspase-3 and caspase-7 via distinct mechanisms in glioblastoma. Proc Natl Acad Sci U S A 2008; 105(31): 10703-8.
105. Austruy E, Cohen-Salmon M, Antignac C, et al. Isolation of kidney complementary DNAs down-expressed in Wilms' tumor by a subtractive hybridization approach. Cancer Res 1993; 53(12): 2888-94.
106. Pinder SE, Balsitis M, Ellis IO, Landon M, Mayer RJ, Lowe J. The expression of B-crystallin in epithelial tumours: a useful tumour marker? J Pathol 1994; 174(3): 209-15.
107. Holcakova J, Hernychova L, Bouchal P, et al. Identification of B-crystallin, a biomarker of renal cell carcinoma by SELDI-TOF MS. Int J Biol Markers 2008; 23(1): 48-53.
108. Takashi M, Sakata T, Ohmura M, Kato K. Elevated concentrations of the small stress protein HSP27 in rat renal tumors. Urol Res 1997; 25(3): 173-7.
109. Takashi M, Katsuno S, Sakata T, Ohshima S, Kato K. Different concentrations of two small stress proteins, B crystallin and HSP27 in human urological tumor tissues. Urol Res 1998; 26(6): 395-9.
110. Shi T, Dong F, Liou LS, Duan ZH, Novick AC, DiDonato JA. Differential protein profiling in renal-cell carcinoma. Mol Carcinog 2004; 40(1): 47-61.
111. Chin D, Boyle GM, Williams RM, et al. B-crystallin, a new independent marker for poor prognosis in head and neck cancer. Laryngoscope 2005; 115(7): 1239-42.
112. Boslooper K, King-Yin Lam A, Gao J, Weinstein S, Johnson N. The clinicopathological roles of αB-crystallin and p53 expression in patients with head and neck squamous cell carcinoma. Pathology 2008; 40(5): 500-4.
113. Mineva I, Gartner W, Hauser P, et al. Differential expression of αB-crystallin and Hsp27-1 in anaplastic thyroid carcinomas because of tumor-specific αB-crystallin gene (CRYAB) silencing. Cell Stress Chaperones 2005; 10(3): 171-84.
114. Lung HL, Lo CC, Wong CC, Cheung AK, et al. Identification of tumor suppressive activity by irradiation microcell-mediated chromosome transfer and involvement of B-crystallin in nasopharyngeal carcinoma. Int J Cancer 2008; 122(6): 1288-96.
115. Solares CA, Boyle GM, Brown I, Parsons PG, Panizza B. Reduced B-crystallin staining in perineural invasion of head and neck cutaneous squamous cell carcinoma. Otolaryngol Head Neck Surg 2010; 142(3 Suppl 1): S15-9.
116. Chen J, He QY, Yuen AP, Chiu JF. Proteomics of buccal squamous cell carcinoma: the involvement of multiple pathways in tumorigenesis. Proteomics 2004; 4(8): 2465-75.
117. He QY, Chen J, Kung HF, Yuen APW, Chiu JF. Identification of tumor-associated proteins in oral tongue squamous cell carcinoma by proteomics. Proteomics 2004; 4(1): 271-8.
118. Tang Q, Liu YF, Zhu XJ, et al. Expression and prognostic significance of the αB-crystallin gene in human hepatocellular carcinoma. Hum Pathol 2009; 40(3): 300-5.
119. Lo WY, Tsai MH, Tsai Y, et al. Identification of over-expressed proteins in oral squamous cell carcinoma (OSCC) patients by clinical proteomic analysis. Clin Chim Acta 2007; 376(1-2): 101-7.
120. Liu XL, Guo KP, Ma F, Xie GY, He Y, Hu CH. Expression profile of heat shock proteins in tissues and cells of lung adenocarcinoma. Zhong Nan Da Xue Xue Bao Yi Xue Ban 2007; 32(4): 660-4.
121. Stronach EA, Sellar GC, Blenkiron C, et al. Identification of clinically relevant genes on chromosome 11 in a functional model of ovarian cancer tumor suppression. Cancer Res 2003; 63(24): 8648-55.
122. Rigas PK, Kase S, Rao NA. Expression of -crystallin in human sebaceous carcinoma of the eyelid. Eur J Ophthalmol 2009; 19(5): 702-7.
123. Bai F, Xi JH, Wawrousek EF, Fleming TP, Andley UP. Hyperproliferation and p53 status of lens epithelial cells derived from αB-crystallin knockout mice. J Biol Chem 2003; 278(38): 36876-86.
124. Mahon KA, Chepelinsky AB, Khillan JS, Overbeek PA, Piatigorsky J, Westphal H. Oncogenesis of the lens in transgenic mice. Science 1987; 235(4796): 1622-8.
