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Structural changes in bovine lens crystallins induced by ascorbate, metal, and oxygen
Archives of Biochemistry and Biophysics
|December 1, 1986
Summary
Oxidative stress from ascorbate, Fe3+, or Cu2+ modified bovine lens crystallins, mimicking age-related changes. These modifications involved protein crosslinking, cleavage, and altered protein acidity, impacting lens clarity.
Area of Science:
- Biochemistry
- Ophthalmology
- Protein Chemistry
Background:
- Bovine lens crystallins undergo modifications with aging.
- Oxidative stress is implicated in age-related lens changes.
Purpose of the Study:
- To investigate the oxidative modification of bovine lens crystallins.
- To mimic age-related changes in lens proteins using specific oxidants.
Main Methods:
- Incubation of bovine lens crystallins with ascorbate, Fe3+, or Cu2+ and oxygen.
- Analysis of protein modifications including crosslinking and cleavage.
- Assessment of changes in protein charge and fluorescence.
Main Results:
- Oxidation induced nondisulfide crosslinks in alpha- and beta H-crystallin.
- Cleavage of alpha-, beta H-, and low molecular weight crystallin fractions occurred.
- Protein fractions showed a shift from basic to acidic species.
- Nontryptophan fluorescence was generated in beta H-crystallin.
Conclusions:
- Ascorbate, Fe3+, and Cu2+ can induce age-like modifications in lens crystallins.
- Metal ions like Fe3+ and Cu2+ play a role in catalyzing these oxidative changes.
- These findings provide insight into the molecular mechanisms of lens aging and cataract formation.