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International Journal of Proteomics
Volume 2010 (2010), Article ID 479571, 8 pages
doi:10.1155/2010/479571
Review Article
Heat Shock Proteins in the Human Eye
Department of Ophthalmology, Aalborg Hospital, Aarhus University Hospital, Hobrovej 18-22, 9100 Aalborg, Denmark
Received 1 July 2010; Revised 11 November 2010; Accepted 17 December 2010
Academic Editor: Jen-Fu Chiu
Copyright © 2010 Lærke Urbak and Henrik Vorum. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Linked References
- F. U. Hartl and M. Hayer-Hartl, “Molecular chaperones in the cytosol: from nascent chain to folded protein,” Science, vol. 295, no. 5561, pp. 1852–1858, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. J. Han, H. Yun, and S. Y. Lee, “Microbial small heat shock proteins and their use in biotechnology,” Biotechnology Advances, vol. 26, no. 6, pp. 591–609, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. J. T. A. Groenen, K. B. Merck, W. W. De Jong, and H. Bloemendal, “Structure and modifications of the junior chaperone α-crystallin—from lens transparency to molecular pathology,” European Journal of Biochemistry, vol. 225, no. 1, pp. 1–19, 1994. View at Publisher · View at Google Scholar · View at Scopus
- Y. S. Kim, J. A. Han, T. B. Cheong, J. C. Ryu, and J. C. Kim, “Protective effect of heat shock protein 70 against oxidative stresses in human corneal fibroblasts,” Journal of Korean Medical Science, vol. 19, no. 4, pp. 591–597, 2004. View at Scopus
- S. Lindquist and E. A. Craig, “The heat-shock proteins,” Annual Review of Genetics, vol. 22, pp. 631–677, 1988. View at Scopus
- C. Georgopoulos and W. J. Welch, “Role of the major heat shock proteins as molecular chaperones,” Annual Review of Cell Biology, vol. 9, pp. 601–634, 1993. View at Scopus
- Y. Li, S. Roth, M. Laser, J. X. Ma, and C. E. Crosson, “Retinal preconditioning and the induction of heat-shock protein 27,” Investigative Ophthalmology and Visual Science, vol. 44, no. 3, pp. 1299–1304, 2003. View at Publisher · View at Google Scholar · View at Scopus
- S. Dasgupta, T. C. Hohman, and D. Carper, “Hypertonic stress induces αB-crystallin expression,” Experimental Eye Research, vol. 54, no. 3, pp. 461–470, 1992. View at Publisher · View at Google Scholar · View at Scopus
- R. Omar and M. Pappolla, “Oxygen free radicals as inducers of heat shock protein synthesis in cultured human neuroblastoma cells: relevance to neurodegenerative disease,” European Archives of Psychiatry and Clinical Neuroscience, vol. 242, no. 5, pp. 262–267, 1993. View at Scopus
- 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 and Development, vol. 12, no. 24, pp. 3788–3796, 1998. View at Scopus
- C. Wu, “Heat shock transcription factors: structure and regulation,” Annual Review of Cell and Developmental Biology, vol. 11, pp. 441–469, 1995. View at Scopus
- T. Gotoh, K. Terada, S. Oyadomari, and M. Mori, “hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria,” Cell Death and Differentiation, vol. 11, no. 4, pp. 390–402, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. M. Beere, B. B. Wolf, K. Cain et al., “Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome,” Nature Cell Biology, vol. 2, no. 8, pp. 469–475, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- AO. L. Hsu, C. T. Murphy, and C. Kenyon, “Regulation of aging and age-related disease by DAF-16 and heat-shock factor,” Science, vol. 300, no. 5622, pp. 1142–1145, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Jäättelä, “Heat shock proteins as cellular lifeguards,” Annals of Medicine, vol. 31, no. 4, pp. 261–271, 1999. View at Scopus
- P. Gain, G. Thuret, C. Chiquet, J. M. Dumollard, J. F. Mosnier, and L. Campos, “In situ immunohistochemical study of Bcl-2 and heat shock proteins in human corneal endothelial cells during corneal storage,” British Journal of Ophthalmology, vol. 85, no. 8, pp. 996–1000, 2001. View at Publisher · View at Google Scholar · View at Scopus
