Abstract
Heat shock proteins (Hsp) are primarily protecting and maintaining cell viability during stressful conditions such as thermal and oxidative challenges through protein refolding and stabilization. Hsp play an essential role to confer eye protection from disease states particularly the diseases affecting the retina. Here, we summarize the Hsp function in normal retina, and their involvement in the pathogenesis of certain retinal diseases such cancer, glaucomatous retina, retinitis pigmentosa, and retinal neurodegeneration, as well as the age-related macular degeneration. This information would provide a better understanding of Hsp function and their involvement in ocular disease pathogenesis that could be a target for therapeutic purposes.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Abbreviations
- AMD:
-
Age-related macular degeneration
- GFAP:
-
Glial fibrillary acidic protein
- Hsp:
-
Heat shock proteins
- IMPDH:
-
Inosine-5′-monophosphate dehydrogenase
- RP:
-
Retinitis pigmentosa
- RPE:
-
Retinal pigment epithelium
References
Aguila M, Bevilacqua D, McCulley C, Schwarz N, Athanasiou D, Kanuga N, Novoselov SS, Lange CA, Ali RR, Bainbridge JW, Gias C, Coffey PJ, Garriga P, Cheetham ME (2014) Hsp90 inhibition protects against inherited retinal degeneration. Hum Mol Genet 23:2164–2175
Anckar J, Sistonen L (2007) Heat shock factor 1 as a coordinator of stress and developmental pathways. Adv Exp Med Biol 594:78–88
Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P, Rosen N (2002) Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 277:39858–39866
Bernstein SL, Borst DE, Neuder ME, Wong P (1996) Characterization of a human fovea cDNA library and regional differential gene expression in the human retina. Genomics 32:301–308
Black JA, Waxman SG, Hildebrand C (1985) Axo-glial relations in the retina-optic nerve junction of the adult rat: freeze-fracture observations on axon membrane structure. J Neurocytol 14:887–907
Bradke F, Dotti CG (1999) The role of local actin instability in axon formation. Science 283:1931–1934
Brown IR (2007) Heat shock proteins and protection of the nervous system. Ann N Y Acad Sci 1113:147–158
Calderwood SK, Khaleque MA, Sawyer DB, Ciocca DR (2006) Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci 31:164–172
Chatterjee S, Burns TF (2017) Targeting heat shock proteins in cancer: a promising therapeutic approach. Int J Mol Sci 18:1978
Chatterjee S, Bhattacharya S, Socinski MA, Burns TF (2016) HSP90 inhibitors in lung cancer: promise still unfulfilled. Clin Adv Hematol Oncol 14:346–356
Chen G, Cao P, Goeddel DV (2002) TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol Cell 9:401–410
Chen W, Zheng R, Baade PD, Zhang S, Zeng H, Bray F, Jemal A, Yu XQ, He J (2016) Cancer statistics in China, 2015. CA Cancer J Clin 66:115–132
Chiosis G (2006) Targeting chaperones in transformed systems – a focus on Hsp90 and cancer. Expert Opin Ther Targets 10:37–50
Chiosis G (2016) Heat shock proteins in disease–from molecular mechanisms to therapeutics. Curr Top Med Chem 16:2727
Chuang J-Z, Vega C, Jun W, Sung C-H (2004) Structural and functional impairment of endocytic pathways by retinitis pigmentosa mutant rhodopsin-arrestin complexes. J Clin Invest 114:131–140
Csermely P, Schnaider T, Soti C, Prohaszka Z, Nardai G (1998) The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 79:129–168
Czar MJ, Welsh MJ, Pratt WB (1996) Immunofluorescence localization of the 90-kDa heat-shock protein to cytoskeleton. Eur J Cell Biol 70:322–330
