Multiple and Additive Functions of ALDH3A1 and ALDH1A1

• DOI: 10.1074/jbc.m702076200
• Publication Date: 2007-06-14T06:34:59Z
• Authors: Natalie Lassen; J. Bronwyn Bateman; Tia Estey; Jer R. Kuszak; David W. Nees; Joram Piatigorsky; Gregg Duester; Brian J. Day; Jie Huang; Lisa M. Hines; Vasilis Vasiliou
• Keywords: Mice, Knockout; 0301 basic medicine; Aging; Proteasome Endopeptidase Complex; Ultraviolet Rays; Retinal Dehydrogenase; Aldehyde Dehydrogenase; Glutathione; Aldehyde Dehydrogenase 1 Family; Cataract; Cornea; Mice; Oxidative Stress; 03 medical and health sciences; Phenotype; Lens, Crystalline; Animals; Eye Proteins; Oxidation-Reduction

ALDH3A1 (aldehyde dehydrogenase 3A1) is abundant in the mouse cornea but undetectable lens, and ALDH1A1 present at lower (catalytic) levels lens. To test hypothesis that protect anterior segment of eye against environmentally induced oxidative damage, Aldh1a1(-/-)/Aldh3a1(-/-) double knock-out Aldh1a1(-/-) Aldh3a1(-/-) single mice were evaluated for biochemical changes cataract formation (lens opacification). The Aldh1a1/Aldh3a1- Aldh3a1-null develop cataracts posterior subcapsular regions as well punctate opacities cortex by 1 month age. Aldh1a1-null also later life (6-9 months age). One- to three-month-old Aldh-null exposed UVB exhibited accelerated lens opacification, which was more pronounced Aldh3a1(-/-)/Aldh1a1(-/-) compared with wild type animals. Cataract associated decreased proteasomal activity, increased protein oxidation, GSH levels, 4-hydroxy-2-nonenal- malondialdehyde-protein adducts. In conclusion, these findings support corneal via nonenzymatic (light filtering) enzymatic (detoxification) functions.