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J M Burke, S S Twining; Regional comparisons of cathepsin D activity in bovine retinal pigment epithelium.. Invest. Ophthalmol. Vis. Sci. 1988;29(12):1789-1793.
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Cathepsin D is the lysosomal protease in the retinal pigment epithelium which is presumed to be the major enzyme involved in the degradation of shed discs during the photoreceptor renewal process. In this study, the cathepsin D activity in RPE cells from the posterior area centralis was compared to the activity in cells from the equatorial region of the same bovine eyes. Enzyme activities were measured both in paired fresh RPE isolates from the two retinal regions and in paired regional RPE cultures. Cultures were further analyzed for changes in enzyme activity with time in vitro from 3 to 11 weeks. Analysis of freshly isolated RPE cells from 30 eyes indicated that cells from the area centralis have significantly higher cathepsin D activity than cells from the more peripheral retina. Paired cultures of RPE from the two regions did not express the intraeye topographical differences in enzyme activity which were observed in fresh isolates. There were significant variations in enzyme activity in cultured RPE cells with time in vitro, but activity levels did not show progressive increases or decreases with in vitro aging. After 11 weeks in vitro, but not at earlier times, the enzyme activities in the paired regional cultures from the same eye were highly correlated. The data suggest that the higher levels of cathepsin D activity observed in the freshly isolated RPE from the area centralis result from modulators of enzyme activity which are not present in culture.
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