Da Silva JS, Dotti CG (2002) Breaking the neuronal sphere: regulation of the actin cytoskeleton in neuritogenesis. Nat Rev Neurosci 3:694
Darimont BD (1999) The Hsp90 chaperone complex-a potential target for cancer therapy? World J Gastroenterol 5:195–198
Dean DO, Tytell M (2001) Hsp25 and −90 immunoreactivity in the normal rat eye. Invest Ophthalmol Vis Sci 42:3031–3040
Dean DO, Kent CR, Tytell M (1999) Constitutive and inducible heat shock protein 70 immunoreactivity in the normal rat eye. Invest Ophthalmol Vis Sci 40:2952–2962
Decanini A, Nordgaard CL, Feng X, Ferrington DA, Olsen TW (2007) Changes in select redox proteins of the retinal pigment epithelium in age-related macular degeneration. Am J Ophthalmol 143:607–615
Ellis RJ (2007) Protein misassembly. In: Csermely P, VÃgh L (eds) Molecular aspects of the stress response: chaperones, membranes and networks. Springer New York, New York, pp 1–13
Garcia-Carbonero R, Carnero A, Paz-Ares L (2013) Inhibition of HSP90 molecular chaperones: moving into the clinic. Lancet Oncol 14:e358–e369
Garrido C, Brunet M, Didelot C, Zermati Y, Schmitt E, Kroemer G (2006) Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties. Cell Cycle 5:2592–2601
Goedert M, Jakes R (2005) Mutations causing neurodegenerative tauopathies. Biochim Biophys Acta 1739:240–250
Gyrd-Hansen M, Nylandsted J, Jäättelä M (2004) Heat shock protein 70 promotes cancer cell viability by safeguarding lysosomal integrity. Cell Cycle 3:1484–1485
Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144:646–674
Harris H, Rubinsztein DC (2011) Control of autophagy as a therapy for neurodegenerative disease. Nat Rev Neurol 8:108–117
He S, Zhang C, Shafi AA, Sequeira M, Acquaviva J, Friedland JC, Sang J, Smith DL, Weigel NL, Wada Y (2013) Potent activity of the Hsp90 inhibitor ganetespib in prostate cancer cells irrespective of androgen receptor status or variant receptor expression. Int J Oncol 42:35–43
Honjo M, Tanihara H, Kido N, Inatani M, Okazaki K, Honda Y (2000) Expression of ciliary neurotrophic factor activated by retinal Muller cells in eyes with NMDA- and kainic acid-induced neuronal death. Invest Ophthalmol Vis Sci 41:552–560
Jäättelä M (1999) Escaping cell death: survival proteins in cancer. Exp Cell Res 248:30–43
Jacobson C, Schnapp B, Banker GA (2006) A change in the selective translocation of the Kinesin-1 motor domain marks the initial specification of the axon. Neuron 49:797–804
Jaiswal RK, Weissinger E, Kolch W, Landreth GE (1996) Nerve growth factor-mediated activation of the mitogen-activated protein (MAP) kinase cascade involves a signaling complex containing B-Raf and HSP90. J Biol Chem 271:23626–23629
Jarrett SG, Boulton ME (2012) Consequences of oxidative stress in age-related macular degeneration. Mol Asp Med 33:399–417
Jego G, Hazoumé A, Seigneuric R, Garrido C (2013) Targeting heat shock proteins in cancer. Cancer Lett 332:275–285
Jiang L, Liu X, Li B, He X, Jin Y, Li L, Gao F, Wang N (2008) Heat shock proteins and survivin: relationship and effects on proliferation index of retinoblastoma cells. Histol Histopathol 23:827–832
Johnson J, Corbisier R, Stensgard B, Toft D (1996) The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes. J Steroid Biochem Mol Biol 56:31–37
Jolly C, Morimoto RI (2000) Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J Natl Cancer Inst 92:1564–1572
Jung T, Catalgol B, Grune T (2009) The proteasomal system. Mol Asp Med 30:191–296
