| Abstrakt: |
α- Crystallin, an oligomeric major constituent protein of the eye lens of vertebrates, was originally identified for its role in the lens’ transparency. In addition to having its micelle-like architecture, this protein has molecular chaperoning activity. Lens α-crystallin consists of two subunits, αA and αB, whose aggregate formation is necessary for molecular chaperoning activity. Isolation and characterization of α-crystallin from a wide range of vertebrates will help in understanding a better structure–function relationship in a broader sense, which is yet to be achieved. The stability, structure, aggregation and molecular chaperone activity of α-crystallin differ significantly from species to species. These differences clearly reflect specific structural changes of the protein, which, in turn, may contribute to the transparency and refractive power of the eye lens. Several eye diseases, such as diabetic retinopathy involve oxidative stress, followed by a decrease in total soluble lens proteins and a decreased amount of βB1 crystallins. Intraperitoneal injection of edaravone drugs, a member of the substituted 2-pyrazolin-5-one class, and its analogs are now being tried to revert back crystallin activity and inhibit hyperglycemia and oxidative stress-mediated eye cell damage. In the upcoming future, edaravone-like drugs or their analogs can be synthesized and targeted for better efficacy. |
Full text from SpringerLink