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University of Florida, Gainesville 32611
Abstract
Proteins in uterine secretions have been studied in a variety of species since proteins are known to serve as enzymes, carrier molecules and possible regulators of genetic activity (histone and nonhistone chromosomal proteins). The data presented herein deal specifically with proteins isolated from the uterine lumen of the non-pregnant pigs and fetal fluids of pregnant gilts. Proteins having acid phosphatase, leucine aminopeptidase, lysozyme, cathepsin and non-specific esterase enzymatic activity have been detected. Futhermore, two different size classes of proteins have been shown to bind H3-progesterone, but not tritium labeled estradiol, estrone or prostaglandin F2
. Proteins having these same enzymatic and progesterone binding properties have been found in allantoic fluid from pregnant gilts between 30 and 100 days of gestation. Results of immunofluorescent antibody studies designed to determine the site of synthesis, movement and localization of the porcine purple acid phosphatase suggest that: (1) these proteins are maternal in origin; (2) the proteins are synthesized and secreted by the uterine endometrial surface and glandular epithelium and (3) the proteins are absorbed via the placental areolae, transported across the chorio-allantois membranes and sequestered in the allantoic fluid. Passive immunization of gilts against the purple intra-uterine protein resulted in a reduction in placental development. On the other hand, progesterone therapy designed to increase uterine protein secretions stimulated placental development through increased placental length and allantoic fluid volume. The latter effect may have resulted from an increased rate of conversion of progesterone to estrogens since water transport is an estrogen related phenomenon. In general, the available data suggest that uterine protein secretions may affect placental development primarily and embryonic/fetal development only secondarily.
1 Invitational paper presented at the 66th Annual Meeting of the American Society of Animal Science, University of Maryland, July 29, 1974. Original research supported in part by Hatch funds and in part by U.S.D.A. Cooperative Agreement 12-14-1001-402. Department of Animal Science, Florida Agricultural Experiment Station Journal Series No. 5751.
2 The author wishes to acknowledge that various aspects of this research were conducted in cooperation with Dr. R. M. Roberts, Department of Biochemistry, Dr. B. M. Gebhardt, Department of Pathology, Dr. W. W. Thatcher, Department of Dairy Science and Dr. H. D. Wallace, Department of Animal Science. Support for this research has been provided by U.S.D.A. Cooperative Agreement 12-14-1001-402 (F.W.B.), N.S.F. Grant BMS 74-18016 (R.M.R.) and N.I.H. Grants HD-00384 and AI-00401 (B.M.G.). Excellent technical assistance was provided by Miss Norma J. Baldwin and Mrs. Linda J. Owens.
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