- J. C. Young, “Mechanisms of the Hsp70 chaperone system,” Biochemistry and Cell Biology, vol. 88, no. 2, pp. 291–300, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. Dang, Y. H. Hu, M. Zhang, and LI. Sun, “Identification and molecular analysis of a stress-inducible Hsp70 from Sciaenops ocellatus,” Fish and Shellfish Immunology, vol. 29, no. 4, pp. 600–607, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Ishihara, M. Sato, S. Sato, T. Arai, M. Obara, and M. Kikuchi, “Assessment of expressions of heat shock protein (HSP 72) and apoptosis after ArF excimer laser ablation of the cornea,” Journal of Biomedical Optics, vol. 9, no. 1, pp. 187–192, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. Shi and R. R. Isseroff, “Arsenite pre-conditioning reduces UVB-induced apoptosis in corneal epithelial cells through the anti-apoptotic activity of 27 kDa heat shock protein (HSP27),” Journal of Cellular Physiology, vol. 206, no. 2, pp. 301–308, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. Shi, B. Han, I. R. Schwab, and R. R. Isseroff, “UVB irradiation-induced changes in the 27-kd heat shock protein (HSP27) in human corneal epithelial cells,” Cornea, vol. 25, no. 8, pp. 948–955, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. K. Ko and E. P. Kay, “Hsp47-dependent and -independent intracellular trafficking of type I collagen in corneal endothelial cells,” Molecular Vision, vol. 5, pp. 17–24, 1999. View at Scopus
- X. Gu, M. K. Ko, and E. P. Kay, “Intracellular interaction of Hsp47 and type I collagen in corneal endothelial cells,” Investigative Ophthalmology and Visual Science, vol. 40, no. 2, pp. 289–295, 1999. View at Scopus
- A. Nakai, M. Satoh, K. Hirayoshi, and K. Nagata, “Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum,” Journal of Cell Biology, vol. 117, no. 4, pp. 903–1014, 1992. View at Publisher · View at Google Scholar · View at Scopus
- K. Nagata, “Hsp47: a collagen-specific molecular chaperone,” Trends in Biochemical Sciences, vol. 21, no. 1, pp. 23–26, 1996. View at Publisher · View at Google Scholar · View at Scopus
- Y. Kasagi and H. Yamashita, “HSP47 expression in cornea after excimer laser photoablation,” Japanese Journal of Ophthalmology, vol. 46, no. 2, pp. 123–129, 2002. View at Publisher · View at Google Scholar · View at Scopus
- K. Krishnan, T. Kathiresan, R. Raman et al., “Ubiquitous lens α-, β-, and γ-crystallins accumulate in anuran cornea as corneal crystallins,” Journal of Biological Chemistry, vol. 282, no. 26, pp. 18953–18959, 2007. View at Publisher · View at Google Scholar · View at PubMed
- M. Bagchi, M. Katar, and H. Maisel, “Heat shock proteins of adult and embryonic human ocular lenses,” Journal of Cellular Biochemistry, vol. 84, no. 2, pp. 278–284, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Chiu, Y. Zhou, S. C. Yeung et al., “Up-regulation of crystallins is involved in the neuroprotective effect of wolfberry on survival of retinal ganglion cells in rat ocular hypertension model,” Journal of Cellular Biochemistry, vol. 110, no. 2, pp. 311–320, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Rothstein and M. Bagchi, “Synthesis of macromolecules in epithelial cells of the cultured amphibian lens. 3. Involvement of protein synthesis in mitotic activation,” Archives Internationales de Physiologie et de Biochimie, vol. 77, no. 4, pp. 717–730, 1969. View at Scopus
- G. J. Wistow and J. Piatigorsky, “Lens crystallins: the evolution and expression of proteins for a highly specialized tissue,” Annual Review of Biochemistry, vol. 57, pp. 479–504, 1988. View at Scopus
- J. Horwitz, “The function of alpha-crystallin,” Investigative Ophthalmology and Visual Science, vol. 34, no. 1, pp. 10–22, 1993. View at Scopus
- M. Maiti, M. Kono, and B. Chakrabarti, “Heat-induced changes in the conformation of α- and β-crystallins: unique thermal stability of α-crystallin,” FEBS Letters, vol. 236, no. 1, pp. 109–114, 1988. View at Publisher · View at Google Scholar · View at Scopus
- K. R. Heys, M. G. Friedrich, and R. J. W. Truscott, “Presbyopia and heat: changes associated with aging of the human lens suggest a functional role for the small heat shock protein, α-crystallin, in maintaining lens flexibility,” Aging Cell, vol. 6, no. 6, pp. 807–815, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Wistow, “Domain structure and evolution in α-crystallins and small heat-shock proteins,” FEBS Letters, vol. 181, no. 1, pp. 1–6, 1985. View at Scopus
- A. Laganowsky, J. L. P. Benesch, M. Landau, et al., “Crystal structures of truncated alphaA and alphaB-crystallins reveal structural mechanisms of polydispersity important for eye lens function,” Protein Science, vol. 19, pp. 1031–1043, 2010.
