Relationships between stress, protein damage, nutrition, and age-related eye diseases

Molecular Aspects of Medicine

Volumn 18, Issue 5, 1997, Pages 307-414

  Taylor, A ^a   Shang, F ^a   Obin, M ^a  

^a TUFTS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CALPAIN; CRYSTALLIN; ENZYME; LENS PROTEIN; MATRIX METALLOPROTEINASE; PROTEASOME; PROTEIN; RHODOPSIN; UBIQUITIN; EYE PROTEIN;

AGING; CATARACTOGENESIS; ENZYME SUBSTRATE; EYE DISEASE; HUMAN; LENS; NEUROPROTECTION; NUTRITION; OXIDATION; OXIDATIVE STRESS; PHOTORECEPTOR; PHOTOTRANSDUCTION; PROTEIN DEGRADATION; PROTEIN MODIFICATION; RADIATION EXPOSURE; RETINA DISEASE; RETINA ROD; REVIEW; RISK FACTOR; ANIMAL; METABOLISM; OXIDATION REDUCTION REACTION; PHYSIOLOGY; PSYCHOLOGICAL ASPECT; STRESS;

AGING; ANIMALS; EYE DISEASES; EYE PROTEINS; HUMANS; LENS, CRYSTALLINE; NUTRITION PHYSIOLOGY; OXIDATION-REDUCTION; PHOTORECEPTORS; RISK FACTORS; STRESS;

EID: 0031412659     PISSN: 00982997     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0098-2997(95)00049-6     Document Type: Review

References (529)

1. Agarwal, S. and Sohal, R. S. (1994). Aging and proteolysis of oxidized proteins. Arch. Biochem. Biophys., 309, 24-28.
2. Alcala, J. and Maisel, H. (1985). Biochemistry of the lens membranes and cytoskeleton. In: The Ocular Lens: Structure, Function and Pathology (H. Maisel, ed.), pp. 169-222. Marcel Dekker, New York.
3. Alkalay, I., Yaron, A., Hatzubai, A., Orian, A., Ciechanover, A. and Ben-Neriah, Y. (1995). Stimulation-dependent IkBa phosphorylation marks the NF-kB inhibitor for degradation via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. U.S.A., 92, 10599-10603.
4. Ames, B. N., Shigenaga, M. K. and Hagen, T. M. (1993). Oxidants, antioxidants and the degenerative diseases of aging. Proc. Natl. Acad. Sci. U.S.A., 90, 7915-7922.
5. Anand-Apte, B., Pepper, M. S., Voest, E., Montesano, R., Olsen, B., Murphy, G., Apte, S. S. and Zetter, B. (1997). Inhibition of angiogenesis by tissue inhibitor of metalloproteinase-3. Invest. Opthahnol. Vis. Sci., 38, 817-823.
6. Ananthan, J., Goldberg, A. L. and Voellmy, R. (1986). Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science, 232, 522-524.
7. Anderson, E. I. and Spector, A. (1978). The state of sulfhydryl groups in normal and cataractous lens. I Nuclear region. Exp. Eye Res., 26, 407-417.
8. Aoyama, A., Frohli, E., Schafer, R. and Klemenz, R. (1993). Alpha β-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection. Mol. Cell. Biol., 13, 1824-1835.
9. Apte, S. S., Olsen, B. And Murphy, G. (1995). The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family. J. Biol. Chem. 270, 14313-14318.
10. Armon, T., Ganoth, D. and Hershko, A. (1991). Assembly of the 26S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity. J. Biol. Chem., 265, 20723-20726.
11. Arnason, T. and Ellison, M. J. (1994). Stress resistance in Saccaromyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell. Biol., 14, 7876-7883.
12. Atalla, L. R., Sevanian, A. and Rao, N. A. (1988). Hydrogen peroxide localization in ocular tissue: an electron microscopic cytochemical study. Curr. Eye Res., 7, 931-936.
13. Augusteyn, R. C. (1981). Protein Modification in Cataract, Possible Oxidative Mechanisms. Academic Press, London.
14. Azarian, S. M., Schlamp, C. L. and Williams, D. S. (1993). Characterization of calpain II in the retina and photoreceptor outer segmens. J. Cell Sci., 105, 787-798.
15. Azarian, S. M., King, A. J., Hallett, M. A. and Williams, D. S. (1995). Selective proteolysis of arrestin by calpain: molecular characteristics and its effect on rhodopsin dephosphorylation. J. Biol. Chem., 270, 24375-24384.
16. Azuma, M., David, L. L. and Shearer, T. R. (1991). Cysteine protease inhibitor E64 reduce rate of of formation of selenite cataract in the whole animal. Curr. Eye Res., 10, 657-666.
17. Azuma, M. and Shearer, T. R. (1992). Involvement of calpain in diamide induced cataract in cultured lenses. FEBS Lett., 307, 313-317.
18. Barbe, M. F., Tytell, M., Gower, D. J. and William, J. W. (1988). Hyperthermia protects against light damage in the rat retina Science, 241, 1817-1820.
19. Barchowsky, A., Williams, M. E., Benz, C. C. and Chepenik, K. P. (1994). Oxidation-sensitive protein phosphorylation in endothelial cells. Free Rad. Biol. Med., 16, 771-777.
20. Bassnett, S. and Beebe, D. C. (1992). Coincident loss of mitochondria and nuclei during lens fiber cell differentiation. Dev. Dyn., 194, 85-93.
21. Becerra, S. P., Sagasti, A., Spinella, P. and Notario, V. (1995). Pigment epithelium-derived factor (PEDF) behaves like a noninhibitory serpin: neurotrophic activity does not require the serpin reactive loop. J. Biol. Chem., 270, 25992-25999.
22. Bensch, K. G., Fleming, E. E. and Lohmann, W. (1985). The role of ascorbic acid in senile cataract. Proc. Natl. Acad. Sci. U.S.A., 82, 7193-7196.
23. Berbers, G. A. M., Hoekman, W. A., Bloemendal, H., de Jong, W. W., Kleinschidt, T. and Braunitzer, G. (1984). Homology between the primary structures of the major β-crystallin chains. Eur. J. Biochem., 139, 467-479.
24. Berger, J., Shepard, D., Morrow, F., Sadowski, J., Haire, T. and Taylor, A. (1988a). Reduced and total ascorbate in guinea pig eye tissues in response to dietary intake. Curr. Eye Res., 7, 681-686.
25. Berger, J. J., Eisenhauer, D. A. and Taylor, A. (1988). Intracellular protein degradation in cultured bovine epithelial cells. In Vitro Cell. Dev. Biol., 24, 990-994.
26. Berger, J., Shepard, D., Morrow, F. and Taylor, A. (1989). Relationship between dietary intake and tissue levels of reduced and total vitamin C in the guinea pig. J. Nutr., 119, 1-7.
27. Berman, E. R. (1991). Biochemistry of the Eye, pp. 201-290. Plenum Press, New York.
28. Besharse, J. C., Hollyfield, J. G. and Rayborn, M. E. (1977). Photoreceptor outer segments: accelerated membrane renewal in rods after exposure to light. Science, 196, 536-538.
29. Beswick, H. T. and Harding, J. J. (1987). Conformational changes induced in lens α- and γ-crystallins by modification with glucose 6-phosphate. Biochem. J., 246, 761-769.
30. Betting, J. and Seufert, W. (1996). A yeast Ubc9 mutant protein with temperature-sensitive in vivo function is subject to conditional proteolysis by a ubiquitin- and proteasome-dependent pathway. J. Biol. Chem., 271, 25790-25796.
31. Bhooma, V., Sulochana, K. N., Biswas, J. and Ramakrishnan, S. (1996). Eales' disease: accumulation of reactive oxygen intermediates and lipid peroxides and decrease of antioxidants causing inflammation, neovascularization and retinal damage. Curr. Eye Res., 16, 91-95.
32. Bhuyan, D. K., Podos, S. M., Machlin, L. T., Bhagavan, H. N., Chondhury, D. N., Soja, W. S. and Bhuyan, K. C. (1983). Antioxidant in therapy of cataract II: effect of all-roc-alpha-tocopherol (vitamin E) in sugar-induced cataract in rabbits. Invest. Ophthalmol. Vis. Sci., 24, 74.
33. Bhuyan, K. C. and Bhuyan, D. K. (1984). Molecular mechanism of cataractogenesis: III. Toxic metabolites of oxygen as initiators of lipid peroxidation and cataract. Curr. Eye Res., 3, 67-81.
34. Bindels, J. G., Koppers, A. and Hoenders, H. J. (1981). Structural aspects of bovine β-crystallins: physical characterization including dissociation-association behavior. Exp. Eye Res., 33, 333-343.
35. Bizzi, A., Schaetzle, B., Patton, A., Gambetti, P. and Autilio-Gambetti, L. (1991). Axonal transport of two major components of the ubiquitin system: free ubiquitin and ubiquitin carboxyl-terminal hydrolase PGP 9.5. Brain Res., 548, 292-299.
36. Bloemendal, H., Vermorken, A. J. M., Kibbelaar, M., Dunia, I. and Benedetti, E. L. (1977). Nomenclature for the peptide chains of lens plasma membrane. Exp. Eye Res., 24, 413-415.
37. Bloemendal, H., Piatigorsky, J. and Spector, A. (1989). Recommendations for crystallin nomenclature. Exp. Eye Res., 48, 465-466.
38. Blondin, J. and Taylor, A. (1987). Measures of leucine aminopeptidase can be used to anticipate UV-induced age-related damage to lens proteins: ascorbate can delay this damage. Mech. Age. Devel., 41, 39-46.
39. Blondin, J., Baragi, V., Schwartz, E., Sadowski, J. A. and Taylor, A. (1986). Delay of UV-induced eye lens protein damage in guinea pigs by dietary ascorbate. Free Rad. Biol. Med., 2, 275-281.
40. Blondin, J., Baragi, V. J., Schwartz, E., Sadowski, J. and Taylor, A. (1987). Dietary vitamin C delays UV-indueed age-related eye lens protein damage, Vitamin C. Ann. N.Y. Acad. Sci., 498, 460-463.
41. Blundell, T. L., Lindley, P. F., Miller, L. R., Moss, D. S., Slingsby, C., Turnell, W. G. and Wistow, G. (1993). Interaction of γ-crystallin in relation to eye-lens transparency. Lens Res., 1, 109-131.
42. Bok, D. (1979). Phagocytic properties of the retinal pigment epithelium. In: The Retinal Pigment Epithelium (K. M. Zinn and M. F. Marmour, eds), pp. 148-174. Harvard University Press, Cambridge, MA.
43. Bolton-Smith, C., Casey, C. E., Gey, K. F., Smith, S. C. and Tunstall-Pedoe, H. (1991). Antioxidant intakes assessed using a food-frequency questionnaire: correlation with biochemical status in smokers and nonsmokers. Br. J. Nutr., 65, 337-346.
44. Bond, U. and Schlesinger, M. J. (1985). The chicken ubiquitin gene contains a heat-shock promoter and expresses an unstable mRNA in heat-shocked cells. Mol. Cell. Biol., 5, 949-956.
45. Bonfanti, L., Candeo, P., Piccinini, M., Carmignoto, G., Comelli, M. C., Ghidella, S., Bruno, R., Gobetto, A. and Merighi, A. (1992). Distribution of protein gene product 9.5 (PGP 9.5) in the vertebrate retina: Evidence that immunoreactivity is restricted to mammalian horizontal and ganglion cells. J. Comp. Neurol., 322, 35-44.
46. Bowes, C., Li, T., Danciger, M., Applebury, M. L. and Farber, D. B. (1990). Retinal degeneration in the rd mouse is caused by a defect in the beta subunit of rod cGMP-phosphodiesterase. Nature, 347, 677-680.
47. Bowes, C., Li, T., Frankel, W. N., Danciger, M., Coffin, J. M., Applebury, M. L. and Farber, D. B. (1993). Localization of a retroviral element within the rd gene coding for the beta subunit of cGMP phosphodiesterase. Proc. Natl. Acad. Sci. U.S.A., 90, 2955-2999.
48. Brawn, M. K., Chiou, W. J. and Leach, K. L. (1995). Oxidant-induced activation of protein kinase C in UC11MG cells. Free Rad. Res., 22, 23-37.
49. Bregman, D. B., Halaban, R., van Gool, A. J., Henning, K. A., Friedberg, E. C. and Warren, S. L. (1996). UV-induced ubiquitination of RNA polymerase II: a novel modification deficient in cockayne syndrome cells. Proc. Natl. Acad. Sci. U.S.A., 93, 11586-11590.
50. Brilliant, L. B., Grasset, N. C., Pokhrel, R. P., Kolstad, A., Lepkowski, J. M., Brilliant, G. E., Hawks, W. N. and Parajasegaram, R. (1983). Associations among cataract prevalence, sunlight hours, and altitude in the Himalayas. Am. J. Epidemiol., 118, 250-264.
51. Brown, K., Gerstberger, S., Carlson, L., Franzoso, G. and Siebenlist, U. (1995). Control of IkB proteolysis by site-specific, signal-induced phosphorylation. Science, 267, 1458-1491.
52. Bunce, G. E., Kinoshita, J. and Horwitz, J. (1990). Nutritional factors in cataract. Ann. Rev. Nutr., 10, 233-254.
53. Bunn, H. and Forget, B. (1986). Hemoglobin: Molecular, Genetic and Clinical Aspects, pp. 333-342. W. B. Saunders, Philadelphia, PA.
54. Burton, W. and Ingold, K. U. (1984). Beta-carotene: an unusual type of lipid antioxidant Science, 224, 569-573.
55. Burton, G., W., Wronska, U., Stone, L., Foster, D. O. and Ingold, K. U. (1990). Biokinetics of dietary RRR-alpha-tocopherol in the male guinea pig at three dietary levels of vitamin C and two levels of vitamin E. Evidence that vitamin C does not 'spare' vitamin E in vivo. Lipids, 25, 199-210.
56. Bush, K. T., Goldberg, A. L. and Nigam, S. K. (1997). Froteasome inhibition leads to a heat shock response, induction of endoplasmic reticulum chaperones and thermotolerance. J. Biol. Chem., 272, 9086-9092.
57. Calissendorff, B. M., Lonnqvist, B. and el Azazi, M. (1995). Cataract development in adult bone marrow transplant recipients. Acta Ophthalmol. Scand., 73, 52-154.
