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Science 4 April 1986:
Vol. 232. no. 4746, pp. 68 - 70
DOI: 10.1126/science.3082009
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Articles

Science, Vol 232, Issue 4746, 68-70
Copyright © 1986 by American Association for the Advancement of Science

articles

Stimulation of gonadotropin release by a non-GnRH peptide sequence of the GnRH precursor

RP Millar, PJ Wormald, and RC Milton

The human gonadotropin-releasing hormone (GnRH) precursor comprises the GnRH sequence followed by an extension of 59 amino acids. Basic amino acid residues in the carboxyl terminal extension may represent sites of processing to biologically active peptides. A synthetic peptide comprising the first 13 amino acids (H X Asp-Ala-Glu-Asn-Leu-Ile-Asp-Ser-Phe-Gln-Glu-Ile-Val X OH) of the 59-amino acid peptide was found to stimulate the release of gonadotropic hormones from human and baboon anterior pituitary cells in culture. The peptide did not affect thyrotropin or prolactin secretion. A GnRH antagonist did not inhibit gonadotropin stimulation by the peptide, and the peptide did not compete with GnRH for GnRH pituitary receptors, indicating that the action of the peptide is independent of the GnRH receptor. The GnRH precursor contains two distinct peptide sequences capable of stimulating gonadotropin release from human and baboon pituitary cells.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Differential Splicing of Three Gonadotropin-Releasing Hormone Transcripts in the Ovary of Seabream (Sparus aurata).
M. Nabissi, L. Soverchia, A. M. Polzonetti-Magni, and H. R. Habibi (2000)
Biol Reprod 62, 1329-1334
   Abstract »    Full Text »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)