Kaarniranta K, Sinha D, Blasiak J, Kauppinen A, Vereb Z, Salminen A, Boulton ME, Petrovski G (2013) Autophagy and heterophagy dysregulation leads to retinal pigment epithelium dysfunction and development of age-related macular degeneration. Autophagy 9:973–984
Kanwar JR, Kamalapuram SK, Kanwar RK (2013) Survivin signaling in clinical oncology: a multifaceted dragon. Med Res Rev 33:765–789
Kaplan KB, Li R (2012) A prescription for ‘stress’–the role of Hsp90 in genome stability and cellular adaptation. Trends Cell Biol 22:576–583
Karagoz GE, Rudiger SG (2015) Hsp90 interaction with clients. Trends Biochem Sci 40:117–125
Karunanithi S, Barclay JW, Robertson RM, Brown IR, Atwood HL (1999) Neuroprotection at Drosophila synapses conferred by prior heat shock. J Neurosci 19:4360
Kauppinen A, Niskanen H, Suuronen T, Kinnunen K, Salminen A, Kaarniranta K (2012) Oxidative stress activates NLRP3 inflammasomes in ARPE-19 cells – implications for age-related macular degeneration (AMD). Immunol Lett 147:29–33
Kiang JG, Tsokos GC (1998) Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharmacol Ther 80:183–201
Kimura E, Enns RE, Alcaraz JE, Arboleda J, Slamon DJ, Howell SB (1993) Correlation of the survival of ovarian cancer patients with mRNA expression of the 60-kD heat-shock protein HSP-60. J Clin Oncol Off J Am Soc Clin Oncol 11:891–898
Klettner A (2004) The induction of heat shock proteins as a potential strategy to treat neurodegenerative disorders. Drug News Perspect 17:299–306
Kobayashi K, Kobayashi H, Ueda M, Honda Y (1998) Estrogen receptor expression in bovine and rat retinas. Invest Ophthalmol Vis Sci 39:2105–2110
Kojima M, Hoshimaru M, Aoki T, Takahashi JB, Ohtsuka T, Asahi M, Matsuura N, Kikuchi H (1996) Expression of heat shock proteins in the developing rat retina. Neurosci Lett 205:215–217
Kosik KS, Shimura H (2005) Phosphorylated tau and the neurodegenerative foldopathies. Biochim Biophys Acta 1739:298–310
Labbadia J, Cunliffe H, Weiss A, Katsyuba E, Sathasivam K, Seredenina T, Woodman B, Moussaoui S, Frentzel S, Luthi-Carter R, Paganetti P, Bates GP (2011) Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease. J Clin Invest 121:3306–3319
Lau LF, Schachter JB, Seymour PA, Sanner MA (2002) Tau protein phosphorylation as a therapeutic target in Alzheimer’s disease. Curr Top Med Chem 2:395–415
Li J, Buchner J (2013) Structure, function and regulation of the hsp90 machinery. Biom J 36:106–117
Li Y, Wang YS, Shen XF, Hui YN, Han J, Zhao W, Zhu J (2008) Alterations of activity and intracellular distribution of the 20S proteasome in ageing retinal pigment epithelial cells. Exp Gerontol 43:1114–1122
Li Y, Zhang T, Schwartz SJ, Sun D (2009) New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential. Drug Resist Updat 12:17–27
Lin T-Y, Guo W, Long Q, Ma A, Liu Q, Zhang H, Huang Y, Chandrasekaran S, Pan C, Lam KS (2016) HSP90 inhibitor encapsulated photo-theranostic nanoparticles for synergistic combination cancer therapy. Theranostics 6:1324
Lindquist S, Craig E (1988) The heat-shock proteins. Annu Rev Genet 22:631–677
Luo W, Dou F, Rodina A, Chip S, Kim J, Zhao Q, Moulick K, Aguirre J, Wu N, Greengard P, Chiosis G (2007) Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. Proc Natl Acad Sci USA 104:9511–9516
Luo W, Rodina A, Chiosis G (2008) Heat shock protein 90: translation from cancer to Alzheimer’s disease treatment? BMC Neurosci 9:S7–S7
Martinon F (2008) Detection of immune danger signals by NALP3. J Leukoc Biol 83:507–511
Mayor A, Martinon F, De Smedt T, Petrilli V, Tschopp J (2007) A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses. Nat Immunol 8:497–503