58. Campanero, M. R. and Flemington, E. K. (1997). Regulation of E2F through ubiquitin-proteasome-dependent degradation: stabilization by the pRB tumor suppressor protein. Proc. Natl. Acad. Sci. U.S.A., 94, 2221-2226.
59. Casey, E. B., Zhao, H. R. and Abraham, E. C. (1995). Role of glycine 1 and lysine 2 in the glycation of bovine gamma B-crystallin. Site-directed mutagenesis of lysine to threonine. J. Biol. Chem., 270, 20781-20786.
60. Chain, D. G., Hedge, A. N., Yamamoto, N., Liu-Marsh, B. and Schwartz, J. H. (1995). Persistent activation of cAMP-dependent protein kinase by regulated proteolysis suggests a neuron-specific function of the ubiquitin system in Aplysia. J. Neurosci., 15, 7592-7603.
61. Chan, C. W. and Billson, F. A. (1991). Visual disability and major causes of blindness in NSW: a study of people aged 50 and over attending the Royal Blind Society 1984 to 1989. Aust. N. Zealand J. Ophthalmol., 19, 321-325.
62. Charbre, M. and Deterre, P. (1989). Molecular mechanisms of visual transduction. Eur. J. Biochem., 179, 55-266.
63. Chatterjee, A., Milton, R. C. and Thyle, S. (1982). Prevalence and etiology of cataract in Punjab. Br. J. Ophthalmol., 66, 35-42.
64. Chen, Z. J., Parent, L. and Maniatis, T. (1996). Site-specific phosphorylation of IkBa by a novel ubiquitination-dependent protein kinase activity. Cell, 84, 853-862.
65. Cheng, H., Parish, C. A., Gilbert, B. A. and Rando, R. R. (1995). A novel enoprotease reponsible for the specific cleavage of transducin gamma subunit. Biochemistry, 34, 16662-16671.
66. Cheng, L., Watt, R. and Piper, P. W. (1994). Polyubiquitin gene expression contributes to oxidative stress resistance in respiratory yeast (Saccharomyces cerevisiae). Mol. Gen. Genet., 246, 358-362.
67. Chiesa, R., Gawinowicz-Kolks, M. A. and Spector, A. (1987). The phosphorylation of the primary gene products of α-crystallin. J. Biol. Chem., 262, 1438-1441.
68. Chiesa, R., Gawinowicz-Kolks, M. A., Kleiman, N. J. and Spector, A. (1988). Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin. Exp. Eye Res., 46, 199-208.
69. Chiou, S.-H., Chylack, L. T., Tung, W. H. and Bunn, H. F. (1981). Nonenzymatic glycosylation of bovine lens crystallins: effect of aging. J. Biol. Chem., 256, 5176-5180.
70. Chow, C. K., Thacker, R. R., Changchit, C., Bridges, R. B., Rehm, S. R., Humble, J. and Turbek, J. (1986). Lower levels of vitamin C and carotenes in plasma of cigarette smokers. J. Am. Coll. Nutr., 5, 305-312.
71. Chylack, L. T., Wolfe, J. K., Singer, D. M., Leske, M. C., Bullimore, M. A., Bailey, I. L., Friend, J., McCarthy, D. and Wu, S. (1993). The lens opacities classification system III. Arch. Ophthalmol., 111, 831-836.
72. Chylack, L. T., Wolfe, J. K., Friend, J., Singer, D. M., Wu, S. Y. and Leske, M. C. (1994). Nuclear cataract: relative contributions to vision loss of opalescence and brunescence. Invest. Ophthalmol. Vis. Sci., 35, 42632 abstract.
73. Ciechanover, A. and Schwartz, A. L. (1994). The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins. FASEB J., 8, 182-191.
74. Ciechanover, A., Elias, S., Heller, H. and Hershko, A. (1982). 'Covalent affinity' purification of ubiquitin-activating enzyme. J. Biol. Chem., 257, 2537-2542.
75. Ciechanover, A., Finley, D. and Varshavsky, A. (1984). Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell, 37, 57-66.
76. 2 exposure on lens morphology and biochemistry. Exp. Eye Res., 57, 157-167.
77. Clark, J. I., Livesey, J. C. and Steele, J. E. (1996). Delay or inhibition of rat lens opacification using pantethine and WR-77913, Exp. Eye Res., 62, 75-84.
78. Cobb, A. J., Nagase, H., Brew, K., Toth, C., Itoh, Y. and De LaPaz, M. A. (1997). Matrix metalloproteinases and their inhibitors in vitreous in age-related macular degeneration and proliferative diabetic retinopathy. Invest. Opthalmol. Vis. Sci., 38, s354.
79. Collier, I. E., Wilhelm, S. M., Eisen, A. Z., Marmer, B. L., Grant, G. A., Seltxer, J. L., Kronenberger, A., He, C., Bauer, E. A. and Goldberg, G. I. (1988). H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single mettaloproteinase capable of degrading basement membrane collagen. J. Biol. Chem., 263, 6579-6587.
80. Congdon, N. G., Duncan, D. D., Fisher, D., Rieger, K., Urist, J., Sanchez, A. M., Vitale, S., West, S. K., Pham, T., Cole, L. and McNaughton, C. (1997). UV light and lenticular opacities in the Emory Mouse. Invest. Ophthalmol. Vis. Sci., 38, 1020.
81. Cook, J. M. and Chock, P. B. (1995). Phosphorylation of ubiquitin-activating enzyme in cultured cells. Proc. Natl. Acacl. Sci. U.S.A., 92, 3454-3457.
82. Corsi, D., Galluzzi, L., Lecomte, M. C. and Magnani, M. (1997). Identification of alpha-specrin domains susceptible to ubiquitination. J. Biol. Chem., 272, 2977-2983.
83. Costagliola, C., Iuliano, G., Menzione, M., Rinaldi, E., Vito, P. and Auricchio, G. (1986). Effect of vitamin E on glutathione content in red blood cells, aqueous humor and lens of humans and other species. Exp. Eye Res., 43, 905-914.
84. Creighton, M. O., Ross, W. M., Stewart-DeHaan, P. J., Sanwai, M. and Trevithick, J. R. (1985). Modeling cortical cataractogenesis. VII: Effects of vitamin E treatment on galactose induced cataracts. Exp. Eye Res., 40, 213-222.
85. Croft, L. R. (1972). The amino acid sequence of γ-crystallin (fraction II) from calf lens. Biochem. J., 128, 961-970.
86. Cruickshanks, K. J., Klein, B. E. and Klein, R. (1992). Ultraviolet light exposure and lens opacities: the Beaver Dam Eye Study. Am. J. Public Health, 82, 1658-1662.
87. Daicker, B., Schiedt, K., Adnet, J. J. and Bermond, P. (1987). Canthaxamin retinopathy. An investigation by light and electron microscopy and physiochemical analyses. Graefe's Arch. Clin. Exp. Ophthalmol., 225, 189-197.
88. Dana, M. R., Tielsch, J. M., Enger, C., Joyce, E., Santoli, J. M. and Taylor, H. R. (1990). Visual impairment in a rural Appalachian community: prevalence and causes. J. Am. Med. Assoc., 264, 2400-2405.
89. Danciger, M., Heilbron, V., Gao, Y-Q., Zhao, D-Y., Jacobson, S. G. and Farber, D. B. (1996). A homozygous PDE6B mutation in a family with autosomal recessive retinitis pigmentosa. Mol. Vis. 2, 10. 〈http://www.emory.edu/molvis/v2/danciger〈.
90. David, L. L., Dickey, B. M. and Shearer, T R. (1987). Origin of urea soluble protein in the selenite cataract. Role of β-crystallin proteolysis and calpain II. Invest. Ophthalmol. Vis. Sci., 28, 1148-1156.
91. David, L. L. and Shearer, T. R. (1984). Calcium-activated proteolysis in the lens nucleus during selenite cataractogenesis. Invest. Ophthalmol. Vis. Sci., 25, 1275-1283.
92. David, L. L. and Shearer, T. R. (1986). Purification of calpain II from rat lens and determination of endogenous substrates. Exp. Eye Res., 42, 227-238.
93. David, L. L., Takemoto, L., Anderson, R. S. and Shearer, T. R. (1988). Proteolytic changes in main intrinsic polypeptide (MIP26) from membranes in selenite cataract. Curr. Eye Res., 7, 411-417.
94. David, L. L., Varnum, M. D., Lampi, K. J. and Shearer, T. R. (1989). Calpain II in human lens. Invest. Ophthalmol. Vis. Sci., 30, 269-275.
95. David, L. L., Wright, J. W. and Shearer, T. R. (1992). Calpain II induced insolubilization of lens β-crystallin polypeptides may induce cataract. Biochim. Biophys. Acta, 1139, 210-216.
96. Davie, E. W., Fujikawa, K., Legaz, M. E. and Kato, H. (1975). Role of proteases in blood coagulation. In: Proteases and Biological Control,Cold Spring Harbor Conferences On Cell Proliferation, Vol. 2 (E. Reich, D. B. Rifkin and E. Shaw, eds.), pp. 65-77. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
97. Davies, K. J. A. (1986). Intracellular proteolytic systems may function as antioxidant defenses: an hypothesis. Free Rad. Biol. Med., 2, 155-173.
98. Delaye, M. and Tardieu, A. (1983). Short-range order of crystallin proteins accounts for eye lens transparency. Nature, 302, 415-417.
99. DeMartino, G. N., McCullough, M. L., Reckelhoff, J. F., Croall, D. E., Ciechanover, A. and McGuire, M. J. (1991). ATP-stimulated degradation of endogenous proteins in cell-free extracts of BHK 21/C13 fibroblasts. A key role for the proteinase, macropain, in the ubiquitin-dependent degradation of short-lived proteins. Biochim. Biophys. Acta, 1073, 299-308.
100. Devamanoharan, P. S., Ramachandran, S. and Varma, S. D. (1991). Hydrogen peroxide in the eye lens: radioisotopic determination. Curr. Eye Res., 10, 831-838.
101. Devamanoharan, P. S., Henein, M., Morris, S., Ramaehandran, S., Richards, R. D. and Varma, S. D. (1991). Prevention of selenite cataract by vitamin C. Exp. Eye Res., 52, 563-568.
102. 2 determination in rat lens: Chemiluminescent versus radioisotopic methods. Opthalmic Res., 27, Suppl. 39-43.
103. Dice, J. F. (1993). Cellular and molecular mechanisms of aging. Physiol. Rev., 73, 149-159.
104. Di Mascio, P., Murphy, M. E. and Sies, H. (1991). Antioxidant defense systems: the role of carotenoids, tocopherols and thiols. Am. J. Clin. Nutr., 53, 194S-200S.
105. Dolin, P. (1995). Assessment of the epidemiological evidence that exposure to solar ultraviolet radiation causes cataract. Documenta Ophthalmol., 88, 327-337.
106. Dryja, T. P., Hahn, L. B., Cowley, G. S., McGee, T. L. and Berson, E. L. (1991). Mutation spectrum of the rhodopsin gene among patients with autosomal dominant retinitis pigmentosa. Proc. Natl. Acad. Sci. U.S.A., 88, 6481-6485.
107. Dubiel, W. and Rapoport, S. M. (1989). ATP-dependent proteolysis of mitochondria of reticulocytes. Rev. Biol. Cel., 21, 505-521.
108. Dumonde, D. C., Limb, G. A., Hollified, R. D., Chignell, A. H., Miller, K. and Williamson, T. H. (1997). Relationships between metallop[roteinases, TIMP-1 and TNF-Rs in vitreous from eyes with proliferative vitreoretinopathy. Invest. Ophthalmol. Vis. Sci., 38, s1176.
109. Duncan, G. and Jacob, T. J. C. (1984). The lens as a physiochemical system. In: The Eye (H. Davson, ed.), Vol. 1b, pp. 169-206. Academic Press, Orlando, FL.
110. Dunia, I., Manenti, S., Rousselet, A. and Benedetti, E. L. (1987). Electron microscopic observation of reconstituted proteoliposomes with the purified major intrinsic membrane protein of eye lens fibers. J. Cell Biol., 105, 1679-1689.
111. Dunn, J. A., Patrick, J. S., Thorpe, S. R. and Baynes, J. W. (1989). Oxidation of glycated proteins: age-dependent accumulation of N epsilon-(carboxymethyl)lysine in lens proteins. Biochemistry, 28, 9464-9468.
112. Eisenhauer, D. A., Berger, J. J., Peltier, C. Z. and Taylor, A. (1988). Protease activities in cultured beef lens epithelial cells peak and then decline upon progressive passage. Exp. Eye Res., 46, 579-590.
113. Enari, M., Hug, H. and Nagata, S. (1995). Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature, 375, 78-81.
114. Erdman, J. (1988). The physiologic chemistry of carotenes in man. Clin. Nutr., 7, 101-106.
115. Evans, M. D. And Pryor, W. A. (1994). Cigarette smoking, emphysema, and damage to alpha 1-proteinase inhibitor. Am. J. Physiol. (Pt 1) 266, L593-611.
116. Farber, D. B., Danciger, J. S. and Organisciak, D. T. (1991). Levels of mRNA encoding proteins of the cGMP cascade as a function of light environment. Exp. Eye Res., 53, 781-786.
117. Farber, D. B., Danciger, J. H. and Aguirre, G. (1992). The beta subunit of cyclic GMP hosphodiesterase mRNA is deficient in canine rod-cone dysplasia 1. Neuron, 9, 349-356.
118. Fariss, R. N., Apte, S. S., Olsen, B. R., Iwata, K. and Milam, A. H. (1997). Tissue inhibitor of metallopreoteinase-3 is a component of Bruch's membrane of the eye. Am J. Pathol., 150, 3223-3228.
119. Faucheu, C., Diu, A., Chan, A. W., Blanchet, A. M., Miossec, C., Herve, F., CollardDutilleul, V., Gu, Y., Aldape, R. A., Lippke, J. A., Rocher, C., Su, M. S.-S., Livingston, D. J., Hercend, T. and Lalanne, J-L. (1995). A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells. EMBO J., 14, 1914-1922.
120. Faucheu, C., Blanchet, A. M., Collard-Dutilleul, V., Lalanne, J. L. and Diu-Hercend, A. (1996). Identification of a cysteine proteae closely related to interleukin-1 beat-converting enzyme. Eur. J. Biochem., 236, 207-213.
121. Finley, D., Ozkavnak, E. and Varshavsky, A. (1987). The yeast polyubiquitin gene is essential for resistance to high temperature, starvation and other stresses. Cell, 48, 1035-1046.
