The overall objective of the proposed research is to investigate the neurochemical mechanisms by which estradiol and progesterone control the secretion of luteinizing hormone (LH) and prolactin (PRL) from the anterior pituitary gland. This research will test the hypothesis that ovarian hormones regulate LH and PRL secretion by activating endogenous opiate peptide systems that exert localized control over the release of norepinephrine, epinephrine and serotonin. It is also hypothesized that monoaminergic control over LH and PRL is modified by the presence or absence of testosterone during a perinatal critical period. These hypotheses will be tested by the following approaches. First, ovarian hormones will be administered in specific regimens that depress or elevate LH and PRL, and the effects of these treatments on the turnover of serotonin in discrete brain nuclei will be assessed. This will identify those sites where ovarian hormones alter serotonergic activity. The second phase will attempt to establish causal relationships between the changes of serotonin activity and the changes in LH and PRL induced by the ovarian hormones. This will involve attempts to alter the expected ovarian hormonal feedback effects by producing local denervations with the neurotoxic indoleamine, 5,7-dihydroxytryptamine. The third phase will test whether ovarian hormones interact with endogenous opiate neuropeptides that influence the release of monoamines to regulate LH and PRL secretion. This will be accomplished by testing whether ovarian hormonal effects on both pituitary hormone secretion and on monoamine turnover can be affected by opiate agonists and antagonists. A fourth aspect of the project will investigate whether castration of neonatal males or administration of testosterone to neonatal females, manipulations that alter ovarian hormonal control over LH and PRL in adulthood, also alter the effects of ovarian hormones on LH-releasing hormone and on monoamine turnover.

Agency
National Institute of Health (NIH)
Institute
Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD)
Type
Research Project (R01)
Project #
5R01HD013703-07
Application #
3312270
Study Section
Biochemical Endocrinology Study Section (BCE)
Project Start
1979-12-01
Project End
1987-01-31
Budget Start
1986-02-01
Budget End
1987-01-31
Support Year
7
Fiscal Year
1986
Total Cost
Indirect Cost
Name
University of Tennessee Health Science Center
Department
Type
Schools of Medicine
DUNS #
941884009
City
Memphis
State
TN
Country
United States
Zip Code
38163
Parker, Michael S; Balasubramaniam, Ambikaipakan; Sallee, Floyd R et al. (2018) The Expansion Segments of 28S Ribosomal RNA Extensively Match Human Messenger RNAs. Front Genet 9:66
Parker, Michael S; Park, Edwards A; Sallee, Floyd R et al. (2016) Canonical Matches of Human MicroRNAs with mRNAs: A Broad Matrix of Position and Size. Microrna 5:211-221
Parker, Michael S; Sallee, Floyd R; Park, Edwards A et al. (2015) Homoiterons and expansion in ribosomal RNAs. FEBS Open Bio 5:864-76
Parker, Michael S; Park, Edwards A; Sallee, Floyd R et al. (2015) G and C Iterons and Strings in MicroRNAs Should be Important in Regulation of mRNAs(†). Microrna 4:175-84
Parker, Michael S; Sah, Renu; Balasubramaniam, Ambikaipakan et al. (2014) On the expansion of ribosomal proteins and RNAs in eukaryotes. Amino Acids 46:1589-604
Parker, Michael S; Sah, Renu; Balasubramaniam, Ambikaipakan et al. (2014) Dimers of G-protein coupled receptors as versatile storage and response units. Int J Mol Sci 15:4856-77
Parker, Michael S; Balasubramaniam, Ambikaipakan; Parker, Steven L (2012) On the segregation of protein ionic residues by charge type. Amino Acids 43:2231-47
Parker, Michael S; Sah, Renu; Parker, Steven L (2012) Surface masking shapes the traffic of the neuropeptide Y Y2 receptor. Peptides 37:40-8
Parker, Michael S; Park, Edwards A; Sallee, Floyd R et al. (2011) Two intracellular helices of G-protein coupling receptors could generally support oligomerization and coupling with transducers. Amino Acids 40:261-8
Estes, Anne-Marie; McAllen, Kathleen; Parker, Michael S et al. (2011) Maintenance of Y receptor dimers in epithelial cells depends on interaction with G-protein heterotrimers. Amino Acids 40:371-80

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