Meli M, Pennati M, Curto M, Daidone MG, Plescia J, Toba S, Altieri DC, Zaffaroni N, Colombo G (2006) Small-molecule targeting of heat shock protein 90 chaperone function: rational identification of a new anticancer lead. J Med Chem 49:7721–7730
Mendes HF, Cheetham ME (2008) Pharmacological manipulation of gain-of-function and dominant-negative mechanisms in rhodopsin retinitis pigmentosa. Hum Mol Genet 17:3043–3054
Mimnaugh EG, Worland PJ, Whitesell L, Neckers LM (1995) Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the hsp90 stress protein and the pp60v-src tyrosine kinase. J Biol Chem 270:28654–28659
Mirshahi M, Nicolas C, Mirshahi A, Hecquet C, d’Hermies F, Faure JP, Agarwal MK (1996) The mineralocorticoid hormone receptor and action in the eye. Biochem Biophys Res Commun 219:150–156
Miyata Y, Nakamoto H, Neckers L (2013) The therapeutic target Hsp90 and cancer hallmarks. Curr Pharm Des 19:347–365
Moore SK, Kozak C, Robinson EA, Ullrich SJ, Appella E (1989) Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome assignments, and evolutionary origins. J Biol Chem 264:5343–5351
Muchowski PJ, Wacker JL (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6:11–22
Nathan DF, Lindquist S (1995) Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol 15:3917–3925
Nathan DF, Vos MH, Lindquist S (1997) In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci USA 94:12949–12956
Neckers L, Workman P (2012) Hsp90 molecular chaperone inhibitors: are we there yet? Clin Cancer Res 18:64–76
Park JW, Moon C, Yun S, Kim SY, Bae YC, Chun M-H, Moon J-I (2007) Differential expression of heat shock protein mRNAs under in vivo glutathione depletion in the mouse retina. Neurosci Lett 413:260–264
Parsell D, Lindquist S (1993) The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 27:437–496
Pearl LH, Prodromou C, Workman P (2008) The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J 410:439–453
Pratt WB (1997) The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase. Annu Rev Pharmacol Toxicol 37:297–326
Pratt WB (1998) The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 217:420–434
Proia DA, Kaufmann GF (2015) Targeting heat-shock protein 90 (HSP90) as a complementary strategy to immune checkpoint blockade for cancer therapy. Cancer Immunol Res 3:583–589
Qin S, Ni M, Wang X, Maurier-Mahe F, Shurland DL, Rodrigues GA (2011) Inhibition of RPE cell sterile inflammatory responses and endotoxin-induced uveitis by a cell-impermeable HSP90 inhibitor. Exp Eye Res 93:889–897
Rui Z, Xiao-Yun G, Xing-Chuang X, You J, Ze-Jian H, Xiang F (2018) Progress in molecular chaperone regulation of heat shock protein 90 and cancer. Chin J Anal Chem 46:301–308
Rutherford SL, Lindquist S (1998) Hsp90 as a capacitor for morphological evolution. Nature 396:336
Saif M, Erlichman C, Dragovich T, Mendelson D, Toft D, Burrows F, Storgard C, Von Hoff D (2013) Open-label, dose-escalation, safety, pharmacokinetic, and pharmacodynamic study of intravenously administered CNF1010 (17-(allylamino)-17-demethoxygeldanamycin [17-AAG]) in patients with solid tumors. Cancer Chemother Pharmacol 71:1345–1355
Sakai M, Sakai H, Nakamura Y, Fukuchi T, Sawaguchi S (2003) Immunolocalization of heat shock proteins in the retina of normal monkey eyes and monkey eyes with laser-induced glaucoma. Jpn J Ophthalmol 47:42–52
Sanchez ER, Redmond T, Scherrer LC, Bresnick EH, Welsh MJ, Pratt WB (1988) Evidence that the 90-kilodalton heat shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells. Mol Endocrinol 2:756–760