122. Flaye, D. E., Sullivan, K. N., Cullinan, T. R., Silver, J. H. and Whitelocke, R. A. F. (1989). Cataracts and cigarette smoking: the City Eye Study. Eye, 3, 379-384.
123. Fleshman, K. R. and Wagner, B. J. (1984). Changes during aging in rats lens endopeptidase activity. Exp. Eye Res., 39, 543-551.
124. Fraser, J., Luu, H. A., Neculcea, J., Thomas, D. Y. and Storms, R. K. (1991). Ubiquitin gene expression: response to environmental changes. Curr. Genet., 20, 17-23.
125. Frei, B., Stocker, R. and Ames, B. N. (1988). Antioxidant defenses and lipid peroxidation in human blood plasma. Proc. Natl. Acad. Sci. U.S.A., 85, 9748-9752.
126. Fridovich, I. (1984). Oxygen: aspects of its toxicity and elements of defense. Curr. Eye Res., 3, 1-2
127. Fukada, Y., Takao, T., Ohguro, H., Yoshizawa, T., Akino, T. and Shimonishi, Y. (1990). Farnesylated gamma-subunit of photoreceptor G protein indispensable for GTP-binding. Nature, 346, 658-660.
128. Fukada, Y., Matsuda, T., Kokame, K., Takao, T., Shimonishi, Y., Akino, T. and Yoshizawa, T. (1994). Effects of carboxyl methylation of photoreceptor G protein gamma-subunit in visual transduction. J. Biol. Chem., 269, 5163-5170.
129. Fung, B. K.-K. and Nash, C. R. (1983). Characterization of transducin from bovine retinal rod outer segments. II. Evidence for distinct binding sites and conformational changes revealed by limited proteolysis with trypsin. J. Biol. Chem., 258, 10503-10510.
130. Fung, B. K.-K., Hurley, J. and Stryer, L. (1981). Flow of information in the light-triggered cyclic nucleotide cascade of vision. Proc. Natl. Acad. Sci. U.S.A., 78, 152-156.
131. Garland, D. D. (1991). Ascorbic acid and the eye. Am. J. Clin. Nutr., 54, 1198S-1202S.
132. Garlick, R. L., Mazer, J. S., Chylack, L. T., Tung, W. H. and Bunn, H. F. (1984). Nonenzymatic glycation of human lens crystallin. Effect of aging and diebetes mellitus. J. Clin. Invest., 74, 1742-1749.
133. Garner, M. H. and Spector, A. (1980). Selective oxidation of cysteinc and methionine in normal and senile cataractous lenses. Proc. Natl. Acad. Sci. U.S.A., 77, 1274-1277.
134. Garner, W. H., Garner, M. H. and Spector, A. (1979). Comparison of the 10000 and 43000 dalton polypeptide population isolated from the water soluble and insoluble fractions of human cataractous lenses. Exp. Eye Res., 29, 257-276.
135. 2 in aqueous humor. Exp. Eye Res., 38, 87-93.
136. Giblin, F. J., Schrimscher, L., Chakrapani, B. and Reddy, V. N. (1988). Exposure of rabbit lens to hyperbaric oxygen in vitro: regional effects on GSH level. Invest. Ophthalmol. Vis. Sci., 29, 1312-1313.
137. 2 in rabbit lens. Invest. Ophthalmol. Vis. Sci., 22, 330-335.
138. Giblin, F. J., Padgaonkar, V. A., Leverenz, V. R., Lin, L. R., Lou, M. F., Unakar, N. J., Dang, L., Dickerson, J. E. J. and Reddy, V. N. (1995). Nuclear light scattering, disulfide formation and membrane damage in lenses of older guinea pigs treated with hyperbaric oxygen. Exp. Eye Res., 60, 219-235.
139. Giraud, D. W., Martin, H. D. and Driskell, J. A. (1995). Plasma and dietary vitamin C and E levels of tobacco chewers, smokers, and nonusers. J. Am. Diet. Assoc., 95, 798-800.
140. Glotzer, M., Murray, A. W. and Kirschner, M. W. (1991). Cyclin is degraded by the ubiquitin pathway. Nature, 349, 132-138.
141. Goebl, M. G., Goetsch, L. and Byers, B. (1994). The Ubc3 (Cdc34) ubiquitin-conjugating enzyme is ubiquitinated and phosphorylated in vivo. Mol. Cell. Biol., 14, 3022-3029.
142. Gorin, M. B., Yanecy, S. B., Cline, J., Revel, J. P. and Horwitz, J. (1984). The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning. Cell, 39, 49-59.
143. Gregori, L., Fuchs, C., Figueiredo-Pereira, M. E., Van Nostrand, W. E. and Goldgaber, D. (1995). Amyloid beta-protein inhibits ubiquitin-dependent protein degradation in vitro. J. Biol. Chem., 270, 19702-19708.
144. Green, C. B. and Besharse, J. C. (1996). Identification of a novel vertebrate circadian clock-regulated gene encoding the protein nocturnin. Proc. Natl. Acad. Sci. U.S.A., 93, 14884-14888.
145. Grune, T., Reinheckel, T. and Davies, K. J. A. (1996). Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J. Biol. Chem., 271, 15504-15505.
146. Grune, T., Reinheckel, T. and Davies, K. J. (1997). Degradation of oxidized proteins in mammalian cells. FASEB J., 11, 526-534.
147. Guey-Shuang, W., Zhang, J. and Rao, N. A. (1997). Peroxynitrite and oxidative damage in experimental autoimmune uveitis. Invest. Opthalmol. Vis. Sci., 38, 1333-1339.
148. Guo, L., Hussain, A. A., Kundaiker, S. and Marshall, J. (1997). Metalloproteinase activity of human Bruch's membrane-choroid samples as a function of age. Invest. Opthalmol. Vis. Sci., 38, s354.
149. Guo-min, W., Spector, A., Lus, C-q., Tang, L-q., Xu, L-h., Guo, W-Y. and Huang, Y-q. (1990). Prevalence of age-related cataract in Ganzi and Shanghai. Chinese Med. J., 103, 945-951.
150. Gurevich, V. V. and Benovic, J. L. (1993). Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. J. Biol. Chem, 268, 11628-11638.
151. Haas, A. L. (1990). Role of ubiquitin in protein degradation. In: Protein Metabolism in Aging (H. L. Segal, M. Rothstein and E. Bergamini, eds.), pp. 135-149. Wiley-Liss, New York, NY.
152. Haas, A. L., Warms, J. V. B., Hershko, A. and Rose, I. A. (1982). Ubiquitin-activating enzyme, mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem., 257, 2537-2548.
153. Hafezi, F., Steinbach, J. P., Marti, A., Munz, K., Aguzzi, A. and Reme, C. E. (1997). Lack of c-fos protects retinal photoreceptors from delayed light-induced apoptosis in vivo. Invest. Ophthalmol. Vis. Sci., 38, s719.
154. Hammond, B. R., Wooten, B. R. and Snodderly, D. M. (1997). The retinal carotenoids lutein and zeaxanthin associated with the clarity of the human crystalline lens. Invest. Ophthalmol. Vis. Sci., 38, 1795-1801.
155. Hankinson, S. E., Willett, W. C., Colditz, G. A., Seddon, J. M., Rosner, B., Speizer, F. E. and Stamper, M. J. (1992). A prospective study of cigarette smoking and risk of cataract surgery in women. J. Am. Med. Assoc., 268, 994-998.
156. Hankinson, S. E., Stampfer, M. J., Seddon, J. M., Colditz, G. A., Rosner, B., Speizer, F. E. and Willett, W. C. (1992). Intake and cataract extraction in women: a prospective study. Br. Med. J., 305, 335-339.
157. Hankinson, S. E., Willett, W. C., Colditz, G. A., Seddon, J. M., Rosner, B., Speizer, F. E. and Stamfer, M. J. (1992). A prospective study of cigarette smoking and risk of cataract surgery in women. J. Am. Med. Assoc., 268, 994-998.
158. Hanna, C. and O'Brien, J. E. (1961). Cell production and migration in the epithelial layer of the lens. Arch. Ophthalmol., 66, 103-107.
159. Harding, J. J. (1985). Nonenzymatic covalent posttranslational modification of proteins in vivo. Adv. Protein Chem., 37, 247-334.
160. Harding, J. J. and Crabbe, M. J. C. (1984). The lens: development, proteins, metabolism and cataract. In: The Eye (M. Davson, ed.), Vol. 1B, pp. 207-492. Academic Press, New York.
161. Harding, J. J. and van Heyningen, R. (1987). Epidemiology and risk factors for cataract. Eye, 1, 537-541.
162. Hargrave, P. A. and McDowell, J. H. (1992). Rhodopsin and phototransduction: a model system for G protein-linked receptors. FASEB J., 6, 2323-2331.
163. Heinemayer, W., Kleinschmidt, J. A., Saidowsky, J., Escher, C. and Wolf, D. H. (1991). Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress-induced proteolysis and uncover its necessity for cell survival. EMBO J., 10, 555-562.
164. Hershko, A. and Ciechanover, A. (1992). The ubiquitin system for protein degradation. Ann. Rev. Biochem, 61, 761-807.
165. Hershko, A., Eytan, E. and Ciechanover, A. (1982). Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells. J. Biol. Chem., 257, 13964-13970.
166. Hershko, A., Heller, H., Elias, S. and Ciechanover, A. (1983). Components of the ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem., 258, 8206-8214.
167. Hershko, A., Ganoth, D., Sudakin, V., Dahan, A., Cohen, L. H., Luca, F. C., Ruderman, J. V. and Eytan, E. (1994). Components of a system that ligates cyclin to ubiquitin and their regulation by the protein kinase cdc2. J. Biol. Chem., 269, 4940-4946.
168. van Heyningen, R. and Waley, S. G. (1963). Neutral proteinases in the lens. 2. Partial purification and properties. Biochem. J., 86, 92-101.
169. Hickey, L. and Riezman, H. (1996). Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell, 84, 277-287.
170. Hightower, K. R., David, L. L. and Shearer, T. R. (1987). Regional distribution of free calcium in selenite cataract. Relation to calpain II. Invest. Ophthalmol. Vis. Sci., 28, 1433-1436.
171. Hiller, R., Giacometti, L. and Yuen, K. (1977). Sunlight and cataract: an epidemiologic investigation. Am. J. Epidemiol., 105, 450-459.
172. Hirvela, H., Luukinen, H. and Laatikainen, L. (1995). Prevalence and risk factors of lens opacities in the elderly in Finland. A population-based study. Ophthalmology, 102, 108-117.
173. Hochstrasser, M. (1995). Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol., 7, 215-223.
174. Hofmann, K. P., Pulvermuller, A., Buczylko, J., Hooser, P. V. and Palczewki, K. (1992). The role of arrestin and retinoids in the regeneration pathway of rhodopsin. J. Biol. Chem., 267, 15701-15706.
175. Hoffman, D. W., Wiebkin, P. and Rybak, L. P. (1995). Inhibition of glutathione-related enzymes and cytotoxicity of ethacrynic acid and cyclosporine. Biochem. Pharmacol., 49, 411-415.
176. Horwitz, J. (1992). α-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U.S.A., 89, 10449-10453.
177. Huang, L. L., Jahngen-Hodge, J. and Taylor, A. (1993). Bovine lens epithelial cells have a ubiquitin-dependent proteolysis system. Biochim. Biophys. Acta, 1175, 181-187.
178. Huang, L-L., Shang, F., Nowell, T. R. and Taylor, A. (1995). Degradation of differentially oxidized α-crystallins in bovine lens epithelial cells. Exp. Eye Res., 61, 45-54.
179. Huang, S. H., Pittler, S. J., Huang, X., Oliveira, L., Berson, E. L. and Dryja, T. P. (1995). Autosomal recessive retinitis pigmentosa caused by mutations in the α subunit of rod cGMP phosphodiesterase. Nature Genet., 11, 468-471.
180. Huang, Y., Baker, R. T. and Fischer-Vize, J. A. (1995). Control of cell fate by a deubiqutinating enzyme encoded by the fat facets gene. Science, 270, 1828-1831.
181. Huby, R. and Harding, J. J. (1988). Non-enzymatic glycosylation (glycation) of lens proteins by galactose and protection by aspirin and reduced glutathione. Exp. Eye Res., 47, 53-59.
182. Ireland, M. E. and Maisel, H. (1984). Evidence for a calcium activated protease specific for lens intermediate filaments. Curr. Eye Res., 3, 423-429.
183. Jacob, R. A., Otradovec, C. L., Russell, R. M., Munro, H. N., Hartz, S. C., McGandy, R. B., Morrow, F. and Sadowski, J. A. (1988). Vitamin C status and interactions in a healthy elderly population. Am. J. Clin. Nutr., 48, 1436-1442.
184. Jacques, P. F. and Chylack, L. T. (1991). Epidemiologic evidence of a role for the antioxidant vitamins and carotenoids in cataract prevention. Am. J. Clin. Nutr., 53, 352S-355S.
185. Jacques, P. F. and Taylor, A. (1991). Micronutrients and age-related cataracts. In: Micronutrients in Health and in Disease Prevention (A. Bendich and C. E. Butterworth, eds.), pp. 359-379. Marcel Dekker, New York.
186. Jacques, P. F., Lahav, M., Willett, W. C. and Taylor, A. (1992). Relationship between long-term vitamin C intake and prevalence of cataract and macular degeneration. Exp. Eye Res., 55, suppl. 1, 152 abstract.
187. Jacques, P. F., Chylack, L. T. Jr and Taylor, A. (1994). Relationships between natural antioxidants and cataract formation. In: Natural Antioxidants Human Health and Disease (Frei B, ed.), pp. 513-533. Academic Press, Orlando, FL.
188. Jacques, P. F., Taylor A., Hankinson S. E., Lahav M., Mahnken B., Lee, Y., Vaid K. and Willett W. C. (1997). Long-term vitamin C supplement use and prevalence of early age-related lens opacities. Am. J. Clin. Nutr., 66, 911-916.
189. Jahngen, J. H., Haas, A. L., Ciechanover, A., Blondin, J., Eisenhauer, D. and Taylor, A. (1986). The eye lens has an active ubiquitin-protein conjugation system. J. Biol. Chem., 261, 13760-13767.
190. Jahngen, J. H., Lipman, R. D., Eisenhauer, D. A., Jahngen, E. G. E. and Taylor, A. (1990). Aging and cellular maturation causes changes in ubiquitin-eye lens protein conjugates. Arch. Biochem. Biophys., 276, 32-37.
