Role of the unfolded protein response (UPR) in cataract formation

Experimental Eye Research

Volumn 83, Issue 3, 2006, Pages 508-516

  Ikesugi, Kengo ^a   Yamamoto, Ryoko ^a   Mulhern, Michael L ^a   Shinohara, Toshimichi ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

apoptosis; cataract; endoplasmic reticulum stress; reactive oxygen species; unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; CALCIMYCIN; CASPASE 12; GLUCOSE REGULATED PROTEIN 78; GLUTATHIONE; HOMOCYSTEINE; REACTIVE NITROGEN SPECIES; TUNICAMYCIN;

ANIMAL CELL; ARTICLE; CATARACT; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVATION; HUMAN; HUMAN CELL; LENS EPITHELIUM; MITOCHONDRION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; UNFOLDED PROTEIN RESPONSE;

ANIMALS; CALCIMYCIN; CATARACT; CELL LINE, TRANSFORMED; EPITHELIAL CELLS; GLUCOSE; GLUTATHIONE; GLYCOSYLATION; HOMOCYSTEINE; HUMANS; IONOPHORES; LENS, CRYSTALLINE; MOLECULAR CHAPERONES; PROTEIN FOLDING; RATS; RATS, SPRAGUE-DAWLEY; REACTIVE OXYGEN SPECIES; TISSUE CULTURE TECHNIQUES; TUNICAMYCIN;

EID: 33745135040     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2006.01.033     Document Type: Article

References (36)

