Abstract

The primary aim of this research is to delineate regulatory features of the ovary as they relate to the action of gonadotropins and/or prostaglandins. In this coming period we propose: 1. To determine the primary structure of the rat luteal LH receptor. 2. To raise antibodies against it to investigate the subunits composition and biosynthesis of the LH receptor. 3. To purify the luteal coupling proteins Ns and Ni responsible for transmission of the signal generated by occupancy of LH and FSH receptors into altered rates of cyclic AMP formation, and to determine the properties of these N proteins as they compare to N proteins from other tissues. 4. To purify, if possible, biologically active LH receptors and study their coupling to luteal, as well as other, Ns proteins. 5. To perform a comparative study on the structure of LH receptors in luteal, follicular and Leydig cell tissues. 6. To delineate the genomic organization of LH receptor gene(s) and their possible homologies to other receptor genes. 7. To initiate studies on the effects of PGF2alpha and oxytocin on the expression of oxytocin-like peptides and LH receptor in regressing luteal tissue. The information gained and the tools developed through this research will contribute significantly in the definition of the role of LH receptors in the regulation of ovarian functions and may aid in development of new type of contraceptives.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD)
Type
Research Project (R01)
Project #
2R01HD009581-09
Application #
3311101
Study Section
Biochemical Endocrinology Study Section (BCE)
Project Start
1976-06-30
Project End
1989-03-31
Budget Start
1986-04-01
Budget End
1987-03-31
Support Year
9
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
Baylor College of Medicine
Department
Type
Schools of Medicine
DUNS #
074615394
City
Houston
State
TX
Country
United States
Zip Code
77030

  Publications

Gudermann, T; Levy, F O; Birnbaumer, M et al. (1993) Human S31 serotonin receptor clone encodes a 5-hydroxytryptamine1E-like serotonin receptor. Mol Pharmacol 43:412-8
Zhu, X; Gudermann, T; Birnbaumer, M et al. (1993) A luteinizing hormone receptor with a severely truncated cytoplasmic tail (LHR-ct628) desensitizes to the same degree as the full-length receptor. J Biol Chem 268:1723-8
Themmen, A P; Hinrichs, V; Birnbaumer, M (1993) In situ assay of hormone-stimulated adenylyl cyclase in 96-well microtitration plates: an aide to rapid identification of transformed cell clones. J Recept Res 13:69-78
Levy, F O; Gudermann, T; Birnbaumer, M et al. (1992) Molecular cloning of a human gene (S31) encoding a novel serotonin receptor mediating inhibition of adenylyl cyclase. FEBS Lett 296:201-6
Graf, R; Mattera, R; Codina, J et al. (1992) A truncated recombinant alpha subunit of Gi3 with a reduced affinity for beta gamma dimers and altered guanosine 5'-3-O-(thio)triphosphate binding. J Biol Chem 267:24307-14
Levy, F O; Gudermann, T; Perez-Reyes, E et al. (1992) Molecular cloning of a human serotonin receptor (S12) with a pharmacological profile resembling that of the 5-HT1D subtype. J Biol Chem 267:7553-62
Gudermann, T; Birnbaumer, M; Birnbaumer, L (1992) Evidence for dual coupling of the murine luteinizing hormone receptor to adenylyl cyclase and phosphoinositide breakdown and Ca2+ mobilization. Studies with the cloned murine luteinizing hormone receptor expressed in L cells. J Biol Chem 267:4479-88
Graf, R; Mattera, R; Codina, J et al. (1992) Studies on the interaction of alpha subunits of GTP-binding proteins with beta gamma dimers. Eur J Biochem 210:609-19
Birnbaumer, L; Perez-Reyes, E; Bertrand, P et al. (1991) Molecular diversity and function of G proteins and calcium channels. Biol Reprod 44:207-24
Codina, J; Grenet, D; Chang, K J et al. (1991) Urea gradient/SDS-PAGE;a useful tool in the investigation of signal transducing G proteins. J Recept Res 11:587-601

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