Summary
Uterine peroxidase enzyme activity has been studied as a marker for estrogen action in the uterus to help clarify the mechanism of estrogen action and its modulation by antiestrogens and progestins. Estrogen-induced increases in peroxidase were found to closely parallel increases in uterine weight and DNA content in the castrate rat. In the cycling female rat, uterine peroxidase levels were highest during proestrus and estrus and the lower levels of metestrous and diestrous uteri could be raised to estrous levels by administration of estrogen. However, the estrous levels were not further increased by estrogen treatment.
The antiestrogen, CI628, while a very weak inducer of uterine peroxidase, is an effective antagonist of the estrogen induction of the enzyme. The prolonged duration of this CI628-effected inhibition corresponds to the prolonged depletion of cytoplasmic estrogen receptor seen with CI628 treatment.
Progesterone, R5020 and norethindrone were also found to be effective antagonists of estrogen-induced uterine peroxidase. Medrogestone and clogestrone, less potent progestins in the rat, were also less effective antagonists of peroxidase induction. Since progesterone was found to inhibit peroxidase induction due to both estrone and diethylstilbestrol, as well as estradiol, it is considered unlikely that this antagonism relates to progestin-induced increases in uterine 17β-hydroxysteroid dehydrogenase. Rather, it is proposed that progestins, acting through progestin receptor, may have a more direct role, possibly acting at the level of the genome to repress the expression of estrogen-induced products.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Jensen, E. V., Numata, M., Brecher, P.I., and DeSombre, E.R. (1971). In “The Biochemistry of Steroid Hormone Action, ” R. M. S. Smellie, ed. Academic Press, London. pp 133–159.
Jensen, E. V., and DeSombre, E.R. (1973). Science 182: 126–134.
O’Malley, B. W., and Means, A.R. (1974). Science 183: 610–620
Yamamoto, K.R., and Alberts, B.M. (1976). Annu. Rev. Biochem. 45: 721–746.
Gorski, J., and Gannon, F. (1976). Annu. Rev. Physiol. 38: 425–450.
Liao, S. (1975). Int. Rev. Cytol. 41: 87–172.
McKnight, G. S., Pennequin, P., and Schimke, R. T. (1975). J. Biol. Chem. 250: 8105–8110.
Palmiter, R. D., Moore, P. B., Mulvihill, E. R. (1976). Cell 8: 557–572.
Tsai, S. Y., Tsai, M. J., Schwartz, R., Kalimi, M., Clark, J. H., and O’Malley, B. W. (1975). Proc. Natl. Acad. Sci. U.S. 72: 4228–4232.
Lyttle, C.R., and DeSombre, E.R. (1977). Nature 268: 337–339.
Lyttle, C. R., and DeSombre, E. R. (1977). Proc. Natl. Acad. Sci. U. S. 74: 3162–3166.
Burton, K. (1956). Biochem. J. 62: 315–323.
Lucas, F. V., Neufeld, H. A., Utterback, J. G., Martin, A. P., and Stotz, E. (1955). J. Biol. Chem. 214: 775–780.
Klebanoff, S. J. (1965). Endocrinology 76: 301–311.
Jellinck, P. H., and Lyttle, C.R. (1972). Adv. Enzyme Regul. 11: 17–33.
Jellinck, P. H., McNabb, T., Cleveland, S., and Lyttle, C.R. (1976). Adv. Enzyme Reg. 14: 447–465.
Brokelmann, J., and Fawcett, D.W. (1969). Biol. Reprod. 1: 59–71.
Churg, A., and Anderson, W.A. (1974). J. Cell Biol. 62: 449–459.
Anderson, W.A., Kang, Y. H., and DeSombre, E.R. (1975). J. Cell Biol. 64: 668–681.
Lerner, L. J., Holthause, F. J., Jr., and Thompson, C. R. (1958). Endocrinology 63: 295–318.
Jensen, E. V., Jacobson, H. I., Smith, S., Jungblut, P. W., and DeSombre, E.R. (1972). Gynec. Invest. 3: 108–122.
Clark, J. H., Peck, E.J., Jr., and Anderson, J.N. (1974). Nature 251: 446–448.
Katzenellenbogen, B. S. (1978). In “Progress in Cancer Research and Therapy, Vol 10, Hormones, Receptors and Breast Cancer, ” W. L. McGuire, ed. Raven Press, N.Y. pp 135–157.
DeSombre, E.R., and Lyttle, C.R. (1978). In “Progress in Cancer Research and Therapy, Vol 10, Hormones, Receptors and Breast Cancer, ” W. L. McGuire, ed. Raven Press, N.Y. pp 181–197.
McNabb, T., and Jellinck, P. H. (1976). Steroids 27: 681–689.
Lerner, L. J. (1964). Rec. Prog. Hormone Res. 20: 435490.
Brenner, R.M. (1969). In “The Mammalian Oviduct, ” E. S. E. Hafez and R.J. Blandau, eds. Univ. Chicago Press, Chicago, pp 203–229.
Anderson, W. A., DeSombre, E. R., and Kang, Y. H. (1977). Biol. Reprod. 16: 409–419.
Raynaud, J. P. (1977). In “Progesterone Receptors in Normal and Neoplastic Tissues, ” W. L. McGuire, J. P. Raynaud and E.E. Saulieu, eds. Raven Press, N. Y. pp 9–21.
Revesz, C., Banik, U.K., and Herr, F. (1967). Steroids 10: 291–305.
Tseng, L., and Gurpide, E. (1975). Endocrinology 97: 825833.
Tseng, L., and Gurpide, E. (1973). Endocrinology 93: 245248.
Leung, B. S., and Sasaki, G. H. (1973). Biochem. Biophys. Res. Commun 55: 1180–1185.
Mester, J., Martel, D., Baulieu, E. E. (1974). Nature 250: 766–767.
Brenner, R. M., Resko, J. A., and West, N.B. (1974). Endocrinology 95: 1094–1099.
Hsueh, A. J. W., Peck, E. J,, Jr., and Clark, J. H. (1975). Nature 254: 337–339.
Bhakoo, H. S., and Katzenellenbogen, B. S. (1977). Mol. Cell. Endocrinol. 8: 121–134.
Clark, J. H., Hsueh, A.J.W., and Peck, E. J., Jr. (1977). Ann. N. Y. Acad. Sci. 286: 161–176.
Jensen, E. V., Numata, M., Smith, S., Suzuki, T., Brecher, P. I., and DeSombre, E. R. (1969). Dev. Biology Suppl. 3: 151–171.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1979 Springer Science+Business Media New York
About this chapter
Cite this chapter
DeSombre, E.R., Lyttle, C.R. (1979). Steroid Hormone Regulation of Uterine Peroxidase Activity. In: Leavitt, W.W., Clark, J.H. (eds) Steroid Hormone Receptor Systems. Advances in Experimental Medicine and Biology, vol 117. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-6589-2_8
Download citation
DOI: https://doi.org/10.1007/978-1-4757-6589-2_8
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-6591-5
Online ISBN: 978-1-4757-6589-2
eBook Packages: Springer Book Archive