191. Jahngen-Hodge, J., Laxman, E., Zuliani, A. and Taylor, A. (1991). Evidence for ATP ubiquitin-dependent degradation of proteins in cultured bovine lens epithelial cells. Exp. Eye Res., 52, 341-347.
192. Jahngen-Hodge, J., Cyr, D., Laxman, E. and Taylor, A. (1992). Ubiquitin and ubiquitin conjugates in human lens. Exp. Eye Res., 55, 897-902.
193. Jahngen-Hodge, J., Taylor, A., Shang, F., Huang, L. L. and Mura, C. (1994). Oxidative stress to lens crystallins. Meth. Enzymol., 233, 512-522.
194. Jahngen-Hodge, J., Obin, M., Gong, X., Shang, F., Nowell, T., Gong, J., Abasi, H., Blumberg, J. and Taylor, A. (1997). Regulation of ubiquitin conjugating enzymes by glutathione following oxidative stress. J. Biol. Chem. 272, 28218-28226.
195. Javitt, J. C. and Taylor, H. R. (1995). Cataract and latitude. Documenta Ophthalmol., 88, 307-325.
196. Jedziniak, J. A., Nicoli, D. F., Baram, H. and Benedek, G. B. (1978). Quantitative verification of the existence of high molecular weight protein aggregates in the intact normal human lens by light-scattering spectroscopy. Invest. Ophthalmol. Vis. Sci., 17, 51-57.
197. Jennissen, H. P. (1995). Ubiquitin and the enigma of intracellular protein degradation. Eur. J. Biochem., 231, 1-30.
198. Jentsch, S. (1992). The ubiquitin-conjugating system. Ann. Rev. Genet., 26, 179-207.
199. Johnson, E. S., Bartel, B., Seufert, W. and Varshavsky, A. (1992). Ubiquitin as a degradation signal. EMBO J., 11, 497-505.
200. Johnson, M. D., Kim, H., Chesler, L., Tsao-Wu, G., Bouck, N. and Olverini, P. (1994). Inhibition of angiogenesis by tissue inhibitor of metalloproteinase. J. Cell Physiol., 160, 194-202.
201. Johnston, C. S., Meyer, C. G. and Srilakshmi. (1993). Vitamin C elevates red blood cell glutathione in healthy adults. Am. J. Clin. Nutr., 58, 103-105.
202. Jones, D. P., Samiec, P. S., Kurtz, J. C., Drews-Botsch, C. and Sternberg, P. (1997). Oxidation of plasma glutathione (GSH) in association with aging, age-related macular degeneration (ARMD) and diabetes. Invest. Ophthalmol. Vis. Sci., 38, s355.
203. Jones, E. B., Moshyedi, P., Gallo, S., Tmbran-Tink, J., Arand, G., Reid, D. A., Thompson, E. W., Chader, G. J. and Waldbillig, R. J. (1994). Characterization and novel activation of 72-kDa mettaloproteinase in retinal interphotoreceptor matrix and Y-79 cell culture medium. Exp. Eye Res., 59, 257-269.
204. Jordan, J., Galindo, M. F. and Miller, R. J. (1997). Role of calpain- and interleukin-1 beta converting enzyme-like proteases in the beta-amyloid-induced death of rat hippocampal neurons in culture. J. Neurochem., 68, 1612-1621.
205. Jungmann, J., Reins, H.-A., Schobert, C. and Jentsch, S. (1993). Resistance to cadmium mediated by ubiquitin-dependent proteolysis. Nature, 361, 369-371.
206. Kadoya, K., Azuma, M., David, L. L. and Shearer, T. R. (1993). Role of calpain in hydrogen peroxide induced cataract. Curr. Eye Res., 12, 341-346.
207. Kajiwara, K., Berson, E. L. and Dryja, T. P. (1994). Digenic retinitis pigmentosa due to mutations at the unlinked peripherin/RDS and ROM1 loci. Science, 264, 1604-1608.
208. Kelley, M. J., David, L. L., Iwasaki, N., Wright, J. and Shearer, T. R. (1993). α-crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract. J. Biol. Chem., 268, 18844-18849.
209. Kim, T. K. and Maniatis, T. (1996). Regulation of interferon-γ-activated STAT1 by the ubiquitin-proteasome pathway. Science, 273, 1717-1719.
210. King, R. W., Deshaics, R. J., Peters, J. M. and Kirschner, M. W. (1996). How proteolysis drives the cell cycle. Science, 274, 1652-1659.
211. Kinsky, S. C. and Six, H. R. (1975). A model for the lytic action of complement. In: Proteases and Biological Control, Cold Spring Harbor Conferences On Cell Proliferation, Vol. 2 (E. Reich, D. B. Rifkin and E. Shaw, eds.), pp 243-253. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
212. Klein, B. E., Cruickshanks, K. J. and Klein, R. (1995). Leisure time, sunlight exposure and cataracts (Review). Documenta Ophthalmol., 88, 295-305.
213. Klein, R., Klein, B. E., Linton, K. L. and DeMets, D. L. (1993). The Beaver Dam eye study: the relation of age-related maculopathy to smoking. Am. J. Epidemiol., 37, 190-200.
214. Knauer, M. F., Sorehegan, B., Burdick, D., Kosmoski, J. and Glabe, C. (1992). Intracellular accumulation and resistance to degradation of the Alzhcimer amyloid A4/β protein. Proc. Natl. Acad. Sci. U.S.A., 89, 7437-7441.
215. Knekt, P., Heliovaara, M., Rissanen, A., Aromaa, A. and Aaran, R. (1992). Serum antioxidant vitamins and risk of cataract. Br. Med. J. 1392-1394.
216. Kodama, T. and Takemoto, L. (1987). Characterization of disulfide-linked crystallins associated with human cataractous lens membranes. Invest. Ophthalmol. Vis. Sci., 29, 145-149.
217. Kon, C. H., Occleston, N. L., Daniels, J. T., Cherteris, D. G., Aylward, G. W. and Khaw, P. T. (1997). The role of matrix metalloproteinases (MMPs) in proliferative vitreoretinopathy (PVR)-a prospective study. Invest. Opthalmol. Vis. Sci., 38, s1176.
218. Kong, S.-K. and Chock, P. B. (1992). Protein ubiquitination is regulated by phosphorylation. J. Biol. Chem., 267, 14189-14192.
219. Kosegarten, D. C. and Mayer, T. J. (1978). Use of guinea pigs as model to study galactose-induced cataract formation. J. Pharm. Sci., 67, 1478-1479.
220. Kowluru, R., Kern, T. S. and Engerman, R. L. (1994). Abnormalities in retinal metabolism in diabetes or galactosemia. II. Comparison of gamma-glutamyl transpeptidase in retina and cerebral cortex, and effects of antioxidant therapy. Curr. Eye Res., 13, 891-896.
221. Krinsky, N. I. and Deneke, S. S. (1982). Interaction of oxygen and oxy-radicals with carotenoids. J. Natl. Cancer Inst., 69, 205-210.
222. Krontiris, T. G. (1995). Oncogenes. N. Engl. J. Med., 333, 303-306.
223. Kuck, J. F. R., Yu, N. T. and Askren, C. C. (1982). Total sulfhydryl by Raman spectroscopy in the intact lens of several species: variations in the nucleus and along optical axis during aging. Exp. Eye Res., 34, 23-37.
224. Kupfer, C. (1984). The conquest of cataract: a global challenge. Trans. Ophthal. Soc. U.K., 104, 1-10.
225. Kuwabara, T. (1975). The maturation of lens cells: a morphological study. Exp. Eye Res., 20, 427-433.
226. Kuwabara, T. and Imaizumi, M. (1974). Denucleation process of the lens. Invest. Ophthalmol. Vis. Sci., 13, 973-981.
227. Kwan, M., Niinikoski, J. and Hunt, T. K. (1972). In vivo measurement of oxygen tension in the cornea, aqueous humor, and the anterior lens of the open eye. Invest. Ophthalmol. Vis. Sci., 11, 108-114.
228. Lea, E. J. A., Marcantonio, J. M., Jones, S. P. and Duncan, G. (1986). Discrete channel activity of lens gap junction protein in planer bilayer membranes. In: The Lens: Transparency and Cataract (G. Duncan, ed.), pp. 153-158. Eurage, Rijiswijk. .
229. Lee, F. S., Hagler, J., Chen, Z. J. and Maniatis, T. (1997). Activation of IκBα kinase complex by MEKK1, a kinase of the JNK pathway. Cell, 88, 213-222.
230. Leibowitz, H., Krueger, D., Maunder, C., Milton, R. C., Mohandas, M. K., Kahn, H. A., Nickerson, R. J., Pool, J., Colton, T. L., Ganley, J. P., Loewenstein, J. I. and Dawber, T. R. (1980). The Framingham Eye Study Monograph. Surv. Ophthalmol., 24, Suppl. 335-610.
231. Leske, M. C., Chylack, L. T. and Wu, S. (1991). The lens opacities case-control study: risk factors for cataract. Arch. Ophthalmol., 109, 244-251.
232. Leske, M. C., Wu, S. Y., Hyman, L., Sperduto, R., Underwood, B., Chylack, L. T., Milton, R. C., Srivastava, S. and Ansari, N. (1995). Biochemical factors in the lens opacities. Case-control study. The Lens Opacities Case-Control Study Group. Arch. Ophthalmol., 113, 1113-1119.
233. Leske, M. C., Wu, S. Y., Connell, A. M. S., Hyman, L. et al. (1997). Lens opacities, demographic factors and nutritional supplements in the Barbados Eye Study. Int. J. Epidemiology, 26, 1314-1322.
234. Leske, M. C., Chylack, L. T. Jr, He, Q., Wu, S. Y., Schoenfeld, E., Friend, J., Wolfe, J. and the LSC Group. (1998a). Antioxidant vitamins and nuclear opacities - The longitudinal study of cataract. Ophthalmology, in press.
235. Leske, M. C., Chylack, L. T. Jr., He, Q. et al. (1998b). Risk factors for nuclear opalescence in a longitudinal study. Am. J. Epidemiology, in press.
236. Levine, M. (1986). New concepts in the biology and biochemistry of ascorbic acid. N. Engl. J. Med., 314, 892-902.
237. Lewis, B. S. and Harding, J. J. (1990). The effect of aminoguanidine on the glycation (non-enzymatic glycosylation) of lens proteins. Exp. Eye Res., 50, 463-467.
238. Li, L. K., Roy, D. and Spector, A. (1986). Changes in lens protein in concentric fractions from individual normal human lenses. Curr. Eye Res., 5, 127-153.
239. Li, S., Chang, C. J., Abler, A. S., Fu, J., Tso, M. O. and Lam, T. T. (1996). A comparison of continuous vs. intermittent light exposure on apoptosis. Curr. Eye Res., 15, 914-922.
240. Liang, J. N. (1987). Fluorescence study of the effects of aging and diabetes mellitus on human lens α-crystallin. Curr. Eye Res., 6, 351-355.
241. Liang, J. N., Bose, S. K. and Chakrabarti, B. (1985). Age-related changes in protein conformation in bovine lens crystallins. Exp. Eye Res., 40, 461-469.
242. Libondi, T., Menzione, M. and Auricchio, G. (1985). In vitro effect of alpha-tocopherol on lysophosatiphatidylcholine-induced lens damage. Exp. Eye Res., 40, 661-666.
243. Linetsky, M. and Ortwerth, B. J. (1997). Quantitation of the singlet oxygen produced by UVA irradiation of human lens proteins. Photochem. photobiol., 65, 522-529.
244. Linetsky, M., James, H. L. and Ortwerth, B. J. (1996). The generation of superoxide anion by the UVA irradiation of human lens proteins. Exp. Eye Res., 63, 67-74.
245. Lipman, R. D., Cyr, D. E., David, L. L. and Taylor, A. (1991). Calpain in culture bovine lens epithelial cells. Curr. Eye Res., 10, 11-17.
246. Lo, W. K. and Kuck, J. F. R. (1987). Alteration in fiber cell membranes of Emory mouse cataract: A morphological studies. Curr. Eye Res., 6, 433-444.
247. Lolley, R. N. (1994). The rd gene defect triggers programmed rod cell death. Invest. Ophthalmol. Vis. Sci., 35, 182-4191.
248. Los, M., Van de Craen, M., Penning, L. C., Schenk, H., Westendorp, M., Baeuerle, P. A., Droge, W., Krammer, P. H., Fiers, W. and Schulze-Osthoff, K. (1995). Requirements of an ICE/CED-3 protease for Fas/APO-1-mediated apoptosis. Nature, 375, 81-83.
249. Lubsen, N. H., Aarts, H. J. M. and Schoemakers, J. G. G. (1988). The evolution of lenticular proteins: the β- and γ-crystallin super gene family. Prog. Biophys. Mol. Biol., 51, 47-76.
250. Luthra, M. and Balasubramanian, D. (1993). Nonenzymatic glycation alters protein structure and stability. A study of two eye lens crystallins. J. Biol. Chem., 268, 18119-18127.
251. Luthra, R., Wa, S-Y. and Leske, M. C. B. N. Q. H. (1997). Lens opacities and use of nutritional supplements: the Barbados study. Invest. Ophthalmol. Vis. Sci., 8, S450.
252. Machlin, L. J. and Bendich, A. (1987). Free radical tissue damage: protective role of antioxidants. FASEB J., 1, 441-445.
253. Madura, K. and Varshavsky, A. (1994). Degradation of Gα by the N-end rule pathway. Science, 265, 1454-1458.
254. Maisel, H. (1985). The Ocular Lens; Structure, Function and Pathology. Marcel Dekker, New York.
255. Maiti, M., Kono, M. and Chakrabarti, B. (1988). Heat-induced changes in the conformation of alpha- and beta-crystallins: unique thermal stability of alpha-crystallin. FEBS Lett., 236, 109-114.
256. Maki, C. J., Huibregtse, J. M. and Howley, P. M. (1996). In vivo ubiquitination and proteasome-mediated degradation of p53. Cancer Res., 56, 2649-2654.
257. Mangini, N. J. (1991). Selective degradation of arrestin in rod outer segments (ROS): a possible role for cytosolic proteases in downregulating phototransduction processes. J. Cell. Biol., 115, 210a.
