Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 427, Issue 2, Pages 197-203Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2004.05.006
Keywords
proteasome; human eye lens; aging; protein glycation
Categories
Ask authors/readers for more resources
The proteasome is known to be the main enzymatic complex responsible for the intracellular degradation of altered proteins, and the age-related accumulation of modified lens proteins is associated to the formation of cataracts. The aim of this study was to determine whether the human lens proteasome becomes functionally impaired with age. The soluble and insoluble protein fractions of human lenses corresponding to various age-groups were characterized in terms of their levels of glyco-oxidative damage and found to show increasing anti-carboxymethyl-lysine immunoreactivity with age. Concomitantly, decreasing proteasome contents and peptidase activities were observed in the water-soluble fraction. The fact that peptidylglutamyl-peptide hydrolase activity is most severely affected with age suggests that specific changes are undergone by the proteasome itself. In particular, increasing levels of carboxymethylation were observed with age in the proteasome. It was concluded that the lower levels of soluble active enzymatic complex present in elderly lenses and the post-translational modifications affecting the proteasome may at least partly explain the decrease in proteasome activity and the concomitant accumulation of carboxymethylated and ubiquitinated proteins which occur with age. (C) 2004 Elsevier Inc. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available