1. Austin R.C., Lentz S.R., and Werstuck G.H. Role of hyperhomocysteinemia in endothelial dysfunction and atherothrombotic disease. Cell Death Differ. 11 Suppl. 1 (2004) S56-S64
2. Benedek G.B. Cataract as a protein condensation disease: the Proctor Lecture. Invest. Ophthalmol. Vis. Sci. 38 (1997) 1911
3. Bloemendal H., de Jong W., Jaenicke R., Lubsen N.H., Slingsby C., and Tardieu A. Ageing and vision: structure, stability and function of lens crystallins. Prog. Biophys. Mol. Biol. 86 (2004) 407-485
4. Chen K.C., Zhou Y., Xing K., Krysan K., and Lou M.F. Platelet derived growth factor (PDGF)-induced reactive oxygen species in the lens epithelial cells: the redox signaling. Exp. Eye Res. 78 (2004) 1057-1067
5. Doerrler W.T., and Lehrman M.A. Regulation of the dolichol pathway in human fibroblasts by the endoplasmic reticulum unfolded protein response. Proc. Natl. Acad. Sci. USA 96 (1999) 13050-13055
6. Fribley A., Zeng Q., and Wang C.Y. Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells. Mol. Cell. Biol. 24 (2004) 9695-9704
7. Gao Y., Feng H.C., Walder K., Bolton K., Sunderland T., Bishara N., Quick M., Kantham L., and Collier G.R. Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress-SelS is a novel glucose-regulated protein. FEBS Lett. 563 (2004) 185-190
8. Giblin F.J. Glutathione: a vital lens antioxidant. J. Ocul. Pharmacol. Ther. 16 (2000) 121-135
9. Giblin F.J., McCready J.P., Schrimscher L., and Reddy V.N. Peroxide-induced effects on lens cation transport following inhibition of glutathione reductase activity in vitro. Exp. Eye Res. 45 (1987) 77-91
10. Guggenmoos-Holzmann I., Engel B., Henke V., and Naumann G.O. Cell density of human lens epithelium in women higher than in men. Invest. Ophthalmol. Vis. Sci. 30 (1989) 330-332
11. Harding J.J., and Crabbe J.C. The lens: development, proteins, metabolism and cataract. In: Davson H. (Ed). The Eye. 3rd Edition (1984), Academic Press, New York 207-492
12. Harding H.P., Zhang Y., Zeng H., Novoa I., Lu P.D., Calfon M., Sadri N., Yun C., Popko B., Paules R., Stojdl D.F., Bell J.C., Hettmann T., Leiden J.M., and Ron D. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell 11 (2003) 619-633
13. Harris A.L. Hypoxia-a key regulatory factor in tumour growth. Nat. Rev. Cancer 2 (2002) 38-47
14. Haynes C.M., Titus E.A., and Cooper A.A. Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. Mol. Cell 15 (2004) 767-776
15. Hightower K.R. The importance of membrane sulfhydryl groups to calcium homeostasis in the lens. Curr. Eye Res. 4 (1995) 857-865
16. Hwang C., Sinskey A.J., and Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257 (1992) 1496-1502
17. Kaufman R.J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13 (1999) 1211-1233
18. Kaufman R.J. Regulation of mRNA translation by protein folding in the endoplasmic reticulum. Trends Biochem. Sci. 29 (2004) 152-158
19. Klein B.E., Klein R., and Lee K.E. Incidence of age-related cataract over a 10-year interval: the Beaver Dam Eye Study. Ophthalmology 109 (2002) 2052-2057
20. Li W.C., Kuszak J.R., Dunn K., Wang R.R., Ma M., Wang G.M., Spector A., Leib M., Coltliar A.M., Weiss M., et al. Lens epithelial cell apoptosis appears to be a common cellular basis for non-congenital cataract development in humans and animals. J. Cell Biol. 130 (1995) 169-181
21. Liu C.Y., Schroder M., and Kaufman R.J. Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J. Biol. Chem. 275 (2000) 24881-24885
22. Lou M.F. Redox regulation in the lens. Prog. Retin. Eye Res. 22 (2003) 657-682
23. Mandic A., Hansson J., Linder S., and Shoshan M.C. Cisplatin induces ER stress and nucleus-independent apoptotic signaling. J. Biol. Chem. 278 (2003) 9100-9106
24. McCarty C.A., and Taylor H.R. A review of the epidemiologic evidence linking ultraviolet radiation and cataracts. Dev. Ophthalmol. 35 (2002) 21-31
25. McCullough K.D., Martindale J.L., Klotz L.O., Aw T.Y., and Holbrook N.J. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol. Cell. Biol. 21 (2001) 1249-1259
26. Palmquist B.M., Philipson B., and Barr P.O. Nuclear cataract and myopia during hyperbaric oxygen therapy. Br. J. Ophthalmol. 68 (1984) 113-117
27. Rao P.V., Maddala R., John F., and Zigler Jr. J.S. Expression of nonphagocytic NADPH oxidase system in the ocular lens. Mol. Vis. 10 (2004) 112-121
28. Shen J., Chen X., Hendershot L., and Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3 (2002) 99-111
29. Shi Y., Vattem K.M., Sood R., An J., Liang J., Stramm L., and Wek R.C. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol. Cell. Biol. 18 (1998) 7499-7509
30. Shinohara T., Ikesugi K., and Mulhern L.M. Cataracts: role of the unfolded protein response. Med. Hypothesis 66 (2006) 365-370
31. Singh D.P., Ohguro N., Kikuchi T., Sueno T., Reddy V.N., Yuge K., Chylack Jr. L.T., and Shinohara T. Lens epithelium-derived growth factor: effects on growth and survival of lens epithelial cells, keratinocytes, and fibroblasts. Biochem. Biophys. Res. Commun. 267 (2000) 373-381
32. Spector A. Review: Oxidative stress and disease. J. Ocul. Pharmacol. Ther. 16 (2000) 193-201
33. Szegezdi E., Fitzgerald U., and Samali A. Caspase-12 and ER-stress-mediated apoptosis: the story so far. Ann. N.Y. Acad. Sci. 1010 (2003) 186-194
34. Tu B.P., and Weissman J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 164 (2004) 341-346
35. Xie Q., Khaoustov V.I., and Chung C.C. Effect of tauroursodeoxycholic acid on endoplasmic reticulum stress-induced caspase-12 activation. Hepatology 36 (2002) 592-601
36. Zigler S.J., and Hess H.H. Cataracts in the Royal College of Surgeons rat: evidence for initiation by lipid peroxidation products. Exp. Eye Res. 41 (1985) 67-76