engleski

Novel Nonenzymatic Modifications of Lens Crystallins by Vitamin C Target Arginine Residues

Lens crystallins are prone to chemical modifications that affect chaperone function and favor toward aggregation and cataractogenesis. Vitamin C degradation products participate significantly in these chemical pathways in the lens. However, the products described so far can be formed from sugars other than Vitamin C and therefore do not reflect the specific role of Vitamin C in the modification. Here we characterized the structure of novel crystallin ascorbylation adducts and crosslinks with target amino acids and lens crystallins in vitro and from mice expressing the human vitamin C transporter 2 (hSCVT2) in the lens. Novel products of protein modifications by Vitamin C which target arginine in crystallins were characterized and identified in vitro and in vivo systems. They could destabilize arginine residues and contribute toward impaired chaperone function during aging.

Nonenzymatic Modifications; Lens Crystallins; Aggregation; Cataractogenesis; Vitamin C; Sugars; Arginine; Aging

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