- B. Raman, T. Ramakrishna, and C. M. Rao, “Temperature dependent chaperone-like activity of alpha-crystallin,” FEBS Letters, vol. 365, no. 2-3, pp. 133–136, 1995. View at Publisher · View at Google Scholar · View at Scopus
- U. Jakob, M. Gaestel, K. Engel, and J. Buchner, “Small heat shock proteins are molecular chaperones,” Journal of Biological Chemistry, vol. 268, no. 3, pp. 1517–1520, 1993. View at Scopus
- F. Baneyx and M. Mujacic, “Recombinant protein folding and misfolding in Escherichia coli,” Nature Biotechnology, vol. 22, no. 11, pp. 1399–1407, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Ehrnsperger, S. Gräber, M. Gaestel, and J. Buchner, “Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation,” EMBO Journal, vol. 16, no. 2, pp. 221–229, 1997. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. J. Lee, A. M. Roseman, H. R. Saibil, and E. Vierling, “A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state,” EMBO Journal, vol. 16, no. 3, pp. 659–671, 1997. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. H. Kim, Y. S. Yu, H. Chung, J. W. Heo, and J. S. Seo, “Effect of the absence of heat shock protein 70.1 (hsp70.1) on retinal photic injury,” Korean Journal of Ophthalmology, vol. 17, no. 1, pp. 7–13, 2003. View at Scopus
- M. Kojima, M. Hoshimaru, T. Aoki et al., “Expression of heat shock proteins in the developing rat retina,” Neuroscience Letters, vol. 205, no. 3, pp. 215–217, 1996. View at Publisher · View at Google Scholar · View at Scopus
- M. Tytell, M. F. Barbe, and I. R. Brown, “Induction of heat shock (stress) protein 70 and its mRNA in the normal and light-damaged rat retina after whole body hyperthermia,” Journal of Neuroscience Research, vol. 38, no. 1, pp. 19–31, 1994. View at Scopus
- G. Tezel and M. B. Wax, “The mechanisms of hsp27 antibody-mediated apoptosis in retinal neuronal cells,” Journal of Neuroscience, vol. 20, no. 10, pp. 3552–3562, 2000. View at Scopus
- Y. Tanaka, K. Kobayashi, M. Kita, S. Kinoshita, and J. Imanishi, “Messenger RNA expression of heat shock proteins (HSPs) during ocular development,” Current Eye Research, vol. 14, no. 12, pp. 1125–1133, 1995. View at Scopus
- H. K. Dinh, B. Zhao, S. T. Schuschereba, G. Merrill, and P. D. Bowman, “Gene expression profiling of the response to thermal injury in human cells,” Physiol Genomics, vol. 7, no. 1, pp. 3–13, 2001. View at Scopus
- G. H. Ochoa, Y. M. Clark, B. Matsumoto, J. A. Torres-Ruiz, and L. J. Robles, “Heat shock protein 70 and heat shock protein 90 expression in light- and dark-adapted adult octopus retinas,” Journal of Neurocytology, vol. 31, no. 2, pp. 161–174, 2002. View at Publisher · View at Google Scholar · View at Scopus
- J. H. Kim, J. H. Kim, Y. S. Yu, S. M. Jeong, and K. W. Kim, “Protective effect of heat shock proteins 70.1 and 70.3 on retinal photic injury after systemic hyperthermia,” Korean Journal of Ophthalmology, vol. 19, no. 2, pp. 116–121, 2005. View at Scopus
- D. O. Zamora, M. Riviere, D. Choi et al., “Proteomic profiling of human retinal and choroidal endothelial cells reveals molecular heterogeneity related to tissue of origin,” Molecular Vision, vol. 13, pp. 2058–2065, 2007. View at Scopus