Santarosa M, Favaro D, Quaia M, Galligioni E (1997) Expression of heat shock protein 72 in renal cell carcinoma: possible role and prognostic implications in cancer patients. Eur J Cancer 33:873–877
Sauvage F, Messaoudi S, Fattal E, Barratt G, Vergnaud-Gauduchon J (2017) Heat shock proteins and cancer: how can nanomedicine be harnessed? J Control Release 248:133–143
Scheibel T, Buchner J (1998) The Hsp90 complex – a super-chaperone machine as a novel drug target. Biochem Pharmacol 56:675–682
Schwamborn JC, Müller M, Becker AH, Püschel AW (2007) Retracted: ubiquitination of the GTPase Rap1B by the ubiquitin ligase Smurf2 is required for the establishment of neuronal polarity. EMBO J 26:1410–1422
Shapley R, Perry VH (1986) Cat and monkey retinal ganglion cells and their visual functional roles. Trends Neurosci 9:229–235
Shi S-H, Jan LY, Jan Y-N (2003) Hippocampal neuronal polarity specified by spatially localized mPar3/mPar6 and PI 3-kinase activity. Cell 112:63–75
Shi S-H, Cheng T, Jan LY, Jan Y-N (2004) APC and GSK-3β are involved in mPar3 targeting to the nascent axon and establishment of neuronal polarity. Curr Biol 14:2025–2032
Singh A, Singh A, Sand JM, Bauer SJ, Hafeez BB, Meske L, Verma AK (2015) Topically applied Hsp90 inhibitor 17AAG inhibits UVR-induced cutaneous squamous cell carcinomas. J Invest Dermatol 135:1098–1107
Sittler A, Lurz R, Lueder G, Priller J, Hayer-Hartl MK, Hartl FU, Lehrach H, Wanker EE (2001) Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington’s disease. Hum Mol Genet 10:1307–1315
Sliutz G, Karlseder J, Tempfer C, Orel L, Holzer G, Simon MM (1996) Drug resistance against gemcitabine and topotecan mediated by constitutive hsp70 overexpression in vitro: implication of quercetin as sensitiser in chemotherapy. Br J Cancer 74:172–177
Sudhakar J, Venkatesan N, Lakshmanan S, Khetan V, Krishnakumar S, Biswas J (2013) Hypoxic tumor microenvironment in advanced retinoblastoma. Pediatr Blood Cancer 60:1598–1601
Taipale M, Jarosz DF, Lindquist S (2010) HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 11:515–528
Taiyab A, Sreedhar AS, Rao CM (2009) Hsp90 inhibitors, GA and 17AAG, lead to ER stress-induced apoptosis in rat histiocytoma. Biochem Pharmacol 78:142–152
Takayama S, Reed JC, Homma S (2003) Heat-shock proteins as regulators of apoptosis. Oncogene 22:9041–9047
Tam LC, Kiang AS, Campbell M, Keaney J, Farrar GJ, Humphries MM, Kenna PF, Humphries P (2010) Prevention of autosomal dominant retinitis pigmentosa by systemic drug therapy targeting heat shock protein 90 (Hsp90). Hum Mol Genet 19:4421–4436
Tanaka Y, Kobayashi K, Kita M, Kinoshita S, Imanishi J (1995) Messenger RNA expression of heat shock proteins (Hsp) during ocular development. Curr Eye Res 14:1125–1133
Tanihara H, Hangai M, Sawaguchi S, Abe H, Kageyama M, Nakazawa F, Shirasawa E, Honda Y (1997) Up-regulation of glial fibrillary acidic protein in the retina of primate eyes with experimental glaucoma. Arch Ophthalmol 115:752–756
Tapia M, Wandosell F, Garrido JJ (2010) Impaired function of HDAC6 slows down axonal growth and interferes with axon initial segment development. PLoS One 5:e12908
Tarallo V, Hirano Y, Gelfand BD, Dridi S, Kerur N, Kim Y, Cho WG, Kaneko H, Fowler BJ, Bogdanovich S, Albuquerque RJ, Hauswirth WW, Chiodo VA, Kugel JF, Goodrich JA, Ponicsan SL, Chaudhuri G, Murphy MP, Dunaief JL, Ambati BK, Ogura Y, Yoo JW, Lee DK, Provost P, Hinton DR, Nunez G, Baffi JZ, Kleinman ME, Ambati J (2012) DICER1 loss and Alu RNA induce age-related macular degeneration via the NLRP3 inflammasome and MyD88. Cell 149:847–859
