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Science 13 June 1980:
Vol. 208. no. 4449, pp. 1278 - 1280
DOI: 10.1126/science.7375939
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Articles

Science, Vol 208, Issue 4449, 1278-1280
Copyright © 1980 by American Association for the Advancement of Science

articles

Cross-linking of lens crystallins in a photodynamic system: a process mediated by singlet oxygen

JD Goosey, JS Zigler Jr, and JH Kinoshita

In a dye-sensitized photooxidation system, lens crystallin polypeptides become cross-linked, and a blue fluorescence that is associated with the proteins is produced. These changes are similar to those seen in vivo in the aging human lens. Evidence implicating singlet oxygen as the causative agent of the effects in vitro is presented, and the possibility that this species may play a role in aging and cataractogenesis in vivo is discussed.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Metabolic Changes in Rat Lens after In Vivo Exposure to Ultraviolet Irradiation: Measurements by High Resolution MAS 1H NMR Spectroscopy.
O. Risa, O. Saether, S. Lofgren, P. G. Soderberg, J. Krane, and A. Midelfart (2004)
Invest. Ophthalmol. Vis. Sci. 45, 1916-1921
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Cloning, Expression, and Chaperone-like Activity of Human alpha A-Crystallin.
U. P. Andley, S. Mathur, T. A. Griest, and J. M. Petrash (1996)
J. Biol. Chem. 271, 31973-31980
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Dye-Enhanced Tissue Welding Using Fibrinogen and Continuous-Wave Argon Lasers.
S. K. Libutti, M. C. Oz, R. S. Chuck, M. R. Treat, and R. Nowygrod (1990)
Vascular and Endovascular Surgery 24, 671-676
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Nonenzymatic browning in vivo: possible process for aging of long-lived proteins.
V. Monnier and A Cerami (1981)
Science 211, 491-493
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