258. Mangini, N. J. and Garner, G. L. (1991). Arrestin is a PEST protein. Invest. Opthalmol. Vis. Sci., 32, s1150.
259. Mangini, N. J., Podlasek, C., Zou, Y., Naash, M. I. and Al-Ubaidi, M. R. (1995). Ubiquitin in the retina of the rd mouse. Invest. Ophthalmol. Vis. Sci., 36, s918.
260. Mares-Perlman, J. A., Klein, B. E. K., Klein, R. and Ritter, L. L. (1994). Relationship beween lens opacities and vitamin and mineral supplement use. Ophthalmology, 101, 315-355.
261. Mares-Perlman, J. A., Brady, W. E., Klein, B. E. K., Klein, R., Haus, G. J., Palta, M., Ritter, L. L. and Shoff, S. M. (1995). Diet and nuclear lens opacities. Am. J. Epidemiol., 141, 322-334.
262. Mares-Perlman, J. A., Brady, W. E., Klein, B. E. K., Klein, R., Palta, M., Bowen, P. and Stacewicz-Sapuntzakis, M. (1995). Serum carotenoids and tocopherols and severity of nuclear and cortical opacities. Invest. Ophthalmol. Vis. Sci., 36, 276-288.
263. Mares-Perlman, J. A., Brady, W. E., Klein, B. E. K., Klein, R. and Palta, M. (1996). Supplement use and 5-year progression of cortical opacities. Invest. Ophthalmol. Vis. Sci., 37, S237.
264. Martensson, J., Steinhertz, R., Jain, A. and Meister, A. (1989). Glutathione ester prevents buthionine sulfoximine-induced cataracts and lens epithelial cell damage. Biochemistry, 86, 8727-8731.
265. Martin, S. J. and Green, D. R. (1995). Protease activation during apoptosis: death by a thousand cuts? Cell, 82, 349-352.
266. Matrisian, L. M. (1992). The matrixdegrading metalloproteinases. Bioessays, 14, 455-463.
267. McAvoy, J. W. (1980). β- And γ-crystallin synthesis in rat lens epithelium explants with neural retina. Differentiation, 17, 85-91.
268. McLaren, D. S. (1980). Nutritional Ophthalmology, 2nd ed. Academic Press, London.
269. McLaughlin, M. E., Sandberg, M. A., Berson, E. L. and Dryja, T. P. (1993). Recessive mutations in the gene encoding the beta-subunit of rod phosphodiesterase in patients with retinitis pigmentosa. Nature Genet., 4, 130-134.
270. Mclaughlin, M. E., Erhart, T. L., Berson, E. L. and Dryja, T. P. (1995). Mutation spectrum of the gene encoding the B subunit of rod phosphodiesterase among patients with autosomal recessive retinitis pigmentosa. Proc. Natl. Acad. Sci. U.S.A., 92, 3249-3253.
271. Medina, R., Wing, S. S. and Goldberg, A. L. (1995). Increase in levels of polyubiquitin and protcasome mRNA in skeletal muscle during starvation and denervation atrophy. Biochem. J., 307, 631-637.
272. Mellgren, R. L. (1980). Canine cardiac calcium-dependent proteases: resolution of two forms with different requirements for calcium. FEBS Lett., 109, 129-133.
273. Messier, B. and Leblond, C. P. (1960). Cell proliferation and migration as revealed by radioautography after injection of thymidine[3H] into male rats and mice. Am. J. Anat., 106, 247-285.
274. Mezzetti, A., Lapenna, D., Pierdomenico, S. D., Calafiore, A. M., Costantini, F., Riario-Sforza, G., Imbastaro, T., Neri, M. and Cuccurollo, F. (1995). Vitamins E, C, and lipid peroxidation in plasma and arterial tissue of smokers and non-smokers. Atherosclerosis, 112, 91-99.
275. Micozzi, M. S., Beecher, G. R., Taylor, H. R. and Khachik, F. (1990). Carotenoid analyses of selected raw and cooked foods associated with a lower risk for cancer. J. Natl Cancer Inst., 82, 282-285.
276. Miller, D. K., Myerson, J. and Becker, J. W. (1997). The interleukin-1 beta converting enzyme family of cysteine proyeases. J. Cell. Biochem., 64, 2-10.
277. Minassian, D. C., Baasanhu, J., Johnson, G. J. and Burendei, G. (1994). The relationship between cataract and climatic droplet keratopathy in Mongolia. Acta Ophthalmol., 72, 490-495.
278. Mitton, K. P., Kamiya, T., Tumminia, S. J. and Russell, P. (1996). Cysteine protease activated by expression of HIV-1 protease in transgenic mice. MIP26 (aquaporin-0) cleavage and cataract formation in vivo and ex vivo. J. Biol. Chem., 271, 31803-31806.
279. Miura, M., Zhu, H., Rotelloo, R., Hartwieg, E. A. and Yuan, J. (1993). Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell, 75, 653-660.
280. Mohan, M., Sperduto, R. D., Angra, S. K., Milton, R. C., Mathur, R. L., Underwood, B., Jafery, N. and Pandya, C. B. (1989). India-US case-control study of age-related cataract Arch. Ophthalmol., 107, 670-676.
281. Monnier, V. M. and Cerami, A. (1981). Nonenzymatic browning in vivo: possible process for aging of long lived proteins. Science, 211, 491-493.
282. Monnier, V. M. and Cerami, A. (1983). Detection of nonenzymatic browning products in human lens. Biochim. Biophys. Acta, 760, 97-103.
283. Mori, S., Tanaka, K., Omura, S. and Saito, Y. (1995). Degradation process of ligand-simulated platelet-derived growth factor B receptor involves ubiquitin-proteasomee proteolytic pathway. J. Biol. Chem., 270, 29447-29452.
284. Mori, S., Tanaka, K., Omura, S. and Saito, Y. (1995). Degradation process of ligand-stimulated platelet-derived growth factor β-receptor involves ubiquity-proteasome proteolytic pathway. J. Biol. Chem., 270, 29447-29452.
285. Muller, H. K. and Buschke, W. (1934). Vitamin C in linse, kammerwasser und blut normalem und pathologischem linsentstoffwech. Arch. F. Augenh, 108, 368-390.
286. Muller, S. and Schwartz, L. M. (1995). Ubiquitin in homeostasis, development and disease. Bioessays, 17, 677-684.
287. Mullins, D. E. and Rohrlich, S. T. (1983). The role of proteinases in cellular invasiveness. Biochim. Biophys. Acta., 695, 177-214.
288. Mune, M., Meydani, M., Jahngen-Hodge, J., Martin, A., Smith, D., Palmer, V., Blumberg, J. B. and Taylor, A. (1995). Effect of calorie restriction on liver and kidney glutathione in aging Emory mice. AGE, 18, 49-49.
289. Mura, C. V., Roh, S., Smith, D., Palmer, V., Padhye, N. and Taylor, A. (1993). Cataract incidence and analysis of lens crystallins in the water-, urea-, and SDS-soluble fractions of Emory mice fed a diet restricted by 40% in calories. Curr. Eye Res., 12, 1081-1091.
290. Murachi, T. (1989). Intracellular regulatory system involving calpain and calpastatin. Biochem. Int., 18, 263-294.
291. Murakami, K., Jahngen, J. H., Lin, S. W., Davies, K. J. A. and Taylor, A. (1990). Lens proteasome shows enhanced rates of degradation of hydroxyl radical modified alpha-crystallin. Free Rad. Biol. Med., 8, 217-222.
292. Muralidhar, M. G. and Thomas, J. B. (1993). The Drosophile bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes. Neuron, 11, 253-266.
293. Murphy, G. and Willenbrock, F. (1995). Tissue inhibitors of matrix metalloendopetidases. Meth. Enzymol., 248, 496-509.
294. Murphy, M. E., Scholich, H. and Sies, H. (1992). Protection by glutathione and other thiol compounds against the loss of protein thiols and tocopherol homologs during microsomal lipid peroxidation. Eur. J. Biochem., 210, 139-146.
295. Muzio, M., Salvesen, G. S. and Dixit, V. M. (1997). FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens. J. Biol. Chem., 272, 2952-2956.
296. Naash, M. (1990). Characterization of the ubiquitin pathway in the rat retina. Ph.D. Thesis, Baylor College of Medicine, Houston, TX.
297. Naash, M. and Anderson, R. E. (1991). Ubiquitin in light stressed rat retina (Abstract). Invest. Opthalmol. Vis. Sci., 31, s293.
298. Naash, M., Zbicka, E. and Anderson, R. E. (1991). Rat retina has an active and stable ubiquitin-protein conjugating system. J. Neurosci. Res., 30, 433-441.
299. Nagai, Y., Kaneda, S., Nomura, K., Yasuda, H., Seno, T. and Yamao, F. (1995). Ubiquitin-activating enzyme, E1 is phosphorylated in mammalian cells by the protein kinase Cdc2. J. Cell Sci., 108, 2145-2152.
300. Nakamura, B. and Nakamura, O. (1935). Ufer das vitamin C in der linse und dem Kammerwasser der menschlichen katarakte. Graefes Arch. Clin. Exp. Ophthalmol., 134, 197-200.
301. Nakatani, M. and Linden, R. (1997). Neurotrophins prevent apoptosis of retinal cells in the developing retina in intro. Invest. Ophthalmol. Vis. Sci., 38, s35.
302. Naraj, R. M. and Monnier, V. M. (1992). Isolation and characterization of a blue fluorophore from human eye lens crystallins: in vitro formation from Maillard action with ascorbate and ribose. Biochim. Biophys. Acta, 1116, 34-42.
303. Neurath, H. (1975). Limited proteolysis and zymogen activation. In: Proteases and Biological Control,Cold Spring Harbor Conferences On Cell Proliferation, Vol. 2 (E. Reich, D. B. Rifkin and E. Shaw, eds), pp. 651-664. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
304. Nishigori, H., Lee, J. W., Yamauchi, Y. and Iwatsuru, M. (1986). The alteration of lipid peroxide in glucocorticoid-induced cataract of developing chick embryos and the effect of ascorbic acid. Curr. Eye Res., 5, 37-40.
305. t) is a substrate for ubiquitin-dependent proteolysis. Biochem. Biophys. Res. Commun., 200, 1169-1176.
306. Obin, M. S., Nowell, T. and Taylor, A. (1995). A comparison of ubiquitin-dependent proteolysis of rod outer segment proteins in reticulocyte lysate and a retinal pigment epithelial cell line. Curr. Eye Res., 14, 751-760.
307. Obin, M. S., Jahngen-Hodge, J., Nowell, T. and Taylor, A. (1996). Ubiquitinylation and ubiquitin-dependent proteolysis in vertebrate photoreeeptors (rod outer segments). J. Biol. Chem., 271, 14473-14484.
308. Obin, M. S., Gong, X., Shang, F., Jahngen-Hodge, J. and Taylor, A. (1997). Thiol-dependent regulation of protein ubiquitination in RPE cells following oxidative stress. Invest. Ophthalmol. Vis. Sci., 38, s1030.
309. Oh, C. E., McMahon, R., Benzer, S. and Tanouye, M. A. (1994). Bendless, a Drosophila gene affecting neuronal connectivity, encodes a ubiquitin-conjugating enzyme homolog. J. Neurosci., 14, 3166-3179.
310. Ohguro, H., Fukada, Y., Takao, T., Shimonishi, Y., Yoshizawa, T. and Akino, T. (1991). Carboxyl methylation and farnesylation of transducin gamma-subunit synergistically enhance its coupling with metarhodopsin II. EMBO J., 10, 3669-3674.
311. Oldenburg, K. R. and Hubbell, W. L. (1991). Invertebrate rhodopsin cleavage by an endogenous calcium activated protease. Exp. Eye Res., 51, 463-472.
312. Organisciak, D. T., Xie, A., Wang, H. M., Jiang, Y. L., Darrow, R. M. and Donoso, L. A. (1991). Adaptive changes in visual cell transduction protein levels: effect of light. Exp. Eye Res., 53, 773-779.
313. Ortolani, O., Caggiano, M., Mannelli, R., Gogliettino, A. and Tufano, R. (1995). Protection from ischemia-reperfusion damage in patients with stroke: the role of rutin and GSH. Transplant. Proc., 27, 2877-2878.
314. Ortwerth, B. J. and Olesen, P. P. (1988a). Ascorbic acid-induced crosslinking of lens proteins: evidence supporting a Maillard reaction. Biochim. Biophys. Acta, 956, 10-22.
315. Ortwerth, B. J. and Olesen, P. P. (1988b). Glutathione inhibits the glycation of and cross-linking of lens protein by ascorbic acid. Exp. Eye Res., 47, 737-750.
316. Ortwerth, B. J., Feather, M. S. and Olesen, P. P. (1988). The precipitation and cross-linking of lens crystallins by ascorbic acid. Exp. Eye Res., 47, 155-168.
317. Ozaki, Y., Mizuno, A., Itoh, K., Yoshiura, M., Iwanioto, T. and Iriyama, K. (1983). Raman spectroscopic study of age-related structure changes in the lens proteins of an intact mouse lens. Biochemistry, 22, 6254-6259.
318. Ozaki, Y., Mizuno, A., Itoh, K. and Iriyama, K. (1987). Inter- and intramolecular disulfide bond formation and related structure changes in the lens protein. A Raman spectroscopic study in vivo of lens aging. J. Biol. Chem., 262, 15545-15551.
319. Pacifici, R. E., Salo, D. C. and Davies, K. J. A. (1989). Macroxyproteinase (M.O.P.): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells. Free Rad. Biol. Med., 7, 521-536.
320. Pagano, M., Tam, S. W., Theodoras, A. M., Beer-Romero, P., Del Sal, G., Chau, V., Renee Yew, P., Draetta, G. F. and Rolfe, M. (1995). Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science, 269, 682-685.
321. Palczewski, K., McDowell, J. H., Jakes, S., Ingebritsen, T. S. and Hargrave, P. A. (1989). Regulation of rhodopsin dephosphorylation by arrestin. J. Biol. Chem., 264, 15770-15773.
322. Palmquist, B. M., Phillipson, B. and Barr, P. O. (1984). Nuclear cataract and myopia during hyperbaric oxygen therapy. Br. J. Ophthalmol., 60, 113-117.
323. Pan, Z. and Perez-Polo, R. (1993). Role of nerve growth factor in oxidant homeostasis: glutathione metabolism. J. Neurochem., 61, 1713-1721.
324. Pande, J., Lomakin, A., Fine, B., Ogun, O., Sokolinski, I. and Benedek, G. (1995). Oxidation of γII-crystallin solutions yields dimers with a high phase separation temperature. Proc. Natl. Acad. Sci. U. S.A., 92, 1067-1071.