- J. A. Ko, R. Yanai, W. Y. Quan, N. Morishige, and T. Nishida, “Up-regulation of HSP70 by the fibronectin-derived peptide PHSRN in human corneal epithelial cells,” Biochemical and Biophysical Research Communications, vol. 370, no. 3, pp. 424–428, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Oberringer, H. P. Baum, V. Jung et al., “Differential expression of heat shock protein 70 in well healing and chronic human wound tissue,” Biochemical and Biophysical Research Communications, vol. 214, no. 3, pp. 1009–1014, 1995. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Mushtaq, Z. A. Naqvi, A. A. Siddiqui, C. Palmberg, J. Shafqat, and N. Ahmed, “Changes in albumin precursor and heat shock protein 70 expression and their potential role in response to corneal epithelial wound repair,” Proteomics, vol. 7, no. 3, pp. 463–468, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Mushtaq, Z. A. Naqvi, A. A. Siddiqui, and N. Ahmed, “Albumin precursor and Hsp70 modulate corneal wound healing in an organ culture model,” Acta Histochemica, vol. 113, no. 1, pp. 36–42, 2011. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- O. D. Schein, C. Vicencio, B. Munoz et al., “Ocular and dermatologic health effects of ultraviolet radiation exposure from the ozone hole in Southern Chile,” American Journal of Public Health, vol. 85, no. 4, pp. 546–550, 1995. View at Scopus
- D. Kulms, E. Zeise, B. Pöppelmann, and T. Schwarz, “DNA damage, death receptor activation and reactive oxygen species contribute to ultraviolet radiation-induced apoptosis in an essential and independent way,” Oncogene, vol. 21, no. 38, pp. 5844–5851, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Ringvold, “Corneal epithelium and UV-protection of the eye,” Acta Ophthalmologica Scandinavica, vol. 76, no. 2, pp. 149–153, 1998. View at Scopus
- S. Shimmura, M. Suematsu, M. Shimoyama, K. Tsubota, Y. Oguchi, and Y. Ishimura, “Subthreshold UV radiation-induced peroxide formation in cultured corneal epithelial cells: the protective effects of lactoferrin,” Experimental Eye Research, vol. 63, no. 5, pp. 519–526, 1996. View at Publisher · View at Google Scholar · View at Scopus
- M. Kennedy, K. H. Kim, B. Harten et al., “Ultraviolet irradiation induces the production of multiple cytokines by human corneal cells,” Investigative Ophthalmology and Visual Science, vol. 38, no. 12, pp. 2483–2491, 1997. View at Scopus
- P. J. Francis, V. Berry, A. T. Moore, and S. Bhattacharya, “Lens biology: development and human cataractogenesis,” Trends in Genetics, vol. 15, no. 5, pp. 191–196, 1999. View at Publisher · View at Google Scholar · View at Scopus
- U. P. Andley, “Effects of α-crystallin on lens cell function and cataract pathology,” Current Molecular Medicine, vol. 9, no. 7, pp. 887–892, 2009. View at Publisher · View at Google Scholar · View at Scopus
- S. P. Bhat, “Crystallins, genes and cataract,” Progress in Drug Research, vol. 60, pp. 205–262, 2003. View at Scopus
- B. K. Derham and J. J. Harding, “α-crystallin as a molecular chaperone,” Progress in Retinal and Eye Research, vol. 18, no. 4, pp. 463–509, 1999. View at Publisher · View at Google Scholar · View at Scopus
- R. Ishikura, S. Kato, M. Nagata, A. Tamai, and E. Ohama, “Expression of stress-response protein 60 in lens epithelial cells in atopic cataract,” Japanese Journal of Ophthalmology, vol. 43, no. 2, pp. 89–96, 1999. View at Publisher · View at Google Scholar · View at Scopus
