Background/Objective: The aim of this systematic review is to identify all the available data on human lens proteomics
with a critical role to age-related cataract formation in order to elucidate the physiopathology of the aging lens.
Materials and Methods: We searched on Medline and Cochrane databases. The search generated 328 manuscripts. We included
nine original proteomic studies that investigated human cataractous lenses.
Results: Deamidation was the major age-related post-translational modification. There was a significant increase in the
amount of αA-crystallin D-isoAsp58 present at all ages, while an increase in the extent of Trp oxidation was apparent in cataract
lenses when compared to aged normal lenses. During aging, enzymes with oxidized cysteine at critical sites included
GAPDH, glutathione synthase, aldehyde dehydrogenase, sorbitol dehydrogenase, and PARK7.
Conclusion: D-isoAsp in αA crystallin could be associated with the development of age-related cataract in human, by contributing
to the denaturation of a crystallin, and decreasing its ability to act as a chaperone. Oxidation of Trp may be associated
with nuclear cataract formation in human, while the role of oxidant stress in age-related cataract formation is dominant.