Trabulo S, Cardoso A, Santos-Ferreira T, Cardoso A, Simoes S, Pedroso de Lima M (2011) Survivin silencing as a promising strategy to enhance the sensitivity of cancer cells to chemotherapeutic agents. Mol Pharm 8:1120–1131
Tukaj S, Bieber K, Kleszczyński K, Witte M, Cames R, Kalies K, Zillikens D, Ludwig RJ, Fischer TW, Kasperkiewicz M (2017) Topically applied Hsp90 blocker 17AAG inhibits autoantibody-mediated blister-inducing cutaneous inflammation. J Investig Dermatol 137:341–349
Vanden Berghe T, Kalai M, van Loo G, Declercq W, Vandenabeele P (2003) Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis. J Biol Chem 278:5622–5629
Venkatesan N, Kanwar JR, Deepa PR, Navaneethakrishnan S, Joseph C, Krishnakumar S (2016) Targeting HSP90/Survivin using a cell permeable structure based peptido-mimetic shepherdin in retinoblastoma. Chem Biol Interact 252:141–149
Wainberg ZA, Anghel A, Rogers AM, Desai AJ, Kalous O, Conklin D, Ayala R, O’Brien NA, Quadt C, Akimov M (2013) Inhibition of HSP90 with AUY922 induces synergy in HER2-amplified trastuzumab-resistant breast and gastric cancer. Mol Cancer Ther 12(4):509–519
Walton-Diaz A, Khan S, Bourboulia D, Trepel JB, Neckers L, Mollapour M (2013) Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity. Future Med Chem 5:1059–1071
Wang YQ, Zhang XM, Wang XD, Wang BJ, Wang W (2010) 17-AAG, a Hsp90 inhibitor, attenuates the hypoxia-induced expression of SDF-1alpha and ILK in mouse RPE cells. Mol Biol Rep 37:1203–1209
Wang C, Zhang Y, Guo K, Wang N, Jin H, Liu Y, Qin W (2016) Heat shock proteins in hepatocellular carcinoma: molecular mechanism and therapeutic potential. Int J Cancer 138:1824–1834
Waza M, Adachi H, Katsuno M, Minamiyama M, Sang C, Tanaka F, Inukai A, Doyu M, Sobue G (2005) 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration. Nat Med 11:1088
Whitesell L, Lindquist SL (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5:761–772
Workman P, Burrows F, Neckers L, Rosen N (2007) Drugging the cancer chaperone HSP90. Ann N Y Acad Sci 1113:202–216
Wu W-C, Kao Y-H, Hu P-S, Chen J-H (2007) Geldanamycin, a HSP90 inhibitor, attenuates the hypoxia-induced vascular endothelial growth factor expression in retinal pigment epithelium cells in vitro. Exp Eye Res 85:721–731
Xu Y, Lindquist S (1993) Heat-shock protein hsp90 governs the activity of pp60v-src kinase. Proc Natl Acad Sci USA 90:7074–7078
Yan D, Guo L, Wang Y (2006) Requirement of dendritic Akt degradation by the ubiquitin–proteasome system for neuronal polarity. J Cell Biol 174:415–424
Ylikomi T, Wurtz JM, Syvälä H, Passinen S, Pekki A, Haverinen M, Bläuer M, Tuohimaa P, Gronemeyer H (1998) Reappraisal of the role of heat shock proteins as regulators of steroid receptor activity. Crit Rev Biochem Mol Biol 33:437–466
Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94:471–480
Acknowledgements
We would like to thank the Deanship of Scientific Research and RSSU at King Saud University for their technical support.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2019 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Aboelnour, A., Noreldin, A.E., Saadeldin, I.M. (2019). Hsp90 Is a Pivotal Player in Retinal Disease and Cancer. In: Asea, A., Kaur, P. (eds) Heat Shock Protein 90 in Human Diseases and Disorders. Heat Shock Proteins, vol 19. Springer, Cham. https://doi.org/10.1007/978-3-030-23158-3_9
Download citation
DOI: https://doi.org/10.1007/978-3-030-23158-3_9
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-23157-6
Online ISBN: 978-3-030-23158-3
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)