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Journal of Ophthalmology
Volume 2010, Article ID 274317, 7 pages
Research Article

Inhibition of Methylglyoxal-Mediated Protein Modification in Glyoxalase I Overexpressing Mouse Lenses

1Department of Ophthalmology & Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA
2Mason Eye Institute, University of Missouri, Columbia, MO 65212, USA

Received 1 March 2010; Accepted 1 June 2010

Academic Editor: Mark Petrash

Copyright © 2010 Mahesha H. Gangadhariah et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Objective. Here we tested the role of Glo I in the prevention of advanced glycation end product (AGE) formation in transgenic mouse lenses. Methods. A transgenic animal line that expressed high levels of human Glo I in the lens was developed from the C57B6 mouse strain. The role of Glo I in the inhibition of MGO-AGE formation was tested in organ-cultured lenses. Results. Organ culture of Wt and Glo I lenses with 5 mM D, L-glyceraldehyde (GLD) enhanced MGO by 29-fold and 17-fold in Wt lenses and Glo I lenses, respectively. Argpyrimidine levels were pmoles/mg protein, and hydroimidazolone levels were units/ protein in GLD-incubated Wt lenses. In Glo I lenses, formation of AGEs was significantly inhibited; the argpyrimidine levels were pmoles/mg protein, and the HI levels were units/ protein. Incubation of Wt lens proteins with 5 mM ribose for 7 days resulted in the formation of pentosidine. However, the levels were substantially higher in Glo I lens proteins incubated with ribose. Conclusion. Our study provides direct evidence that Glo I activity plays an important role in the regulation of AGE synthesis in the lens; while Glo I activity blocks the formation of MGO-AGEs, it might promote the formation of sugar-derived AGEs.