The objective is to examine the neural mechanisms by which the ovarian hormones, estradiol and progesterone, regulate the secretion of luteinizing hormone (LH) from the anterior pituitary gland. The experiments will test the hypothesis that the inhibitory and stimulatory feedback actions of the ovarian hormones are mediated in part via changes in the activity of noradrenergic and adrenergic neural systems that control the neurosecretion of LH-releasing hormone (LHRH). It is proposed that estradiol and progesterone affect activity in intrahypothalamic neuronal systems, such as the endogenous opioid neuropeptides and Gamma-aminobutyric acid, which regulate catecholamine release, and of neuropeptide Y (NPY), which modulates the response of the pituitary gland to LHRH. To test this hypothesis further, discrete hypothalamic areas will be incubated understatic or perifusion conditions in vitro. The release of LHRH and NPY into the medium will be measured by radioimmunoassays, while catecholamines will be measured by radioenzymatic assay. The first group of experiments will examine the postsynaptic mechanisms, especially the involvement of the Ca++ messenger system, mediating the stimulatory effect of norepinephrine (NE), epinephrine (EPI) and NPY on LHRH release. These studies will also test whether NPY alters the response of LHRH neurons to the catecholamines. A second set of studies will examine the interaction of NPY with the catecholamines in the regulation of LHRH release, and in particular, will test whether NE or EPI stimulates the release of NPY. A third set of studies will test whether the inhibitory effects of low dosage E2 treatment in vivo on the release of LHRH in vitro is due to activation of opioid systems that depress the release of NE and NPY. Other experiments will test whether the effect of in vitro progesterone to stimulate LHRH release is mediated by increased release of NE, EPI or NPY, and whether this can be inhibited by opioid or by GABA agonists. A fourth set of studies will test further the mechanisms underlying the facilitation of LHRH-induced LH release by NPY, using dispersed anterior pituitary cells in culture.

Agency
National Institute of Health (NIH)
Institute
Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD)
Type
Research Project (R01)
Project #
5R01HD013703-09
Application #
3312271
Study Section
Biochemical Endocrinology Study Section (BCE)
Project Start
1979-12-01
Project End
1990-01-31
Budget Start
1988-02-01
Budget End
1989-01-31
Support Year
9
Fiscal Year
1988
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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