The effect of 17 beta-estradiol on collagen and noncollagenous protein synthesis in the uterus and some periodontal tissues.
The effect of a single dose of 17 beta-estradiol on collagen metabolism in the uterus and various oral tissues was determined in ovariectomized nulliparous rats. Eight days after ovariectomy, 200-g rats were given 100 micrograms estradiol ip. Forty hours later, 2 mCi [3H]proline were administered by ip injection, and the animals were killed 2 h later. The specific radioactivities of hydroxyproline and proline in both salt-soluble and salt-insoluble proteins were used as a measure of collagen and noncollagenous protein metabolism. Estradiol was found to induce a 2-fold increase in the specific radioactivity of newly synthesized collagen and an 8-fold increase in the specific radioactivity of the insoluble collagen in the uterus. The discrepancy between these results could be largely accounted for by a 2- to 3-fold increase in the size of the newly synthesized collagen pool. Stimulation of noncollagenous protein synthesis was also observed. The total collagen content of the uterus was not significantly altered in estradiol-treated animals, suggesting that estradiol stimulates both the synthesis and degradation of collagen. Using [14C]glycine as a precursor, the nature of the collagens synthesized in the uterus was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Estradiol was found to stimulate the synthesis of both type I and type III collagens, but no change in the pattern of procollagen conversion could be discerned. In contrast to the uterine tissues, the only significant effect of estradiol on protein metabolism in the oral tissues was a decrease in the newly synthesized collagen specific radioactivity in the molar periodontal ligament.