Endogenous circadian clock regulation is essential to normal rhythmicity, particularly the timing of hormone release in the brain. In the context of mammalian reproduction, a surge of a specific hormone, gonadotrophin-releasing hormone (GnRH), initiates a surge of luteinizing hormone (LH) from the pituitary gland, which is required for ovulation in females. Ordinarily, GnRH is secreted in a pulsatile pattern distinct from the surging that promotes ovulation. These surges occur with an approximately 24-hour release pattern and require elevated levels of ovarian estradiol (E2), the most common form of estrogen in human mammals, originating from the granulosa cells of the developing follicle. GnRH neurons express the estrogen receptor isoform estrogen receptor β (ERβ). Currently, little is known about mechanisms underlying GnRH/LH surge timing and how E2 acts directly on GnRH neurons. To better understand how endogenous clocks interact with sex-steroid hormone signalling, we explored protein-protein interactions between ERβ and the circadian clock transcription factor BMAL1 in multiple representative cell lines, in both the absence and presence of E2. It was hypothesized that direct protein-protein interactions may exist among clock components and ERβ in immortalized GnRH neurons (GT1-7 cell lines), exhibiting altered interactions in the presence of E2. Co-Immunoprecipitation (Co-IP) and Western blot procedures provided unclear results as some data supported the hypothesis, while other data contradict it.
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description.provenance : Submitted by Wanda Crannell (email@example.com) on 2012-06-19T18:24:26ZNo. of bitstreams: 2seminar grimwood In vitro Protein-Protein interactions in Gonadotropin-Releasing Hormone Neurons.pptx: 4037346 bytes, checksum: c429354311e2e39bc72faa0a7d005ca2 (MD5)Grimwood BRR thesis.pdf: 655644 bytes, checksum: 22eb5cda2c0b7ea2b7e585805844dd7a (MD5)