Abstract

Background: Long-lived proteins (LLPs) are essential for cellular architecture, especially in tissues like the eye lens. However, due to their extended lifespan, they are susceptible to post translational modifications like oxidative damage and glycation. Maintaining the redox status within cells is crucial for LLP functionality. Cataracts, caused by the clouding of the eye's natural lens, are a primary cause of visual impairment and blindness. Chronic hyperglycemia in diabetes increases the risk of cataract formation due to metabolic disturbances. Objectives: This study investigates the redox status of lens proteins and its role in diabetic cataract formation. By evaluating carbonyl and sulfhydryl groups, the study aims to understand the oxidative damage to lens proteins. Oxidative modifications, such as carbonylation and cross linking, lead to protein aggregation and reduced solubility, resulting in lens opacity. Methods: Using in-vitro goat lens models, this research explores oxidative changes and antioxidative response mechanisms under diabetic conditions. Goat lenses, due to their physiological similarities to human lenses, provide valuable insights into diabetic cataractogenesis. A total of 64 goat lenses were divided into experimental diabetic cataract (n=32) and control groups (n=32), incubated in glucose-rich and normal conditions, respectively. Protein carbonyl and sulfhydryl contents were measured using spectrophotometric techniques. Results: Oxidation of lens protein was found to be significantly associated with diabetic cataract. In diabetic cataract, a statistically significant increase in the level of protein carbonyl and significant decrease in the level of protein sulfhydryl was seen as compared to controls

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