Abstract:
:Two peptides, rHRnG and hproHRnG, which were encoded by the nucleotide sequences complementary to mRNA of rat hypothalamic gonadotropin-releasing hormone (GnRH) and human placental proGnRH(-3-13), respectively, were synthesized. A remarkable hydropathic anti-complementarity was observed in the N-terminal region between hproHRnG and human proGnRH(-3-13). Neither hproHRnG nor rHRnG bound GnRH in ELISA unless extremely high concentrations of peptides were used. 125I-GnRH failed to bind with either rHRnG or hproHRnG previously coated polypropylene tubes. Antisera against these peptides were generated in rabbits. All the rabbits produced antibodies with high titer as tested by ELISA. One rabbit immunized with hproHRnG showed markedly reduced serum testosterone levels as compared with those of other rabbits. Intravenous administration of 1 ml serum from this rabbit, antiserum R281, into ovariectomized rats significantly decreased plasma LH. Using antiserum R281, about 10% of female rat pituitary cells were stained by immunohistochemistry. The staining was specific to hproHRnG since it was abolished by preabsorption of the antiserum with hproHRnG, but not with rHRnG, GnRH, LH nor any other peptide tested. This particular antiserum may have recognized the GnRH receptor, and thereby interfered with the action of endogenous GnRH. These results appear to be in agreement with the view that there is a structural similarity between the receptor for a peptide and the so-called complementary peptide.
journal_name
Peptidesjournal_title
Peptidesauthors
Görcs TJ,Gottschall PE,Coy DH,Arimura Adoi
10.1016/0196-9781(86)90144-0subject
Has Abstractpub_date
1986-11-01 00:00:00pages
1137-45issue
6eissn
0196-9781issn
1873-5169pii
0196-9781(86)90144-0journal_volume
7pub_type
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