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EXPERIMENTAL STUDY |
Department of Gynecology and Obstetrics, Georg-August-University, Robert-Koch-Street 40, D-37075 Göttingen, Germany, 1 Department of Nuclear Medicine, Philipps-University, Marburg, Germany and 2 Department of Veterinary Medicine and Primate Husbandry, German Primate Center, Göttingen, Germany
(Correspondence should be addressed to C Gründker; Email: grundker{at}med.uni-goettingen.de)
We have recently demonstrated that the antiproliferative activity of GnRH-II on human endometrial and ovarian cancer cell lines is not mediated through the GnRH-I receptor. A functional receptor for human GnRH-II has not yet been identified. In this study, we have generated a polyclonal antiserum to the putative human GnRH-II receptor using a peptide (YSPTMLTEVPPC) corresponding to the third extracellular domain coupled to keyhole limpet haemocyanin via the Cys residue. A database search showed no identical peptide sequences in any other human gene. To avoid cross-reactions against two similar amino acid sequences the antiserum was pre-absorbed using these peptides. Immune histological sections of human placenta and human endometrial, ovarian and prostate cancers using rabbit anti-human GnRH-II receptor antiserum showed GnRH-II receptor-like staining. Western blot analysis of cell membrane preparations of human endometrial and ovarian cancer cell lines yielded a band at approximately 43 kDa whereas Western blot analysis of cell membrane preparations of ovaries obtained from the marmoset monkey (Callithrix jacchus) yielded a band at approximately 54 kDa. To identify the GnRH-II receptor-like antigen we used the photo-affinity labelling technique. Photochemical reaction of 125I-labelled (4-azidobenzoyl)-N-hydroxysuccinimide-[D-Lys6]-GnRH-II (10–9 M) with cell membrane preparations of human endometrial and ovarian cancer cells yielded a band at approximately 43 kDa. In competition experiments, the GnRH-I agonist Triptorelin (10–7 M) showed a weak decrease of 125I-labelled (4-azidobenzoyl)-N-hydroxysuccinimide-[D-Lys6]-GnRH-II binding to its binding site. The GnRH-I antagonist Cetrorelix (10–7 M) showed a clearly stronger decrease, whereas GnRH-II agonist [D-Lys6]-GnRH-II (10–7 M) was the most potent competitor. Western blot analysis of the same gel using rabbit anti-human GnRH-II receptor antiserum identified this band as GnRH-II receptor-like antigen.
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