325. Papermaster, D. S. and Windle, J. (1995). Death at an early age: apoptosis in inherited retinal degenerations. Invest. Ophthalmol. Vis. Sci., 36, 977-983.
326. Parag, H. A., Bilha, R. and Kulka, R. G. (1987). Effect of heat shock on protein degradation in mammalian cells: involvement of the ubiquitin system. EMBO J., 6, 55-61.
327. Parish, C. A. and Rando, R. R. (1994). Functional significance of G protein carboxymethylation. Biochemistry, 33, 9986-9991.
328. Pepper, M. S. and Montesano, R. (1990). Proteolytic balance and capillary morphogenesis. Cell Differ. Dev., 32, 319-328.
329. Peracchia, C., Girsch, S. J., Bernardini, G. and Perracchia, L. L. (1985). Lens junctions are communicating junctions. Curr. Eye Res., 4, 1155-1169.
330. Peters, J. (1994). Proteasomes-protein degradation machines of the cell. Trends Biochem. Sci., 19, 377-382.
331. Philip, N. J., Chanf, W. and Long, K. (1987). Light-stimulated protein movement in rod photoreceptor cells of the rat retina. FEBS. Lett., 225, 127-132.
332. Piatigorsky, J. (1981). Lens differentiation in vertebrate: a review of cellular and molecular features. Differentiation, 19, 134-153.
333. Piatigorsky, J. (1987). Gene expression and genetic engineering in the lens. Invest. Ophthalmol. Vis. Sci., 28, 9-28.
334. Pittler, S. J. and Baehr, W. (1991). Identification of a nonsense mutation in the rod photoreceptor cGMP phosphodiesterase β-subunit gene of the rd mouse. Proc. Natl. Acad. Sci. U.S.A., 88, 8322-8326.
335. Plantner, J. and Drew, W. T. A. (1994). Polarized distribution of metalloproteinases in the bovine interphotoreceptor matrix. Exp. Eye Res., 59, 577-585.
336. Poblenz, A. T. and Fox, D. A. (1997). Signaling pathways underlying the rod cell apoptosis due to calcium overload. Invest. Ophthalmol. Vis. Sci., 38, s35.
337. Polkinghorne, P. J., Capon, M. R. C., Berninger, T., Lyness, A. L., Sehmi, K. and Bird, A. C. (1989). Sorsby's fundus dystrophy. A clinical study. Opthalmology, 96, 1763-1768.
338. Ramachandran, S., Morris, S. M., Devamanoharan, P., Henei, M. and Varma, S. D. (1991). Radio-isotopic determination of hydrogen peroxide in aqueous humor and urine. Exp. Eye Res., 53, 503-506.
339. Rao, C. M., Qin, C., Robison, W. G. and Zigler, J. S. (1984). Effect of smoke condensate on the physiological integrity and morphology of organ cultured rat lenses. Curr. Eye Res., 14, 295-301.
340. Raport, C. J., Lem, J., Makino, C., Chen, C-K., Fitch, C. L., Hobson, A., Baylor, D., Simon, M.I and Hurley, J. (1994). Downregulation of cGMP phosphodiesterase induced by expression of GTPase-deficient cone transducin in mouse rod photoreceptors. Invest. Ophtalmol. Vis. Sci. 35, 932-2947.
341. Rathbun, W. B., Killen, C. E., Holleschau, A. M. and Nagasawa, H. T. (1996). Maintenance of hepatic glutathione homeostasis and prevention of acetaminophen-induced cataract in mice by L-cysteine prodrugs. Biochem. Pharmacol., 51, 1111-1116.
342. Rathbun, W. B., Holleschau, A. M., Cohen, J. F. and Nagasawa, H. T. (1996). Prevention of acetaminophen- and naphthalene-induced cataract and glutathione loss by CySSME. Invest. Ophthalmol. Vis. Sci., 37, 923-929.
343. Ray, K. and Harris, H. (1985). Purification of neutral lens endopeptidase; close similarity to a neutral proteinase in pituitary. Proc. Natl. Acad. Sci. U.S.A., 82, 7545-7549.
344. Rechsteiner, M. (1991). Natural substrates of the ubiquitin proteolytic pathway. Cell, 66, 615-618.
345. Rechsteiner, M., Hoffman, L. and Dubiel, W. (1993). The multicatalytic and 26 S proteases. J. Biol. Chem., 268, 6065-6068.
346. Reddy, V. N. (1990). Glutathione and its function in the lens - an overview. Exp. Eye Res., 150, 771-778.
347. Rivett, A. J. (1993). Proteasomes: multicatalytic proteinase complexes. Biochem. J., 291, 1-10.
348. Rivett, A. J., Mason, G. G., Thomson, S., Pike, A. M., Savory, P. J. and Murray, R. Z. (1995). Catalytic components of proteasomes and the regulation of proteinase activity. Mol. Biol. Reports, 21, 35-41.
349. Robertson, J.McD., Donner, A. P. and Trevithick, J. R. (1989). Vitamin E intake and risk for cataracts in humans. Ann. N.Y. Acad. Sci., 570, 372-382.
350. Roederer, M., Staal, F. J., Anderson, M., Rabin, R., Raju, P. A. and Herzenberg, L. A. (1993). Disregulation of leukocyte glutathione in AIDS. Ann. N.Y. Acad. Sci., 677, 113-125.
351. Rogers, S., Wells, R. and Rechsteiner, M. (1986). Amino acid sequences common to rapidly-degraded proteins: the PEST hypothesis. Science, 234, 363-368.
352. Rosen, A. and Casciola-Rosen, L. (1997). Macromolecular substrates for ICE-like proteases during apoptosis. J. Cell. Biochem., 64, 50-54.
353. Rouhianen, P., Rouhiainen, H. and Salonen, T. J. (1996). Association between low plasma vitamin E concentration and progression of early cortical lens opacities. Am. J. Epidemiol., 144, 496-500.
354. Roy, D. and Spector, A. (1978). Human insoluble lens protein. II. Isolation and characterization of a 9600 dalton polypeptide. Exp. Eye Res., 26, 445-459.
355. Roy, D., Spector, A. and Farnsworth, P. N. (1979). Human lens membrane: Comparison of major intrinsic polypeptides from young and old lenses isolated by a new methodology. Exp. Eye Res., 28, 353-358.
356. Rubin, D. M. and Finley, D. (1995). Proteolysis. The proteasome: a protein-degrading organelle?. Curr. Biol., 5, 8 854-858.
357. Rudolphus, A., Heinzel-Weiland, R., Vincent, V. A., Saunders, D., Steffens, G. J., Dijkman, J. H. and Kramps, J. A. (1991). Oxidation-resistant variants of recombinant antileucoprotease are better inhibitors of human-neutrophil-elastase-induced emphysema in hamsters than natural recombinant antileucoprotease. Clin. Sci., 81, 777-784.
358. Russell, P., Garland, D., Zigler, J. S. J., Meakin, S. Q., Tsui, L. C. and Breitman, M. L. (1987). Aging effects of vitamin C on a human lens protein produced in vitro. FASEB J., 1, 32-35.
359. Russell-Briefel, R., Bates, M. W. and Kuller, L. H. (1985). The relationship of plasma carotenoids to health and biochemical factors in middle-aged men. Am. J. Epidemiol., 22, 741-749.
360. Saido, T. C., Sorimachi, H. and Suzuki, K. (1994). Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J., 8, 814-822.
361. Salive, M. E., Guralnik, J., Christian, W., Glynn, R. J., Colsher, P. and Ostfeld, A. M. (1992). Functional blindness and visual impairment in older adults from three communities. Ophthalmology, 99, 1840-1847.
362. Sandilands, A., Prescott, A. R., Carter, J. M., Hutcheson, A. M., Quinlan, R. A., Richards, J. and FitzGerald, P. G. (1995). Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fiber differentiation. J. Cell Sci., 108, 1397-1406.
363. Sasaki, H., Giblin, F. J., Winkler, B. S., Chakrapani, B., Leverenz, V. and Chu-Chen, S. (1995). A protective role for glutathione-dependent reduction of dehydroascorbic acid in lens epithelium. Invest. Ophthalmol. Vis. Sci., 36, 1804.
364. Sastre, J., Meydani, M., Martin, A., Biddle, L., Taylor, A. and Blumberg, J. (1994). Effect of glutathione monoethyl ester administration on galactose-induced cataract in the rat. Life Chem. Reports, 12, 89-95.
365. Saxena, P., Saxena, A. K. and Monnier, V. M. (1996). High galactose levels in vitro and in vivo impair ascorbate regeneration and increase ascorbate-mediated glycation in cultured rat lens. Exp. Eye Res., 63, 535-545.
366. Schalch, W. and Weber, P. (1994). Vitamins and carotenoids - a promising approach to reducing the risk of coronary heart disease, cancer and eye diseases. Adv. Exp Med. Biol., 366, 335-3350.
367. Schectman, G., Byrd, J. C. and Gruchow, H. W. (1989). The influence of smoking on vitamin C status in adults. Am. J. Health, 79, 158-162.
368. Scheffner, M., Huibregtse, J. M., Vierstra, R. D. and Howley, P. M. (1993). The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell, 75, 495-505.
369. Schimke, R. T. and Bradley, M. O. (1975). Properties of protein turnover in animal cells and a possible role for turnover in 'quality' control of proteins. In: Proteases and Biological Control, Cold Spring Harbor Conferences On Cell Proliferation, Vol. 2 (E. Reich, D. B. Rifkin and E. Shaw, eds.), pp. 515-530. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
370. Schocket, S. S., Esterson, J., Bradford, B., Michaelis, M. and Richards, R. D. (1972). Induction of cataracts in mice by exposure to oxygen. Israel J. Med., 8, 1596-1601.
371. Schwab, L. (1990). Cataract blindness in developing nations. Int. Ophthalmol. Clinics, 30, 16-18.
372. Seddon, J. M., Ajani, U. A., Sperduto, R. D., Hiller, R., Blair, N., Burton, T. C., Farber, M. D., Gragoudas, E. S., Haller, J., Miller, D. T., Yannuzzi, L. A. and Willett, W. (1993). Dietary carotenoids, vitamins A, C, and E, and advanced age-related macular degneration. J. Am. Med. Assoc., 272, 1413-1420.
373. Seddon, J. M., Christen, W. G., Manson, J. E., LaMotte, F. S., Glynn, R. J., Buring, J. E. and Hennekens, C. H. (1994). The use of vitamin supplements and the risk of cataract among US male physicians. Am. J. Public Health, 84, 788-792.
374. Sell, D. R. and Monnier, V. M. (1989). Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process. J. Biol. Chem., 264, 21597-21602.
375. Shaeffer, J. R. (1988). ATP-dependent proteolysis of hemoglobin alpha chains in beta-thalassemic hemolysates is ubiquitin-dependent. J. Biol. Chem., 263, 13663-13669.
376. Shaeffer, J. R. and Kania, M. A. (1995). Degradation of monoubiquitinated α-globin by 26S proteasomes. Biochemistry, 34, 45015-45021.
377. Shalini, V. K., Luthra, M., Srinivas, L., Rao, S. H., Basti, S., Reddy, M. and Balasubramanian, D. (1994). Oxidative damage to the eye lens caused by cigarette smoke and fuel smoke condensates. Ind. J. Biochem. Biophys., 31, 261-266.
378. Shang, F. and Taylor, A. (1995). Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells. Biochem. J., 307, 297-303.
379. Shang, F., Huang, L. and Taylor, A. (1994). Degradation of native and oxidized beta- and gamma-crystallins using bovine lens epithelial cell and rabbit reticulocyte extracts. Curr. Eye Res., 13, 423-431.
380. Shang, F., Gong, X., Palmer, H. J., Nowell, T. R. and Taylor, A. (1997a). Age-related decline in ubiquitin conjugation in response to oxidative stress in the lens. Exp. Eye Res., 64, 21-23.
381. Shang, F., Gong, X. and Taylor, A. (1997b). Activity of ubiquitin dependent pathway in response to oxidative stress: Ubiquitin activating enzyme (E1) is transiently upregulated. J. Biol. Chem. 272, 23086-23093.
382. Shearer, T. R., David, L. L., Anderson, R. S. and Azuma, M. (1992). Review of selenite cataract. Curr. Eye Res., 11, 357-369.
383. Shearer, T. R., Shih, M., Azuma, M. and David, L. L. (1995). Precipitation of crystallins from young rat lens by endogenous calpain. Exp. Eye Res., 61, 141-150.
384. Shin, R.-W., Bramblett, G., Lee, V. M.-Y. and Trojanowski, J. Q. (1993). Alzheimer disease A68 proteins injected into rat brain induce codeposits of β-amyloid, ubiquitin and α1-antichymotrypsin. Proc. Natl. Acad. Sci. U.S.A., 90, 6825-6828.
385. Sies, H., Brigelius, R. and Graf, P. (1987). Hormones, glutathione status and protein S-thiolation. Adv. Enzyme Regul., 26, 175-189.
386. Siezen, R. J., Fisch, M. R., Slingsby, C. and Benedek, G. B. (1985). Opacification of γ-crystallin from calf lens in relation to cold cataract formation. Proc. Natl. Acad. Sci. U.S.A. 82, 1701-1705.
387. Siezen, R. J., Coppin, C. M., Kaplan, E., Dwyer, D. and Thomson, J. A. (1989). Oxidative modifications to crystallins induced in calf lenses in vitro by hydrogen peroxide. Exp. Eye Res., 48, 225-235.
388. Silvius, J. R. and l'Heureux, F. (1994). Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers. Biochemistry, 33, 3014-3022.
389. Slingsby, C. and Bateman, O. A. (1990). Rapid separation of bovine β-crystallin subunits βB1, βB2, βB3, βA3 and βA4. Exp. Eye Res., 51, 21-26.
390. Smine, A. and Plantner, J. J. (1997). Measurement of matrix metalloproteinases in human interphotoreceptor matrix and vitreous. Invest. Ophthalmol. Vis. Sci., 38, s306.
391. Smith, W. C. (1995). Splice variants of arrestin in bovine, human, rabbit, mouse, and frog retina. Invest. Opthalmol. Vis. Sci., 36, s223.
392. Smith, D., Palmer, V., Kehyias, J. and Taylor, A. (1993). Induction of cataracts by X-ray exposure of guinea pig eyes. Lab Animal, 22, 34-39.
393. Spector, A. (1984). The search for a solution to senile cataract. Invest. Ophthalmol. Vis. Sci., 25, 130-146.
394. Spector, A. (1985). Aspects of the biochemistry of cataract. In: The Ocular Lens. Structure, Function and Pathology (H. Maisel, ed.), pp. 405-438. Marcel Dekker, New York.
395. Spector, A. (1995). Oxidative stress-induced cataract: mechanism of action. FASEB J., 9, 1173-1182.
396. Spector, A. and Garner, W. H. (1981). Hydrogen peroxide and human cataract. Exp. Eye Res., 33, 673-681.
397. Spector, A., Chiesa, R., Sredy, J. and Garner, W. (1985). cAMP-dependent phosphorylation of bovine lens α-crystallin. Proc. Natl. Acad. Sci. U.S.A., 82, 4712-4716.
398. Spence, J., Sadis, S., Haas, A. L. and Finley, D. (1995). A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol., 15, 1265-1273.
399. Sperduto, R. D., Hu, T-S., Milton, R. C., Zhao, J., Everett, D. F., Cheng, Q., Blot, W. J., Bing, L., Taylor, P. R., Jun-Yao, L., Dawsey, S. and Guo, W. (1993). The Linxian cataract studies: two nutrition intervention trials. Arch. Ophthalmol., 111, 1246-1253.
400. Squier, M. K. and Cohen, J. J. (1997). Calpain, an upstream regulator of thymocyte apoptosis. J. Immunol., 158, 3690-3697.
401. Srivastava, O. P. (1988a). Age-related increase in concentration and aggregation of degraded polypeptides in human lenses. Exp. Eye Res., 47, 525-543.
402. Srivastava, O. P. (1988b). Characterization of a highly purified membrane proteinase from bovine lens. Exp. Eye Res., 46, 269-283.
403. Srivastava, A. N. H. (1988). Prevention of sugar induced cataractogenesis in rats by butylated hydroxytoluene. Diabetes, 37, 1505-1508.
404. Srivastava, O. P. and Ortwerth, B. J. (1983a). Age-related and distributional changes in the trypsin inhibitor activity of bovine lens. Exp. Eye Res., 36, 695-709.
405. Srivastava, O. P. and Ortwerth, B. J. (1983b). Isolation and characterization of a 25K serine proteinase from bovine lens cortex Exp. Eye Res., 37, 597-612.
406. Srivastava, O. P. and Ortwerth, B. J. (1989). The effects of aging and cataract formation on the trypsin inhibitor activity of human lens. Exp. Eye Res., 48, 25-36.
407. 6-benzylguanine or 1,3-bis(2-chloroethyl)-1-nitrosourea. Biochemistry, 35, 1328-1334.
408. Stadtman, E. R. (1986). Oxidation of proteins by mixed-function oxidation systems: implications in protein turnover, aging and neutrophil function. Trends Biochem. Sci., 11, 11-12.
409. Stadtman, E. R. (1992). Protein oxidation and aging. Science, 257, 1220-1224.
410. Starke-Reed, P. E. and Oliver, C. N. (1989). Protein oxidation and proteolysis during aging and oxidative stress. Arch. Biochem. Biophys., 275, 559-567.
411. Steele, F. R., Chader, G. J., Johnson, L. V. and Tombran-Tink, J. (1993). Pigment epithelium-derived factor: neurotrophic activity and identification as a member of the serine protease inhibitor gene family. Proc. Natl. Acad. Sci. U.S.A., 90, 1526-1530.
412. Stevens, R. J., Negi, D. S., Short, S. M., van Kuijk, F. J. G. M., Dratz, E. A. and Thomas, D. W. (1988). Vitamin E distribution in ocular tissues following long-term dietary-depletion and supplementation as determined by microdissection and gas chromatography-mass spectrometry. Exp. Eye Res., 47, 237-245.
413. Stevens, V. J., Rouzer, C. A., Monnier, V. M. and Cerami, A. (1978). Diabetic cataract formation: potential role of glycosylation of lens crystallins. Proc. Natl. Acad. Sci. U.S.A., 75, 2918-2922.
414. Suber, M. L., Pittler, S. J., Qin, N., Wright, G. C., Holcombe, V., Lee, R. H., Craft, C. M., Lolley, R. N., Baehr, W. and Hurwitz, R. L. (1993). Irish setter dogs affected with rod/cone dysplasia contain a nonsense mutation in the rod cGMP phosphodiesterase beta-subunit gene. Proc. Natl. Acad. Sci U.S.A., 90, 3968-3972.
415. Sung, C.-H., Davenport, C. M. and Nathans, J. (1994). Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain. J. Biol. Chem., 268, 26645-26649.
416. Suzuki, K. and Ohno, S. (1990). Calcium activated neutral protease-structure-function relationship andfunctional implications. Cell Struct. Funct., 15, 1-6.
417. Swamy, M., Tsai, C., Abraham, A. and Abraham, E. C. (1993). Glycation mediated lens crystallin aggregation and cross-linking by various sugars and sugar phosphates in vitro. Exp. Eye Res., 56, 177-185.
418. Swamy, M. S. and Abraham, E. C. (1987). Lens protein composition, glycation and high molecular weight aggregates in aging rats. Invest. Ophthalmol. Vis. Sci., 28, 1693-1701.
419. Swamy, M. S. and Abraham, E. C. (1991). Differential glycation of rat alpha-, beta- and gamma-crystallins. Exp. Eye Res., 52, 439-444.
420. Swamy, M. S. and Abraham, E. C. (1992a). Glycation of lens membrane intrinsic proteins. Curr. Eye Res., 11, 833-842.
421. Swamy, M. S. and Abraham, E. C. (1992b). Glycation of lens MIP26 affects the permeability in reconstituted liposomes. Biochem. Biophys. Res. Commun., 186, 632-638.
422. Swamy, M. S., Abraham, A. and Abraham, E. C. (1992b). Glycation of human lens proteins: Preferential glycation of αA subunits. Exp. Eye Res., 54, 337-345.
423. Szatrowski, T. P. and Nathan, C. F. (1991). Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res., 51, 794-798.
424. Takahashi, K. (1990). Calpain substrate specificity. In: Intracellular Calcium-dependent Proteolysis (T. Murachi and R. Mellgren, eds.), pp. 55-74. CRC Press, New York.
425. Takemoto, L. (1994). Release of α-A sequence of 158-173 correlates with a decrease in the molecular chaperone properties of native α-crystallin. Exp. Eye Res., 59, 239-242.
426. Takemoto, L. and Emmons, T. (1991). Truncation of αA-crystallin from human lens. Exp. Eye Res., 53, 811-813.
427. Takemoto, L., Kodama, T. and Takemoto, D. (1987a). Covalent changes in the N-terminal and C-terminal regions of gamma crystallin during aging of the normal human lens. Exp. Eye Res., 45, 207-214.
428. Takemoto, L., Takemoto, D. and Brown, G. (1987b). Cleavage from the N-terminal region of βBp crystallin during aging of human lens. Exp. Eye Res., 45, 385-392.
429. Takemoto, L., Horwitz, J. and Emmons, T. (1992). Oxidation of the N-terminal methionine of lens alpha-A crystallin. Curr. Eye Res., 11, 651-655.
430. Takigawa, M. Y., Nishida, Y., Suzuki, F., Kishi, J., Yamashita, K. and Hayakawa, T. (1990). Induction of angiogcncsis in chick yolk-sac membrane by polyamincs and its inhibition by tissue inhibitor of metalloproteinases (TIMP-1 and TIMP-2). Biochem. Biophys. Res. Commun., 171, 1264-1271.
431. Tan, X., Martin, S. J., Green, D. R. and Wang, J. Y. J. (1997). Degradation of retinoblastoma protein in tumor necrosis factor- and CD95-induced cell death. J. Biol. Chem., 272, 9613-9616.
432. Taniwaki, T., Hiroshima, N., Becerra, S. P., Chader, G. J., Etcheberrigaray, R. and Schwartz, J. P. (1997). Pigment epithelim-derived factor protects cerebellar granule cells in culture against glutamate-induced neurotoxicity. J. Neurochem., 68, 26-32.
433. Taylor, A. and Davies, K. J. A. (1987). Protein oxidation and loss of protease activity may lead to cataract formation in the aged lens. Free Rad. Biol. Med., 3, 371-377.
434. Taylor, A., Jahngen-Hodge, J., Huang, L. L. and Jacques, P. (1991a). Aging in the eye lens: roles for proteolysis and nutrition in formation of cataract. Age, 14, 65-71.
435. Taylor, A., Jacques, P., Nadler, D., Morrow, F., Sulsky, S. I. and Shepard, D. (1991b). Relationship between ascorbic acid consumption and levels of total and reduced ascorbic in lens, aqueous humor, and plasma. Curr. Eye Res., 10, 751-759.
436. Taylor, A., Berger, J., Reddan, J. and Zuliani, A. (1991c). Effects of aging in vitro on intracellular proteolysis in cultured rabbit lens epithelial cells in the presence and absence of serum. In Vitro Cell. Develop. Biol., 27A, 287-292.
437. Taylor, A. (1992a). Vitamin C. In: Nutrition in the Elderly: the Boston Nutritional Status Survey (S. C. Hartz, R. M. Russell and I. H. Rosenberg, eds.), pp. 147-150. Smith Gordon, London.
438. Taylor, A. (1992b). Effects of photooxidation on the eye lens and role of nutrients in delaying cataract. In: Free Radicals and Aging (I. Emerit and B. Chance, eds.), pp. 266-279. Birhauser Verlag, Basel.
439. Taylor, A. (1993). Aminopeptidases: structure and function. FASEB J., 7, 290-298.
440. Taylor, A. (1993). Aminopeptidases: towards a mechanism of action. TIBS, 18, 167-172.
441. Taylor, A. (1993). Cataract: relationships between nutrition and oxidation. J. Am. Coll. Nutr., 12, 138-146.
442. Taylor, A. (1997). Cataract. In: Antioxidants in Disease Mechanisms and Therapeutic Strategies (A Volume of Advances in Pharmacology Series) (H. Sies, ed.), pp. 515-536. Academic Press, San Diego, CA.
443. Taylor, A. and Davies, K. J. A. (1987). Protein oxidation and loss of protease activity may lead to cataract formation in the aged lens. Free Rad. Biol. Med., 3, 371-377.
444. Taylor, A. and Jacques, P. F. (1995). Relationships between aging, antioxidant status, and cataract. Am. J. Clin. Nutr., 62, 1439S-1447S.
445. Taylor, A. and Jacques, P. (1997). Antioxidant status and risk for cataract. In: Preventive Nutrition: The Guide for Health Professionals (A. Bendich and R. J. Deckelbaum, eds.), pp. 267-283. Humana Press, Totawa, NJ.
446. Taylor, A., Tisdell, F. E. and Carpenter, F. H. (1981). Leucine aminopeptidase (bovine lens): synthesis and kinetic properties of ortho, meta, and para substituted leucylanilides. Arch. Biochem. Biophys., 210, 90-97.
447. Taylor, A., Brown, M. J., Daims, M. A. and Cohen, J. (1983). Localization of leucine aminopeptidase in hog lenses using immunofluorescence and activity assays. Invest. Ophthalmol. Vis. Sci., 24, 1172-1181.
448. Taylor, A., Zuliani, A. M., Hopkins, R. E., Dallal, G. E., Treglia, P., Kuck, J. F. R. and Kuck, K. (1989). Moderate caloric restriction delays cataract formation in the Emory mouse. FASEB J., 3, 1741-1746.
449. Taylor, A., Jahngen-Hodge, J., Huang, L. L. and Jaques, P. (1991). Aging in the eye lens: roles for proteolysis and nutrition in formation of cataract. AGE, 14, 65-71.
450. Taylor, A., Jacques, P. F., Nadler, D., Morrow, F., Sulsky, S. I. and Shepard, D. (1991). Relationship in humans between ascorbic acid consumption and levels of total and reduced ascorbic acid in lens, aqueous humor, and plasma. Curr. Eye Res., 10, 751-759.
451. Taylor, A., Berger, J., Reddan, J. and Zuliani, A. (1991). Effects of aging in vitro on intracellular proteolysis in cultured rabbit lens epithelial cells in the presence and absence of serum. In Vitro Cell. Dev. Biol., 27A, 287-292.
452. Taylor, A., Jacques, P. F. and Dorey, C. K. (1993). Oxidation and aging: impact on vision. J. Toxicol. Indust. Health, 9, 349-371.
453. Taylor, A., Jahngen-Hodge, J., Smith, D., Palmer, V., Dallal, G., Lipman, R., Padhye, N. and Frei, B. (1995). Dietary restriction delays cataract and reduces ascorbate levels in Emory mice. Exp. Eye Res., 61, 55-62.
454. Taylor, A., Lipman, R. D., Jahngen-Hodge, J., Palmer, V., Smith, D., Padhye, N., Dallal, G. E., Cyr, D. E., Laxman, E., Shepard, D., Morrow, F., Solomon, R., Perrone, G., Asmundsson, G., Meydani, M., Mune, M., Harrison, D. and Archer, J. (1995). Dietary calorie restriction in the Emory Mouse: effects on lifespan, eye lens cataract prevalence and progression, levels of ascorbate, glutathione, glucose, and glycohemoglobin, tail collagen breaktime, DNA and RNA oxidation, skin integrity, fecundity and cancer. Mech. Ageing Dev., 79, 33-57.
455. Taylor, A., Sanford, D. and Nowell, T. (1996). Structure and function of bovine lens aminopeptidase and comparison with homologous aminopeptidases. In: Aminopeptidases (A. Taylor, ed.), pp. 21-59. R. G. Landes Co, Austin, TX.
456. Taylor, A., Jacques, P., Nowell, T. Jr, Perrone, G., Nadler, D. and Joswiak, B. (1997). Vitamin C in human and guinea pig aqueous, lens, and plasma in relation to intake. Curr. Eye Res. 16, 857-864.
457. Taylor, H. R., West, S. K., Rosenthal, F. S., Newland, H. S., Abbey, H. and Emmett, E. A. (1988). Effect of ultraviolet radiation on cataract formation. N. Engl. J. Med., 319, 1429-1433.
458. Taylor, H. R., West, S., Munoz, B., Rosenthal, F. S., Bressler, S. B. and Bressler, N. M. (1992). The long-term effects of visible light on the eye. Arch. Ophthalmol., 110, 99-104.
459. The Italian-American Cataract Study Group (1991). Risk factors for age-related cortical, nuclear, and posterior subcapsular cataracts. Am. J. Epidemiol. 133, 541-553.
460. Thornberry, N. A. (1994). Interleukin-1 beta converting enzyme. Meth. Enzymol., 244, 615-631.
461. Trayhurn, P. and van Heyningen, R. (1976). Neutral proteinase activity in the human lens. Exp. Eye Res., 22, 251-257.
462. Treier, M., Staszewski, L. M. and Bohmann, D. (1994). Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell, 78, 787-798.
463. Tsang, H. T., Gouras, P., Yamashita, C. K., Kjeldbye, H., Fisher, J., Farber, D. B. and Goff, S. P. (1996). Retinal degeneration in mice lacking the γ subunit of the rod cGMP phosphodiesterase. Science, 272, 1026-1029.
464. Tse, S. S. and Ortwerth, B. J. (1981). Activation of proteases with trypsin-like specificity from bovine and human lenses. Exp. Eye Res., 32, 605-614.
465. 2+-requiring neutral proteases in rat retina. Exp. Eye Res., 41, 97-103.
466. Tumminia, S. J., Jonak, G. J., Focht, R. J., Cheng, Y. S. and Russell, P. (1996). Cataractogenesis in transgenic mice containing the HIV-1 protease linked to the lens alpha A-crystallin promoter. J. Biol. Chem., 271, 425-431.
467. Tytell, M., Barbe, M. F. and Gower, D. J. (1989). Photoreceptor protection from light damage by hyperthermia. Progr. Clin. Biol. Res., 314, 523-538.
468. Uchida, K. and luvone, P. M. (1997). Intracellular calcium concentrations of cultured photoreceptor cells: sustained elevation in depolarized cells and effects of calmodulin kinase inhibitors. Invest. Ophthalmol. Vis. Sci., 38, s615.
469. Vanags, D. M., Pörn-Ares, M. I., Coppola, S., Burgess, D. H. and Orrenius, S. (1996). Protease involvement in fodrin cleavage and phosphatidylserine exposure in apoptosis. J. Biol. Chem., 271, 31075-31085.
470. Varma, S. D., Chand, D., Sharma, Y. R., Kuck, J. F. and Richards, R. D. (1984). Oxidative stress on lens and cataract formation: role of light and oxygen. Curr. Eye Res., 3, 35-57.
471. Varnum, M. D., David, L. L. and Shearer, T. R. (1989). Age-related changes in calpain II and calpastatin in rat lens. Exp. Eye Res., 49, 1053-1065.
472. Varshavsky, A. (1996). The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. U.S.A., 93, 12142-12149.
473. Vasan, S., Zhang, X., Zhang, X., Kapurniotu, A., Bernhagen, J., Teichberg, S., Basgen, J., Wagle, D., Shih, D., Terlecky, I., Bucala, R., Cerami, A., Egan, J. and Ulrich, P. (1996). An agent cleaving glucose-derived protein crosslinks in vitro and in vivo. Nature, 382, 275-278.
474. Vina, J., Perez, C., Furukawa, T., Palacin, M. and Vina, J. R. (1989). Effect of oral glutathione on hepatic glutathione levels on rats and mice. Br. J. Nutr., 62, 683-691.
475. Vinson, J. A., Possanza, C. J. and Drack, A. V. (1986). The effect of ascorbic acid on galactose-induced cataracts. Nutr. Reports Int., 33, 665-668.
476. Vitale, S., West, S., Hallfrisch, J., Alston, C., Wang, F., Moorman, C., Muller, D., Singh, V. and Taylor, H. R. (1994). Plasma antioxidants and risk of cortical and nuclear cataract. Epidemiology, 4, 195-203.
477. Wagner, B. J., Margolis, J. W., Farnsworth, P. N. and Fu, S. C. J. (1982). Calf lens neutral proteinase activity using calf lens crystallin substrates. Exp. Eye Res., 35, 293-303.
478. Wagner, B. J., Fu, S. C. J., Margolis, J. W. and Fleshman, K. R. (1984). A synthetic endopeptidase substrate hydrolyzed by the bovine lens neutral proteinase preparation. Exp. Eye Res., 38, 477-483.
479. Wagner, B. J., Margolis, J. W. and Abramovitz, A. S. (1986a). The bovine lens neutral proteinase comprises a family of cysteme-dependent proteolytic activities. Curr. Eye Res., 5, 863-868.
480. Wagner, B. J., Margolis, J. W., Garland, D. and Roseman, J. E. (1986b). Bovine lens neutral proteinase preferentially hydrolyses oxidatively modified glutamine synthetase. Exp. Eye Res., 43, 1141-1143.
481. Wang, G-m., Spector, A., Luo, C-q., Tang, L. Q., Xu, L. H., Guo, W. Y. and Huang, Y. Q. (1990). Prevalence of age-related cataract in Ganzi and Shanghai. The Epidemiological Study Group. Chinese Med. J., 103, 945-951.
482. Wang, K. and Spector, A. (1994). The chaperone activity of bovine α-crystallin. J. Biol. Chem., 269, 13601-13608.
483. Wang, K. and Spector, A. (1995). α-crystallin can act as a chaperone under conditions of oxidative stress. Invest. Ophthalmol. Vis. Sci., 36, 311-321.
484. Wang, K. K., Vilalobo, A. and Roufogalis, B. D. (1989). Calmodulin-binding proteins as calpain substrates. Biochem J., 262, 693-706.
485. Wang, L., Miura, M., Bergeron, L., Zhu, H. and Yuan, J. (1994). Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell, 78, 739-750.
486. Ward, C. L., Omura, S. and Kopito, R. R. (1995). Degradation of CFTR by the ubiquitin-proteasome pathway. Cell, 83, 121-127.
487. Weber, B. H., Vogt, G., Pruett, R. C., Stohr, H. and Felbor, U. (1994). Mutations in the tissue inhibitor of metalloproteinase-3 (TIMP-3) in patients with Sorsby's fundus dystrophy. Nature Genetics, 8, 352-356.
488. Wefers, H. and Sies, H. (1988). The protection by ascorbate and glutathione against microsomal lipid peroxidation is dependent on vitamin E. FEBS, 174, 353-357.
489. Weiss, E. R. Osawa, S., Shi, W. and Dickerson, C. D. (1994). Effects of carboxyl-terminal truncation on the stability and G protein-coupling activity of bovine rhodopsin. Biochemistry 33, 7587-7593.
490. West, S. (1992). Does smoke get in your eyes? J. Am. Med. Assoc., 268, 1025-1026.
491. West, S. K., Munoz, B., Emmett, E. A. and Taylor, H. R. (1989). Cigarette smoking and risk of nuclear cataracts. Arch. Ophthalmol., 107, 1166-1169.
492. Whisler, R. L., Newhouse, Y. G., Beiqing, L., Karanfilov, B. K., Goyette, M. A. and Hackshaw, K. V. (1994). Regulation of protein kinase enzymatic activity in Jurkat T cells during oxidative stress uncoupled from protein tyrosine kinases: role of oxidative changes in protein kinase activation requirements and generation of second messengers. Lymphokine Cytokine Res., 13, 399-410.
493. Whitfield, R., Schwab, L., Ross-Degnan, D., Steinkuller, P. and Swartwood, J. (1990). Blindness and eye disease in Kenya: ocular status survey results from the Kenya Rural Blindness Prevention Project. Br. J. Ophthalmol., 74, 333-340.
494. Wilczek, M. and Zygulska-Machowa, H. (1968). Zawartosc witaminy C W. roznych typackzaem. J. Klin. Oczna, 38, 477-480.
495. Wilkinson, K. D. (1995). Roles of ubiquitinylation in proteolysis and cellular regulation. Ann. Rev. Nutr., 15, 161-189.
496. Wilkinson, K. D., Lee, K. M., Deshpande, S., Duerksen-Hughes, P., Ross, J. M. and Pohl, J. (1989). The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase. Science, 246, 670-673.
497. Williams, D. S. (1991). Actin filaments and photoreceptor membrane turnover. Bioessays, 13, 172-178.
498. Williams, D. S., Hallet, M. A. and Arikawa, K. (1992). Association of myosin with the connecting cilium of rod photoreceptors. J. Cell. Sci., 103, 183-190.
499. Wing, S. S. and Banville, D. (1994). 14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin. Am. J. Physiol., 267, E39-E48.
500. Wistow, G. J. and Piatigorsky, J. (1988). Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Ann. Rev. Biochem., 57, 479-504.
501. Wolfe, J. K., Chylack, L. T. Jr, Leske, M. C., Wu, S. Y. and LSC Group. (1993). Lens nuclear color and visual function. Invest. Ophthalmol. Vis. Sci. 34(4), 2550, abstr.
502. Wolff, S. P. (1995). Cataract and UV radiation. Documenta Ophthalmol., 88, 201-204.
503. Wong, L., Ho, S. C., Coggon, D., Cruddas, A. M., Hwang, C. H., Ho, C. P., Robertshaw, A. M. and MacDonald, D. M. (1993). Sunlight exposure, antioxidant status, and cataract in Hong Kong fishermen. J. Epidemiol. Community Health, 47, 46-49.
504. Wormald, R. P. L., Wright, L. A., Courtney, P., Beaumont, B. and Haines, A. P. (1992). Visual problems in the elderly population and implications for services. Br. Med. J., 304, 1226-1229.
505. World Health Organization (1991). Use of intraocular lenses in cataract surgery in developing countries. Bull. World Health Organ. 69, 657-666.
506. Wu, Y. and Becerra, S. P. (1996). Proteolytic activity directed towards pigment epithelium-derived factor in vitreous of bovine eyes: implications of protcolytic processing. Invest. Ophthalmol. Vis. Sci., 10, 1984-1993.
507. Wu, Y., Notario, V., Chader, G. J. and Becerra, S. P. (1995). Identification of pigment epithelim-derived factor in the interphotoreceptor matrix of bovine eyes. Protein Express. Purif., 6, 447-456.
508. Yamaguchi, T., Kim, N. S., Sekine, S., Seino, H., Osaka, F., Yamao, F. and Kato, S. (1996). Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product. J. Biol. Chem., 120, 494-497.
509. Yamashita, H., Horie, K., Yamamoto, T., Nagano, T. and Hirano, T. (1992). Light-induced retinal degeneration in mice: hydrogen peroxide production and superoxide dismutase activity in retina. Retina, 12, 59-66.
510. Yamashita, K., Eguschi, Y., Kajiwara, K. and Ito, H. (1991). Mild hypothermia ameliorates ubiquitin synthesis and prevents delayed neuronal death in the gerbil hippocampus. Stroke, 22, 1574-1581.
511. Yancey, S. C., Koh, K., Chung, J. and Revel, J. P. (1988). Expression of the gene for main intrinsic polypeptide (MIP): separate spatial distribution of MIP and β-crystallin gene transcripts in rat lens development. J. Cell Biol., 106, 705-714.
512. Yarfitz, S. and Hurley, J. B. (1994). Transduction mechanisms of vertebrate and invertebrate photoreceptors. J. Biol. Chem., 269, 14329-14332.
513. Yau, K. (1994). Phototransduction mechanism in retinal rods and cones. Invest. Ophthalmol. Vis. Sci., 35, 29-32.
514. Yeum, K., Taylor, A., Tang, G. and Russell, R. M. (1995). Measurement of carotenoids, retinoids, and tocopherols in human lenses. Invest. Ophthalmol. Vis. Sci., 36, 2756-2761.
515. 2+-dependent cysteine proteinase, isolated from the same tissue. Biochim. Biophys. Acta, 798, 252-259.
516. Yoshida, H., Murachi, T. and Tsukahara, I. (1985). Distribution of calpain I, calpain II, and calpastatin in bovine lens. Invest. Ophthalmol. Vis. Sci., 26, 953-956.
517. Yoshida, H., Yumoto, T., Tsukahara, I. and Murachi, T. (1986). The degradation of α-crystallin at its carboxyl terminal portion by calpain in bovine lens. Invest. Ophthalmol. Vis. Sci., 27, 1269-1273.
518. Young R. W. (1992). Optometry and the preservation of visual health. Eye Communication.
519. Young, R. W. (1984). Cell death during differentiation of the retina in the mouse. J. Comp. Neurol., 229, 362-373.
520. Yu, N. T., DeNagel, D. C., Pruett, P. L. and Kuck, J. F. R. J. (1985). Disulfide bond formation in the eye lens. Proc. Natl. Acad. Sci. U.S.A., 82, 7965-7968.
521. Yuan, J., Shaham, S., Ledoux, S., Ellis, H. M. and Horvitz, H. R. (1993). The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1-beta-converting enzyme. Cell, 75, 641-652.
522. Zampighi, G. A., Hall, J. E., Ehring, G. R. and Simon, S. A. (1985). Purified lens junctional protein forms channels in lipid films. Proc. Natl. Acad. Sci. U.S.A., 82, 8468-8472.
523. Ziegenhagen, R. and Jennissen, H. P. (1988). Multiple ubiquitination of vertebrate calmodulin by reticulocyte lysate and inhibition of calmodulin conjugation by phosphorylase kinase. Biol. Chem. Hoppe-Seyler, 369, 1317-1324.
524. Zigler, J. S. and Goosey, J. D. (1984). Singlet oxygen as a possible factor in human senile nuclear cataract development. Curr. Eye Res., 3, 59-65.
525. Zigler, J. S. and Horwitz, J. (1981). Immunochemical studies on the major intrinsic polypeptides from human lens membrane. Invest. Ophthalmol. Vis. Sci., 13, 237-251.
526. Zigman, S. (1983). Effects of near ultraviolet radiation on the lens and retina. Documenta Ophthalmol., 55, 375-391.
527. Zigman, S., Datiles, M. and Torczynski, E. (1979). Sunlight and human cataract. Invest. Ophthalmol. Vis. Sci. 18462-18467.
528. Zigman, S., Paxhia, T., McDaniel, T., Lou, M. F. and Yu, N-T. (1991). Effect of chronic near-ultraviolet radiation on the gray squirrel lens in vivo. Invest. Ophthalmol. Vis. Sci., 32, 1723-1732.
529. Zigman, S., McDaniel, T., Schultz, J. B., Reddan, J. and Meydani, M. (1995). Damage to cultured lens epithelial cells of squirrels and rabbits by UV-A (99.9%) plus UV-B (0.1%) radiation and alpha tocopherol protection. Mol. Cell Biochem., 143, 35-46.