Uterine Lysosomal Cathepsin D Activity, Rate of Synthesis, and Immunohistochemical Localization Following Initiation of Decidualization in Pseudopregnant Rats

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Abstract
Initiation of decidualization in pseudopregnant rats by intrauterine administration of an oil stimulus resulted in significant decreases in the activity of the lysosomal protease, cathepsin D, and significant decreases in the rate of synthesis of the enzyme. Decreases in uterine cathepsin D activity after the decidualizing stimulus required delivery of the stimulus on day 4 of pseudopregnancy. Major concentrations of cathepsin D protein identified by immunohistochemical staining were observed in glandular and luminal epithelial cells. The accumulation of cathepsin D in the luminal epithelial cells during early pseudopregnancy could provide these cells with the means for cellular autophagic activity and eventual destruction during the uterine decidual response.