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Biology of Reproduction, Vol 25, 393-398, Copyright © 1981 by Society for the Study of Reproduction
1 Departments of Obstetrics and Gynecology,
Biological Chemistry, and Physiology,
University of Cincinnati, College of Medicine,
Cincinnati, Ohio 45267 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.
Note:
ACKNOWLEDGMENTS
The authors would like to thank Dr. James Lessard
for his assistance with immunohistochemical staining
techniques and fluorescence photography. We thank
Dr. Roger Ganschow for assistance with the methods
of measuring amino acid incorporation into immunoprecipitable protein. Matthew McBride provided
valuable technical assistance. This research was supported by grants from NIH (HD-07255 and HD-10721).
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