High impact information on GNRHR

• On the basis of the high-resolution X-ray structure of bovine rhodopsin as well as available data on GnRH-R mutants, models for ligand-receptor interactions are proposed [1].
• To investigate the impact of aromatic residues within transmembrane helix 6 (TMH6) of the human gonadotropin-releasing hormone receptor (GnRH-R) on agonist and antagonist binding, residues Y(283), Y(284), W(289), Y(290), W(291), and F(292) were exchanged to alanine and analyzed comprehensively in functional reporter gene and ligand binding assays [1].
• Solubilization of the gonadotropin-releasing hormone receptor from bovine pituitary plasma membranes [2].
• Interaction of adenosine 3',5'-monophosphate derivatives with the gonadotropin-releasing hormone receptor on pituitary and ovary [3].
• Effects of bovine follicular fluid and passive immunization against gonadotropin-releasing hormone (GnRH) on messenger ribonucleic acid for GnRH receptor and gonadotropin subunits in ovariectomized ewes [4].

Biological context of GNRHR

• These results do not support the hypothesis that inhibin increases concentrations of GnRH receptor mRNA in the ewe, and they provide evidence that inhibin is not an acute regulator of ovine GnRH receptor gene expression in vivo [4].
• In conclusion, CHAPS appears to be quite suitable for the solubilization of the binding site moiety of the pituitary GnRH receptor with good retention of the binding characteristics, thus offering a new possibility for the purification and characterization of the GnRH receptor protein [5].
• Amino acid sequence analysis showed that the protein is different from the cloned GnRH receptor, but homologous with a similar protein recently purified from bovine pituitary [6].
• At slaughter (d 12 to 14 of the estrous cycle), anterior pituitary LH and FSH content and steady-state mRNA encoding alpha, LHbeta, and GnRH receptor did not differ (P > 0.10) among treatments [7].

Anatomical context of GNRHR

• Cows were exsanguinated within 1 to 2 h after removal of intravaginal inserts and pituitary glands were collected and stored at -80 degrees C until messenger ribonucleic acid (mRNA) for gonadotropin-releasing hormone receptor (GnRH-R) and gonadotropin subunits, pituitary content of GnRH-R, and LH and FSH were quantified [8].
• Thus, GnRH receptor protein appears to be an intrinsic constituent of the cell membrane, and perhaps, other membranous organelles [9].

Associations of GNRHR with chemical compounds

• The mRNA level for gonadotropin-releasing hormone receptor in the pituitary was decreased by DES, but not by toluene [10].
• Purification of the GnRH receptor protein (GnRH.R) resulted in about 500 000-fold increase of binding activity and yielded a single protein species on polyacrylamide gel electrophoresis in SDS, of estimated molecular weight 60 000 [11].

Other interactions of GNRHR

• Abundance of mRNA for GnRH-R, common alpha-subunit, and FSHbeta were not affected by treatments [8].

Analytical, diagnostic and therapeutic context of GNRHR

• Northern blot analysis of the RNA from bovine pituitary, probed with 32P-labeled bovine GnRH receptor cDNA, revealed the presence of four different transcripts (5.0, 3.5, 2.5 and 1.5 kb) in the pituitary of which the 5.0 kb form was most abundant [12].
• Passive immunization against GnRH did not affect concentrations of GnRH receptor mRNA but resulted in a reduction (p < 0.05) in amount of LHbeta mRNA [4].

References