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Abstract
This study aims to investigate the effect of mild heating on lens epithelial cells and to explore its possibility as an in vitro model for lens aging. Human lens epithelial cells (LECs) were heated at 50 °C for a cellular lens aging study. Analysis of the head group order of lens membranes was performed using Laurdan labeling. Immunofluorescence was performed to detect changes in α-crystallin expression and its cellular distribution. The chaperone-like activity of α-crystallin was also assessed. After mild heating, α-crystallin in LECs showed a tendency towards accumulation around the nucleus. The membrane head group environment of lens epithelial cells became more fluid with increasing time of exposure to mild heating, as indicated by increased water penetration. Furthermore, the chaperone activity of α-crystallin decreased, and suggests a relatively lower protective effect on other functional proteins in LECs. Thus, compared to the mild heating model based on lens tissue, this cellular model could provide a more convenient and accurate method for studying lens aging in vitro, including changes in membrane head group order in each cell, the real-time observation of crystallin distribution, and the monitoring of functional changes in the chaperone activity of crystallins as a result of aging.
Highlights
With aging, modifications of lens crystallins, including amorphous-aggregation and cross-linking, can contribute to protein insolubilization[2]
Using the Cell Counting Kit-8 (CCK-8) kit, we studied the viability of lens epithelial cells (LECs) incubated at 50 °C over different time periods (0, 15, 30, 45, 60, and 75 min)
In the experiments reported here, LECs subjected to mild heating could provide an alternative model for studying lens aging, through inducing a diminished regulatory function for α-crystallin in maintaining the lens membrane head group environment, in addition to attenuating its function as a molecular chaperone that exhibits a protective effect on other proteins
Summary
Modifications of lens crystallins, including amorphous-aggregation and cross-linking, can contribute to protein insolubilization[2]. Our previous study[6] showed that there are age-related changes in membrane head group structures in the lens. Further research into changes in head group order in lens membranes and crystallin function is important in for extending existing knowledge of lens aging and cataract development. Analysis of membrane head group environments and crystallin function through a cellular mild heating model could provide new insights into the controlling mechanisms behind lens aging in vivo. This study aims to establish a model for lens aging in vitro in which changes in head group order in cellular membranes and α-crystallin function can be detected. Using the mild heating model in LECs, we have developed an innovative platform and provide a new direction for lens aging research
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