125. Kerr JFR, Wyllie AH, Currrie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972; 6, 239-57.
126. Arends MJ, Wyllie A H. Apoptosis: mechanisms and roles in pathology. Int Rev Exp Path 1991; 2: 223-54.
127. Thompson CB. Apoptosis in the pathogenesis and treatment of disease. Science 1995; 267: 1456-62.
128. Vaux, D.L., Korsmeyer, S.J. Cell death in development. Cell 1999; 96(2): 245-54.
129. Li H, Yuan J. Deciphering the pathways of life and death. Curr Opin Cell Biol 1999;11: 261-6.
130. Budihardjo I, Oliver H, Lutter M, Luo X, Wang X. Biochemical pathways of caspase activation during apoptosis. Annu Rev Cell Dev Biol 1999; 15: 269-90.
131. Aggeli IK, Beis I, Gaitanaki C. Oxidative stress and calpain inhibition induce αB crystallin phosphorylation via p38-MAPK and calcium signalling pathways in H9c2 cells. Cell Signal 2008; 20(7): 1292-302. Erratum in: Cell Signal 2008; 20(9): 1695.
132. Chin L, Stegh AH, Kim H, et al. Bcl2L12 inhibits postmitochondrial apoptosis signaling in glioblastoma. Genes Dev 2007; 21(1): 98-111.
133. Stegh AH, Chin L, Louis DN, DePinho RA. What drives intense apoptosis resistance and propensity for necrosis in glioblastoma? A role for Bcl2L12 as a multifunctional cell death regulator. Cell Cycle 2008; 7(18): 2833-9.
134. Moorozov V, Wawrousek EF. Caspase-dependent secondary lens fiber cell disintegration in αA/ αB-crystallin double knockout mice. Development 2006; 133: 813-21.
135. Wen-Feng Hu, Gong Lili, Zhi-Jun Cao, et al. a-Crystallins interact with caspase-3 and Bax to guard mouse lens development. Curr Mol Med 2012. 12(2): 177-87.
136. den Engelsman J, Keijsers V, de Jong WW, Boelens WC. The small heat-shock protein B-crystallin promotes FBX4- dependent ubiquitination. J Biol Chem 2003; 278:4699-704.
137. Lin DI, Barbash O, Kumar KG, et al. Phosphorylation-dependent ubiquitination of cyclin D1 by the SCF(FBX4- B crystallin) complex. Mol Cell 2006; 24(3): 355-66.
138. Lin DI, Lessie MD, Gladden AB, Bassing CH, Wagner KU, Diehl JA. Disruption of cyclin D1 nuclear export and proteolysis accelerates mammary carcinogenesis. Oncogene. 2008 Feb 21;27(9):1231-42.
139. Barbash O, Lin DI, Diehl JA. SCF Fbx4/ B-crystallin cyclin D1 ubiquitin ligase: a license to destroy. Cell Div 2007; 2: 2.
140. Hu R, Aplin AE. B-crystallin is mutant B-RAF regulated and contributes to cyclin D1 turnover in melanocytic cells. Pigment Cell Melanoma Res 2010; 23(2): 201-9.
141. Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B. A model for p53-induced apoptosis. Nature 389: 300-305.
142. Mihara M, Erster S, Zaika A, Petrenko O, Chittenden T, Pancoska P, Moll UM. p53 has a direct apoptogenic role at the mitochondria. Mol Cell 2003; 11: 577-590.
143. Shen Y, White E. P53-dependent apoptosis pathways. Adv Cancer Res 2001; 82: 55-84.
144. El-Deiry WS. The role of p53 in chemosensitivity and radiosensitivity. Oncogene 2003; 22: 7486-95.
145. Deng M, Chen P, Liu F-Y, et al. The p53-Bak Apoptotic Signaling Axis Plays An Essential Role in Regulating Differentiation of the Ocular Lens. Curr Mol Med 2012; 12(8): 901-916.
146. Liu F-Y, Tang X-C, Deng M, et al. The Tumor Suppressor p53 directly Regulates c-Maf and Prox-1 to Control Lens Differentiation. Curr Mol Med 2012; 12(8): 917-928.
147. Liu S, Li J, Tao Y, Xiao X. Small heat shock protein αB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis. Biochem Biophys Res Commun 2007; 354(1): 109-14.
148. Watanabe G, Kato S, Nakata H, Ishida T, Ohuchi N, Ishioka C. B-crystallin: a novel p53-target gene required for p53-dependent apoptosis. Cancer Sci 2009; 100(12): 2368-75.
