Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 45, Pages 16912-16917Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0605101103
Keywords
advanced glycation end products; ascorbic acid; cataract; diabetes; oxidation
Categories
Funding
- NEI NIH HHS [P30 EY011373, P30 EY 11373, R01 EY007099-18, R01 EY007070, EY 07099, R01 EY013146, EY 07070, R01 EY007099, EY 13146, T32 EY 07157, T32 EY007157] Funding Source: Medline
- NIA NIH HHS [AG 18629] Funding Source: Medline
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Senile cataracts are associated with progressive oxidation, fragmentation, cross-linking, insolubilization, and yellow pigmentation of lens crystallins. We hypothesized that the Maillard reaction, which leads browning and aroma development during the baking of foods, would occur between the lens proteins and the highly reactive oxidation products of vitamin C. To test this hypothesis, we engineered a mouse that selectively overexpresses the human vitamin C transporter SVCT2 in the lens. Consequently, lenticular levels of vitamin C and its oxidation products were 5- to 15-fold elevated, resulting in a highly compressed aging process and accelerated formation of several protein-bound advanced Maillard reaction products identical with those of aging human lens proteins. These data strongly implicate vitamin C in lens crystallin aging and may serve as a model for protein aging in other tissues particularly rich in vitamin C, such as the hippocampal neurons and the adrenal gland. The hSVCT2 mouse is expected to facilitate the search for drugs that inhibit damage by vitamin C oxidation products.
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