- A. W. Lohse, H. P. Dienes, J. Herkel, E. Hermann, W. Van Eden, and K. H. M. Zum Buschenfelde, “Expression of the 60 kDa heat shock protein in normal and inflamed liver,” Journal of Hepatology, vol. 19, no. 1, pp. 159–166, 1993. View at Publisher · View at Google Scholar · View at Scopus
- P. Fagerholm, B. M. Palmquist, and B. Philipson, “Atopic cataract: changes in the lens epithelium and subcapsular cortex,” Graefe's Archive for Clinical and Experimental Ophthalmology, vol. 221, no. 4, pp. 149–152, 1984. View at Scopus
- K. Kaarniranta, A. Salminen, E. L. Eskelinen, and J. Kopitz, “Heat shock proteins as gatekeepers of proteolytic pathways-Implications for age-related macular degeneration (AMD),” Ageing Research Reviews, vol. 8, no. 2, pp. 128–139, 2009. View at Publisher · View at Google Scholar · View at Scopus
- N. Strunnikova, J. Baffi, A. Gonzalez, W. Silk, S. W. Cousins, and K. G. Csaky, “Regulated heat shock protein 27 expression in human retinal pigment epithelium,” Investigative Ophthalmology and Visual Science, vol. 42, no. 9, pp. 2130–2138, 2001. View at Scopus
- K. Nakata, M. Ohji, Y. Ikuno et al., “Wide-angle viewing lens for vitrectomy,” American Journal of Ophthalmology, vol. 137, no. 4, pp. 760–762, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Pineda, C. C. Chan, M. Ni et al., “Human retinoblastoma cells express αB-crystallin in vivo and in vitro,” Current Eye Research, vol. 12, no. 3, pp. 239–245, 1993. View at Scopus
- S. Kase, J. G. Parikh, and N. Rao, “Expression of α-crystallin in retinoblastoma,” Archives of Ophthalmology, vol. 127, no. 2, pp. 187–192, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. B. Jiang, X. Q. Liu, B. Li et al., “Heat shock proteins and survivin: relationship and effects on proliferation index of retinoblastoma cells,” Histology and Histopathology, vol. 23, no. 7–9, pp. 827–831, 2008. View at Scopus
- C. F. Chen, Y. Chen, K. Dai, P. L. Chen, D. J. Riley, and W. H. Lee, “A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock,” Molecular and Cellular Biology, vol. 16, no. 9, pp. 4691–4699, 1996. View at Scopus
- M. Pardo, A. García, B. Thomas et al., “Proteome analysis of a human uveal melanoma primary cell culture by 2-DE and MS,” Proteomics, vol. 5, no. 18, pp. 4980–4993, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. Zuidervaart, P. J. Hensbergen, M. C. Wong et al., “Proteomic analysis of uveal melanoma reveals novel potential markers involved in tumor progression,” Investigative Ophthalmology and Visual Science, vol. 47, no. 3, pp. 786–793, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. S. Missotten, J. G. Journée-de Korver, D. De Wolff-Rouendaal, J. E. Keunen, R. O. Schlingemann, and M. J. Jager, “Heat shock protein expression in the eye and in uveal melanoma,” Investigative Ophthalmology and Visual Science, vol. 44, no. 7, pp. 3059–3065, 2003. View at Publisher · View at Google Scholar · View at Scopus
- S. E. Coupland, H. Vorum, N. Mandal et al., “Proteomics of uveal melanomas suggests HSP-27 as a possible surrogate marker of chromosome 3 loss,” Investigative Ophthalmology & Visual Science, vol. 51, no. 1, pp. 12–20, 2010. View at Scopus
- L. Whitesell and S. L. Lindquist, “HSP90 and the chaperoning of cancer,” Nature Reviews Cancer, vol. 5, no. 10, pp. 761–772, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. T. L. Soo, G. W. C. Yip, Z. M. Lwin, S. D. Kumar, and B. H. Bay, “Heat shock proteins as novel therapeutic targets in cancer,” In Vivo, vol. 22, no. 3, pp. 311–316, 2008. View at Scopus