149. Evans JR, Bosman JD, Brown-Endres L, Yehiely F, Cryns VL. Induction of the small heat shock protein αB-crystallin by genotoxic stress is mediated by p53 and p73. Breast Cancer Res Treat 2010; 122(1): 159-68.
150. Jin X, Moskophidis D, Hu Y, Phillips A, Mivechi NF. Heat shock factor 1 deficiency via its downstream target gene B-crystallin (Hspb5) impairs p53 degradation. J Cell Biochem 2009; 107(3): 504-15.
151. Andley UP, Song Z, Wawrousek EF, Brady JP, Bassnett S, Fleming TP. Lens epithelial cells derived from B-crystallin knockout mice demonstrate hyperproliferation and genomic instability. FASEB J 2001; 15(1): 221-9.
152. Pearson G, Robinson F, Beers Gibson T, et al. Mitogenactivated protein (MAP) kinase pathways: regulation and physiological functions. Endocr Rev 2001; 22: 153-83.
153. Vivanco I, Sawyers CL. The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat Rev Cancer 2002; 2: 489-501.
154. Ousman SS, Tomooka BH, van Noort JM, Protective and therapeutic role for αB-crystallin in autoimmune demyelination. Nature 2007; 448: 474-9.
155. Golenhofen N, Perng MD, Quinlan RA, Drenckhahn D. Comparison of the small heat shock proteins αB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochem Cell Biol 2004; 122(5): 415-25.
156. Preville X, Salvemini F, Giraud S, et al. Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery. Exp Cell Res 1999; 247(1): 61-78.
157. Paul, C. and A.P. Arrigo, Comparison of the protective activities generated by two survival proteins: Bcl-2 and Hsp27 in L929 murine fibroblasts exposed to menadione or staurosporine. Exp Gerontol 2000; 35(6-7): 757-66.
158. Caughey, B. and P.T. Lansbury, Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003; 26: 267-98.
159. Schaffar G, Breuer P, Boteva R, et al. Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol Cell 2004; 15(1): 95-105.
160. Cherneva R, Petrov D, Georgiev O, et al. Expression profile of the small heat-shock protein B-crystallin in operated-on nonsmall-cell lung cancer patients: clinical implication. Eur J Cardiothorac Surg 2010; 37(1): 44-50.
161. Cvekl A, Piatigorsky J. Lens development and crystallin gene expression: many roles for Pax-6. Bioessays. 1996;18(8): 621-30.
162. Cvekl A, Duncan MK. Genetic and epigenetic mechanisms of gene regulation during lens development. Prog Retin Eye Res 2007; 26(6): 555-97.
163. Morimoto RI. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 1998; 12: 3788-96.
164. Arts HJ, Hollema H, Lemstra W, et al. Heat-shock-protein-27 (hsp27) expression in ovarian carcinoma: relation in response to chemotherapy and prognosis. Int J Cancer 1999; 84(3): 234-8.
165. Foss AJ, Alexander RA, Guille MJ, Hungerford JL, McCartney AC, Lightman S. Estrogen and progesterone receptor analysis in ocular melanomas. Ophthalmology 1995; 102(3): 431-5.
166. Hamilton KL, Gupta S, Knowlton AA. Estrogen and regulation of heat shock protein expression in female cardiomyocytes: crosstalk with NF kappa B signaling. J Mol Cell Cardiol 2004; 36(4): 577-84.
167. Wataba K, Saito T, Fukunaka K, Ashihara K, Nishimura M, Kudo R. Over-expression of heat shock proteins in carcinogenic endometrium. Int J Cancer 2001; 91(4): 448-56.
168. Yang X, Dale EC, Diaz J, Shyamala G. Estrogen dependent expression of heat shock transcription factor: implications for uterine synthesis of heat shock proteins. J Steroid Biochem Mol Biol 1995; 52(5): 415-9.
169. Ninkovic J, Pinto L, Petricca S, et al. The transcription factor Pax6 regulates survival of dopaminergic olfactory bulb neurons via crystallin A. Neuron 2010; 68(4): 682-94.
170. Yan Q, Gong L, Deng M, et al. Sumoylation activates the transcriptional activity of Pax-6, an important transcription factor for eye and brain development. Proc Natl Acad Sci U S A 2010; 107(49): 21034-9.
171. Rocchi P, Jugpal P, So A, et al. Small interference RNA targeting heat-shock protein 27 inhibits the growth of prostatic cell lines and induces apoptosis via caspase-3 activation in vitro. BJU Int 2006; 98(5): 1082-9.
172. Kamada M, So A, Muramaki M, Rocchi P, Beraldi E, Gleave M. Hsp27 knockdown using nucleotide-based therapies inhibit tumor growth and enhance chemotherapy in human bladder cancer cells. Mol Cancer Ther 2007; 6(1): 299-308.