Abstract
Many post-translational modifications of lens proteins occur during aging.1 Since the lens continues to grow throughout life and its cells and proteins are not turned over, these modifications accumulate in the older fiber cells.
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References
H. J. Hoenders and H. Bloemendal, Aging of Lens Proteins, in: “Molecular and Cellular Biology of the Eye Lens,” H. Bloemendal, ed., John Wiley & Sons, Inc., New York (1981).
L. Fucci, C. N. Oliver, M. J. Coon, and E. R. Stadtman, Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and aging, Proc.Natl.Acad.Sci.U.S.A. 80:1521 (1983).
K.-W. Kim, S. G. Rhee, and E. R. Stadtman, Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron, J.Biol.Chem. 260:15394 (1985).
R. L. Levine, Oxidative modification of glutamine synthetase, J.Biol.Chem. 258:11823 (1983).
R. L. Levine, Mixed-function oxidation of histidine residues, in: “Methods of Enzymology,” F. Wold and K. Moldave, eds., Academic Press, New York (1984).
B. Chance, The reactions of catalase in the presence of the notation system, Biochem.J. 46:387 (1950).
A. J. Rivett, Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular proteases, J.Biol.Chem. 260:300 (1985).
D. L. Garland, J. S. Zigler, Jr., and J. Kinoshita, Structural changes in bovine lens crystallins induced by ascorbate, metal, and oxygen, Arch.Biochem.Biophys. 251:771 (1986).
K. G. Bensch, J. E. Fleming, and W. Lohmann, The role of ascorbic acid in senile cataract, Proc.Natl.Acad.Sci.U.S.A. 82:7193 (1985).
J. S. Zigler, Jr., P. Russell, L. J. Takemoto, S. J. Schwab, J. S. Hansen, J. Horwitz, and J. H. Kinoshita, Partial characterization of three distinct populations of human γ crystallins, Invest.Ophthamol.Vis.Sci. 26:525 (1985).
S. O. Meakin, M. L. Breitman, and L.-C. Tsui, Structural and evolutionary relationships among five members of the human-crystallin gene family, Mol.Cell.Biol. 5:1408 (1985).
P. Russell, D. L. Garland, J. S. Zigler, Jr., S. O. Meakin, L.-C. Tsui, and M. L. Breitman, Aging effects of vitamin C on a human lens protein produced in vitro, FASEB Journal 1:32 (1987).
W. Lohmann, W. Schmehl, and J. Strobel, Nuclear cataract: Oxidative damage to the lens, Exp.EyeRes. 43:859–862 (1986).
J. Bellows, Biochemistry of lens: Some studies in vitamin C and the lens, Arch. Ophth. 16:58 (1936).
M. Testa, S. Daniels, and M. Bocci, The reactivity of the serum protein-SH groups in the senile cataract, Ophthalmologica 147:485 (1964).
R. Nath, S. K. Srivastava, and K. Singh, Accumulation of Cu and inhibition of LDH activity in human senile cataractous lens, Indian J.Exp.Biol. 7:25 (1969).
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© 1988 Plenum Press, New York
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Garland, D., Russell, P., Zigler, J.S. (1988). The Oxidative Modification of Lens Proteins. In: Simic, M.G., Taylor, K.A., Ward, J.F., von Sonntag, C. (eds) Oxygen Radicals in Biology and Medicine. Basic Life Sciences, vol 49. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5568-7_52
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DOI: https://doi.org/10.1007/978-1-4684-5568-7_52
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