- D. R. Ciocca and S. K. Calderwood, “Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications,” Cell Stress and Chaperones, vol. 10, no. 2, pp. 86–103, 2005. View at Publisher · View at Google Scholar · View at Scopus
- R. A. Hitchings and G. L. Spaeth, “Fluorescein angiography in chronic simple and low tension glaucoma,” British Journal of Ophthalmology, vol. 61, no. 2, pp. 126–132, 1977. View at Scopus
- H. A. Quigley, R. W. Nickells, L. A. Kerrigan, M. E. Pease, D. J. Thibault, and D. J. Zack, “Retinal ganglion cell death in experimental glaucoma and after axotomy occurs by apoptosis,” Investigative Ophthalmology and Visual Science, vol. 36, no. 5, pp. 774–786, 1995. View at Scopus
- E. Garcia-Valenzuela, S. Shareef, J. Walsh, and S. C. Sharma, “Programmed cell death of retinal ganglion cells during experimental glaucoma,” Experimental Eye Research, vol. 61, no. 1, pp. 33–44, 1995. View at Publisher · View at Google Scholar · View at Scopus
- G. Tezel, M. R. Hernandez, and M. B. Wax, “Immunostaining of heat shock proteins in the retina and optic nerve head of normal and glaucomatous eyes,” Archives of Ophthalmology, vol. 118, no. 4, pp. 511–518, 2000. View at Scopus
- B. K. Windisch, T. L. LeVatte, M. L. Archibald, and B. C. Chauhan, “Induction of heat shock proteins 27 and 72 in retinal ganglion cells after acute pressure-induced ischaemia,” Clinical and Experimental Ophthalmology, vol. 37, no. 3, pp. 299–307, 2009. View at Publisher · View at Google Scholar · View at Scopus
- W. Huang, J. B. Fileta, T. Filippopoulos, A. Ray, A. Dobberfuhl, and C. L. Grosskreutz, “Hsp27 phosphorylation in experimental glaucoma,” Investigative Ophthalmology and Visual Science, vol. 48, no. 9, pp. 4129–4135, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Qing, X. Duan, and Y. Jiang, “Heat shock protein 72 protects retinal ganglion cells in rat model of acute glaucoma,” Yan Ke Xue Bao, vol. 21, no. 3, pp. 163–168, 2005. View at Scopus
- G. Tezel, G. M. Seigel, and M. B. Wax, “Autoantibodies to small heat shock proteins in glaucoma,” Investigative Ophthalmology and Visual Science, vol. 39, no. 12, pp. 2277–2287, 1998. View at Scopus
- M. B. Wax, G. Tezel, K. Kawase, and Y. Kitazawa, “Serum autoantibodies to heat shock proteins in glaucoma patients from Japan and the United States,” Ophthalmology, vol. 108, no. 2, pp. 296–302, 2001. View at Publisher · View at Google Scholar · View at Scopus
- N. Awasthi and B. J. Wagner, “Upregulation of heat shock protein expression by proteasome inhibition: an antiapoptotic mechanism in the lens,” Investigative Ophthalmology and Visual Science, vol. 46, no. 6, pp. 2082–2091, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. L. Yu, R. Fuchshofer, M. Birke, A. Kampik, H. Bloemendal, and U. Welge-Lüssen, “Oxidative stress and TGF-β2 increase heat shock protein 27 expression in human optic nerve head astrocytes,” Investigative Ophthalmology and Visual Science, vol. 49, no. 12, pp. 5403–5411, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Aghdassi, P. Phillips, V. Dudeja et al., “Heat shock protein 70 increases tumorigenicity and inhibits apoptosis in pancreatic adenocarcinoma,” Cancer Research, vol. 67, no. 2, pp. 616–625, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus